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Conserved domains on  [gi|1720426625|ref|XP_030099191|]
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unconventional myosin-IXb isoform X7 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
160-971 0e+00

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


:

Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 1330.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd01385      1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd01385     81 ESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01385    161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  400 QIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd01385    241 QIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  480 SMAKSLYSALFDWIVLRINHALLNKKDMEEaVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01385    321 AMAKCLYSALFDWIVLRINHALLNKKDLEE-AKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGR 639
Cdd:cd01385    400 YKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  640 VKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAagisspa 719
Cdd:cd01385    480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGRRRAQRTAGH------- 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  720 trshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedprrllqslsl 799
Cdd:cd01385        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  800 fqkprtsflkskgikqkqiipknlldskslrliiSMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFF 879
Cdd:cd01385    553 ----------------------------------SLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFF 598
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  880 IRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEKLQVDRQ 959
Cdd:cd01385    599 IRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDRD 678
                          810
                   ....*....|..
gi 1720426625  960 NYQIGKTKVFLK 971
Cdd:cd01385    679 NYQIGKTKVFLK 690
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1700-1885 5.67e-128

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


:

Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 398.98  E-value: 5.67e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1779
Cdd:cd04407      1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1780 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1859
Cdd:cd04407     81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160
                          170       180
                   ....*....|....*....|....*.
gi 1720426625 1860 PDNSDPLTSMKDVLKITTCVEMLIKE 1885
Cdd:cd04407    161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
RA_Myosin-IXb cd17217
Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is ...
16-112 1.78e-55

Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is a motor protein with a Rho GTPase activating domain (RhoGAP); it is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen and in several immune cells including dendritic cells, macrophages and CD4+ T. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a RhoGAP domain. Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells.


:

Pssm-ID: 340737  Cd Length: 96  Bit Score: 188.08  E-value: 1.78e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   16 TYHLHIYPQLSSAgSQTSCRVTATKDSTTSDVIQDVVASLHLDGSKHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRA 95
Cdd:cd17217      1 VYALQIYPQLSAE-SSTCCIVLATKEATASDVIKDAVATLGLDSSKPYVLAEVKESGGEEWVLDANDSPVQRVLLWPRKA 79
                           90
                   ....*....|....*..
gi 1720426625   96 QDEHPQEDGYYFLLQER 112
Cdd:cd17217     80 QDDHPQSDGYYFLLQER 96
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
1630-1687 1.89e-36

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


:

Pssm-ID: 410434  Cd Length: 58  Bit Score: 132.29  E-value: 1.89e-36
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720426625 1630 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1687
Cdd:cd20884      1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCSSTC 58
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
1002-1031 3.35e-05

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


:

Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 42.53  E-value: 3.35e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720426625 1002 ERKHFVQMKHAALTIQACWRSYRVRRALER 1031
Cdd:cd23767      1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30
PHA02682 super family cl31817
ORF080 virion core protein; Provisional
2023-2117 4.50e-05

ORF080 virion core protein; Provisional


The actual alignment was detected with superfamily member PHA02682:

Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 47.55  E-value: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 2023 PAPALPCPISPTLSPLPEAAAPPRGRPTSFVTVRVKTPRR-TPIMPMANIKLPPGLPLHLTSWAPALQEAVVPvKRREPP 2101
Cdd:PHA02682    96 PACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARpAPACPPSTRQCPPAPPLPTPKPAPAAKPIFLH-NQLPPP 174
                           90
                   ....*....|....*.
gi 1720426625 2102 ARRQDQVHSVYIAPGA 2117
Cdd:PHA02682   175 DYPAASCPTIETAPAA 190
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1030-1052 1.22e-04

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


:

Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.77  E-value: 1.22e-04
                            10        20
                    ....*....|....*....|...
gi 1720426625  1030 ERTQAAVYLQAAWRGYLQRQAYH 1052
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
SepH super family cl48966
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
1926-2067 3.93e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


The actual alignment was detected with superfamily member NF040712:

Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 41.68  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1926 FSSPYEGVRIKSPRTPVVQDLELGALPEEAAGGDEDREKEI---LMERIQSIKEEKEDITYRLPELDPRGSDEENLDSET 2002
Cdd:NF040712   192 FGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDpaeAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPD 271
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720426625 2003 SASTESLLEERGVRGAVEGPPAPALPCPISPTLSPLPEAAAPPRGRPTsfVTVRVKTPRRTPIMP 2067
Cdd:NF040712   272 EATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPP--PAPKPKRRRRRASVP 334
 
Name Accession Description Interval E-value
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
160-971 0e+00

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 1330.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd01385      1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd01385     81 ESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01385    161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  400 QIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd01385    241 QIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  480 SMAKSLYSALFDWIVLRINHALLNKKDMEEaVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01385    321 AMAKCLYSALFDWIVLRINHALLNKKDLEE-AKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGR 639
Cdd:cd01385    400 YKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  640 VKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAagisspa 719
Cdd:cd01385    480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGRRRAQRTAGH------- 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  720 trshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedprrllqslsl 799
Cdd:cd01385        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  800 fqkprtsflkskgikqkqiipknlldskslrliiSMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFF 879
Cdd:cd01385    553 ----------------------------------SLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFF 598
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  880 IRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEKLQVDRQ 959
Cdd:cd01385    599 IRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDRD 678
                          810
                   ....*....|..
gi 1720426625  960 NYQIGKTKVFLK 971
Cdd:cd01385    679 NYQIGKTKVFLK 690
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
141-980 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 889.59  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   141 LPRPQADFDDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALAD 220
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   221 VAYYAMLRKHVNQCIVISGESGSGKTQSTNFLIHCLTALS-QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKF 299
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSgSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKF 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   300 IQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKH 379
Cdd:smart00242  161 IEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDAE 240
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   380 DFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGlEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTV 459
Cdd:smart00242  241 EFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAS-TVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   460 TVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFERNSFEQFCINY 539
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-----STYFIGVLDIYGFEIFEVNSFEQLCINY 394
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   540 ANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK 619
Cdd:smart00242  395 ANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHP 474
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   620 YFLGTPVL-EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavl 698
Cdd:smart00242  475 HFSKPKKKgRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASL------------------------ 530
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   699 reagrlraeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnaFEDimafYESRNDlhnqiik 778
Cdd:smart00242  531 ------------------------------------------------------------FPS----GVSNAG------- 539
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   779 slkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSIS 858
Cdd:smart00242  540 -----------------------------------------------------------------------SKKRFQTVG 548
                           730       740       750       760       770       780       790       800
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   859 AQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK 938
Cdd:smart00242  549 SQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPD 628
                           810       820       830       840
                    ....*....|....*....|....*....|....*....|....*.
gi 1720426625   939 DVQPC----REAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQE 980
Cdd:smart00242  629 TWPPWggdaKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEE 674
Myosin_head pfam00063
Myosin head (motor domain);
149-971 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 679.77  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  149 DDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLR 228
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  229 KHVNQCIVISGESGSGKTQSTNFLIHCLTALSQKGYASGVER---TILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYL 305
Cdd:pfam00063   82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRleeQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  306 ENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQ 385
Cdd:pfam00063  162 AKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKITD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  386 QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKL 465
Cdd:pfam00063  242 KAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKER--NDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  466 ILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQ 545
Cdd:pfam00063  320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASF----IGVLDIYGFEIFEKNSFEQLCINYVNEKLQ 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  546 YYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDN-KYFLGT 624
Cdd:pfam00063  396 QFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHpHFQKPR 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  625 PVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrl 704
Cdd:pfam00063  476 LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAEL------------------------------ 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  705 raeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglp 784
Cdd:pfam00063      --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  785 WQGEDPrrllQSLSLFQKPRTSFLKSKgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSISAQFQTS 864
Cdd:pfam00063  526 FPDYET----AESAAANESGKSTPKRT--------------------------------------KKKRFITVGSQFKES 563
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  865 LNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDV 940
Cdd:pfam00063  564 LGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILapktWPKWK 643
                          810       820       830
                   ....*....|....*....|....*....|.
gi 1720426625  941 QPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:pfam00063  644 GDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
149-1073 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 649.83  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  149 DDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLR 228
Cdd:COG5022     69 DDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLS 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  229 KHVNQCIVISGESGSGKTQSTNFLIHCLTAL--SQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE 306
Cdd:COG5022    149 EKENQTIIISGESGAGKTENAKRIMQYLASVtsSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDE 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  307 NGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQ 386
Cdd:COG5022    229 NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLD 308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  387 AMEMVGFLPATKKQIFSVLSAILYLGNVTYKKratGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLI 466
Cdd:COG5022    309 ALKTIGIDEEEQDQIFKILAAILHIGNIEFKE---DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIV 385
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  467 LPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQY 546
Cdd:COG5022    386 VPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASN-----FIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQ 460
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  547 YFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKK-PTGLFYLLDEESNFPHATSHTLLAKFKQQ--HEDNKYFLG 623
Cdd:COG5022    461 FFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRlnKNSNPKFKK 540
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  624 TPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagr 703
Cdd:COG5022    541 SRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTL----------------------------- 591
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  704 lraeraekaagisspatrshmeelprgastpseklyrctgldfsFERSEELDvnafedimafyesrndlhnqiikslkgl 783
Cdd:COG5022    592 --------------------------------------------FDDEENIE---------------------------- 599
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  784 pwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSISAQFQT 863
Cdd:COG5022    600 ------------------------------------------------------------------SKGRFPTLGSRFKE 613
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  864 SLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP------ 937
Cdd:COG5022    614 SLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPskswtg 693
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  938 --KDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLKeTERQTLQEKLHGEVLRRIL-QLQSWFRMVLERKHFVQMKHAAL 1014
Cdd:COG5022    694 eyTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFK-AGVLAALEDMRDAKLDNIAtRIQRAIRGRYLRRRYLQALKRIK 772
                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720426625 1015 TIQACWRSYRVRRALER---TQAAVYLQAAWRGYLQRQAYHHQRHSIIRLQSLCRGHLQRRS 1073
Cdd:COG5022    773 KIQVIQHGFRLRRLVDYelkWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRE 834
PTZ00014 PTZ00014
myosin-A; Provisional
148-1046 1.80e-132

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 437.15  E-value: 1.80e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  148 FDDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYEN-QQLGKLEPHVFALADVAYYAM 226
Cdd:PTZ00014    98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENL 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  227 LRKHVNQCIVISGESGSGKTQSTNFLIhcltalsqKGYASGV--------ERTILGAGPVLEAFGNAKTAHNNNSSRFGK 298
Cdd:PTZ00014   178 HGVKKSQTIIVSGESGAGKTEATKQIM--------RYFASSKsgnmdlkiQNAIMAANPVLEAFGNAKTIRNNNSSRFGR 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  299 FIQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLK 378
Cdd:PTZ00014   250 FMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVK 329
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  379 hDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAT-GRDEGLEVGP--PEVLDTLSQLLKVKRETLVEVLTK 455
Cdd:PTZ00014   330 -DFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEgGLTDAAAISDesLEVFNEACELLFLDYESLKKELTV 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  456 RKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQF 535
Cdd:PTZ00014   409 KVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFK-----VFIGMLDIFGFEVFKNNSLEQL 483
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  536 CINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH 615
Cdd:PTZ00014   484 FINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNL 563
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  616 EDNKYFLGTPV-LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraaira 694
Cdd:PTZ00014   564 KNNPKYKPAKVdSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDL-------------------- 623
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  695 mavlreagrlraeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnaFEDIMAfyesrndlhn 774
Cdd:PTZ00014   624 ----------------------------------------------------------------FEGVEV---------- 629
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  775 qiikslkglpwqgedprrllqslslfqkprtsflkskgikQKQIIPKNLLdskslrliismtlhdrttksllhlhkkkkp 854
Cdd:PTZ00014   630 ----------------------------------------EKGKLAKGQL------------------------------ 639
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  855 psISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQV 934
Cdd:PTZ00014   640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  935 L-LP----KDVQPcREAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQEKLHgevlrriLQLQSWfrmvlerKHFVQM 1009
Cdd:PTZ00014   718 LdLAvsndSSLDP-KEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQR-------EKLAAW-------EPLVSV 782
                          890       900       910
                   ....*....|....*....|....*....|....*...
gi 1720426625 1010 khaaltIQACWRSYRVRRAL-ERTQAAVYLQAAWRGYL 1046
Cdd:PTZ00014   783 ------LEALILKIKKKRKVrKNIKSLVRIQAHLRRHL 814
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1700-1885 5.67e-128

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 398.98  E-value: 5.67e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1779
Cdd:cd04407      1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1780 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1859
Cdd:cd04407     81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160
                          170       180
                   ....*....|....*....|....*.
gi 1720426625 1860 PDNSDPLTSMKDVLKITTCVEMLIKE 1885
Cdd:cd04407    161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
1713-1886 3.85e-58

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 198.64  E-value: 3.85e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  1713 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVK-LEDFPIHAITGVLKQWLRELPEPLMTFAQYG 1791
Cdd:smart00324    2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLdLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  1792 DFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPltSMKD 1871
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVA--SLKD 159
                           170
                    ....*....|....*
gi 1720426625  1872 VLKITTCVEMLIKEQ 1886
Cdd:smart00324  160 IRHQNTVIEFLIENA 174
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
1715-1861 6.71e-56

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 191.22  E-value: 6.71e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1715 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPA-AVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1793
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDvDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720426625 1794 LRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPD 1861
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RA_Myosin-IXb cd17217
Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is ...
16-112 1.78e-55

Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is a motor protein with a Rho GTPase activating domain (RhoGAP); it is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen and in several immune cells including dendritic cells, macrophages and CD4+ T. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a RhoGAP domain. Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells.


Pssm-ID: 340737  Cd Length: 96  Bit Score: 188.08  E-value: 1.78e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   16 TYHLHIYPQLSSAgSQTSCRVTATKDSTTSDVIQDVVASLHLDGSKHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRA 95
Cdd:cd17217      1 VYALQIYPQLSAE-SSTCCIVLATKEATASDVIKDAVATLGLDSSKPYVLAEVKESGGEEWVLDANDSPVQRVLLWPRKA 79
                           90
                   ....*....|....*..
gi 1720426625   96 QDEHPQEDGYYFLLQER 112
Cdd:cd17217     80 QDDHPQSDGYYFLLQER 96
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
1630-1687 1.89e-36

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410434  Cd Length: 58  Bit Score: 132.29  E-value: 1.89e-36
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720426625 1630 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1687
Cdd:cd20884      1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCSSTC 58
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-114 1.40e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 73.91  E-value: 1.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   15 ATYHLHIYPQLSSAGSqTSCRVTATKDSTTSDVIQDVVASLHLDGSK-HYVLVEVKESGGEEWVLDASDSPVHRVLLWPR 93
Cdd:pfam00788    1 DDGVLKVYTEDGKPGT-TYKTILVSSSTTAEEVIEALLEKFGLEDDPrDYVLVEVLERGGGERRLPDDECPLQIQLQWPR 79
                           90       100
                   ....*....|....*....|.
gi 1720426625   94 RAQDehpqedgYYFLLQERNA 114
Cdd:pfam00788   80 DASD-------SRFLLRKRDD 93
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-113 7.24e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 71.95  E-value: 7.24e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625    15 ATYHLHIYPQLSSagSQTSCRVTATKDSTTSDVIQDVVASLHLDGS-KHYVLVEVKEsGGEEWVLDASDSPVHRVLLWPR 93
Cdd:smart00314    1 DTFVLRVYVDDLP--GGTYKTLRVSSRTTARDVIQQLLEKFHLTDDpEEYVLVEVLP-DGKERVLPDDENPLQLQKLWPR 77
                            90       100
                    ....*....|....*....|
gi 1720426625    94 RaqdehpqEDGYYFLLQERN 113
Cdd:smart00314   78 R-------GPNLRFVLRKRD 90
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1635-1683 2.10e-12

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 63.64  E-value: 2.10e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1720426625  1635 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKqGLRCSECKVKCHKKCADKVPKAC 50
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
1635-1683 2.34e-07

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 49.36  E-value: 2.34e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGKqGLKCSWCKLNVHKRCHEKVPPEC 50
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
1002-1031 3.35e-05

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 42.53  E-value: 3.35e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720426625 1002 ERKHFVQMKHAALTIQACWRSYRVRRALER 1031
Cdd:cd23767      1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30
PHA02682 PHA02682
ORF080 virion core protein; Provisional
2023-2117 4.50e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 47.55  E-value: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 2023 PAPALPCPISPTLSPLPEAAAPPRGRPTSFVTVRVKTPRR-TPIMPMANIKLPPGLPLHLTSWAPALQEAVVPvKRREPP 2101
Cdd:PHA02682    96 PACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARpAPACPPSTRQCPPAPPLPTPKPAPAAKPIFLH-NQLPPP 174
                           90
                   ....*....|....*.
gi 1720426625 2102 ARRQDQVHSVYIAPGA 2117
Cdd:PHA02682   175 DYPAASCPTIETAPAA 190
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1030-1052 1.22e-04

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.77  E-value: 1.22e-04
                            10        20
                    ....*....|....*....|...
gi 1720426625  1030 ERTQAAVYLQAAWRGYLQRQAYH 1052
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
1032-1052 2.10e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 37.30  E-value: 2.10e-03
                           10        20
                   ....*....|....*....|.
gi 1720426625 1032 TQAAVYLQAAWRGYLQRQAYH 1052
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
1926-2067 3.93e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 41.68  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1926 FSSPYEGVRIKSPRTPVVQDLELGALPEEAAGGDEDREKEI---LMERIQSIKEEKEDITYRLPELDPRGSDEENLDSET 2002
Cdd:NF040712   192 FGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDpaeAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPD 271
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720426625 2003 SASTESLLEERGVRGAVEGPPAPALPCPISPTLSPLPEAAAPPRGRPTsfVTVRVKTPRRTPIMP 2067
Cdd:NF040712   272 EATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPP--PAPKPKRRRRRASVP 334
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1008-1029 5.83e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 5.83e-03
                            10        20
                    ....*....|....*....|..
gi 1720426625  1008 QMKHAALTIQACWRSYRVRRAL 1029
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
 
Name Accession Description Interval E-value
MYSc_Myo9 cd01385
class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play ...
160-971 0e+00

class IX myosin, motor domain; Myosin IX is a processive single-headed motor, which might play a role in signalling. It has a N-terminal RA domain, an IQ domain, a C1_1 domain, and a RhoGAP domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276836 [Multi-domain]  Cd Length: 690  Bit Score: 1330.09  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd01385      1 QTLLENLRARFKHGKIYTYVGSILIAVNPFKFLPIYNPKYVKMYQNRRLGKLPPHIFAIADVAYHAMLRKKKNQCIVISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd01385     81 ESGSGKTESTNFLLHHLTALSQKGYGSGVEQTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYRENGMVRGAVVEKYL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01385    161 LEKSRIVSQEKNERNYHVFYYLLAGASEEERKELHLKQPEDYHYLNQSDCYTLEGEDEKYEFERLKQAMEMVGFLPETQR 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  400 QIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd01385    241 QIFSVLSAVLHLGNIEYKKKAYHRDESVTVGNPEVLDIISELLRVKEETLLEALTTKKTVTVGETLILPYKLPEAIATRD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  480 SMAKSLYSALFDWIVLRINHALLNKKDMEEaVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01385    321 AMAKCLYSALFDWIVLRINHALLNKKDLEE-AKGLSIGVLDIFGFEDFGNNSFEQFCINYANEHLQYYFNQHIFKLEQEE 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGR 639
Cdd:cd01385    400 YKKEGISWHNIEYTDNTGCLQLISKKPTGLLCLLDEESNFPGATNQTLLAKFKQQHKDNKYYEKPQVMEPAFIIAHYAGK 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  640 VKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEKAagisspa 719
Cdd:cd01385    480 VKYQIKDFREKNLDLMRPDIVAVLRSSSSAFVRELIGIDPVAVFRWAVLRAFFRAMAAFREAGRRRAQRTAGH------- 552
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  720 trshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedprrllqslsl 799
Cdd:cd01385        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  800 fqkprtsflkskgikqkqiipknlldskslrliiSMTLHDRTTKSLLHLHKKKKPPSISAQFQTSLNKLLEALGKAEPFF 879
Cdd:cd01385    553 ----------------------------------SLTLHDRTTKSLLHLHKKKKPPSVSAQFQTSLSKLMETLGQAEPFF 598
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  880 IRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIAALLEKLQVDRQ 959
Cdd:cd01385    599 IRCIKSNAEKKPLRFDDELVLRQLRYTGMLETVRIRRSGYSVRYTFQEFITQFQVLLPKGLISSKEDIKDFLEKLNLDRD 678
                          810
                   ....*....|..
gi 1720426625  960 NYQIGKTKVFLK 971
Cdd:cd01385    679 NYQIGKTKVFLK 690
MYSc smart00242
Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical ...
141-980 0e+00

Myosin. Large ATPases; ATPase; molecular motor. Muscle contraction consists of a cyclical interaction between myosin and actin. The core of the myosin structure is similar in fold to that of kinesin.


Pssm-ID: 214580 [Multi-domain]  Cd Length: 677  Bit Score: 889.59  E-value: 0e+00
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   141 LPRPQADFDDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALAD 220
Cdd:smart00242    1 NPPKFEGVEDLVLLTYLNEPAVLHNLKKRYLKDLIYTYIGLVLVAVNPYKQLPIYTDEVIKKYRGKSRGELPPHVFAIAD 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   221 VAYYAMLRKHVNQCIVISGESGSGKTQSTNFLIHCLTALS-QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKF 299
Cdd:smart00242   81 NAYRNMLNDKENQSIIISGESGAGKTENTKKIMQYLASVSgSNTEVGSVEDQILESNPILEAFGNAKTLRNNNSSRFGKF 160
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   300 IQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKH 379
Cdd:smart00242  161 IEIHFDAKGKIIGAKIETYLLEKSRVVSQAKGERNYHIFYQLLAGASEELKKELGLKSPEDYRYLNQGGCLTVDGIDDAE 240
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   380 DFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGlEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTV 459
Cdd:smart00242  241 EFKETLNAMRVLGFSEEEQESIFKILAAILHLGNIEFEEGRNDNAAS-TVKDKEELSNAAELLGVDPEELEKALTKRKIK 319
                           330       340       350       360       370       380       390       400
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   460 TVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFERNSFEQFCINY 539
Cdd:smart00242  320 TGGEVITKPLNVEQALDARDALAKALYSRLFDWLVKRINQSLSFKDG-----STYFIGVLDIYGFEIFEVNSFEQLCINY 394
                           410       420       430       440       450       460       470       480
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   540 ANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK 619
Cdd:smart00242  395 ANEKLQQFFNQHVFKLEQEEYEREGIDWTFIDFFDNQDCIDLIEKKPPGILSLLDEECRFPKGTDQTFLEKLNQHHKKHP 474
                           490       500       510       520       530       540       550       560
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   620 YFLGTPVL-EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavl 698
Cdd:smart00242  475 HFSKPKKKgRTEFIIKHYAGDVTYDVTGFLEKNKDTLSDDLIELLQSSKNPLIASL------------------------ 530
                           570       580       590       600       610       620       630       640
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   699 reagrlraeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnaFEDimafYESRNDlhnqiik 778
Cdd:smart00242  531 ------------------------------------------------------------FPS----GVSNAG------- 539
                           650       660       670       680       690       700       710       720
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   779 slkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSIS 858
Cdd:smart00242  540 -----------------------------------------------------------------------SKKRFQTVG 548
                           730       740       750       760       770       780       790       800
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   859 AQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK 938
Cdd:smart00242  549 SQFKEQLNELMDTLNSTNPHFIRCIKPNEEKKPGDFDSSLVLHQLRYLGVLENIRIRRAGFPYRLPFDEFLQRYRVLLPD 628
                           810       820       830       840
                    ....*....|....*....|....*....|....*....|....*.
gi 1720426625   939 DVQPC----REAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQE 980
Cdd:smart00242  629 TWPPWggdaKKACEALLQSLGLDEDEYQLGKTKVFLRPGQLAELEE 674
MYSc cd00124
Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase ...
160-971 0e+00

Myosin motor domain superfamily; Myosin motor domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276950 [Multi-domain]  Cd Length: 633  Bit Score: 778.69  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGK-LEPHVFALADVAYYAMLRKHVNQCIVIS 238
Cdd:cd00124      1 AAILHNLRERYARDLIYTYVGDILVAVNPFKWLPLYSEEVMEKYRGKGRSAdLPPHVFAVADAAYRAMLRDGQNQSILIS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  239 GESGSGKTQSTNFLIHCLTALSQKG------YASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd00124     81 GESGAGKTETTKLVLKYLAALSGSGssksssSASSIEQQILQSNPILEAFGNAKTVRNDNSSRFGKFIELQFDPTGRLVG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLL----LGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAM 388
Cdd:cd00124    161 ASIETYLLEKSRVVSQAPGERNFHIFYQLLaglsDGAREELKLELLLSYYYLNDYLNSSGCDRIDGVDDAEEFQELLDAL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILP 468
Cdd:cd00124    241 DVLGFSDEEQDSIFRILAAILHLGNIEFEEDEEDEDSSAEVADDESLKAAAKLLGVDAEDLEEALTTRTIKVGGETITKP 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDmeeAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd00124    321 LTVEQAEDARDALAKALYSRLFDWLVNRINAALSPTDA---AESTSFIGILDIFGFENFEVNSFEQLCINYANEKLQQFF 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  549 TQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLE 628
Cdd:cd00124    398 NQHVFKLEQEEYEEEGIDWSFIDFPDNQDCLDLIEGKPLGILSLLDEECLFPKGTDATFLEKLYSAHGSHPRFFSKKRKA 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  629 P-AFIIQHFAGRVKYQIKDFREKNMDYMRPDIVAllrgsdssyvrqligmdpvavfrwavlraairamavlreagrlrae 707
Cdd:cd00124    478 KlEFGIKHYAGDVTYDADGFLEKNKDTLPPDLVD---------------------------------------------- 511
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  708 raekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqg 787
Cdd:cd00124        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  788 edprrLLQSlslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppsiSAQFQTSLNK 867
Cdd:cd00124    512 -----LLRS-------------------------------------------------------------GSQFRSQLDA 525
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  868 LLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCR--- 944
Cdd:cd00124    526 LMDTLNSTQPHFVRCIKPNDEKKPGLFDPELVLEQLRCAGVLEAVRIRRAGYPVRLPFDEFLKRYRILAPGATEKASdsk 605
                          810       820
                   ....*....|....*....|....*...
gi 1720426625  945 -EAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd00124    606 kAAVLALLLLLKLDSSGYQLGKTKVFLR 633
MYSc_Myo7 cd01381
class VII myosin, motor domain; These monomeric myosins have been associated with functions in ...
160-971 0e+00

class VII myosin, motor domain; These monomeric myosins have been associated with functions in sensory systems such as vision and hearing. Mammalian myosin VII has a tail with 2 MyTH4 domains, 2 FERM domains, and a SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276832  Cd Length: 648  Bit Score: 695.15  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd01381      1 AGILRNLLIRYREKLIYTYTGSILVAVNPYQILPIYTAEQIRLYRNKKIGELPPHIFAIADNAYTNMKRNKRDQCVVISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLTALSqkGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd01381     81 ESGAGKTESTKLILQYLAAIS--GQHSWIEQQILEANPILEAFGNAKTIRNDNSSRFGKYIDIHFNKNGVIEGAKIEQYL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01381    159 LEKSRIVSQAPDERNYHIFYCMLAGLSAEEKKKLELGDASDYYYLTQGNCLTCEGRDDAAEFADIRSAMKVLMFTDEEIW 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  400 QIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd01381    239 DIFKLLAAILHLGNIKFEATVVDNLDASEVRDPPNLERAAKLLEVPKQDLVDALTTRTIFTRGETVVSPLSAEQALDVRD 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  480 SMAKSLYSALFDWIVLRINHALlnKKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01381    319 AFVKGIYGRLFIWIVNKINSAI--YKPRGTDSSRTSIGVLDIFGFENFEVNSFEQLCINFANENLQQFFVRHIFKLEQEE 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLgTP--VLEPAFIIQHFA 637
Cdd:cd01381    397 YDKEGINWQHIEFVDNQDVLDLIALKPMNIMSLIDEESKFPKGTDQTMLEKLHSTHGNNKNYL-KPksDLNTSFGINHFA 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  638 GRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGmdpvavfrwavlraairamavlreagrlraeraekaagiss 717
Cdd:cd01381    476 GVVFYDTRGFLEKNRDTFSADLLQLVQSSKNKFLKQLFN----------------------------------------- 514
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  718 patrshmEELPRGASTpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedprrllqsl 797
Cdd:cd01381    515 -------EDISMGSET---------------------------------------------------------------- 523
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  798 slfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkKKKPPSISAQFQTSLNKLLEALGKAEP 877
Cdd:cd01381    524 -----------------------------------------------------RKKSPTLSSQFRKSLDQLMKTLSACQP 550
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  878 FFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPkDVQP-----CREAIAALLE 952
Cdd:cd01381    551 FFVRCIKPNEYKKPMLFDRELCVRQLRYSGMMETIRIRKAGYPIRHTFEEFVERYRVLVP-GIPPahktdCRAATRKICC 629
                          810
                   ....*....|....*....
gi 1720426625  953 KLQVDRQNYQIGKTKVFLK 971
Cdd:cd01381    630 AVLGGDADYQLGKTKIFLK 648
Myosin_head pfam00063
Myosin head (motor domain);
149-971 0e+00

Myosin head (motor domain);


Pssm-ID: 395017 [Multi-domain]  Cd Length: 674  Bit Score: 679.77  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  149 DDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLR 228
Cdd:pfam00063    2 EDMVELSYLNEPSVLHNLKKRYKSDLIYTYSGLVLVAVNPYKQLPIYSEDMIKAYRGKRRGELPPHIFAIADEAYRSMLQ 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  229 KHVNQCIVISGESGSGKTQSTNFLIHCLTALSQKGYASGVER---TILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYL 305
Cdd:pfam00063   82 DKENQSILISGESGAGKTENTKKIMQYLASVSGSGSAGNVGRleeQILQSNPILEAFGNAKTVRNNNSSRFGKYIEIQFD 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  306 ENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQ 385
Cdd:pfam00063  162 AKGDIVGGKIETYLLEKSRVVYQAEGERNYHIFYQLLAGASAQLKKELRLTNPKDYHYLSQSGCYTIDGIDDSEEFKITD 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  386 QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKL 465
Cdd:pfam00063  242 KAMDILGFSDEEQMGIFRIVAAILHLGNIEFKKER--NDEQAVPDDTENLQKAASLLGIDSTELEKALCKRRIKTGRETV 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  466 ILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQ 545
Cdd:pfam00063  320 SKPQNVEQANYARDALAKAIYSRLFDWLVDRINKSLDVKTIEKASF----IGVLDIYGFEIFEKNSFEQLCINYVNEKLQ 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  546 YYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDN-KYFLGT 624
Cdd:pfam00063  396 QFFNHHMFKLEQEEYVREGIEWTFIDFGDNQPCIDLIEKKPLGILSLLDEECLFPKATDQTFLDKLYSTFSKHpHFQKPR 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  625 PVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrl 704
Cdd:pfam00063  476 LQGETHFIIKHYAGDVEYNVEGFLEKNKDPLNDDLVSLLKSSSDPLLAEL------------------------------ 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  705 raeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglp 784
Cdd:pfam00063      --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  785 WQGEDPrrllQSLSLFQKPRTSFLKSKgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSISAQFQTS 864
Cdd:pfam00063  526 FPDYET----AESAAANESGKSTPKRT--------------------------------------KKKRFITVGSQFKES 563
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  865 LNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDV 940
Cdd:pfam00063  564 LGELMKTLNSTNPHYIRCIKPNEKKRAGVFDNSLVLHQLRCNGVLEGIRIRRAGFPNRITFQEFVQRYRILapktWPKWK 643
                          810       820       830
                   ....*....|....*....|....*....|.
gi 1720426625  941 QPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:pfam00063  644 GDAKKGCEAILQSLNLDKEEYQFGKTKIFFR 674
COG5022 COG5022
Myosin heavy chain [General function prediction only];
149-1073 0e+00

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 649.83  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  149 DDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLR 228
Cdd:COG5022     69 DDLTELSYLNEPAVLHNLEKRYNNGQIYTYSGLVLIAVNPYRDLGIYTDDIIQSYSGKNRLELEPHVFAIAEEAYRNLLS 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  229 KHVNQCIVISGESGSGKTQSTNFLIHCLTAL--SQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE 306
Cdd:COG5022    149 EKENQTIIISGESGAGKTENAKRIMQYLASVtsSSTVEISSIEKQILATNPILEAFGNAKTVRNDNSSRFGKYIKIEFDE 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  307 NGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQ 386
Cdd:COG5022    229 NGEICGAKIETYLLEKSRVVHQNKNERNYHIFYQLLAGDPEELKKLLLLQNPKDYIYLSQGGCDKIDGIDDAKEFKITLD 308
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  387 AMEMVGFLPATKKQIFSVLSAILYLGNVTYKKratGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLI 466
Cdd:COG5022    309 ALKTIGIDEEEQDQIFKILAAILHIGNIEFKE---DRNGAAIFSDNSVLDKACYLLGIDPSLFVKWLVKRQIKTGGEWIV 385
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  467 LPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQY 546
Cdd:COG5022    386 VPLNLEQALAIRDSLAKALYSNLFDWIVDRINKSLDHSAAASN-----FIGVLDIYGFEIFEKNSFEQLCINYTNEKLQQ 460
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  547 YFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKK-PTGLFYLLDEESNFPHATSHTLLAKFKQQ--HEDNKYFLG 623
Cdd:COG5022    461 FFNQHMFKLEQEEYVKEGIEWSFIDYFDNQPCIDLIEKKnPLGILSLLDEECVMPHATDESFTSKLAQRlnKNSNPKFKK 540
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  624 TPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagr 703
Cdd:COG5022    541 SRFRDNKFVVKHYAGDVEYDVEGFLDKNKDPLNDDLLELLKASTNEFVSTL----------------------------- 591
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  704 lraeraekaagisspatrshmeelprgastpseklyrctgldfsFERSEELDvnafedimafyesrndlhnqiikslkgl 783
Cdd:COG5022    592 --------------------------------------------FDDEENIE---------------------------- 599
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  784 pwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSISAQFQT 863
Cdd:COG5022    600 ------------------------------------------------------------------SKGRFPTLGSRFKE 613
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  864 SLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP------ 937
Cdd:COG5022    614 SLNSLMSTLNSTQPHYIRCIKPNEEKSPWTFDNQMVLSQLRCCGVLETIRISRAGFPSRWTFDEFVQRYRILSPskswtg 693
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  938 --KDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLKeTERQTLQEKLHGEVLRRIL-QLQSWFRMVLERKHFVQMKHAAL 1014
Cdd:COG5022    694 eyTWKEDTKNAVKSILEELVIDSSKYQIGNTKVFFK-AGVLAALEDMRDAKLDNIAtRIQRAIRGRYLRRRYLQALKRIK 772
                          890       900       910       920       930       940
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720426625 1015 TIQACWRSYRVRRALER---TQAAVYLQAAWRGYLQRQAYHHQRHSIIRLQSLCRGHLQRRS 1073
Cdd:COG5022    773 KIQVIQHGFRLRRLVDYelkWRLFIKLQPLLSLLGSRKEYRSYLACIIKLQKTIKREKKLRE 834
MYSc_Myo15 cd01387
class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, ...
160-971 0e+00

class XV mammal-like myosin, motor domain; The class XV myosins are monomeric. In vertebrates, myosin XV appears to be expressed in sensory tissue and play a role in hearing. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are 2 MyTH4 domain, a FERM domain, and a SH3 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276838 [Multi-domain]  Cd Length: 657  Bit Score: 633.71  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd01387      1 TTVLWNLKTRYERNLIYTYIGSILVSVNPYKMFDIYGLEQVQQYSGRALGELPPHLFAIANLAFAKMLDAKQNQCVVISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLTALSQKGYASGVERtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVnYLENGIVRGAVVEKYL 319
Cdd:cd01387     81 ESGSGKTEATKLIMQYLAAVNQRRNNLVTEQ-ILEATPLLEAFGNAKTVRNDNSSRFGKYLEV-FFEGGVIVGAITSQYL 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01387    159 LEKSRIVTQAKNERNYHVFYELLAGLPAQLRQKYGLQEAEKYFYLNQGGNCEIAGKSDADDFRRLLAAMQVLGFSSEEQD 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  400 QIFSVLSAILYLGNVTYKKR-ATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITAR 478
Cdd:cd01387    239 SIFRILASVLHLGNVYFHKRqLRHGQEGVSVGSDAEIQWVAHLLQISPEGLQKALTFKVTETRRERIFTPLTIDQALDAR 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  479 DSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQE 558
Cdd:cd01387    319 DAIAKALYALLFSWLVTRVNAIVYSGTQ-----DTLSIAILDIFGFEDLSENSFEQLCINYANENLQYYFNKHVFKLEQE 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  559 EYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAG 638
Cdd:cd01387    394 EYIREQIDWTEIAFADNQPVINLISKKPVGILHILDDECNFPQATDHSFLEKCHYHHALNELYSKPRMPLPEFTIKHYAG 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  639 RVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreAGRLRAERAEKaagissp 718
Cdd:cd01387    474 QVWYQVHGFLDKNRDQLRQDVLELLVSSRTRVVAHL--------------------------FSSHRAQTDKA------- 520
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  719 atrshmeeLPRGAStpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedprrllqSLS 798
Cdd:cd01387    521 --------PPRLGK---------------------------------------------------------------GRF 529
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  799 LFQKPRTsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkpPSISAQFQTSLNKLLEALGKAEPF 878
Cdd:cd01387    530 VTMKPRT-------------------------------------------------PTVAARFQDSLLQLLEKMERCNPW 560
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  879 FIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL------PKDVQPCREAIAALLE 952
Cdd:cd01387    561 FVRCLKPNHKKEPMLFDMDVVMAQLRYSGMLETIRIRKEGYPVRLPFQVFIDRYRCLValklprPAPGDMCVSLLSRLCT 640
                          810
                   ....*....|....*....
gi 1720426625  953 klQVDRQNYQIGKTKVFLK 971
Cdd:cd01387    641 --VTPKDMYRLGATKVFLR 657
MYSc_Myo22 cd14883
class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ ...
162-971 0e+00

class XXII myosin, motor domain; These myosins possess an extended neck with multiple IQ motifs such as found in class V, VIII, XI, and XIII myosins. These myosins are defined by two tandem MyTH4 and FERM domains. The apicomplexan, but not diatom myosins contain 4-6 WD40 repeats near the end of the C-terminal tail which suggests a possible function of these myosins in signal transduction and transcriptional regulation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276849 [Multi-domain]  Cd Length: 661  Bit Score: 631.28  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14883      3 INTNLKVRYKKDLIYTYTGSILVAVNPYKELPIYTQDIVKQYFGKRMGALPPHIFALAEAAYTNMQEDGKNQSVIISGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALSQKgyASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYLLE 321
Cdd:cd14883     83 GAGKTETTKLILQYLCAVTNN--HSWVEQQILEANTILEAFGNAKTVRNDNSSRFGKFIEVCFDASGHIKGAIIQDYLLE 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  322 KSRLVSQEKDERNYHVFYYLLLG--VSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd14883    161 QSRITFQAPGERNYHVFYQLLAGakHSKELKEKLKLGEPEDYHYLNQSGCIRIDNINDKKDFDHLRLAMNVLGIPEEMQE 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  400 QIFSVLSAILYLGNVTYKKrATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd14883    241 GIFSVLSAILHLGNLTFED-IDGETGALTVEDKEILKIVAKLLGVDPDKLKKALTIRQINVRGNVTEIPLKVQEARDNRD 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  480 SMAKSLYSALFDWIVLRINhallnkkdmeeavSCLS--------IGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQH 551
Cdd:cd14883    320 AMAKALYSRTFAWLVNHIN-------------SCTNpgqknsrfIGVLDIFGFENFKVNSFEQLCINYTNEKLHKFFNHY 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  552 IFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFL-GTPVL-EP 629
Cdd:cd14883    387 VFKLEQEEYEKEGINWSHIVFTDNQECLDLIEKPPLGILKLLDEECRFPKGTDLTYLEKLHAAHEKHPYYEkPDRRRwKT 466
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  630 AFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrlraera 709
Cdd:cd14883    467 EFGVKHYAGEVTYTVQGFLDKNKDTQQDDLFDLMSRSKNKFVKEL----------------------------------- 511
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  710 ekaagisspatrshmeelprgastpseklyrctgldFSFERSEELDvnafedimafyesrndlhnqiikslkglpwqged 789
Cdd:cd14883    512 ------------------------------------FTYPDLLALT---------------------------------- 521
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  790 prrllqslslfqkprtsflkskgikQKQIIPKNLLDSKSlrliismtlhdrttksllhlhKKKKPPSISAQFQTSLNKLL 869
Cdd:cd14883    522 -------------------------GLSISLGGDTTSRG---------------------TSKGKPTVGDTFKHQLQSLV 555
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  870 EALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK--DVQPCREAI 947
Cdd:cd14883    556 DVLSATQPWYVRCIKPNSLKEPNVFDDELVLAQLRYAGMLEIIRIRKEGFPIHLTFKEFVDRYLCLDPRarSADHKETCG 635
                          810       820
                   ....*....|....*....|....*.
gi 1720426625  948 A--ALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14883    636 AvrALMGLGGLPEDEWQVGKTKVFLR 661
MYSc_Myo5 cd01380
class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins ...
163-971 0e+00

class V myosin, motor domain; Myo5, also called heavy chain 12, myoxin, are dimeric myosins that transport a variety of intracellular cargo processively along actin filaments, such as melanosomes, synaptic vesicles, vacuoles, and mRNA. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains a IQ domain and a globular DIL domain. Myosin V is a class of actin-based motor proteins involved in cytoplasmic vesicle transport and anchorage, spindle-pole alignment and mRNA translocation. The protein encoded by this gene is abundant in melanocytes and nerve cells. Mutations in this gene cause Griscelli syndrome type-1 (GS1), Griscelli syndrome type-3 (GS3) and neuroectodermal melanolysosomal disease, or Elejalde disease. Multiple alternatively spliced transcript variants encoding different isoforms have been reported, but the full-length nature of some variants has not been determined. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Note that the Dictyostelium myoVs are not contained in this child group. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276831 [Multi-domain]  Cd Length: 629  Bit Score: 617.63  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  163 LQNLKLRFMQQK-IYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd01380      4 LHNLKVRFCQRNaIYTYCGIVLVAINPYEDLPIYGEDIIQAYSGQNMGELDPHIFAIAEEAYRQMARDEKNQSIIVSGES 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALS-QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYLL 320
Cdd:cd01380     84 GAGKTVSAKYAMRYFATVGgSSSGETQVEEKVLASNPIMEAFGNAKTTRNDNSSRFGKYIEILFDKNYRIIGANMRTYLL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  321 EKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQ 400
Cdd:cd01380    164 EKSRVVFQAEEERNYHIFYQLCAAASLPELKELHLGSAEDFFYTNQGGSPVIDGVDDAAEFEETRKALTLLGISEEEQME 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  401 IFSVLSAILYLGNVTYKKRatgRDEGLEVGPPEV-LDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd01380    244 IFRILAAILHLGNVEIKAT---RNDSASISPDDEhLQIACELLGIDESQLAKWLCKRKIVTRSEVIVKPLTLQQAIVARD 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  480 SMAKSLYSALFDWIVLRINHALLNKKDmEEAVSClsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd01380    321 ALAKHIYAQLFDWIVDRINKALASPVK-EKQHSF--IGVLDIYGFETFEVNSFEQFCINYANEKLQQQFNQHVFKLEQEE 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  560 YQGEGISWHNIDYTDNVGCIHLISKKPtGLFYLLDEESNFPHATSHTLLAKFKQQHE--DNKYFLGTPVLEPAFIIQHFA 637
Cdd:cd01380    398 YVKEEIEWSFIDFYDNQPCIDLIEGKL-GILDLLDEECRLPKGSDENWAQKLYNQHLkkPNKHFKKPRFSNTAFIVKHFA 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  638 GRVKYQIKDFREKNMDYMRPDIVALLRGSDSsyvrqligmdpvavfrwavlraairamavlreagrlraeraekaagiss 717
Cdd:cd01380    477 DDVEYQVEGFLEKNRDTVSEEHLNVLKASKN------------------------------------------------- 507
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  718 patrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedprrllqsl 797
Cdd:cd01380        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  798 slfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlHKkkkpPSISAQFQTSLNKLLEALGKAEP 877
Cdd:cd01380    508 ---------------------------------------------------RK----KTVGSQFRDSLILLMETLNSTTP 532
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  878 FFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDV---QPCREAIAALLEKL 954
Cdd:cd01380    533 HYVRCIKPNDEKLPFTFDPKRVVQQLRACGVLETIRISAAGFPSRWTYEEFFSRYRVLLPSKEwlrDDKKKTCENILENL 612
                          810
                   ....*....|....*..
gi 1720426625  955 QVDRQNYQIGKTKVFLK 971
Cdd:cd01380    613 ILDPDKYQFGKTKIFFR 629
MYSc_Myo3 cd01379
class III myosin, motor domain; Myosin III has been shown to play a role in the vision process ...
162-971 0e+00

class III myosin, motor domain; Myosin III has been shown to play a role in the vision process in insects and in hearing in mammals. Myosin III, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They are characterized by an N-terminal protein kinase domain and several IQ domains. Some members also contain WW, SH2, PH, and Y-phosphatase domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276830 [Multi-domain]  Cd Length: 633  Bit Score: 608.12  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd01379      3 IVSQLQKRYSRDQIYTYIGDILIAVNPFQNLGIYTEEHSRLYRGAKRSDNPPHIFAVADAAYQAMIHQKKNQCIVISGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALSQKGYASgVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYLLE 321
Cdd:cd01379     83 GAGKTESANLLVQQLTVLGKANNRT-LEEKILQVNPLMEAFGNARTVINDNSSRFGKYLEMKFTSTGAVTGARISEYLLE 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  322 KSRLVSQEKDERNYHVFYYLLLGVSEEERLE-FQLKQPQDYFYLNQHNLNIEDGEDL---KHDFERLQQAMEMVGFLPAT 397
Cdd:cd01379    162 KSRVVHQAIGERNFHIFYYIYAGLAEDKKLAkYKLPENKPPRYLQNDGLTVQDIVNNsgnREKFEEIEQCFKVIGFTKEE 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  398 KKQIFSVLSAILYLGNVTYKKRATG--RDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAI 475
Cdd:cd01379    242 VDSVYSILAAILHIGDIEFTEVESNhqTDKSSRISNPEALNNVAKLLGIEADELQEALTSHSVVTRGETIIRNNTVEEAT 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  476 TARDSMAKSLYSALFDWIVLRINhALLnKKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKL 555
Cdd:cd01379    322 DARDAMAKALYGRLFSWIVNRIN-SLL-KPDRSASDEPLSIGILDIFGFENFQKNSFEQLCINIANEQIQYYFNQHIFAW 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  556 EQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFkqqhEDN---KYFLGTPVLEPAFI 632
Cdd:cd01379    400 EQQEYLNEGIDVDLIEYEDNRPLLDMFLQKPMGLLALLDEESRFPKATDQTLVEKF----HNNiksKYYWRPKSNALSFG 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  633 IQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQligmdpvavfrwavlraairamavlreagrlraeraeka 712
Cdd:cd01379    476 IHHYAGKVLYDASGFLEKNRDTLPPDVVQLLRSSENPLVRQ--------------------------------------- 516
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  713 agisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedprr 792
Cdd:cd01379        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  793 llqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEAL 872
Cdd:cd01379    517 ---------------------------------------------------------------TVATYFRYSLMDLLSKM 533
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  873 GKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL---LPKDVQPCREAIAA 949
Cdd:cd01379    534 VVGQPHFVRCIKPNDSRQAGKFDREKVLKQLRYTGVLETTRIRRQGFSHRILFADFLKRYYFLafkWNEEVVANRENCRL 613
                          810       820
                   ....*....|....*....|..
gi 1720426625  950 LLEKLQVDrqNYQIGKTKVFLK 971
Cdd:cd01379    614 ILERLKLD--NWALGKTKVFLK 633
MYSc_Myo8 cd01383
class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated ...
162-971 0e+00

class VIII myosin, motor domain; These plant-specific type VIII myosins has been associated with endocytosis, cytokinesis, cell-to-cell coupling and gating at plasmodesmata. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. It also contains IQ domains Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276834  Cd Length: 647  Bit Score: 604.69  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYenQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd01383      3 VLHNLEYRYSQDIIYTKAGPVLIAVNPFKDVPLYGNEFITAY--RQKLLDSPHVYAVADTAYREMMRDEINQSIIISGES 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALSqkGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYLLE 321
Cdd:cd01383     81 GAGKTETAKIAMQYLAALG--GGSSGIENEILQTNPILEAFGNAKTLRNDNSSRFGKLIDIHFDAAGKICGAKIQTYLLE 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  322 KSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQI 401
Cdd:cd01383    159 KSRVVQLANGERSYHIFYQLCAGASPALREKLNLKSASEYKYLNQSNCLTIDGVDDAKKFHELKEALDTVGISKEDQEHI 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  402 FSVLSAILYLGNVTYKkrATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSM 481
Cdd:cd01383    239 FQMLAAVLWLGNISFQ--VIDNENHVEVVADEAVSTAASLLGCNANDLMLALSTRKIQAGGDKIVKKLTLQQAIDARDAL 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  482 AKSLYSALFDWIVLRINHALlnkkDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQ 561
Cdd:cd01383    317 AKAIYASLFDWLVEQINKSL----EVGKRRTGRSISILDIYGFESFQKNSFEQLCINYANERLQQHFNRHLFKLEQEEYE 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  562 GEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPvlEPAFIIQHFAGRVK 641
Cdd:cd01383    393 LDGIDWTKVDFEDNQECLDLIEKKPLGLISLLDEESNFPKATDLTFANKLKQHLKSNSCFKGER--GGAFTIRHYAGEVT 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  642 YQIKDFREKNMDYMRPDIVALLrgsdssyvrqligmdpvavfrwavlraairamavlreagrlraeraekaagisspatr 721
Cdd:cd01383    471 YDTSGFLEKNRDLLHSDLIQLL---------------------------------------------------------- 492
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  722 shmeelprgaSTPSEKLYRCTGldfSFERSEeldvnafedimafyesrndlhnqiikslkglpwqgedprrllqslslFQ 801
Cdd:cd01383    493 ----------SSCSCQLPQLFA---SKMLDA-----------------------------------------------SR 512
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  802 KPRTSFLKSKGIKQKQiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIR 881
Cdd:cd01383    513 KALPLTKASGSDSQKQ--------------------------------------SVATKFKGQLFKLMQRLENTTPHFIR 554
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  882 CIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAIA---ALLEKLQVDR 958
Cdd:cd01383    555 CIKPNNKQLPGVFDQDLVLQQLRCCGVLEVVRISRSGYPTRMTHQEFARRYGFLLPEDVSASQDPLStsvAILQQFNILP 634
                          810
                   ....*....|...
gi 1720426625  959 QNYQIGKTKVFLK 971
Cdd:cd01383    635 EMYQVGYTKLFFR 647
MYSc_Myo10 cd14873
class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a ...
160-971 0e+00

class X myosin, motor domain; Myosin X is an unconventional myosin motor that functions as a monomer. In mammalian cells, the motor is found to localize to filopodia. Myosin X walks towards the barbed ends of filaments and is thought to walk on bundles of actin, rather than single filaments, a unique behavior. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to the head domain are a variable number of IQ domains, 2 PH domains, a MyTH4 domain, and a FERM domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276840 [Multi-domain]  Cd Length: 651  Bit Score: 592.15  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVIS 238
Cdd:cd14873      1 GSIMYNLFQRYKRNQIYTYIGSILASVNPYQPIAgLYEPATMEQYSRRHLGELPPHIFAIANECYRCLWKRHDNQCILIS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  239 GESGSGKTQSTNFLIHCLTALSQ-------KGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVR 311
Cdd:cd14873     81 GESGAGKTESTKLILKFLSVISQqslelslKEKTSCVEQAILESSPIMEAFGNAKTVYNNNSSRFGKFVQLNICQKGNIQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  312 GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMV 391
Cdd:cd14873    161 GGRIVDYLLEKNRVVRQNPGERNYHIFYALLAGLEHEEREEFYLSTPENYHYLNQSGCVEDKTISDQESFREVITAMEVM 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  392 GFLPATKKQIFSVLSAILYLGNVTYKKRAtgrdeGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSL 471
Cdd:cd14873    241 QFSKEEVREVSRLLAGILHLGNIEFITAG-----GAQVSFKTALGRSAELLGLDPTQLTDALTQRSMFLRGEEILTPLNV 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  472 SEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQH 551
Cdd:cd14873    316 QQAVDSRDSLAMALYARCFEWVIKKINSRIKGKEDFK------SIGILDIFGFENFEVNHFEQFNINYANEKLQEYFNKH 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  552 IFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKpTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAF 631
Cdd:cd14873    390 IFSLEQLEYSREGLVWEDIDWIDNGECLDLIEKK-LGLLALINEESHFPQATDSTLLEKLHSQHANNHFYVKPRVAVNNF 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  632 IIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrlraeraek 711
Cdd:cd14873    469 GVKHYAGEVQYDVRGILEKNRDTFRDDLLNLLRESRFDFIYDL------------------------------------- 511
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  712 aagisspatrshmeelprgastpseklyrctgldfsferseeldvnaFEDImafyESRNDlhnqiikslkglpwqgedpr 791
Cdd:cd14873    512 -----------------------------------------------FEHV----SSRNN-------------------- 520
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  792 rllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttKSLLHLHKKKKPPSISAQFQTSLNKLLEA 871
Cdd:cd14873    521 ---------------------------------------------------QDTLKCGSKHRRPTVSSQFKDSLHSLMAT 549
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  872 LGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP--KDVQPCREAIAA 949
Cdd:cd14873    550 LSSSNPFFVRCIKPNMQKMPDQFDQAVVLNQLRYSGMLETVRIRKAGYAVRRPFQDFYKRYKVLMRnlALPEDVRGKCTS 629
                          810       820
                   ....*....|....*....|..
gi 1720426625  950 LLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14873    630 LLQLYDASNSEWQLGKTKVFLR 651
MYSc_Myo1 cd01378
class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, ...
162-971 0e+00

class I myosin, motor domain; Myosin I generates movement at the leading edge in cell motility, and class I myosins have been implicated in phagocytosis and vesicle transport. Myosin I, an unconventional myosin, does not form dimers. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. There are 5 myosin subclasses with subclasses c/h, d/g, and a/b have an IQ domain and a TH1 domain. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276829  Cd Length: 652  Bit Score: 578.35  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd01378      3 INENLKKRFENDEIYTYIGHVLISVNPFKDLGIYTDEVLESYRGKNRYEVPPHVFALADSAYRNMKSEKENQCVIISGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALSQKGYAS--GVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd01378     83 GAGKTEASKRIMQYIAAVSGGSESEveRVKDMLLASNPLLEAFGNAKTLRNDNSSRFGKYMEIQFDFKGEPVGGHITNYL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01378    163 LEKSRVVGQIKGERNFHIFYQLLKGASQEYLQELGLQRPEQYYYYSKSGCFDVDGIDDAADFKEVLNAMKVIGFTEEEQD 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  400 QIFSVLSAILYLGNVTYKKRATGrdeGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDK---LILPYSLSEAIT 476
Cdd:cd01378    243 SIFRILAAILHLGNIQFAEDEEG---NAAISDTSVLDFVAYLLGVDPDQLEKALTHRTIETGGGGrsvYEVPLNVEQAAY 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  477 ARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLE 556
Cdd:cd01378    320 ARDALAKAIYSRLFDWIVERINKSLAAKSGGKKKV----IGVLDIYGFEIFEKNSFEQFCINYVNEKLQQIFIELTLKAE 395
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  557 QEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPH-ATSHTLLAKFKQQHEDNKYFLGTP----VLEPAF 631
Cdd:cd01378    396 QEEYVREGIEWTPIKYFNNKIICDLIEEKPPGIFAILDDACLTAGdATDQTFLQKLNQLFSNHPHFECPSghfeLRRGEF 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  632 IIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrlraeraek 711
Cdd:cd01378    476 RIKHYAGDVTYNVEGFLDKNKDLLFKDLKELMQSSSNPFLRSL------------------------------------- 518
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  712 aagisspatrshmeeLPRGASTPSeklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedpr 791
Cdd:cd01378    519 ---------------FPEGVDLDS-------------------------------------------------------- 527
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  792 rllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkKKKPPSISAQFQTSLNKLLEA 871
Cdd:cd01378    528 -----------------------------------------------------------KKRPPTAGTKFKNSANALVET 548
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  872 LGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK-------DVQpcr 944
Cdd:cd01378    549 LMKKQPSYIRCIKPNDNKSPGEFDEELVLHQVKYLGLLENVRVRRAGFAYRQTYEKFLERYKLLSPKtwpawdgTWQ--- 625
                          810       820
                   ....*....|....*....|....*..
gi 1720426625  945 EAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd01378    626 GGVESILKDLNIPPEEYQMGKTKIFIR 652
MYSc_class_II cd01377
class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, ...
160-971 0e+00

class II myosins, motor domain; Myosin motor domain in class II myosins. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. Thus, myosin II has two heads. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276951 [Multi-domain]  Cd Length: 662  Bit Score: 577.11  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd01377      1 ASVLHNLRERYYSDLIYTYSGLFCVAVNPYKRLPIYTEEVIDKYKGKRREEMPPHIFAIADNAYRNMLQDRENQSILITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQST----NFLIHCLTALSQKGYASG----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVR 311
Cdd:cd01377     81 ESGAGKTENTkkviQYLASVAASSKKKKESGKkkgtLEDQILQANPILEAFGNAKTVRNNNSSRFGKFIRIHFGSTGKIA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  312 GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQ-PQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEM 390
Cdd:cd01377    161 GADIETYLLEKSRVVRQAKGERNYHIFYQLLSGADPELKEKLLLTGdPSYYFFLSQGELTIDGVDD-AEEFKLTDEAFDI 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  391 VGFLPATKKQIFSVLSAILYLGNVTYKKRatGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTK------RKTVTVNdk 464
Cdd:cd01377    240 LGFSEEEKMSIFKIVAAILHLGNIKFKQR--RREEQAELDGTEEADKAAHLLGVNSSDLLKALLKprikvgREWVTKG-- 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  465 lilpYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQL 544
Cdd:cd01377    316 ----QNKEQVVFSVGALAKALYERLFLWLVKRINKTLDTKSKRQ-----YFIGVLDIAGFEIFEFNSFEQLCINYTNEKL 386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  545 QYYFTQHIFKLEQEEYQGEGISWHNIDYtdnvG-----CIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK 619
Cdd:cd01377    387 QQFFNHHMFVLEQEEYKKEGIEWTFIDF----GldlqpTIDLIEKPNMGILSILDEECVFPKATDKTFVEKLYSNHLGKS 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  620 YFLGTPV---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairama 696
Cdd:cd01377    463 KNFKKPKpkkSEAHFILKHYAGDVEYNIDGWLEKNKDPLNENVVALLKKSSDPLVASLF--------------------- 521
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  697 vlreagrlraeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqi 776
Cdd:cd01377        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  777 ikslkglpwqgEDPRRLLQSLSLFQKPRTSFlkskgikqkqiipknlldskslrliismtlhdRTtksllhlhkkkkpps 856
Cdd:cd01377    522 -----------KDYEESGGGGGKKKKKGGSF--------------------------------RT--------------- 543
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  857 ISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL 936
Cdd:cd01377    544 VSQLHKEQLNKLMTTLRSTHPHFVRCIIPNEEKKPGKIDAPLVLHQLRCNGVLEGIRICRKGFPNRIIFAEFKQRYSILA 623
                          810       820       830
                   ....*....|....*....|....*....|....*....
gi 1720426625  937 PKDVQPC----REAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd01377    624 PNAIPKGfddgKAACEKILKALQLDPELYRIGNTKVFFK 662
MYSc_Myo11 cd01384
class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle ...
163-971 0e+00

class XI myosin, motor domain; These plant-specific type XI myosin are involved in organelle transport. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle.


Pssm-ID: 276835  Cd Length: 647  Bit Score: 576.94  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  163 LQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd01384      4 LHNLKVRYELDEIYTYTGNILIAVNPFKRLPhLYDAHMMEQYKGAPLGELSPHVFAVADAAYRAMINEGKSQSILVSGES 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALSQKGYASG--VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd01384     84 GAGKTETTKMLMQYLAYMGGRAVTEGrsVEQQVLESNPLLEAFGNAKTVRNNNSSRFGKFVEIQFDDAGRISGAAIRTYL 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKK 399
Cdd:cd01384    164 LERSRVVQVSDPERNYHCFYQLCAGAPPEDREKYKLKDPKQFHYLNQSKCFELDGVDDAEEYRATRRAMDVVGISEEEQD 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  400 QIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEV---LDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAIT 476
Cdd:cd01384    244 AIFRVVAAILHLGNIEFSKGE--EDDSSVPKDEKSefhLKAAAELLMCDEKALEDALCKRVIVTPDGIITKPLDPDAATL 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  477 ARDSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLE 556
Cdd:cd01384    322 SRDALAKTIYSRLFDWLVDKINRSIGQDPN-----SKRLIGVLDIYGFESFKTNSFEQFCINLANEKLQQHFNQHVFKME 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  557 QEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFlGTPVLEP-AFIIQH 635
Cdd:cd01384    397 QEEYTKEEIDWSYIEFVDNQDVLDLIEKKPGGIIALLDEACMFPRSTHETFAQKLYQTLKDHKRF-SKPKLSRtDFTIDH 475
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  636 FAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrlraeraekaagi 715
Cdd:cd01384    476 YAGDVTYQTDLFLDKNKDYVVAEHQALLNASKCPFVAGL----------------------------------------- 514
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  716 sspatrshMEELPRGASTPSEKlyrctgldFSferseeldvnafedimafyesrndlhnqiikslkglpwqgedprrllq 795
Cdd:cd01384    515 --------FPPLPREGTSSSSK--------FS------------------------------------------------ 530
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  796 slslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKA 875
Cdd:cd01384    531 ------------------------------------------------------------SIGSRFKQQLQELMETLNTT 550
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  876 EPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP---KDVQPCREAIAALLE 952
Cdd:cd01384    551 EPHYIRCIKPNNLLKPGIFENANVLQQLRCGGVLEAVRISCAGYPTRKPFEEFLDRFGLLAPevlKGSDDEKAACKKILE 630
                          810
                   ....*....|....*....
gi 1720426625  953 KLQVdrQNYQIGKTKVFLK 971
Cdd:cd01384    631 KAGL--KGYQIGKTKVFLR 647
MYSc_Myo36 cd14897
class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain ...
160-971 9.95e-164

class XXXVI myosin, motor domain; This class of molluscan myosins contains a motor domain followed by a GlcAT-I (Beta1,3-glucuronyltransferase I) domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276862 [Multi-domain]  Cd Length: 635  Bit Score: 518.09  E-value: 9.95e-164
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQL-GKLEPHVFALADVAYYAMLRKHVNQCIVIS 238
Cdd:cd14897      1 NTIVQTLKSRYNKDKFYTYIGDILVAVNPCKPLPIFDKKHHEEYSNLSVrSQRPPHLFWIADQAYRRLLETGRNQCILVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  239 GESGSGKTQSTNFLIHCLTALSQKGYASGVERtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKY 318
Cdd:cd14897     81 GESGAGKTESTKYMIKHLMKLSPSDDSDLLDK-IVQINPLLEAFGNASTVMNDNSSRFGKFIELHFTENGQLLGAKIDDY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYL---NQHNLNIEDGEDLKHD---FERLQQAMEMVG 392
Cdd:cd14897    160 LLEKSRVVHRGNGEKNFHIFYALFAGMSRDRLLYYFLEDPDCHRILrddNRNRPVFNDSEELEYYrqmFHDLTNIMKLIG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  393 FLPATKKQIFSVLSAILYLGNVTYKKraTGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLS 472
Cdd:cd14897    240 FSEEDISVIFTILAAILHLTNIVFIP--DEDTDGVTVADEYPLHAVAKLLGIDEVELTEALISNVNTIRGERIQSWKSLR 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  473 EAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHI 552
Cdd:cd14897    318 QANDSRDALAKDLYSRLFGWIVGQINRNLWPDKDFQIMTRGPSIGILDMSGFENFKINSFDQLCINLSNERLQQYFNDYV 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  553 FKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFI 632
Cdd:cd14897    398 FPRERSEYEIEGIEWRDIEYHDNDDVLELFFKKPLGILPLLDEESTFPQSTDSSLVQKLNKYCGESPRYVASPGNRVAFG 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  633 IQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdpvavfrwavlraairamavlreagrlraeraeka 712
Cdd:cd14897    478 IRHYAEQVTYDADGFLEKNRDNLSSDIVGCLLNSN--------------------------------------------- 512
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  713 agisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhNQIIKSLkglpwqgedprr 792
Cdd:cd14897    513 -------------------------------------------------------------NEFISDL------------ 519
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  793 llqslslfqkprtsFLKskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppsisaQFQTSLNKLLEAL 872
Cdd:cd14897    520 --------------FTS--------------------------------------------------YFKRSLSDLMTKL 535
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  873 GKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKdvqpCREAIAALLE 952
Cdd:cd14897    536 NSADPLFVRCIKPNNFLRPNKFDDELVRRQLLCNGLMEIAKIRRDGYPIRIKYEDFVKRYKEICDF----SNKVRSDDLG 611
                          810       820
                   ....*....|....*....|....
gi 1720426625  953 KLQV-----DRQNYQIGKTKVFLK 971
Cdd:cd14897    612 KCQKilktaGIKGYQFGKTKVFLK 635
MYSc_Myo28 cd14889
class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The ...
162-971 1.42e-159

class XXVIII myosin, motor domain; These myosins are found in fish, chicken, and mollusks. The tail regions of these class-XXVIII myosins consist of an IQ motif, a short coiled-coil region, and an SH2 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276854  Cd Length: 659  Bit Score: 507.91  E-value: 1.42e-159
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAML----RKHVNQCIVI 237
Cdd:cd14889      3 LLEVLKVRFMQSNIYTYVGDILVAINPFKYLHIYEKEVSQKYKCEKKSSLPPHIFAVADRAYQSMLgrlaRGPKNQCIVI 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  238 SGESGSGKTQSTNFLIHCLTALSQKGyaSGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYlENGIVRGAVVEK 317
Cdd:cd14889     83 SGESGAGKTESTKLLLRQIMELCRGN--SQLEQQILQVNPLLEAFGNAQTVMNDNSSRFGKYIQLRF-RNGHVKGAKINE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  318 YLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPAT 397
Cdd:cd14889    160 YLLEKSRVVHQDGGEENFHIFYYMFAGISAEDRENYGLLDPGKYRYLNNGAGCKREVQYWKKKYDEVCNAMDMVGFTEQE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  398 KKQIFSVLSAILYLGNVTYKKRATG--RDEGLEVGPpevLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAI 475
Cdd:cd14889    240 EVDMFTILAGILSLGNITFEMDDDEalKVENDSNGW---LKAAAGQFGVSEEDLLKTLTCTVTFTRGEQIQRHHTKQQAE 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  476 TARDSMAKSLYSALFDWIVLRINHALLNKKDMEeaVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKL 555
Cdd:cd14889    317 DARDSIAKVAYGRVFGWIVSKINQLLAPKDDSS--VELREIGILDIFGFENFAVNRFEQACINLANEQLQYFFNHHIFLM 394
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  556 EQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQH 635
Cdd:cd14889    395 EQKEYKKEGIDWKEITYKDNKPILDLFLNKPIGILSLLDEQSHFPQATDESFVDKLNIHFKGNSYYGKSRSKSPKFTVNH 474
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  636 FAGRVKYQIKDFREKNMDYMRPDIVALLRGSdssyvrqligmdpvavfrwavlraAIRAMAVLREAGRLRaeraekaagi 715
Cdd:cd14889    475 YAGKVTYNASGFLEKNRDTIPASIRTLFINS------------------------ATPLLSVLFTATRSR---------- 520
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  716 sspatrshmeelpRGASTPSEKlyrctgldfsferseeldvnafedimafyesrndlhnqiikslkgLPWQGEDprrllq 795
Cdd:cd14889    521 -------------TGTLMPRAK---------------------------------------------LPQAGSD------ 536
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  796 slslfqkprtsflkSKGIKQKQiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKA 875
Cdd:cd14889    537 --------------NFNSTRKQ--------------------------------------SVGAQFKHSLGVLMEKMFAA 564
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  876 EPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK-DVQPCREAIAALLEKL 954
Cdd:cd14889    565 SPHFVRCIKPNHVKVPGQLDSKYIQDQLRYNGLLETIRIRREGFSWRPSFAEFAERYKILLCEpALPGTKQSCLRILKAT 644
                          810
                   ....*....|....*..
gi 1720426625  955 QVdrQNYQIGKTKVFLK 971
Cdd:cd14889    645 KL--VGWKCGKTRLFFK 659
MYSc_Myo6 cd01382
class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the ...
160-971 1.46e-158

class VI myosin, motor domain; Myosin VI is a monomeric myosin, which moves towards the minus-end of actin filaments, in contrast to most other myosins which moves towards the plus-end of actin filaments. It is thought that myosin VI, unlike plus-end directed myosins, does not use a pure lever arm mechanism, but instead steps with a mechanism analogous to the kinesin neck-linker uncoupling model. It has been implicated in a myriad of functions including: the transport of cytoplasmic organelles, maintenance of normal Golgi morphology, endocytosis, secretion, cell migration, border cell migration during development, and in cancer metastasis playing roles in deafness and retinal development among others. While how this is accomplished is largely unknown there are several interacting proteins that have been identified such as disabled homolog 2 (DAB2), GIPC1, synapse-associated protein 97 (SAP97; also known as DLG1) and optineurin, which have been found to target myosin VI to different cellular compartments. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the minus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276833  Cd Length: 649  Bit Score: 504.48  E-value: 1.46e-158
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVIS 238
Cdd:cd01382      1 ATLLNNIRVRYSKDKIYTYVANILIAVNPYFDIPkLYSSETIKSYQGKSLGTLPPHVFAIADKAYRDMKVLKQSQSIIVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  239 GESGSGKTQSTNFLIHCLTAlSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKY 318
Cdd:cd01382     81 GESGAGKTESTKYILRYLTE-SWGSGAGPIEQRILEANPLLEAFGNAKTVRNNNSSRFGKFVEIHFNEKSSVVGGFVSHY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERlEFQLKQPQdyfyLNQHNlniedgedlkhDFERLQQAMEMVGFLPATK 398
Cdd:cd01382    160 LLEKSRICVQSKEERNYHIFYRLCAGAPEDLR-EKLLKDPL----LDDVG-----------DFIRMDKAMKKIGLSDEEK 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  399 KQIFSVLSAILYLGNVTYKKRATGRDEGLEVGP--PEVLDTLSQLLKVKRETLVEVLTKRKTVT----VNDKLIL-PYSL 471
Cdd:cd01382    224 LDIFRVVAAVLHLGNIEFEENGSDSGGGCNVKPksEQSLEYAAELLGLDQDELRVSLTTRVMQTtrggAKGTVIKvPLKV 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  472 SEAITARDSMAKSLYSALFDWIVLRINHALLNKKdmeeavSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQH 551
Cdd:cd01382    304 EEANNARDALAKAIYSKLFDHIVNRINQCIPFET------SSYFIGVLDIAGFEYFEVNSFEQFCINYCNEKLQQFFNER 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  552 IFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNkYFLGTPVL---- 627
Cdd:cd01382    378 ILKEEQELYEKEGLGVKEVEYVDNQDCIDLIEAKLVGILDLLDEESKLPKPSDQHFTSAVHQKHKNH-FRLSIPRKsklk 456
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  628 -------EPAFIIQHFAGRVKYQIKDFREKNmdymrpdivallrgsdssyvrqligmdpvavfrwavlraairamavlre 700
Cdd:cd01382    457 ihrnlrdDEGFLIRHFAGAVCYETAQFIEKN------------------------------------------------- 487
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  701 agrlraeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrND-LHNqiikS 779
Cdd:cd01382    488 ---------------------------------------------------------------------NDaLHA----S 494
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  780 LKGLPWQGEDPrrLLQslSLFQKPRTSFLKSKGIKQKqiipknlldsksLRLIismtlhdrttksllhlhkkkkppSISA 859
Cdd:cd01382    495 LESLICESKDK--FIR--SLFESSTNNNKDSKQKAGK------------LSFI-----------------------SVGN 535
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  860 QFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKD 939
Cdd:cd01382    536 KFKTQLNLLMDKLRSTGTSFIRCIKPNLKMTSHHFEGAQILSQLQCSGMVSVLDLMQGGFPSRTSFHDLYNMYKKYLPPK 615
                          810       820       830
                   ....*....|....*....|....*....|....*...
gi 1720426625  940 V---QP---CReaiaALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd01382    616 LarlDPrlfCK----ALFKALGLNENDFKFGLTKVFFR 649
MYSc_Myo46 cd14907
class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much ...
160-971 1.87e-156

class XLVI myosin, motor domain; The class XLVI myosins are comprised of Alveolata. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276872 [Multi-domain]  Cd Length: 669  Bit Score: 499.56  E-value: 1.87e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQ--------QLGKLEPHVFALADVAYYAMLRKH 230
Cdd:cd14907      1 AELLINLKKRYQQDKIFTYVGPTLIVMNPYKQIDnLFSEEVMQMYKEQiiqngeyfDIKKEPPHIYAIAALAFKQLFENN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  231 VNQCIVISGESGSGKTQSTNFLIHCLTALSQKGYAS------------------GVERTILGAGPVLEAFGNAKTAHNNN 292
Cdd:cd14907     81 KKQAIVISGESGAGKTENAKYAMKFLTQLSQQEQNSeevltltssiratskstkSIEQKILSCNPILEAFGNAKTVRNDN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  293 SSRFGKF--IQVNYLENGIVrGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQP--QD-YFYLNQ- 366
Cdd:cd14907    161 SSRFGKYvsILVDKKKRKIL-GARIQNYLLEKSRVTQQGQGERNYHIFYHLLYGADQQLLQQLGLKNQlsGDrYDYLKKs 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  367 --HNLNIEDGEDLkhdFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKV 444
Cdd:cd14907    240 ncYEVDTINDEKL---FKEVQQSFQTLGFTEEEQDSIWRILAAILLLGNLQFDDSTLDDNSPCCVKNKETLQIIAKLLGI 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  445 KRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNK---KDMEEAVSCLSIGVLDI 521
Cdd:cd14907    317 DEEELKEALTTKIRKVGNQVITSPLSKKECINNRDSLSKELYDRLFNWLVERLNDTIMPKdekDQQLFQNKYLSIGLLDI 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  522 FGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWH--NIDYTDNVGCIHLISKKPTGLFYLLDEESNF 599
Cdd:cd14907    397 FGFEVFQNNSFEQLCINYTNEKLQQLYISYVFKAEEQEFKEEGLEDYlnQLSYTDNQDVIDLLDKPPIGIFNLLDDSCKL 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  600 PHATSHTLLAKFKQQHEDNKYFLGTPVL-EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmd 678
Cdd:cd14907    477 ATGTDEKLLNKIKKQHKNNSKLIFPNKInKDTFTIRHTAKEVEYNIEGFREKNKDEISQSIINCIQNSK----------- 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  679 pvavfrwavlraairamavlreagrlraeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvna 758
Cdd:cd14907        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  759 fedimafyesrndlhNQIIKSLkglpWQGEDprrlLQSLSLFQKPRTSFLKSKgikqkqiipknlldskslrliismtlh 838
Cdd:cd14907    546 ---------------NRIISSI----FSGED----GSQQQNQSKQKKSQKKDK--------------------------- 575
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  839 drttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSG 918
Cdd:cd14907    576 -----------------FLGSKFRNQMKQLMNELMQCDVHFIRCIKPNEEKKADLFIQGYVLNQIRYLGVLESIRVRKQG 638
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720426625  919 YSAKYTFQDFTEQFQVLlpkdvqpcreaiaalleklqvdRQNYQIGKTKVFLK 971
Cdd:cd14907    639 YPYRKSYEDFYKQYSLL----------------------KKNVLFGKTKIFMK 669
MYSc_Myo4 cd14872
class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or ...
160-968 1.88e-152

class IV myosin, motor domain; These myosins all possess a WW domain either N-terminal or C-terminal to their motor domain and a tail with a MyTH4 domain followed by a SH3 domain in some instances. The monomeric Acanthamoebas were the first identified members of this group and have been joined by Stramenopiles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276839  Cd Length: 644  Bit Score: 487.36  E-value: 1.88e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14872      1 AMIVHNLRKRFKNDQIYTNVGTILISVNPFKRLPLYTPTVMDQYMHKGPKEMPPHTYNIADDAYRAMIVDAMNQSILISG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNfliHCLTALSQ-KGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKY 318
Cdd:cd14872     81 ESGAGKTEATK---QCLSFFAEvAGSTNGVEQRVLLANPILEAFGNAKTLRNNNSSRFGKWVEIHFDNRGRICGASTENY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQhNLNIEdGEDLKHDFERLQQAMEMVGFLPATK 398
Cdd:cd14872    158 LLEKSRVVYQIKGERNFHIFYQLLASPDPASRGGWGSSAAYGYLSLSG-CIEVE-GVDDVADFEEVVLAMEQLGFDDADI 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  399 KQIFSVLSAILYLGNVTYKKRATGRD-EGLEVGPPEVLDTLSQLLKVKRETLVEVLT-KRKTVTVNDKLILPYSLSEAIT 476
Cdd:cd14872    236 NNVMSLIAAILKLGNIEFASGGGKSLvSGSTVANRDVLKEVATLLGVDAATLEEALTsRLMEIKGCDPTRIPLTPAQATD 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  477 ARDSMAKSLYSALFDWIVLRINHALlnkKDMEEAVSCLsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLE 556
Cdd:cd14872    316 ACDALAKAAYSRLFDWLVKKINESM---RPQKGAKTTF-IGVLDIFGFEIFEKNSFEQLCINFTNEKLQQHFNQYTFKLE 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  557 QEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVL--EPAFIIQ 634
Cdd:cd14872    392 EALYQSEGVKFEHIDFIDNQPVLDLIEKKQPGLMLALDDQVKIPKGSDATFMIAANQTHAAKSTFVYAEVRtsRTEFIVK 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  635 HFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdpvavfrwavlraairamavlreagrlraeraekaag 714
Cdd:cd14872    472 HYAGDVTYDITGFLEKNKDTLQKDLYVLLSSSK----------------------------------------------- 504
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  715 isspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhNQIIKSLKglpwqgedprrll 794
Cdd:cd14872    505 -----------------------------------------------------------NKLIAVLF------------- 512
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  795 qslslfqkprtsflkskgikqkqiiPKNLLDSKSLRliismtlhdrttksllhlhkkkkpPSISAQFQTSLNKLLEALGK 874
Cdd:cd14872    513 -------------------------PPSEGDQKTSK------------------------VTLGGQFRKQLSALMTALNA 543
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  875 AEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL-------PKDVqpcREAI 947
Cdd:cd14872    544 TEPHYIRCVKPNQEKRARLFDGFMSLEQLRYAGVFEAVKIRKTGYPFRYSHERFLKRYRFLVktiakrvGPDD---RQRC 620
                          810       820
                   ....*....|....*....|.
gi 1720426625  948 AALLEKLQVDRQNYQIGKTKV 968
Cdd:cd14872    621 DLLLKSLKQDFSKVQVGKTRV 641
MYSc_Myo29 cd14890
class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have ...
160-971 1.85e-148

class XXIX myosin, motor domain; Class XXIX myosins are comprised of Stramenopiles and have very long tail domains consisting of three IQ motifs, short coiled-coil regions, up to 18 CBS domains, a PB1 domain, and a carboxy-terminal transmembrane domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276855 [Multi-domain]  Cd Length: 662  Bit Score: 476.96  E-value: 1.85e-148
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHV----NQC 234
Cdd:cd14890      1 ASLLHTLRLRYERDEIYTYVGPILISINPYKSIPdLYSEERMLLYHGTTAGELPPHVFAIADHAYTQLIQSGVldpsNQS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  235 IVISGESGSGKTQSTNFLIHCL---TALSQKGYASG--------------VERTILGAGPVLEAFGNAKTAHNNNSSRFG 297
Cdd:cd14890     81 IIISGESGAGKTEATKIIMQYLariTSGFAQGASGEgeaaseaieqtlgsLEDRVLSSNPLLESFGNAKTLRNDNSSRFG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  298 KFIQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLnQHNLNIEDGEDL 377
Cdd:cd14890    161 KFIEIQFDHHGKIVGAEISNFLLEKTRIVTQNDGERNYHIFYQLLAGADEALRERLKLQTPVEYFYL-RGECSSIPSCDD 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  378 KHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKkrATGRDEGLE-VGPPEVLDTLSQLLKVKRETLVEVLTKR 456
Cdd:cd14890    240 AKAFAETIRCLSTIGISEENQDAVFGLLAAVLHLGNVDFE--SENDTTVLEdATTLQSLKLAAELLGVNEDALEKALLTR 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  457 kTVTVNDKLIL-PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQF 535
Cdd:cd14890    318 -QLFVGGKTIVqPQNVEQARDKRDALAKALYSSLFLWLVSELNRTISSPDDKWG-----FIGVLDIYGFEKFEWNTFEQL 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  536 CINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPT---GLFYLLD-------EESNfphatsH 605
Cdd:cd14890    392 CINYANEKLQRHFNQHMFEVEQVEYSNEGIDWQYITFNDNQACLELIEGKVNgkpGIFITLDdcwrfkgEEAN------K 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  606 TLLAKFKQQH-------------EDNKYFLgTPVLEPA--FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSy 670
Cdd:cd14890    466 KFVSQLHASFgrksgsggtrrgsSQHPHFV-HPKFDADkqFGIKHYAGDVIYDASGFNEKNNETLNAEMKELIKQSRRS- 543
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  671 vrqligmdpvavfrwavlraairamavLREAgrlraeraekaagisspatrshmeelprgastpseklyrctgldfsfer 750
Cdd:cd14890    544 ---------------------------IREV------------------------------------------------- 547
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  751 seeldvnafedimafyesrndlhnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslr 830
Cdd:cd14890        --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  831 liismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLE 910
Cdd:cd14890    548 -------------------------SVGAQFRTQLQELMAKISLTNPRYVRCIKPNETKAPGKFDGLDCLRQLKYSGMME 602
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720426625  911 TVRIRRSGYSAKYTFQDFTEQFQVLLPkDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14890    603 AIQIRQQGFALREEHDSFFYDFQVLLP-TAENIEQLVAVLSKMLGLGKADWQIGSSKIFLK 662
MYSc_Myo27 cd14888
class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic ...
160-971 1.18e-147

class XXVII myosin, motor domain; Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276853 [Multi-domain]  Cd Length: 667  Bit Score: 474.57  E-value: 1.18e-147
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPiynpkyvKMYENQQLGKL-------EPHVFALADVAYYAMLRKHVN 232
Cdd:cd14888      1 ASILHSLNLRFDIDEIYTFTGPILIAVNPFKTIP-------GLYSDEMLLKFiqpsiskSPHVFSTASSAYQGMCNNKKS 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  233 QCIVISGESGSGKTQSTNF---LIHCLTALSQKGYaSGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGI 309
Cdd:cd14888     74 QTILISGESGAGKTESTKYvmkFLACAGSEDIKKR-SLVEAQVLESNPLLEAFGNARTLRNDNSSRFGKFIELQFSKLKS 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  310 VR---------GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSE--------EERLE--------------FQLKQP 358
Cdd:cd14888    153 KRmsgdrgrlcGAKIQTYLLEKVRVCDQQEGERNYHIFYQLCAAAREakntglsyEENDEklakgadakpisidMSSFEP 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  359 QDYF-YLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtGRDEG--LEVGPPEVL 435
Cdd:cd14888    233 HLKFrYLTKSSCHELPDVDDLEEFESTLYAMQTVGISPEEQNQIFSIVAAILYLGNILFENNE-ACSEGavVSASCTDDL 311
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  436 DTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMeeavSCLS 515
Cdd:cd14888    312 EKVASLLGVDAEDLLNALCYRTIKTAHEFYTKPLRVDEAEDVRDALARALYSCLFDKVVERTNESIGYSKDN----SLLF 387
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  516 IGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDE 595
Cdd:cd14888    388 CGVLDIFGFECFQLNSFEQLCINFTNERLQQFFNNFVFKCEEKLYIEEGISWNPLDFPDNQDCVDLLQEKPLGIFCMLDE 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  596 ESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLi 675
Cdd:cd14888    468 ECFVPGGKDQGLCNKLCQKHKGHKRFDVVKTDPNSFVIVHFAGPVKYCSDGFLEKNKDQLSVDAQEVIKNSKNPFISNL- 546
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  676 gmdpvavfrwavlraairamavlreagrlraeraekaagisspatrshmeelprgastpseklyrctgldfsFERseeld 755
Cdd:cd14888    547 ------------------------------------------------------------------------FSA----- 549
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  756 vnafedimafYESRNDLHNQiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliism 835
Cdd:cd14888    550 ----------YLRRGTDGNT------------------------------------------------------------ 559
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  836 tlhdrttksllhlhKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIR 915
Cdd:cd14888    560 --------------KKKKFVTVSSEFRNQLDVLMETIDKTEPHFIRCIKPNSQNVPDLFDRISVNEQLKYGGVLQAVQVS 625
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426625  916 RSGYSAKYTFQDFTEQFQVLLPKDvqpcreaiaallEKLQVdrQNYQIGKTKVFLK 971
Cdd:cd14888    626 RAGYPVRLSHAEFYNDYRILLNGE------------GKKQL--SIWAVGKTLCFFK 667
MYSc_Myo40 cd14901
class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much ...
160-970 1.24e-143

class XL myosin, motor domain; The class XL myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276866 [Multi-domain]  Cd Length: 655  Bit Score: 463.11  E-value: 1.24e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYN----PKYVKMYENQQLG--KLEPHVFALADVAYYAMLRKHV-- 231
Cdd:cd14901      1 PSILHVLRRRFAHGLIYTSTGAILVAINPFRRLPLYDdetkEAYYEHGERRAAGerKLPPHVYAVADKAFRAMLFASRgq 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  232 --NQCIVISGESGSGKTQSTNFLIHCLTALS--QKGYASGVERT-----ILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 302
Cdd:cd14901     81 kcDQSILVSGESGAGKTETTKIIMNYLASVSsaTTHGQNATEREnvrdrVLESNPILEAFGNARTNRNNNSSRFGKFIRL 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  303 NYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNI-EDGEDLKHDF 381
Cdd:cd14901    161 GFASSGSLLGASISTYLLERVRLVSQAKGERNYHIFYELLRGASSDELHALGLTHVEEYKYLNSSQCYDrRDGVDDSVQY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  382 ERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKrATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTV 461
Cdd:cd14901    241 AKTRHAMTTIGMSPDEQISVLQLVAAVLHLGNLCFVK-KDGEGGTFSMSSLANVRAACDLLGLDMDVLEKTLCTREIRAG 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  462 NDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALlnkKDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYAN 541
Cdd:cd14901    320 GEYITMPLSVEQALLTRDVVAKTLYAQLFDWLVDRINESI---AYSESTGASRFIGIVDIFGFEIFATNSLEQLCINFAN 396
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  542 EQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYF 621
Cdd:cd14901    397 EKLQQLFGKFVFEMEQDEYVAEAIPWTFVEYPNNDACVAMFEARPTGLFSLLDEQCLLPRGNDEKLANKYYDLLAKHASF 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  622 lGTPVLEPA---FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVrqligmdpvavfrwavlraairamavl 698
Cdd:cd14901    477 -SVSKLQQGkrqFVIHHYAGAVCYATDGFCDKNKDHVHSEALALLRTSSNAFL--------------------------- 528
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  699 reagrlraeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiik 778
Cdd:cd14901        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  779 slkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkPPSIS 858
Cdd:cd14901    529 ---------------------------------------------------------------------------SSTVV 533
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  859 AQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP- 937
Cdd:cd14901    534 AKFKVQLSSLLEVLNATEPHFIRCIKPNDVLSPSEFDAKRVLEQLRCSGVLEAVKISRSGYPVRFPHDAFVHTYSCLAPd 613
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|.
gi 1720426625  938 --KDVQPCREAIAALLEKLQV------DRQNYQIGKTKVFL 970
Cdd:cd14901    614 gaSDTWKVNELAERLMSQLQHselnieHLPPFQVGKTKVFL 654
MYSc_Myo31 cd14892
class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of ...
160-971 2.74e-143

class XXXI myosin, motor domain; Class XXXI myosins have a very long neck region consisting of 17 IQ motifs and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276857 [Multi-domain]  Cd Length: 656  Bit Score: 461.92  E-value: 2.74e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYN-PKYVKMYENQQLGKL-EPHVFALADVAYYAMLR----KHVN 232
Cdd:cd14892      1 APLLDVLRRRYERDAIYTFTADILISINPYKSIPlLYDvPGFDSQRKEEATASSpPPHVFSIAERAYRAMKGvgkgQGTP 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  233 QCIVISGESGSGKTQSTNFLIHCLTALSQ-----------KGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQ 301
Cdd:cd14892     81 QSIVVSGESGAGKTEASKYIMKYLATASKlakgastskgaANAHESIEECVLLSNLILEAFGNAKTIRNDNSSRFGKYIQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  302 VNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDF 381
Cdd:cd14892    161 IHYNSDGRIAGASTDHFLLEKSRLVGPDANERNYHIFYQLLAGLDANENAALELTPAESFLFLNQGNCVEVDGVDDATEF 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  382 ERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTV 461
Cdd:cd14892    241 KQLRDAMEQLGFDAEFQRPIFEVLAAVLHLGNVRFEENADDEDVFAQSADGVNVAKAAGLLGVDAAELMFKLVTQTTSTA 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  462 NDK-LILPYSLSEAITARDSMAKSLYSALFDWIVLRINHA------LLNKKDMEEAVSCLsIGVLDIFGFEDFERNSFEQ 534
Cdd:cd14892    321 RGSvLEIKLTAREAKNALDALCKYLYGELFDWLISRINAChkqqtsGVTGGAASPTFSPF-IGILDIFGFEIMPTNSFEQ 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  535 FCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATS-HTLLAKFKQ 613
Cdd:cd14892    400 LCINFTNEMLQQQFNKHVFVLEQEVYASEGIDVSAIEFQDNQDCLDLIQKKPLGLLPLLEEQMLLKRKTTdKQLLTIYHQ 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  614 QHEDNKYFLGTPVLE-PAFIIQHFAGRVKYQIKDFREKNMDymrpdivallrgsdssyvrqligmdpvavfrwavlraai 692
Cdd:cd14892    480 THLDKHPHYAKPRFEcDEFVLRHYAGDVTYDVHGFLAKNND--------------------------------------- 520
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  693 ramavlreagrlraeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrnDL 772
Cdd:cd14892    521 ------------------------------------------------------------------------------NL 522
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  773 HNQIIkslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipkNLLDSKSlrliismtlhdrttksllhlhkkk 852
Cdd:cd14892    523 HDDLR--------------------------------------------DLLRSSS------------------------ 534
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  853 kppsisaQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQF 932
Cdd:cd14892    535 -------KFRTQLAELMEVLWSTTPSYIKCIKPNNLKFPGGFSCELVRDQLIYSGVLEVVRIRREGFPIRRQFEEFYEKF 607
                          810       820       830       840       850
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625  933 QVLL-----------PKDVQPCREAIAALLEKlQVDRQNYQIGKTKVFLK 971
Cdd:cd14892    608 WPLArnkagvaaspdACDATTARKKCEEIVAR-ALERENFQLGRTKVFLR 656
MYSc_Myo42 cd14903
class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not ...
160-971 3.61e-143

class XLII myosin, motor domain; The class XLII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276868 [Multi-domain]  Cd Length: 658  Bit Score: 461.94  E-value: 3.61e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVIS 238
Cdd:cd14903      1 AAILYNVKKRFLRKLPYTYTGDICIAVNPYQWLPeLYTEEQHSKYLNKPKEELPPHVYATSVAAYNHMKRSGRNQSILVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  239 GESGSGKTQSTNFLIHCLTALsqkgyASGVE----RTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAV 314
Cdd:cd14903     81 GESGAGKTETTKILMNHLATI-----AGGLNdstiKKIIEVNPLLESFGNAKTVRNDNSSRFGKFTQLQFDKNGTLVGAK 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  315 VEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQhNLNIEDGEDLKHdFERLQQAMEMVGFL 394
Cdd:cd14903    156 CRTYLLEKTRVISHERPERNYHIFYQLLASPDVEERLFLDSANECAYTGANK-TIKIEGMSDRKH-FARTKEALSLIGVS 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  395 PATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEA 474
Cdd:cd14903    234 EEKQEVLFEVLAGILHLGQLQIQSKPNDDEKSAIAPGDQGAVYATKLLGLSPEALEKALCSRTMRAAGDVYTVPLKKDQA 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  475 ITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFK 554
Cdd:cd14903    314 EDCRDALAKAIYSNVFDWLVATINASLGNDAKMAN-----HIGVLDIFGFEHFKHNSFEQFCINYANEKLQQKFTQDVFK 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  555 LEQEEYQGEGISWHNIDYTDNVGCIHLISKKpTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPA-FII 633
Cdd:cd14903    389 TVQIEYEEEGIRWAHIDFADNQDVLAVIEDR-LGIISLLNDEVMRPKGNEESFVSKLSSIHKDEQDVIEFPRTSRTqFTI 467
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  634 QHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGmdpvavfrwavLRAAIRAmAVLREAGRLRAERAEKAA 713
Cdd:cd14903    468 KHYAGPVTYESLGFLEKHKDALLPDLSDLMRGSSKPFLRMLFK-----------EKVESPA-AASTSLARGARRRRGGAL 535
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  714 GISSPATrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedprrl 793
Cdd:cd14903    536 TTTTVGT------------------------------------------------------------------------- 542
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  794 lqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppsisaQFQTSLNKLLEALG 873
Cdd:cd14903    543 ------------------------------------------------------------------QFKDSLNELMTTIR 556
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  874 KAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP---KDVQPCREAIAAL 950
Cdd:cd14903    557 STNVHYVRCIKPNSIKSPTELDHLMVVSQLRCAGVIEAIRISRAAYPNRLLHEEFLDKFWLFLPegrNTDVPVAERCEAL 636
                          810       820
                   ....*....|....*....|..
gi 1720426625  951 LEKLQVDR-QNYQIGKTKVFLK 971
Cdd:cd14903    637 MKKLKLESpEQYQMGLTRIYFQ 658
MYSc_Myo35 cd14896
class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 ...
163-971 2.56e-140

class XXXV myosin, motor domain; This class of metazoan myosins contains 2 IQ motifs, 2 MyTH4 domains, a single FERM domain, and an SH3 domain. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276861 [Multi-domain]  Cd Length: 644  Bit Score: 453.08  E-value: 2.56e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  163 LQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGESG 242
Cdd:cd14896      4 LLCLKKRFHLGRIYTFGGPILLSLNPHRSLPLFSEEVLASYHPRKALNTTPHIFAIAASAYRLSQSTGQDQCILLSGHSG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  243 SGKTQSTNFLIHCLTALSQKGyASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVnYLENGIVRGAVVEKYLLEK 322
Cdd:cd14896     84 SGKTEAAKKIVQFLSSLYQDQ-TEDRLRQPEDVLPILESFGHAKTILNANASRFGQVLRL-HLQHGVIVGASVSHYLLET 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  323 SRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFLPATKKQIF 402
Cdd:cd14896    162 SRVVFQAQAERSFHVFYELLAGLDPEEREQLSLQGPETYYYLNQGGACRLQGKEDAQDFEGLLKALQGLGLCAEELTAIW 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  403 SVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMA 482
Cdd:cd14896    242 AVLAAILQLGNICFSSSERESQEVAAVSSWAEIHTAARLLQVPPERLEGAVTHRVTETPYGRVSRPLPVEGAIDARDALA 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  483 KSLYSALFDWIVLRINhALLNKKDMEEAVSclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQG 562
Cdd:cd14896    322 KTLYSRLFTWLLKRIN-AWLAPPGEAESDA--TIGVVDAYGFEALRVNGLEQLCINLASERLQLFSSQTLLAQEEEECQR 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  563 EGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPAFIIQHFAGRVKY 642
Cdd:cd14896    399 ELLPWVPIPQPPRESCLDLLVDQPHSLLSILDDQTWLSQATDHTFLQKCHYHHGDHPSYAKPQLPLPVFTVRHYAGTVTY 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  643 QIKDFREKNMDYMRPDIVALLRGSDssyvRQLIGmdpvavfrwavlraairamavlreagrlraeraekaagisspatrs 722
Cdd:cd14896    479 QVHKFLNRNRDQLDPAVVEMLAQSQ----LQLVG---------------------------------------------- 508
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  723 hmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedprrllqslSLFQK 802
Cdd:cd14896    509 ---------------------------------------------------------------------------SLFQE 513
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  803 PRTSFlkskgikqkqiipknlldskslrliismtlhdrttksllhlHKKKKPPSISAQFQTSLNKLLEALGKAEPFFIRC 882
Cdd:cd14896    514 AEPQY-----------------------------------------GLGQGKPTLASRFQQSLGDLTARLGRSHVYFIHC 552
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  883 IRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLpKDVQPC---REAIAALLEK-LQVDR 958
Cdd:cd14896    553 LNPNPGKLPGLFDVGHVTEQLRQAGILEAIGTRSEGFPVRVPFQAFLARFGALG-SERQEAlsdRERCGAILSQvLGAES 631
                          810
                   ....*....|...
gi 1720426625  959 QNYQIGKTKVFLK 971
Cdd:cd14896    632 PLYHLGATKVLLK 644
MYSc_Myo30 cd14891
class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal ...
160-666 4.57e-135

class XXX myosin, motor domain; Myosins of class XXX are composed of an amino-terminal SH3-like domain, two IQ motifs, a coiled-coil region and a PX domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276856  Cd Length: 645  Bit Score: 438.32  E-value: 4.57e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFM--QQKIYTYAGSILVAINPFKFLPiyNPKyVKMYENQQLGKLEPHVFALADVAYYAM-LRKHV--NQC 234
Cdd:cd14891      1 AGILHNLEERSKldNQRPYTFMANVLIAVNPLRRLP--EPD-KSDYINTPLDPCPPHPYAIAEMAYQQMcLGSGRmqNQS 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  235 IVISGESGSGKTQSTNFLIHCLT-----------------ALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFG 297
Cdd:cd14891     78 IVISGESGAGKTETSKIILRFLTtravggkkasgqdieqsSKKRKLSVTSLDERLMDTNPILESFGNAKTLRNHNSSRFG 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  298 KFIQVNYLENGI-VRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGED 376
Cdd:cd14891    158 KFMKLQFTKDKFkLAGAFIETYLLEKSRLVAQPPGERNFHIFYQLLAGASAELLKELLLLSPEDFIYLNQSGCVSDDNID 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  377 LKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAT--GRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLT 454
Cdd:cd14891    238 DAANFDNVVSALDTVGIDEDLQLQIWRILAGLLHLGNIEFDEEDTseGEAEIASESDKEALATAAELLGVDEEALEKVIT 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  455 KRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDmeeavSCLSIGVLDIFGFEDFER-NSFE 533
Cdd:cd14891    318 QREIVTRGETFTIKRNAREAVYSRDAIAKSIYERLFLWIVQQINTSLGHDPD-----PLPYIGVLDIFGFESFETkNDFE 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  534 QFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQ 613
Cdd:cd14891    393 QLLINYANEALQATFNQQVFIAEQELYKSEGIDVGVITWPDNRECLDLIASKPNGILPLLDNEARNPNPSDAKLNETLHK 472
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720426625  614 QHEDNKYFLGTPV--LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGS 666
Cdd:cd14891    473 THKRHPCFPRPHPkdMREMFIVKHYAGTVSYTIGSFIDKNNDIIPEDFEDLLASS 527
PTZ00014 PTZ00014
myosin-A; Provisional
148-1046 1.80e-132

myosin-A; Provisional


Pssm-ID: 240229 [Multi-domain]  Cd Length: 821  Bit Score: 437.15  E-value: 1.80e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  148 FDDLCNLPELTEANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYEN-QQLGKLEPHVFALADVAYYAM 226
Cdd:PTZ00014    98 YGDIGLLPHTNIPCVLDFLKHRYLKNQIYTTADPLLVAINPFKDLGNTTNDWIRRYRDaKDSDKLPPHVFTTARRALENL 177
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  227 LRKHVNQCIVISGESGSGKTQSTNFLIhcltalsqKGYASGV--------ERTILGAGPVLEAFGNAKTAHNNNSSRFGK 298
Cdd:PTZ00014   178 HGVKKSQTIIVSGESGAGKTEATKQIM--------RYFASSKsgnmdlkiQNAIMAANPVLEAFGNAKTIRNNNSSRFGR 249
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  299 FIQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLK 378
Cdd:PTZ00014   250 FMQLQLGEEGGIRYGSIVAFLLEKSRVVTQEDDERSYHIFYQLLKGANDEMKEKYKLKSLEEYKYINPKCLDVPGIDDVK 329
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  379 hDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAT-GRDEGLEVGP--PEVLDTLSQLLKVKRETLVEVLTK 455
Cdd:PTZ00014   330 -DFEEVMESFDSMGLSESQIEDIFSILSGVLLLGNVEIEGKEEgGLTDAAAISDesLEVFNEACELLFLDYESLKKELTV 408
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  456 RKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQF 535
Cdd:PTZ00014   409 KVTYAGNQKIEGPWSKDESEMLKDSLSKAVYEKLFLWIIRNLNATIEPPGGFK-----VFIGMLDIFGFEVFKNNSLEQL 483
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  536 CINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH 615
Cdd:PTZ00014   484 FINITNEMLQKNFVDIVFERESKLYKDEGISTEELEYTSNESVIDLLCGKGKSVLSILEDQCLAPGGTDEKFVSSCNTNL 563
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  616 EDNKYFLGTPV-LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraaira 694
Cdd:PTZ00014   564 KNNPKYKPAKVdSNKNFVIKHTIGDIQYCASGFLFKNKDVLRPELVEVVKASPNPLVRDL-------------------- 623
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  695 mavlreagrlraeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnaFEDIMAfyesrndlhn 774
Cdd:PTZ00014   624 ----------------------------------------------------------------FEGVEV---------- 629
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  775 qiikslkglpwqgedprrllqslslfqkprtsflkskgikQKQIIPKNLLdskslrliismtlhdrttksllhlhkkkkp 854
Cdd:PTZ00014   630 ----------------------------------------EKGKLAKGQL------------------------------ 639
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  855 psISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQV 934
Cdd:PTZ00014   640 --IGSQFLNQLDSLMSLINSTEPHFIRCIKPNENKKPLDWNSSKVLIQLHSLSILEALQLRQLGFSYRRTFAEFLSQFKY 717
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  935 L-LP----KDVQPcREAIAALLEKLQVDRQNYQIGKTKVFLKETERQTLQEKLHgevlrriLQLQSWfrmvlerKHFVQM 1009
Cdd:PTZ00014   718 LdLAvsndSSLDP-KEKAEKLLERSGLPKDSYAIGKTMVFLKKDAAKELTQIQR-------EKLAAW-------EPLVSV 782
                          890       900       910
                   ....*....|....*....|....*....|....*...
gi 1720426625 1010 khaaltIQACWRSYRVRRAL-ERTQAAVYLQAAWRGYL 1046
Cdd:PTZ00014   783 ------LEALILKIKKKRKVrKNIKSLVRIQAHLRRHL 814
MYSc_Myo43 cd14904
class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not ...
160-971 4.82e-130

class XLIII myosin, motor domain; The class XLIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276869  Cd Length: 653  Bit Score: 424.35  E-value: 4.82e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVIS 238
Cdd:cd14904      1 PSILFNLKKRFAASKPYTYTNDIVIALNPYKWIDnLYGDHLHEQYLKKPRDKLQPHVYATSTAAYKHMLTNEMNQSILVS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  239 GESGSGKTQSTNFLIHCLTALSQKGYASGVERTIlGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKY 318
Cdd:cd14904     81 GESGAGKTETTKIVMNHLASVAGGRKDKTIAKVI-DVNPLLESFGNAKTTRNDNSSRFGKFTQLQFDGRGKLIGAKCETY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIE-DGEDLKHDFERLQQAMEMVGFLPAT 397
Cdd:cd14904    160 LLEKSRVVSIAEGERNYHIFYQLLAGLSSEERKEFGLDPNCQYQYLGDSLAQMQiPGLDDAKLFASTQKSLSLIGLDNDA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  398 KKQIFSVLSAILYLGNVTYKKRAtgrDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITA 477
Cdd:cd14904    240 QRTLFKILSGVLHLGEVMFDKSD---ENGSRISNGSQLSQVAKMLGLPTTRIEEALCNRSVVTRNESVTVPLAPVEAEEN 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  478 RDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQ 557
Cdd:cd14904    317 RDALAKAIYSKLFDWMVVKINAAISTDDDRIKG----QIGVLDIFGFEDFAHNGFEQFCINYANEKLQQKFTTDVFKTVE 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  558 EEYQGEGISWHNIDYTDNVGCIHLISKKpTGLFYLLDEESNFPHATSHTLLAKFKQQHE---DNKYFLGTPVLEPAFIIQ 634
Cdd:cd14904    393 EEYIREGLQWDHIEYQDNQGIVEVIDGK-MGIIALMNDHLRQPRGTEEALVNKIRTNHQtkkDNESIDFPKVKRTQFIIN 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  635 HFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGmdpvavfrwavlraairamavlreagrlraeraekaag 714
Cdd:cd14904    472 HYAGPVTYETVGFMEKHRDTLQNDLLDLVLLSSLDLLTELFG-------------------------------------- 513
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  715 iSSPATRSHMEelprgasTPSEKlyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedprrll 794
Cdd:cd14904    514 -SSEAPSETKE-------GKSGK--------------------------------------------------------- 528
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  795 qslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhKKKKPPSISAQFQTSLNKLLEALGK 874
Cdd:cd14904    529 -------------------------------------------------------GTKAPKSLGSQFKTSLSQLMDNIKT 553
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  875 AEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP-----KDV-QPCREAIA 948
Cdd:cd14904    554 TNTHYVRCIKPNANKSPTEFDKRMVVEQLRSAGVIEAIRITRSGYPSRLTPKELATRYAIMFPpsmhsKDVrRTCSVFMT 633
                          810       820
                   ....*....|....*....|...
gi 1720426625  949 ALLEKLQVDrqnYQIGKTKVFLK 971
Cdd:cd14904    634 AIGRKSPLE---YQIGKSLIYFK 653
MYSc_Myh10 cd14920
class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy ...
160-971 1.49e-128

class II myosin heavy chain 10, motor domain; Myosin motor domain of non-muscle myosin heavy chain 10 (also called NMMHCB). Mutations in this gene have been associated with May-Hegglin anomaly and developmental defects in brain and heart. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276952 [Multi-domain]  Cd Length: 673  Bit Score: 420.96  E-value: 1.49e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14920      1 ASVLHNLKDRYYSGLIYTYSGLFCVVINPYKNLPIYSENIIEMYRGKKRHEMPPHIYAISESAYRCMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLT--ALSQKGYASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14920     81 ESGAGKTENTKKVIQYLAhvASSHKGRKDHnipgeLERQLLQANPILESFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEMVG 392
Cdd:cd14920    161 ANIETYLLEKSRAVRQAKDERTFHIFYQLLSGAGEHLKSDLLLEGFNNYRFLSNGYIPIPGQQD-KDNFQETMEAMHIMG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  393 FLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLevgpPE--VLDTLSQLLKVK-RETLVEVLTKRKTVTvNDKLILPY 469
Cdd:cd14920    240 FSHEEILSMLKVVSSVLQFGNISFKKERNTDQASM----PEntVAQKLCHLLGMNvMEFTRAILTPRIKVG-RDYVQKAQ 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  470 SLSEAITARDSMAKSLYSALFDWIVLRINHALlnkkDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFT 549
Cdd:cd14920    315 TKEQADFAVEALAKATYERLFRWLVHRINKAL----DRTKRQGASFIGILDIAGFEIFELNSFEQLCINYTNEKLQQLFN 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  550 QHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISK--KPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGT-- 624
Cdd:cd14920    391 HTMFILEQEEYQREGIEWNFIDFgLDLQPCIDLIERpaNPPGVLALLDEECWFPKATDKTFVEKLVQEQGSHSKFQKPrq 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  625 PVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrwavlraairamavlreagrl 704
Cdd:cd14920    471 LKDKADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLHQSSDRFVAEL------------------------------ 520
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  705 raeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglp 784
Cdd:cd14920        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  785 WQGEDprRLLQSLSLFQKPRTSFlkSKGIKQKqiipKNLLdskslrliismtlhdRTTKSLlhlhkkkkppsisaqFQTS 864
Cdd:cd14920    521 WKDVD--RIVGLDQVTGMTETAF--GSAYKTK----KGMF---------------RTVGQL---------------YKES 562
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  865 LNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDV 940
Cdd:cd14920    563 LTKLMATLRNTNPNFVRCIIPNHEKRAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKGF 642
                          810       820       830
                   ....*....|....*....|....*....|.
gi 1720426625  941 QPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14920    643 MDGKQACERMIRALELDPNLYRIGQSKIFFR 673
MYSc_Myo41 cd14902
class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much ...
160-946 1.58e-128

class XLI myosin, motor domain; The class XLI myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276867 [Multi-domain]  Cd Length: 716  Bit Score: 422.38  E-value: 1.58e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYE--------NQQLGKLEPHVFALADVAYYAMLR-K 229
Cdd:cd14902      1 AALLQALSERFEHDQIYTSIGDILVALNPLKPLPdLYSESQLNAYKasmtstspVSQLSELPPHVFAIGGKAFGGLLKpE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  230 HVNQCIVISGESGSGKTQSTNFLIHCLTAL--------SQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQ 301
Cdd:cd14902     81 RRNQSILVSGESGSGKTESTKFLMQFLTSVgrdqssteQEGSDAVEIGKRILQTNPILESFGNAQTIRNDNSSRFGKFIK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  302 VNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDF 381
Cdd:cd14902    161 IQFGANNEIVGAQIVSYLLEKVRLLHQSPEERSFHIFYELLEGADKTLLDLLGLQKGGKYELLNSYGPSFARKRAVADKY 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  382 ERLQ----QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKrATGRDEGLEVGPP--EVLDTLSQLLKVKRETLVEVLTK 455
Cdd:cd14902    241 AQLYvetvRAFEDTGVGELERLDIFKILAALLHLGNVNFTA-ENGQEDATAVTAAsrFHLAKCAELMGVDVDKLETLLSS 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  456 RKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLR----INHALLNKKDMEEAVSCLSIGVLDIFGFEDFERNS 531
Cdd:cd14902    320 REIKAGVEVMVLKLTPEQAKEICGSLAKAIYGRLFTWLVRRlsdeINYFDSAVSISDEDEELATIGILDIFGFESLNRNG 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  532 FEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKF 611
Cdd:cd14902    400 FEQLCINYANERLQAQFNEFVFVKEQQIYIAEGIDWKNISYPSNAACLALFDDKSNGLFSLLDQECLMPKGSNQALSTKF 479
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  612 KQqhednkYFLGtpvlEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVrQLIGMDPvavfrwavlraa 691
Cdd:cd14902    480 YR------YHGG----LGQFVVHHFAGRVCYNVEQFVEKNTDALPADASDILSSSSNEVV-VAIGADE------------ 536
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  692 iramavlreagrlraeraeKAAGISSPAtrshmeelprgastpSEKLYRctgldfsferseeldvnafedimafyesrnd 771
Cdd:cd14902    537 -------------------NRDSPGADN---------------GAAGRR------------------------------- 551
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  772 lhnqiikslkglpwqgedprrllqslslfqkpRTSFLKSkgikqkqiipknlldskslrliismtlhdrttksllhlhkk 851
Cdd:cd14902    552 --------------------------------RYSMLRA----------------------------------------- 558
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  852 kkpPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQ 931
Cdd:cd14902    559 ---PSVSAQFKSQLDRLIVQIGRTEAHYVRCLKPNEVKKPGIFDRERMVEQMRSVGVLEAVRIARHGYSVRLAHASFIEL 635
                          810
                   ....*....|....*
gi 1720426625  932 FQVLLPKDVQPCREA 946
Cdd:cd14902    636 FSGFKCFLSTRDRAA 650
RhoGAP_myosin_IXB cd04407
RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1700-1885 5.67e-128

RhoGAP_myosin_IXB: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXB. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239872 [Multi-domain]  Cd Length: 186  Bit Score: 398.98  E-value: 5.67e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1779
Cdd:cd04407      1 FGVRVGSLTSNKTSVPIVLEKLLEHVEMHGLYTEGIYRKSGSANRMKELHQLLQADPENVKLENYPIHAITGLLKQWLRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1780 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1859
Cdd:cd04407     81 LPEPLMTFAQYNDFLRAVELPEKQEQLQAIYRVLEQLPTANHNTLERLIFHLVKVALEEDVNRMSPNALAIVFAPCLLRC 160
                          170       180
                   ....*....|....*....|....*.
gi 1720426625 1860 PDNSDPLTSMKDVLKITTCVEMLIKE 1885
Cdd:cd04407    161 PDSSDPLTSMKDVAKTTTCVEMLIKE 186
MYSc_Myo34 cd14895
class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short ...
166-971 9.60e-127

class XXXIV myosin, motor domain; Class XXXIV myosins are composed of an IQ motif, a short coiled-coil region, 5 tandem ANK repeats, and a carboxy-terminal FYVE domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276860 [Multi-domain]  Cd Length: 704  Bit Score: 416.66  E-value: 9.60e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  166 LKLRFMQQKIYTYAGSILVAINPFKFLP-IYNpkyVKMYENQQLG--KLEPHVFALADVAYYAMLRK-------HVNQCI 235
Cdd:cd14895      7 LAQRYGVDQVYCRSGAVLIAVNPFKHIPgLYD---LHKYREEMPGwtALPPHVFSIAEGAYRSLRRRlhepgasKKNQTI 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  236 VISGESGSGKTQSTNFLIHCLTALSQKGYA---SGVERTILG-----AGPVLEAFGNAKTAHNNNSSRFGKFIQVNY--- 304
Cdd:cd14895     84 LVSGESGAGKTETTKFIMNYLAESSKHTTAtssSKRRRAISGsellsANPILESFGNARTLRNDNSSRFGKFVRMFFegh 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  305 -LENGI-VRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLK--QPQDYFYLN-----QHNLNIEDGE 375
Cdd:cd14895    164 eLDTSLrMIGTSVETYLLEKVRVVHQNDGERNFHVFYELLAGAADDMKLELQLEllSAQEFQYISggqcyQRNDGVRDDK 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  376 DlkhdFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTY---KKRATGRDEGLEVGPP-------------EVLDTLS 439
Cdd:cd14895    244 Q----FQLVLQSMKVLGFTDVEQAAIWKILSALLHLGNVLFvasSEDEGEEDNGAASAPCrlasaspssltvqQHLDIVS 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  440 QLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHAL--------LNKKDMEEAV 511
Cdd:cd14895    320 KLFAVDQDELVSALTTRKISVGGETFHANLSLAQCGDARDAMARSLYAFLFQFLVSKVNSASpqrqfalnPNKAANKDTT 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  512 SClsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFY 591
Cdd:cd14895    400 PC--IAVLDIFGFEEFEVNQFEQFCINYANEKLQYQFIQDILLTEQQAHIEEGIKWNAVDYEDNSVCLEMLEQRPSGIFS 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  592 LLDEESNFPHATSHTLLAKFKQQHEDNKYFLG--TPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSS 669
Cdd:cd14895    478 LLDEECVVPKGSDAGFARKLYQRLQEHSNFSAsrTDQADVAFQIHHYAGAVRYQAEGFCEKNKDQPNAELFSVLGKTSDA 557
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  670 YVRQLigMDPVAVfrwavlraairamavlreagrlrAERAEKAAGisSPATRShmeelprgastpseklyrctgldfsfe 749
Cdd:cd14895    558 HLREL--FEFFKA-----------------------SESAELSLG--QPKLRR--------------------------- 583
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  750 rseeldvnafedimafyesrndlhnqiikslkglpwqgedprrllqslslfqkpRTSFLKSKGikqkqiipknlldsksl 829
Cdd:cd14895    584 ------------------------------------------------------RSSVLSSVG----------------- 592
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  830 rliismtlhdrttksllhlhkkkkppsISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGML 909
Cdd:cd14895    593 ---------------------------IGSQFKQQLASLLDVVQQTQTHYIRCIKPNDESASDQFDMAKVSSQLRYGGVL 645
                          810       820       830       840       850       860
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720426625  910 ETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPCREAiAALLEKLQVDrqNYQIGKTKVFLK 971
Cdd:cd14895    646 KAVEIMRQSYPVRMKHADFVKQYRLLVAAKNASDATA-SALIETLKVD--HAELGKTRVFLR 704
MYSc_Myh2_insects_mollusks cd14911
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
160-971 4.58e-123

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in insects and mollusks. This gene encodes a member of the class II or conventional myosin heavy chains, and functions in skeletal muscle contraction. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276876 [Multi-domain]  Cd Length: 674  Bit Score: 405.13  E-value: 4.58e-123
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14911      1 ASVLHNIKDRYYSGLIYTYSGLFCVVVNPYKKLPIYTEKIMERYKGIKRHEVPPHVFAITDSAYRNMLGDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCL----------------TALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVN 303
Cdd:cd14911     81 ESGAGKTENTKKVIQFLayvaaskpkgsgavphPAVNPAVLIGELEQQLLQANPILEAFGNAKTVKNDNSSRFGKFIRIN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  304 YLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEdGEDLKHDFER 383
Cdd:cd14911    161 FDASGFISGANIETYLLEKSRAIRQAKDERTFHIFYQLLAGATPEQREKFILDDVKSYAFLSNGSLPVP-GVDDYAEFQA 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  384 LQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLevgpPE--VLDTLSQLLKVKRETLVEVLTKRKTVTV 461
Cdd:cd14911    240 TVKSMNIMGMTSEDFNSIFRIVSAVLLFGSMKFRQERNNDQATL----PDntVAQKIAHLLGLSVTDMTRAFLTPRIKVG 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  462 NDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYAN 541
Cdd:cd14911    316 RDFVTKAQTKEQVEFAVEAIAKACYERMFKWLVNRINRSLDRTKRQGASF----IGILDMAGFEIFELNSFEQLCINYTN 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  542 EQLQYYFTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKY 620
Cdd:cd14911    392 EKLQQLFNHTMFILEQEEYQREGIEWKFIDFgLDLQPTIDLI-DKPGGIMALLDEECWFPKATDKTFVDKLVSAHSMHPK 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  621 FLGTPVLEPA-FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmDPVAVFRWavlraairamavlr 699
Cdd:cd14911    471 FMKTDFRGVAdFAIVHYAGRVDYSAAKWLMKNMDPLNENIVSLLQGSQ----------DPFVVNIW-------------- 526
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  700 eagrlraeraeKAAGISSPATRShMEELPRGAstpseklyrctgldfsferseeldvnafedimafyesrndlhnqiiks 779
Cdd:cd14911    527 -----------KDAEIVGMAQQA-LTDTQFGA------------------------------------------------ 546
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  780 lkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdRTTKSLLHlhkkkkppSISA 859
Cdd:cd14911    547 ------------------------------------------------------------RTRKGMFR--------TVSH 558
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  860 QFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL---- 935
Cdd:cd14911    559 LYKEQLAKLMDTLRNTNPNFVRCIIPNHEKRAGKIDAPLVLDQLRCNGVLEGIRICRQGFPNRIPFQEFRQRYELLtpnv 638
                          810       820       830
                   ....*....|....*....|....*....|....*.
gi 1720426625  936 LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14911    639 IPKGFMDGKKACEKMIQALELDSNLYRVGQSKIFFR 674
MYSc_Myh15_mammals cd14929
class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy ...
160-971 4.92e-122

class II myosin heavy chain 15, motor domain; Myosin motor domain of sarcomeric myosin heavy chain 15 in mammals (also called KIAA1000) . MYH15 is a slow-twitch myosin. Myh15 is a ventricular myosin heavy chain. Myh15 is absent in embryonic and fetal muscles and is found in orbital layer of extraocular muscles at birth. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276892 [Multi-domain]  Cd Length: 662  Bit Score: 401.66  E-value: 4.92e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14929      1 ASVLHTLRRRYDHWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIH---CLTALSQKGYASGV-ERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVV 315
Cdd:cd14929     81 ESGAGKTVNTKHIIQyfaTIAAMIESKKKLGAlEDQIMQANPVLEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSADI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  316 EKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKhDFERLQQAMEMVGFLP 395
Cdd:cd14929    161 DIYLLEKSRVIFQQPGERNYHIFYQILSGKKELRDLLLVSANPSDFHFCSCGAVAVESLDDAE-ELLATEQAMDILGFLP 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  396 ATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAI 475
Cdd:cd14929    240 DEKYGCYKLTGAIMHFGNMKFKQKP--REEQLEADGTENADKAAFLMGINSSELVKGLIHPRIKVGNEYVTRSQNIEQVT 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  476 TARDSMAKSLYSALFDWIVLRINHALLNKkdmeeAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKL 555
Cdd:cd14929    318 YAVGALSKSIYERMFKWLVARINRVLDAK-----LSRQFFIGILDITGFEILDYNSLEQLCINFTNEKLQQFFNQHMFVL 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  556 EQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPV-----LEP 629
Cdd:cd14929    393 EQEEYRKEGIDWVSIDFgLDLQACIDLI-EKPMGIFSILEEECMFPKATDLTFKTKLFDNHFGKSVHFQKPKpdkkkFEA 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  630 AFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSdssyvrqligmdpvavfrwavlraairamavlreagrlraera 709
Cdd:cd14929    472 HFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKS------------------------------------------- 508
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  710 ekaagisspatrshmeelprgastpseklyrctgldfsferSEELDVNAFEdimafyesrNDlhnqiIKSLKGLPWqGED 789
Cdd:cd14929    509 -----------------------------------------SNRLLASLFE---------NY-----ISTDSAIQF-GEK 532
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  790 PRRllqslslfqkprtsflksKGikqkqiipknlldsKSLRLIISmtlhdrttksllhLHKKkkppsisaqfqtSLNKLL 869
Cdd:cd14929    533 KRK------------------KG--------------ASFQTVAS-------------LHKE------------NLNKLM 555
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  870 EALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPK-----DVQPCR 944
Cdd:cd14929    556 TNLKSTAPHFVRCINPNVNKIPGVLDPYLVLQQLRCNGVLEGIRICREGFPNRLLYADFKQRYCILNPRtfpksKFVSSR 635
                          810       820
                   ....*....|....*....|....*..
gi 1720426625  945 EAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14929    636 KAAEELLGSLEIDHTQYRFGITKVFFK 662
MYSc_Myo39 cd14900
class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much ...
162-663 3.43e-121

class XXXIX myosin, motor domain; The class XXXIX myosins are found in Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276865  Cd Length: 627  Bit Score: 398.14  E-value: 3.43e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNP----KYVKMYE-------NQQLGKLEPHVFALADVAYYAMLR- 228
Cdd:cd14900      3 ILSALETRFYAQKIYTNTGAILLAVNPFQKLPgLYSSdtmaKYLLSFEarssstrNKGSDPMPPHIYQVAGEAYKAMMLg 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  229 ---KHVNQCIVISGESGSGKTQSTNFLIHCLT---------ALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRF 296
Cdd:cd14900     83 lngVMSDQSILVSGESGSGKTESTKFLMEYLAqagdnnlaaSVSMGKSTSGIAAKVLQTNILLESFGNARTLRNDNSSRF 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  297 GKFIQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLefqlkqpqdyfylnqhnlniedged 376
Cdd:cd14900    163 GKFIKLHFTSGGRLTGASIQTYLLEKVRLVSQSKGERNYHIFYEMAIGASEAARK------------------------- 217
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  377 lKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEG---LEVGPPEV--LDTLSQLLKVKRETLVE 451
Cdd:cd14900    218 -RDMYRRVMDAMDIIGFTPHERAGIFDLLAALLHIGNLTFEHDENSDRLGqlkSDLAPSSIwsRDAAATLLSVDATKLEK 296
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  452 VLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHaLLNKKDMEEAVSCLS-IGVLDIFGFEDFERN 530
Cdd:cd14900    297 ALSVRRIRAGTDFVSMKLSAAQANNARDALAKALYGRLFDWLVGKMNA-FLKMDDSSKSHGGLHfIGILDIFGFEVFPKN 375
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  531 SFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAK 610
Cdd:cd14900    376 SFEQLCINFANETLQQQFNDYVFKAEQREYESQGVDWKYVEFCDNQDCVNLISQRPTGILSLIDEECVMPKGSDTTLASK 455
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720426625  611 FKQQHEDNKYFLGTPVLEPA--FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALL 663
Cdd:cd14900    456 LYRACGSHPRFSASRIQRARglFTIVHYAGHVEYSTDGFLEKNKDVLHQEAVDLF 510
MYSc_Myo14 cd14876
class XIV myosin, motor domain; These myosins localize to plasma membranes of the ...
166-971 4.31e-121

class XIV myosin, motor domain; These myosins localize to plasma membranes of the intracellular parasites and may be involved in the cell invasion process. Their known functions include: transporting phagosomes to the nucleus and perturbing the developmentally regulated elimination of the macronucleus during conjugation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. C-terminal to their motor domain these myosins have a MyTH4-FERM protein domain combination. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276843  Cd Length: 649  Bit Score: 398.59  E-value: 4.31e-121
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  166 LKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYEN-QQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGESGSG 244
Cdd:cd14876      7 LKHRYLKNQIYTTADPLLVAINPFKDLGNATDEWIRKYRDaPDLTKLPPHVFYTARRALENLHGVNKSQTIIVSGESGAG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  245 KTQSTNFLIHCLtALSQKGYASG-VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYL-ENGIVRGAVVeKYLLEK 322
Cdd:cd14876     87 KTEATKQIMRYF-ASAKSGNMDLrIQTAIMAANPVLEAFGNAKTIRNNNSSRFGRFMQLDVAsEGGIRYGSVV-AFLLEK 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  323 SRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIeDGEDLKHDFERLQQAMEMVGFLPATKKQIF 402
Cdd:cd14876    165 SRIVTQDDNERSYHIFYQLLKGADSEMKSKYHLLGLKEYKFLNPKCLDV-PGIDDVADFEEVLESLKSMGLTEEQIDTVF 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  403 SVLSAILYLGNVTY-KKRATGRDEGLEVGP--PEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARD 479
Cdd:cd14876    244 SIVSGVLLLGNVKItGKTEQGVDDAAAISNesLEVFKEACSLLFLDPEALKRELTVKVTKAGGQEIEGRWTKDDAEMLKL 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  480 SMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEE 559
Cdd:cd14876    324 SLAKAMYDKLFLWIIRNLNSTIEPPGGFKNF-----MGMLDIFGFEVFKNNSLEQLFINITNEMLQKNFIDIVFERESKL 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  560 YQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLgtpvlePA-------FI 632
Cdd:cd14876    399 YKDEGIPTAELEYTSNAEVIDVLCGKGKSVLSILEDQCLAPGGSDEKFVSACVSKLKSNGKFK------PAkvdsninFI 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  633 IQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPVavfrwavlraairamavlrEAGRLraeraeka 712
Cdd:cd14876    473 VVHTIGDIQYNAEGFLFKNKDVLRAELVEVVQASTNPVVKALFEGVVV-------------------EKGKI-------- 525
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  713 agisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedprr 792
Cdd:cd14876        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  793 llqslslfqkprtsflkSKGikqkqiipknlldskSLrliismtlhdrttksllhlhkkkkppsISAQFQTSLNKLLEAL 872
Cdd:cd14876    526 -----------------AKG---------------SL---------------------------IGSQFLKQLESLMGLI 546
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  873 GKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP-----KDVQPcREAI 947
Cdd:cd14876    547 NSTEPHFIRCIKPNETKKPLEWNSSKVLIQLHALSILEALQLRQLGYSYRRPFEEFLYQFKFLDLgiandKSLDP-KVAA 625
                          810       820
                   ....*....|....*....|....
gi 1720426625  948 AALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14876    626 LKLLESSGLSEDEYAIGKTMVFLK 649
MYSc_Myh18 cd14932
class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain ...
160-971 1.25e-119

class II myosin heavy chain 18, motor domain; Myosin motor domain of muscle myosin heavy chain 18. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276895 [Multi-domain]  Cd Length: 676  Bit Score: 395.17  E-value: 1.25e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14932      1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKYLPIYSEEIVNMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLTAL-----SQKGYASGV------ERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENG 308
Cdd:cd14932     81 ESGAGKTENTKKVIQYLAYVassfkTKKDQSSIAlshgelEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  309 IVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd14932    161 YIVGANIETYLLEKSRAIRQAKDERAFHIFYYLLTGAGDKLRSELCLEDYSKYRFLSNGNVTIPGQQD-KELFAETMEAF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLevgpPEvlDTLSQ----LLKVKRETLVEVLTKRKTVTVNDK 464
Cdd:cd14932    240 RIMSIPEEEQTGLLKVVSAVLQLGNMSFKKERNSDQASM----PD--DTAAQkvchLLGMNVTDFTRAILSPRIKVGRDY 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  465 LILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQL 544
Cdd:cd14932    314 VQKAQTQEQAEFAVEALAKASYERMFRWLVMRINKALDKTKRQGASF----IGILDIAGFEIFELNSFEQLCINYTNEKL 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  545 QYYFTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISKK--PTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYF 621
Cdd:cd14932    390 QQLFNHTMFILEQEEYQREGIEWSFIDFgLDLQPCIELIEKPngPPGILALLDEECWFPKATDKSFVEKVVQEQGNNPKF 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  622 LGTPVL--EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrWavlraairamavlR 699
Cdd:cd14932    470 QKPKKLkdDADFCIIHYAGKVDYKANEWLMKNMDPLNENVATLLNQSTDKFVSEL----------W-------------K 526
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  700 EAGRLRAerAEKAAGisspatrshMEELPRGASTPSEKLYRCTGldfsferseeldvnafedimafyesrndlhnqiiks 779
Cdd:cd14932    527 DVDRIVG--LDKVAG---------MGESLHGAFKTRKGMFRTVG------------------------------------ 559
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  780 lkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllHLHKKKkppsisa 859
Cdd:cd14932    560 -------------------------------------------------------------------QLYKEQ------- 565
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  860 qfqtsLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL---- 935
Cdd:cd14932    566 -----LMNLMTTLRNTNPNFVRCIIPNHEKKAGKLAHHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpna 640
                          810       820       830
                   ....*....|....*....|....*....|....*.
gi 1720426625  936 LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14932    641 IPKGFMDGKQACVLMVKALELDPNLYRIGQSKVFFR 676
MYSc_Myh3 cd14913
class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle ...
162-971 1.01e-117

class II myosin heavy chain 3, motor domain; Myosin motor domain of fetal skeletal muscle myosin heavy chain 3 (MYHC-EMB, MYHSE1, HEMHC, SMHCE) in tetrapods including mammals, lizards, and frogs. This gene is a member of the MYH family and encodes a protein with an IQ domain and a myosin head-like domain. Mutations in this gene have been associated with two congenital contracture (arthrogryposis) syndromes, Freeman-Sheldon syndrome and Sheldon-Hall syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276878 [Multi-domain]  Cd Length: 668  Bit Score: 389.41  E-value: 1.01e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14913      3 VLYNLKDRYTSWMIYTYSGLFCVTVNPYKWLPVYNPEVVEGYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALSQKGYASG---------VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14913     83 GAGKTVNTKRVIQYFATIAATGDLAKkkdskmkgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNL---NIEDGEDLKhdfeRLQQA 387
Cdd:cd14913    163 ADIETYLLEKSRVTFQLKAERSYHIFYQILSN-KKPELIELLLitTNPYDYPFISQGEIlvaSIDDAEELL----ATDSA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  388 MEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLIL 467
Cdd:cd14913    238 IDILGFTPEEKSGLYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKTAYLMGLNSSDLLKALCFPRVKVGNEYVTK 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  468 PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYY 547
Cdd:cd14913    316 GQTVDQVHHAVNALSKSVYEKLFLWMVTRINQQLDTKLPRQHF-----IGVLDIAGFEIFEYNSLEQLCINFTNEKLQQF 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  548 FTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH--EDNKYFLGT 624
Cdd:cd14913    391 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKSNNFQKPK 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  625 PV---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSdssyvrqligmdpvavfrwavlraairamavlreA 701
Cdd:cd14913    470 VVkgrAEAHFSLIHYAGTVDYSVSGWLEKNKDPLNETVVGLYQKS----------------------------------S 515
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  702 GRLRAERAEKAAGISSPATrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslk 781
Cdd:cd14913    516 NRLLAHLYATFATADADSG------------------------------------------------------------- 534
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  782 glpwqgedprrllqslslfqkprtsflKSKGIKQKqiipknlldSKSLRliismtlhdrttksllhlhkkkkppSISAQF 861
Cdd:cd14913    535 ---------------------------KKKVAKKK---------GSSFQ-------------------------TVSALF 553
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  862 QTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQ 941
Cdd:cd14913    554 RENLNKLMSNLRTTHPHFVRCIIPNETKTPGAMEHSLVLHQLRCNGVLEGIRICRKGFPNRILYGDFKQRYRVLNASAIP 633
                          810       820       830
                   ....*....|....*....|....*....|....*
gi 1720426625  942 P-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14913    634 EgqfidSKKACEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo17 cd14879
class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase ...
157-666 4.18e-116

class XVII myosin, motor domain; This fungal myosin which is also known as chitin synthase uses its motor domain to tether its vesicular cargo to peripheral actin. It works in opposition to dynein, contributing to the retention of Mcs1 vesicles at the site of cell growth and increasing vesicle fusion necessary for polarized growth. Class 17 myosins consist of a N-terminal myosin motor domain with Cyt-b5, chitin synthase 2, and a DEK_C domains at it C-terminus. The chitin synthase region contains several transmembrane domains by which myosin 17 is thought to bind secretory vesicles. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276845 [Multi-domain]  Cd Length: 647  Bit Score: 384.21  E-value: 4.18e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  157 LTEANLLQNLKLRFMQQKIYTYAGS-ILVAINPFKFLPIYNPKYVKMYEN-------QQLGKLEPHVFALADVAYYAMLR 228
Cdd:cd14879      1 PSDDAITSHLASRFRSDLPYTRLGSsALVAVNPYKYLSSNSDASLGEYGSeyydttsGSKEPLPPHAYDLAARAYLRMRR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  229 KHVNQCIVISGESGSGKT----QSTNFLIHcLTALSQKGYASGVErtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNY 304
Cdd:cd14879     81 RSEDQAVVFLGETGSGKSesrrLLLRQLLR-LSSHSKKGTKLSSQ--ISAAEFVLDSFGNAKTLTNPNASRFGRYTELQF 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  305 LENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYL---NQHNLNIEDGEDLKHDF 381
Cdd:cd14879    158 NERGRLIGAKVLDYRLERSRVASVPTGERNFHVFYYLLAGASPEERQHLGLDDPSDYALLasyGCHPLPLGPGSDDAEGF 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  382 ERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKrKTVTV 461
Cdd:cd14879    238 QELKTALKTLGFKRKHVAQICQLLAAILHLGNLEFTYDHEGGEESAVVKNTDVLDIVAAFLGVSPEDLETSLTY-KTKLV 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  462 NdklilpyslSEAITA----------RDSMAKSLYSALFDWIVLRINHALLNKkdmEEAVScLSIGVLDIFGFEDF---E 528
Cdd:cd14879    317 R---------KELCTVfldpegaaaqRDELARTLYSLLFAWVVETINQKLCAP---EDDFA-TFISLLDFPGFQNRsstG 383
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  529 RNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEE-SNFPHATSHTL 607
Cdd:cd14879    384 GNSLDQFCVNFANERLHNYVLRSFFERKAEELEAEGVSVPATSYFDNSDCVRLLRGKPGGLLGILDDQtRRMPKKTDEQM 463
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426625  608 LAKFKQQHEDNKYF-----LGTPVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGS 666
Cdd:cd14879    464 LEALRKRFGNHSSFiavgnFATRSGSASFTVNHYAGEVTYSVEGFLERNGDVLSPDFVNLLRGA 527
MYSc_Myh7b cd14927
class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta ...
160-971 5.05e-116

class II myosin heavy chain 7b, motor domain; Myosin motor domain of cardiac muscle, beta myosin heavy chain 7b (also called KIAA1512, dJ756N5.1, MYH14, MHC14). MYH7B is a slow-twitch myosin. Mutations in this gene result in one form of autosomal dominant hearing impairment. Multiple transcript variants encoding different isoforms have been found for this gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276953 [Multi-domain]  Cd Length: 676  Bit Score: 384.69  E-value: 5.05e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14927      1 ASVLHNLRRRYSRWMIYTYSGLFCVTVNPYKWLPVYTAPVVAAYKGKRRSEAPPHIYAIADNAYNDMLRNRENQSMLITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLTALSQKGYASG-------------VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE 306
Cdd:cd14927     81 ESGAGKTVNTKRVIQYFAIVAALGDGPGkkaqflatktggtLEDQIIEANPAMEAFGNAKTLRNDNSSRFGKFIRIHFGP 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  307 NGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEE-ERLEFQLKQPQDYFYLNQHNL---NIEDGEDLKhdfe 382
Cdd:cd14927    161 TGKLASADIDIYLLEKSRVIFQQPGERSYHIYYQILSGKKPElQDMLLVSMNPYDYHFCSQGVTtvdNMDDGEELM---- 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  383 RLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVN 462
Cdd:cd14927    237 ATDHAMDILGFSPDEKYGCYKIVGAIMHFGNMKFKQKQ--REEQAEADGTESADKAAYLMGVSSADLLKGLLHPRVKVGN 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  463 DKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANE 542
Cdd:cd14927    315 EYVTKGQSVEQVVYAVGALAKATYDRMFKWLVSRINQTLDTKLPRQ-----FFIGVLDIAGFEIFEFNSFEQLCINFTNE 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  543 QLQYYFTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYF 621
Cdd:cd14927    390 KLQQFFNHHMFILEQEEYKREGIEWVFIDFgLDLQACIDLI-EKPLGILSILEEECMFPKASDASFKAKLYDNHLGKSPN 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  622 LGTPVL------EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSsyvrqligmdpvavfrwavlraaiRAM 695
Cdd:cd14927    469 FQKPRPdkkrkyEAHFEVVHYAGVVPYNIVGWLDKNKDPLNETVVAIFQKSQN------------------------KLL 524
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  696 AVLREagrlraeraekaagisspatrshmeelprgastpseklyrctgldfSFERSEELDvnafedimafyesrndlhnq 775
Cdd:cd14927    525 ATLYE----------------------------------------------NYVGSDSTE-------------------- 538
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  776 iikslkglpwqgeDPRrllqslslfqkprtsflksKGIKqkqiipknlldskslrliismtlhdrttksllhlHKKKKpp 855
Cdd:cd14927    539 -------------DPK-------------------SGVK----------------------------------EKRKK-- 550
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  856 siSAQFQT-------SLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDF 928
Cdd:cd14927    551 --AASFQTvsqlhkeNLNKLMTNLRATQPHFVRCIIPNETKTPGVMDPFLVLHQLRCNGVLEGIRICRKGFPNRILYADF 628
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*...
gi 1720426625  929 TEQFQVLLPKDVQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14927    629 KQRYRILNPSAIPDdkfvdSRKATEKLLGSLDIDHTQYQFGHTKVFFK 676
MYSc_Myh16 cd14934
class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 ...
160-971 6.28e-116

class II myosin heavy chain 16, motor domain; Myosin motor domain of myosin heavy chain 16 pseudogene (also called MHC20, MYH16, and myh5), encoding a sarcomeric myosin heavy chain expressed in nonhuman primate masticatory muscles, is inactivated in humans. This cd contains Myh16 in mammals. MYH16 has intermediate fibres between that of slow type 1 and fast 2B fibres, but exert more force than any other fibre type examined. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276896 [Multi-domain]  Cd Length: 659  Bit Score: 383.99  E-value: 6.28e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14934      1 ASVLDNLRQRYTNMRIYTYSGLFCVTVNPYKWLPIYGARVANMYKGKKRTEMPPHLFSISDNAYHDMLMDRENQSMLITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLTALSQKGYAS-----GVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAV 314
Cdd:cd14934     81 ESGAGKTENTKKVIQYFANIGGTGKQSsdgkgSLEDQIIQANPVLEAFGNAKTTRNNNSSRFGKFIRIHFGTTGKLAGAD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  315 VEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEE--ERLeFQLKQPQDYFYLNQHNL---NIEDGEDLkhdfERLQQAME 389
Cdd:cd14934    161 IESYLLEKSRVISQQAAERGYHIFYQILSNKKPEliESL-LLVPNPKEYHWVSQGVTvvdNMDDGEEL----QITDVAFD 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  390 MVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPY 469
Cdd:cd14934    236 VLGFSAEEKIGVYKLTGGIMHFGNMKFKQKP--REEQAEVDTTEVADKVAHLMGLNSGELQKGITRPRVKVGNEFVQKGQ 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  470 SLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFT 549
Cdd:cd14934    314 NMEQCNNSIGALGKAVYDKMFKWLVVRINKTLDTKMQRQ-----FFIGVLDIAGFEIFEFNSFEQLCINFTNEKLQQFFN 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  550 QHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATShtllAKFKQQHEDNKYFLGTPVLE 628
Cdd:cd14934    389 HHMFVLEQEEYKREGIEWVFIDFgLDLQACIDLL-EKPMGIFSILEEQCVFPKATD----ATFKAALYDNHLGKSSNFLK 463
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  629 PA----------FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVL 698
Cdd:cd14934    464 PKggkgkgpeahFELVHYAGTVGYNITGWLEKNKDPLNETVVGLFQ------------------------KSSLGLLALL 519
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  699 REAgrlraeraekaagisspatrshmEELPRGASTpseklyrctgldfsferseeldvnafedimafyesrndlhnqiik 778
Cdd:cd14934    520 FKE-----------------------EEAPAGSKK--------------------------------------------- 531
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  779 slkglpwqgedprrllqslslfQKPRTSFLkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSIS 858
Cdd:cd14934    532 ----------------------QKRGSSFM-----------------------------------------------TVS 542
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  859 AQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL--- 935
Cdd:cd14934    543 NFYREQLNKLMTTLHSTAPHFVRCIVPNEFKQSGVVDAHLIMHQLACNGVLEGIRICRKGFPNRLQYPEFKQRYQVLnpn 622
                          810       820       830
                   ....*....|....*....|....*....|....*..
gi 1720426625  936 -LPKDVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14934    623 vIPQGFVDNKKASELLLGSIDLDVNEYKIGHTKVFFR 659
MYSc_Myh9 cd14919
class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy ...
160-971 3.99e-114

class II myosin heavy chain 9, motor domain; Myosin motor domain of non-muscle myosin heavy chain 9 (also called NMMHCA, NMHC-II-A, MHA, FTNS, EPSTS, and DFNA17). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. The encoded protein is a myosin IIA heavy chain that contains an IQ domain and a myosin head-like domain which is involved in several important functions, including cytokinesis, cell motility and maintenance of cell shape. Defects in this gene have been associated with non-syndromic sensorineural deafness autosomal dominant type 17, Epstein syndrome, Alport syndrome with macrothrombocytopenia, Sebastian syndrome, Fechtner syndrome and macrothrombocytopenia with progressive sensorineural deafness. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276883 [Multi-domain]  Cd Length: 670  Bit Score: 379.05  E-value: 3.99e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14919      1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQST----NFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVV 315
Cdd:cd14919     81 ESGAGKTENTkkviQYLAHVASSHKSKKDQGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNGYIVGANI 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  316 EKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEMVGFLP 395
Cdd:cd14919    161 ETYLLEKSRAIRQAKEERTFHIFYYLLSGAGEHLKTDLLLEPYNKYRFLSNGHVTIPGQQD-KDMFQETMEAMRIMGIPE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  396 ATKKQIFSVLSAILYLGNVTYKKRatgRDEGLEVGPPEV-LDTLSQLLKVKRETLVE-VLTKRKTVTvNDKLILPYSLSE 473
Cdd:cd14919    240 EEQMGLLRVISGVLQLGNIVFKKE---RNTDQASMPDNTaAQKVSHLLGINVTDFTRgILTPRIKVG-RDYVQKAQTKEQ 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  474 AITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIF 553
Cdd:cd14919    316 ADFAIEALAKATYERMFRWLVLRINKALDKTKRQGASF----IGILDIAGFEIFDLNSFEQLCINYTNEKLQQLFNHTMF 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  554 KLEQEEYQGEGISWHNIDY-TDNVGCIHLISKK--PTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPA 630
Cdd:cd14919    392 ILEQEEYQREGIEWNFIDFgLDLQPCIDLIEKPagPPGILALLDEECWFPKATDKSFVEKVVQEQGTHPKFQKPKQLKDK 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  631 --FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrWavlraairamavlREAGRLRAer 708
Cdd:cd14919    472 adFCIIHYAGKVDYKADEWLMKNMDPLNDNIATLLHQSSDKFVSEL----------W-------------KDVDRIIG-- 526
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  709 AEKAAGISSPAtrshmeeLPrGASTPSEKLYRCTGldfsferseeldvnafedimafyesrndlhnqiikslkglpwqge 788
Cdd:cd14919    527 LDQVAGMSETA-------LP-GAFKTRKGMFRTVG--------------------------------------------- 553
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  789 dprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllHLHKKKkppsisaqfqtsLNKL 868
Cdd:cd14919    554 ----------------------------------------------------------QLYKEQ------------LAKL 563
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  869 LEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDVQPCR 944
Cdd:cd14919    564 MATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRVVFQEFRQRYEILtpnsIPKGFMDGK 643
                          810       820
                   ....*....|....*....|....*..
gi 1720426625  945 EAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14919    644 QACVLMIKALELDSNLYRIGQSKVFFR 670
RhoGAP_myosin_IX cd04377
RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1700-1885 2.75e-112

RhoGAP_myosin_IX: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in class IX myosins. Class IX myosins contain a characteristic head domain, a neck domain, a tail domain which contains a C6H2-zinc binding motif and a RhoGAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239842  Cd Length: 186  Bit Score: 354.44  E-value: 2.75e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1779
Cdd:cd04377      1 FGVSLSSLTSEDRSVPLVLEKLLEHIEMHGLYTEGIYRKSGSANKIKELRQGLDTDPDSVNLEDYPIHVITSVLKQWLRE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1780 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1859
Cdd:cd04377     81 LPEPLMTFELYENFLRAMELEEKQERVRALYSVLEQLPRANLNTLERLIFHLVRVALQEEVNRMSANALAIVFAPCILRC 160
                          170       180
                   ....*....|....*....|....*.
gi 1720426625 1860 PDNSDPLTSMKDVLKITTCVEMLIKE 1885
Cdd:cd04377    161 PDTADPLQSLQDVSKTTTCVETLIKE 186
MYSc_Myh1_insects_crustaceans cd14909
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
160-971 4.75e-112

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in insects and crustaceans. Myh1 is a type I skeletal muscle myosin that in Humans is encoded by the MYH1 gene. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276874  Cd Length: 666  Bit Score: 373.02  E-value: 4.75e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14909      1 ASVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLTAL--SQKGYASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14909     81 ESGAGKTENTKKVIAYFATVgaSKKTDEAAkskgsLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLG-VSEEERLEFQLKQPQDYFYLNQHNL---NIEDGEdlkhDFERLQQAM 388
Cdd:cd14909    161 ADIETYLLEKARVISQQSLERSYHIFYQIMSGsVPGVKEMCLLSDNIYDYYIVSQGKVtvpNVDDGE----EFSLTDQAF 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRatGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILP 468
Cdd:cd14909    237 DILGFTKQEKEDVYRITAAVMHMGGMKFKQR--GREEQAEQDGEEEGGRVSKLFGCDTAELYKNLLKPRIKVGNEFVTQG 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14909    315 RNVQQVTNSIGALCKGVFDRLFKWLVKKCNETLDTQQKRQHF-----IGVLDIAGFEIFEYNGFEQLCINFTNEKLQQFF 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHednkyfLG--TP 625
Cdd:cd14909    390 NHHMFVLEQEEYKREGIDWAFIDFgMDLLACIDLI-EKPMGILSILEEESMFPKATDQTFSEKLTNTH------LGksAP 462
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  626 VLEPA----------FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPvavfrwavlraairam 695
Cdd:cd14909    463 FQKPKppkpgqqaahFAIAHYAGCVSYNITGWLEKNKDPLNDTVVDQFKKSQNKLLIEIFADHA---------------- 526
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  696 AVLREAGRLRAERAEKAAGISspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnq 775
Cdd:cd14909    527 GQSGGGEQAKGGRGKKGGGFA----------------------------------------------------------- 547
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  776 iikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkpp 855
Cdd:cd14909        --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  856 SISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL 935
Cdd:cd14909    548 TVSSAYKEQLNSLMTTLRSTQPHFVRCIIPNEMKQPGVVDAHLVMHQLTCNGVLEGIRICRKGFPNRMMYPDFKMRYKIL 627
                          810       820       830
                   ....*....|....*....|....*....|....*....
gi 1720426625  936 LPKDVQP---CREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14909    628 NPAGIQGeedPKKAAEIILESIALDPDQYRLGHTKVFFR 666
MYSc_Myh11 cd14921
class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin ...
160-971 9.04e-112

class II myosin heavy chain 11, motor domain; Myosin motor domain of smooth muscle myosin heavy chain 11 (also called SMMHC, SMHC). The gene product is a subunit of a hexameric protein that consists of two heavy chain subunits and two pairs of non-identical light chain subunits. It functions as a major contractile protein, converting chemical energy into mechanical energy through the hydrolysis of ATP. The gene encoding a human ortholog of rat NUDE1 is transcribed from the reverse strand of this gene, and its 3' end overlaps with that of the latter. Inversion of the MYH11 locus is one of the most frequent chromosomal aberrations found in acute myeloid leukemia. Alternative splicing generates isoforms that are differentially expressed, with ratios changing during muscle cell maturation. Mutations in MYH11 have been described in individuals with thoracic aortic aneurysms leading to acute aortic dissections with patent ductus arteriosus. MYH11 mutations are also thought to contribute to human colorectal cancer and are also associated with Peutz-Jeghers syndrome. The mutations found in human intestinal neoplasia result in unregulated proteins with constitutive motor activity, similar to the mutant myh11 zebrafish. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276885 [Multi-domain]  Cd Length: 673  Bit Score: 372.43  E-value: 9.04e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14921      1 ASVLHNLRERYFSGLIYTYSGLFCVVVNPYKHLPIYSEKIVDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLT--ALSQKGYASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14921     81 ESGAGKTENTKKVIQYLAvvASSHKGKKDTsitgeLEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEMVG 392
Cdd:cd14921    161 ANIETYLLEKSRAIRQARDERTFHIFYYLIAGAKEKMRSDLLLEGFNNYTFLSNGFVPIPAAQD-DEMFQETLEAMSIMG 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  393 FLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLevgpPEvlDTLSQ----LLKVKRETLVE-VLTKRKTVTvNDKLIL 467
Cdd:cd14921    240 FSEEEQLSILKVVSSVLQLGNIVFKKERNTDQASM----PD--NTAAQkvchLMGINVTDFTRsILTPRIKVG-RDVVQK 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  468 PYSLSEAITARDSMAKSLYSALFDWIVLRINHALlnKKDMEEAVSCLsiGVLDIFGFEDFERNSFEQFCINYANEQLQYY 547
Cdd:cd14921    313 AQTKEQADFAIEALAKATYERLFRWILTRVNKAL--DKTHRQGASFL--GILDIAGFEIFEVNSFEQLCINYTNEKLQQL 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  548 FTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISK--KPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGT 624
Cdd:cd14921    389 FNHTMFILEQEEYQREGIEWNFIDFgLDLQPCIELIERpnNPPGVLALLDEECWFPKATDKSFVEKLCTEQGNHPKFQKP 468
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  625 PVL--EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrWavlraairamavlreag 702
Cdd:cd14921    469 KQLkdKTEFSIIHYAGKVDYNASAWLTKNMDPLNDNVTSLLNASSDKFVADL----------W----------------- 521
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  703 rlraeraekaagisspatrshmeelprgastpsEKLYRCTGLDFSFERSEeldvnafedimafyesrndlhnqiikslkg 782
Cdd:cd14921    522 ---------------------------------KDVDRIVGLDQMAKMTE------------------------------ 538
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  783 lpwqgedprrllQSLSLFQKPRTSFLKSKGikqkqiipknlldskslrliismtlhdrttksllHLHKKKkppsisaqfq 862
Cdd:cd14921    539 ------------SSLPSASKTKKGMFRTVG----------------------------------QLYKEQ---------- 562
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  863 tsLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPK 938
Cdd:cd14921    563 --LGKLMTTLRNTTPNFVRCIIPNHEKRSGKLDAFLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILaanaIPK 640
                          810       820       830
                   ....*....|....*....|....*....|...
gi 1720426625  939 DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14921    641 GFMDGKQACILMIKALELDPNLYRIGQSKIFFR 673
MYSc_Myo45 cd14906
class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds ...
160-970 1.58e-111

class XLV myosin, motor domain; The class XLVI myosins are comprised of slime molds Dictyostelium and Polysphondylium. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276871 [Multi-domain]  Cd Length: 715  Bit Score: 373.16  E-value: 1.58e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQQLGKLE-PHVFALADVAYYAMLRKHVNQCIVI 237
Cdd:cd14906      1 AIILNNLGKRYKSDSIYTYIGNVLISINPYKDISsIYSNLILNEYKDINQNKSPiPHIYAVALRAYQSMVSEKKNQSIII 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  238 SGESGSGKTQSTNFLIHCLTALSQKGYASG---------VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE-N 307
Cdd:cd14906     81 SGESGSGKTEASKTILQYLINTSSSNQQQNnnnnnnnnsIEKDILTSNPILEAFGNSRTTKNHNSSRFGKFLKIEFRSsD 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  308 GIVRGAVVEKYLLEKSRlVSQEKDERN--YHVFYYLLLGVSEEERLEFQLKQ-PQDYFYLNQH--------------NLN 370
Cdd:cd14906    161 GKIDGASIETYLLEKSR-ISHRPDNINlsYHIFYYLVYGASKDERSKWGLNNdPSKYRYLDARddvissfksqssnkNSN 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  371 IEDGEDLKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGrDEGLEVGPP--EVLDTLSQLLKVKRET 448
Cdd:cd14906    240 HNNKTESIESFQLLKQSMESMSINKEQCDAIFLSLAAILHLGNIEFEEDSDF-SKYAYQKDKvtASLESVSKLLGYIESV 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  449 LVEVLTKRKTVTVNDKLIL--PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLN---KKDMEEAVS---CLSIGVLD 520
Cdd:cd14906    319 FKQALLNRNLKAGGRGSVYcrPMEVAQSEQTRDALSKSLYVRLFKYIVEKINRKFNQntqSNDLAGGSNkknNLFIGVLD 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  521 IFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFP 600
Cdd:cd14906    399 IFGFENLSSNSLEQLLINFTNEKLQQQFNLNVFENEQKEYLSEGIPWSNSNFIDNKECIELIEKKSDGILSLLDDECIMP 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  601 HATSHTLLAKFKQQ-HEDNKYFLGTpVLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdp 679
Cdd:cd14906    479 KGSEQSLLEKYNKQyHNTNQYYQRT-LAKGTLGIKHFAGDVTYQTDGWLEKNRDSLYSDVEDLLLASS------------ 545
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  680 vavfrwavlraairamavlreagrlraeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnaf 759
Cdd:cd14906        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  760 edimafyesrndlhNQIIKSlkglpwqgedprrlLQSLSLFQKPRTSflkskgikqkqiipknlldskslrliismtlhD 839
Cdd:cd14906    546 --------------NFLKKS--------------LFQQQITSTTNTT--------------------------------K 565
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  840 RTTKSLlhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGY 919
Cdd:cd14906    566 KQTQSN----------TVSGQFLEQLNQLIQTINSTSVHYIRCIKPNQTMDCNNFNNVHVLSQLRNVGVLNTIKVRKMGY 635
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720426625  920 SAKYTFQDFTEQFQVLL----------PKD-VQPCREAIAALLEKLQV-----------------DRQNYQIGKTKVFL 970
Cdd:cd14906    636 SYRRDFNQFFSRYKCIVdmynrknnnnPKLaSQLILQNIQSKLKTMGIsnnkkknnsnsnsnttnDKPLFQIGKTKIFI 714
MYSc_Myo47 cd14908
class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not ...
160-712 2.07e-111

class XLVII myosin, motor domain; The class XLVII myosins are comprised of Stramenopiles. Not much is known about this myosin class. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276873 [Multi-domain]  Cd Length: 682  Bit Score: 371.55  E-value: 2.07e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQL---------GKLEPHVFALADVAYYAMLRK- 229
Cdd:cd14908      1 PAILHSLSRRFFRGIIYTWTGPVLIAVNPFQRLPLYGKEILESYRQEGLlrsqgiespQALGPHVFAIADRSYRQMMSEi 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  230 HVNQCIVISGESGSGKTQSTNFLIHCLTAL-----------SQKGYASGVERtILGAGPVLEAFGNAKTAHNNNSSRFGK 298
Cdd:cd14908     81 RASQSILISGESGAGKTESTKIVMLYLTTLgngeegapnegEELGKLSIMDR-VLQSNPILEAFGNARTLRNDNSSRFGK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  299 FIQVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQ--------PQDYFYLNQ---- 366
Cdd:cd14908    160 FIELGFNRAGNLLGAKVQTYLLEKVRLPFHASGERNYHIFYQLLRGGDEEEHEKYEFHDgitgglqlPNEFHYTGQggap 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  367 HNLNIEDgEDlkhDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYK-KRATGRDEGLEVGPPEVLDTLSQLLKVK 445
Cdd:cd14908    240 DLREFTD-ED---GLVYTLKAMRTMGWEESSIDTILDIIAGLLHLGQLEFEsKEEDGAAEIAEEGNEKCLARVAKLLGVD 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  446 RETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVSClsiGVLDIFGFE 525
Cdd:cd14908    316 VDKLLRALTSKIIVVRGKEITTKLTPHKAYDARDALAKTIYGALFLWVVATVNSSINWENDKDIRSSV---GVLDIFGFE 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  526 DFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEE--------- 596
Cdd:cd14908    393 CFAHNSFEQLCINFTNEALQQQFNQFIFKLEQKEYEKESIEWAFIEFPDNQDCLDTIQAKKKGILTMLDDEcrlgirgsd 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  597 SNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPA--FIIQHFAGRVKYQIKD-FREKNMDYMR----------------- 656
Cdd:cd14908    473 ANYASRLYETYLPEKNQTHSENTRFEATSIQKTKliFAVRHFAGQVQYTVETtFCEKNKDEIPltadslfesgqqfkaql 552
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720426625  657 PDIVALLRGSDSSYVRQLIGMD---PVAVFRwavlraaIRAMAVLREAGRLRAERAEKA 712
Cdd:cd14908    553 HSLIEMIEDTDPHYIRCIKPNDaakPDLVTR-------KRVTEQLRYGGVLEAVRVARS 604
MYSc_Myh19 cd15896
class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain ...
160-971 4.29e-110

class II myosin heavy chain19, motor domain; Myosin motor domain of muscle myosin heavy chain 19. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276899 [Multi-domain]  Cd Length: 675  Bit Score: 367.85  E-value: 4.29e-110
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd15896      1 ASVLHNLKERYYSGLIYTYSGLFCVVINPYKNLPIYSEEIVEMYKGKKRHEMPPHIYAITDTAYRSMMQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLTALSQK-----------GYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENG 308
Cdd:cd15896     81 ESGAGKTENTKKVIQYLAHVASShktkkdqnslaLSHGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVNG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  309 IVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd15896    161 YIVGANIETYLLEKSRAIRQAKEERTFHIFYYLLTGAGDKLRSELLLENYNNYRFLSNGNVTIPGQQD-KDLFTETMEAF 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILP 468
Cdd:cd15896    240 RIMGIPEDEQIGMLKVVASVLQLGNMSFKKER--HTDQASMPDNTAAQKVCHLMGMNVTDFTRAILSPRIKVGRDYVQKA 317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd15896    318 QTQEQAEFAVEALAKATYERMFRWLVMRINKALDKTKRQGASF----IGILDIAGFEIFELNSFEQLCINYTNEKLQQLF 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISK--KPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTP 625
Cdd:cd15896    394 NHTMFILEQEEYQREGIEWSFIDFgLDLQPCIDLIEKpaSPPGILALLDEECWFPKATDKSFVEKVLQEQGTHPKFFKPK 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  626 VL--EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLigmdpvavfrWavlraairamavlREAGR 703
Cdd:cd15896    474 KLkdEADFCIIHYAGKVDYKADEWLMKNMDPLNDNVATLLNQSTDKFVSEL----------W-------------KDVDR 530
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  704 LRAerAEKAAGisspatrshMEELPrGASTPSEKLYRCTGldfsferseeldvnafedimafyesrndlhnqiikslkgl 783
Cdd:cd15896    531 IVG--LDKVSG---------MSEMP-GAFKTRKGMFRTVG---------------------------------------- 558
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  784 pwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllHLHKKKkppsisaqfqt 863
Cdd:cd15896    559 ---------------------------------------------------------------QLYKEQ----------- 564
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  864 sLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKD 939
Cdd:cd15896    565 -LSKLMATLRNTNPNFVRCIIPNHEKKAGKLDPHLVLDQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILtpnaIPKG 643
                          810       820       830
                   ....*....|....*....|....*....|..
gi 1720426625  940 VQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd15896    644 FMDGKQACVLMIKSLELDPNLYRIGQSKVFFR 675
MYSc_Myo19 cd14880
class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor ...
160-970 2.80e-108

class XIX myosin, motor domain; Monomeric myosin-XIX (Myo19) functions as an actin-based motor for mitochondrial movement in vertebrate cells. It contains a variable number of IQ domains. Human myo19 contains a motor domain, three IQ motifs, and a short tail. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276846 [Multi-domain]  Cd Length: 658  Bit Score: 361.86  E-value: 2.80e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYENQ-QLGKLEPHVFALADVAYYAM--LRKHVNQCI 235
Cdd:cd14880      1 ETVLRCLQARYTADTFYTNAGCTLVALNPFKPVPqLYSPELMREYHAApQPQKLKPHIFTVGEQTYRNVksLIEPVNQSI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  236 VISGESGSGKTQSTNFLIH-------CLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENG 308
Cdd:cd14880     81 VVSGESGAGKTWTSRCLMKfyavvaaSPTSWESHKIAERIEQRILNSNPVMEAFGNACTLRNNNSSRFGKFIQLQLNRAQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  309 IVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEdgEDlkhDFERLQQAM 388
Cdd:cd14880    161 QMTGAAVQTYLLEKTRVACQAPSERNFHIFYQICKGASADERLQWHLPEGAAFSWLPNPERNLE--ED---CFEVTREAM 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKkratgrDEGLEVGPPEVLD-------TLSQLLKVKRETLVEVLTKRkTVTV 461
Cdd:cd14880    236 LHLGIDTPTQNNIFKVLAGLLHLGNIQFA------DSEDEAQPCQPMDdtkesvrTSALLLKLPEDHLLETLQIR-TIRA 308
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  462 NDKLIL---PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCIN 538
Cdd:cd14880    309 GKQQQVfkkPCSRAECDTRRDCLAKLIYARLFDWLVSVINSSICADTDSWTTF----IGLLDVYGFESFPENSLEQLCIN 384
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  539 YANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLakfkqQHEDN 618
Cdd:cd14880    385 YANEKLQQHFVAHYLRAQQEEYAVEGLEWSFINYQDNQTCLDLIEGSPISICSLINEECRLNRPSSAAQL-----QTRIE 459
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  619 KYFLGTPVL-------EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPvavfrwavlraa 691
Cdd:cd14880    460 SALAGNPCLghnklsrEPSFIVVHYAGPVRYHTAGLVEKNKDPVPPELTRLLQQSQDPLLQKLFPANP------------ 527
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  692 iramavlreagrlraeraekaagisspatRSHMEELPRGAStpseklyRCTGLdfsferseeldvnafedimafyesrnd 771
Cdd:cd14880    528 -----------------------------EEKTQEEPSGQS-------RAPVL--------------------------- 544
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  772 lhnqiikslkglpwqgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkk 851
Cdd:cd14880        --------------------------------------------------------------------------------
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  852 kkppSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQ 931
Cdd:cd14880    545 ----TVVSKFKASLEQLLQVLHSTTPHYIRCIKPNSQCQAQTFLQEEVLSQLEACGLVETIHISAAGFPIRVSHQNFVER 620
                          810       820       830
                   ....*....|....*....|....*....|....*....
gi 1720426625  932 FQVLLPKdvQPCREAIAALLEKLQVDRQNYQIGKTKVFL 970
Cdd:cd14880    621 YKLLRRL--RPHTSSGPHSPYPAKGLSEPVHCGRTKVFM 657
MYSc_Myh4 cd14915
class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin ...
162-971 9.46e-107

class II myosin heavy chain 4, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 4 (also called MYH2B, MyHC-2B, MyHC-IIb). Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276879 [Multi-domain]  Cd Length: 671  Bit Score: 357.89  E-value: 9.46e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14915      3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALSQKG------YASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIV 310
Cdd:cd14915     83 GAGKTVNTKRVIQYFATIAVTGekkkeeAASGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  311 RGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd14915    163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPELIEMLLitTNPYDFAFVSQGEITVPSIDD-QEELMATDSAV 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILP 468
Cdd:cd14915    241 DILGFSADEKVAIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLTSLNSADLLKALCYPRVKVGNEYVTKG 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14915    319 QTVQQVYNSVGALAKAIYEKMFLWMVTRINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH--EDNKYFLGTP 625
Cdd:cd14915    394 NHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgKSNNFQKPKP 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  626 V---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLREAG 702
Cdd:cd14915    473 AkgkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQ------------------------KSGMKTLAFLFSGG 528
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  703 rlRAERAEKAAGisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkg 782
Cdd:cd14915    529 --QTAEAEGGGG-------------------------------------------------------------------- 538
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  783 lpwqgedprrllqslslfqkprtsflkSKGIKQKqiipknlldSKSLRliismtlhdrttksllhlhkkkkppSISAQFQ 862
Cdd:cd14915    539 ---------------------------KKGGKKK---------GSSFQ-------------------------TVSALFR 557
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  863 TSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPK 938
Cdd:cd14915    558 ENLNKLMTNLRSTHPHFVRCLIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPE 637
                          810       820       830
                   ....*....|....*....|....*....|....
gi 1720426625  939 -DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14915    638 gQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh8 cd14918
class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle ...
162-971 1.11e-106

class II myosin heavy chain 8, motor domain; Myosin motor domain of perinatal skeletal muscle myosin heavy chain 8 (also called MyHC-peri, MyHC-pn). Myosin is a hexameric protein composed of a pair of myosin heavy chains (MYH) and two pairs of nonidentical light chains. A mutation in this gene results in trismus-pseudocamptodactyly syndrome. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276882 [Multi-domain]  Cd Length: 668  Bit Score: 357.51  E-value: 1.11e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14918      3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALS--------QKGYASG-VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14918     83 GAGKTVNTKRVIQYFATIAvtgekkkeESGKMQGtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKLAS 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAMEM 390
Cdd:cd14918    163 ADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPDLIEMLLitTNPYDYAFVSQGEITVPSIDD-QEELMATDSAIDI 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  391 VGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYS 470
Cdd:cd14918    241 LGFTPEEKVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKGQT 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  471 LSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQ 550
Cdd:cd14918    319 VQQVYNAVGALAKAVYEKMFLWMVTRINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFFNH 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  551 HIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVL-- 627
Cdd:cd14918    394 HMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPLGIFSILEEECMFPKATDTSFKNKLYDQHLGKSANFQKPKVvk 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  628 ---EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLreagrl 704
Cdd:cd14918    473 gkaEAHFSLIHYAGTVDYNITGWLDKNKDPLNDTVVGLYQ------------------------KSAMKTLASL------ 522
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  705 raeraekaagisspatrshmeelprgastpseklyrctgldFSFERSEELDVNAfedimafyesrndlhnqiikslkglp 784
Cdd:cd14918    523 -----------------------------------------FSTYASAEADSGA-------------------------- 535
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  785 wqgedprrllqslslfqkprtsflkSKGIKQKqiipknlldSKSLRliismtlhdrttksllhlhkkkkppSISAQFQTS 864
Cdd:cd14918    536 -------------------------KKGAKKK---------GSSFQ-------------------------TVSALFREN 556
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  865 LNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPK-D 939
Cdd:cd14918    557 LNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYGDFKQRYKVLnasaIPEgQ 636
                          810       820       830
                   ....*....|....*....|....*....|..
gi 1720426625  940 VQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14918    637 FIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 668
MYSc_Myo13 cd14875
class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain ...
160-971 3.37e-106

class XIII myosin, motor domain; These myosins have an N-terminal motor domain, a light-chain binding domain, and a C-terminal GPA/Q-rich domain. There is little known about the function of this myosin class. Two of the earliest members identified in this class are green alga Acetabularia cliftonii, Aclmyo1 and Aclmyo2. They are striking with their short tail of Aclmyo1 of 18 residues and the maximum of 7 IQ motifs in Aclmyo2. It is thought that these myosins are involved in organelle transport and tip growth. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276842 [Multi-domain]  Cd Length: 664  Bit Score: 356.04  E-value: 3.37e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQ-QKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQ-QLGKLEPHVFALADVAYYAM-LRKHVNQCIV 236
Cdd:cd14875      1 ATLLHCIKERFEKlHQQYSLMGEMVLSVNPFRLMPFNSEEERKKYLALpDPRLLPPHIWQVAHKAFNAIfVQGLGNQSVV 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  237 ISGESGSGKTQSTNFLIHCLTALS--------QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVnYLE-- 306
Cdd:cd14875     81 ISGESGSGKTENAKMLIAYLGQLSymhssntsQRSIADKIDENLKWSNPVMESFGNARTVRNDNSSRFGKYIKL-YFDpt 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  307 NGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEF-QLKQPQDYFYLNQHNLNIEDGEDLK-----HD 380
Cdd:cd14875    160 SGVMVGGQTVTYLLEKSRIIMQSPGERNYHIFYEMLAGLSPEEKKELgGLKTAQDYKCLNGGNTFVRRGVDGKtlddaHE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  381 FERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPpevLDTLSQLLKVKRETLVEV-LTKRKTV 459
Cdd:cd14875    240 FQNVRHALSMIGVELETQNSIFRVLASILHLMEVEFESDQNDKAQIADETP---FLTACRLLQLDPAKLRECfLVKSKTS 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  460 TVNdklILPySLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsCLSIGVLDIFGFEDFERNSFEQFCINY 539
Cdd:cd14875    317 LVT---ILA-NKTEAEGFRNAFCKAIYVGLFDRLVEFVNASITPQGDCSG---CKYIGLLDIFGFENFTRNSFEQLCINY 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  540 ANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHED-N 618
Cdd:cd14875    390 ANESLQNHYNKYTFINDEEECRREGIQIPKIEFPDNSECVNMFDQKRTGIFSMLDEECNFKGGTTERFTTNLWDQWANkS 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  619 KYFLGTPVLEP-AFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIGMDPvavfrwavlraairamav 697
Cdd:cd14875    470 PYFVLPKSTIPnQFGVNHYAAFVNYNTDEWLEKNTDALKEDMYECVSNSTDEFIRTLLSTEK------------------ 531
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  698 lreagrlraeraekaagisspatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqii 777
Cdd:cd14875        --------------------------------------------------------------------------------
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  778 kslkglpwqGEDPRrllqslslfqkprtsflkskgiKQkqiipknlldskslrliismtlhdrttksllhlhkkkkppSI 857
Cdd:cd14875    532 ---------GLARR----------------------KQ----------------------------------------TV 540
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  858 SAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLP 937
Cdd:cd14875    541 AIRFQRQLTDLRTELESTETQFIRCIKPNMEASPSFLDNLLVGSQLESAGVLQTIALKRQGYPVRRPIEQFCRYFYLIMP 620
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....
gi 1720426625  938 KDV------QPCREAIAALLEKLQV----DRQNYQIGKTKVFLK 971
Cdd:cd14875    621 RSTaslfkqEKYSEAAKDFLAYYQRlygwAKPNYAVGKTKVFLR 664
MYSc_Myh2_mammals cd14912
class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle ...
162-971 5.33e-106

class II myosin heavy chain 2, motor domain; Myosin motor domain of type IIa skeletal muscle myosin heavy chain 2 (also called MYH2A, MYHSA2, MyHC-IIa, MYHas8, MyHC-2A) in mammals. Mutations in this gene results in inclusion body myopathy-3 and familial congenital myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276877 [Multi-domain]  Cd Length: 673  Bit Score: 355.58  E-value: 5.33e-106
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14912      3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALSQKG------YASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIV 310
Cdd:cd14912     83 GAGKTVNTKRVIQYFATIAVTGekkkeeITSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  311 RGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd14912    163 ASADIETYLLEKSRVTFQLKAERSYHIFYQITSN-KKPELIEMLLitTNPYDYPFVSQGEISVASIDD-QEELMATDSAI 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILP 468
Cdd:cd14912    241 DILGFTNEEKVSIYKLTGAVMHYGNLKFKQKQ--REEQAEPDGTEVADKAAYLQSLNSADLLKALCYPRVKVGNEYVTKG 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14912    319 QTVEQVTNAVGALAKAVYEKMFLWMVARINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVL 627
Cdd:cd14912    394 NHHMFVLEQEEYKKEGIEWTFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHLGKSANFQKPKV 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  628 -----EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairamavlreAG 702
Cdd:cd14912    473 vkgkaEAHFSLIHYAGVVDYNITGWLDKNKDPLNETVVGLYQKSAMKTLAYLF-------------------------SG 527
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  703 RLRAErAEKAAGisspatrshmeelprGASTPSEKlyrctgldfsferseeldvnafedimafyesrndlhnqiikslKG 782
Cdd:cd14912    528 AQTAE-GASAGG---------------GAKKGGKK-------------------------------------------KG 548
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  783 LPWQgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQ 862
Cdd:cd14912    549 SSFQ---------------------------------------------------------------------TVSALFR 559
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  863 TSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPK 938
Cdd:cd14912    560 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPE 639
                          810       820       830
                   ....*....|....*....|....*....|....
gi 1720426625  939 -DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14912    640 gQFIDSKKASEKLLASIDIDHTQYKFGHTKVFFK 673
MYSc_Myh1_mammals cd14910
class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle ...
162-971 2.48e-105

class II myosin heavy chain 1, motor domain; Myosin motor domain of type IIx skeletal muscle myosin heavy chain 1 (also called MYHSA1, MYHa, MyHC-2X/D, MGC133384) in mammals. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276875 [Multi-domain]  Cd Length: 671  Bit Score: 353.65  E-value: 2.48e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14910      3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVTAYRGKKRQEAPPHIFSISDNAYQFMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALSQKG------YASG-----VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIV 310
Cdd:cd14910     83 GAGKTVNTKRVIQYFATIAVTGekkkeeATSGkmqgtLEDQIISANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGTTGKL 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  311 RGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAM 388
Cdd:cd14910    163 ASADIETYLLEKSRVTFQLKAERSYHIFYQIMSN-KKPDLIEMLLitTNPYDYAFVSQGEITVPSIDD-QEELMATDSAI 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  389 EMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILP 468
Cdd:cd14910    241 EILGFTSDERVSIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAAYLQNLNSADLLKALCYPRVKVGNEYVTKG 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  469 YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14910    319 QTVQQVYNAVGALAKAVYDKMFLWMVTRINQQLDTKQPRQ-----YFIGVLDIAGFEIFDFNSLEQLCINFTNEKLQQFF 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  549 TQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH--EDNKYFLGTP 625
Cdd:cd14910    394 NHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYEQHlgKSNNFQKPKP 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  626 V---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVLREAg 702
Cdd:cd14910    473 AkgkVEAHFSLIHYAGTVDYNIAGWLDKNKDPLNETVVGLYQ------------------------KSSMKTLALLFSG- 527
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  703 rlrAERAEKAAGisspatrshmeelprGASTPSEKlyrctgldfsferseeldvnafedimafyesrndlhnqiikslKG 782
Cdd:cd14910    528 ---AAAAEAEEG---------------GGKKGGKK-------------------------------------------KG 546
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  783 LPWQgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQFQ 862
Cdd:cd14910    547 SSFQ---------------------------------------------------------------------TVSALFR 557
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  863 TSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPK 938
Cdd:cd14910    558 ENLNKLMTNLRSTHPHFVRCIIPNETKTPGAMEHELVLHQLRCNGVLEGIRICRKGFPSRILYADFKQRYKVLnasaIPE 637
                          810       820       830
                   ....*....|....*....|....*....|....
gi 1720426625  939 -DVQPCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14910    638 gQFIDSKKASEKLLGSIDIDHTQYKFGHTKVFFK 671
MYSc_Myh7 cd14917
class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I ...
162-971 4.55e-105

class II myosin heavy chain 7, motor domain; Myosin motor domain of beta (or slow) type I cardiac muscle myosin heavy chain 7 (also called CMH1, MPD1, and CMD1S). Muscle myosin is a hexameric protein containing 2 heavy chain subunits, 2 alkali light chain subunits, and 2 regulatory light chain subunits. It is expressed predominantly in normal human ventrical and in skeletal muscle tissues rich in slow-twitch type I muscle fibers. Changes in the relative abundance of this protein and the alpha (or fast) heavy subunit of cardiac myosin correlate with the contractile velocity of cardiac muscle. Its expression is also altered during thyroid hormone depletion and hemodynamic overloading. Mutations in this gene are associated with familial hypertrophic cardiomyopathy, myosin storage myopathy, dilated cardiomyopathy, and Laing early-onset distal myopathy. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276881 [Multi-domain]  Cd Length: 668  Bit Score: 352.87  E-value: 4.55e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14917      3 VLYNLKERYASWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTAL------SQKGYASG---VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14917     83 GAGKTVNTKRVIQYFAVIaaigdrSKKDQTPGkgtLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLAS 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNL---NIEDGEDLKhdfeRLQQA 387
Cdd:cd14917    163 ADIETYLLEKSRVIFQLKAERDYHIFYQILSN-KKPELLDMLLitNNPYDYAFISQGETtvaSIDDAEELM----ATDNA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  388 MEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLIL 467
Cdd:cd14917    238 FDVLGFTSEEKNSMYKLTGAIMHFGNMKFKQKQ--REEQAEPDGTEEADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTK 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  468 PYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYY 547
Cdd:cd14917    316 GQNVQQVIYATGALAKAVYEKMFNWMVTRINATLETKQPRQ-----YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQF 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  548 FTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH-------EDNK 619
Cdd:cd14917    391 FNHHMFVLEQEEYKKEGIEWTFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKATDMTFKAKLFDNHlgksnnfQKPR 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  620 YFLGTPvlEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdpvavfrwavlraairamavLR 699
Cdd:cd14917    470 NIKGKP--EAHFSLIHYAGTVDYNIIGWLQKNKDPLNETVVGLYQKSS------------------------------LK 517
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  700 EAGRLRAERAekaagisspatrshmeelprGASTPSEKlyrctgldfsferseeldvnafedimafyesrndlhnqiiks 779
Cdd:cd14917    518 LLSNLFANYA--------------------GADAPIEK------------------------------------------ 535
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  780 LKGLPWQGedprrllqslSLFQkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISA 859
Cdd:cd14917    536 GKGKAKKG----------SSFQ------------------------------------------------------TVSA 551
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  860 QFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKD 939
Cdd:cd14917    552 LHRENLNKLMTNLRSTHPHFVRCIIPNETKSPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAA 631
                          810       820       830
                   ....*....|....*....|....*....|....*..
gi 1720426625  940 VQP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14917    632 IPEgqfidSRKGAEKLLSSLDIDHNQYKFGHTKVFFK 668
MYSc_Myh14_mammals cd14930
class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy ...
160-971 2.51e-104

class II myosin heavy chain 14 motor domain; Myosin motor domain of non-muscle myosin heavy chain 14 (also called FLJ13881, KIAA2034, MHC16, MYH17). Its members include mammals, chickens, and turtles. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. Some of the data used for this classification were produced by the CyMoBase team at the Max-Planck-Institute for Biophysical Chemistry. The sequence names are composed of the species abbreviation followed by the protein abbreviation and optional protein classifier and variant designations.


Pssm-ID: 276893 [Multi-domain]  Cd Length: 670  Bit Score: 350.55  E-value: 2.51e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14930      1 ASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLTALS-------QKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRG 312
Cdd:cd14930     81 ESGAGKTENTKKVIQYLAHVAsspkgrkEPGVPGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVAGYIVG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  313 AVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNqHNLNIEDGEDlKHDFERLQQAMEMVG 392
Cdd:cd14930    161 ANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLT-NGPSSSPGQE-RELFQETLESLRVLG 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  393 FLPATKKQIFSVLSAILYLGNVTYKKRatgRDEGLEVGPPEV-LDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSL 471
Cdd:cd14930    239 FSHEEITSMLRMVSAVLQFGNIVLKRE---RNTDQATMPDNTaAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTK 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  472 SEAITARDSMAKSLYSALFDWIVLRINHALlnkkDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQH 551
Cdd:cd14930    316 EQADFALEALAKATYERLFRWLVLRLNRAL----DRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHT 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  552 IFKLEQEEYQGEGISWHNIDY-TDNVGCIHLISK--KPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVL- 627
Cdd:cd14930    392 MFVLEQEEYQREGIPWTFLDFgLDLQPCIDLIERpaNPPGLLALLDEECWFPKATDKSFVEKVAQEQGGHPKFQRPRHLr 471
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  628 -EPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSsyvrqligmdpvavfrwavlraairamavlreagRLRA 706
Cdd:cd14930    472 dQADFSVLHYAGKVDYKANEWLMKNMDPLNDNVAALLHQSTD----------------------------------RLTA 517
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  707 ERAEKAAGISSPATRSHMEELPRGAstpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwq 786
Cdd:cd14930    518 EIWKDVEGIVGLEQVSSLGDGPPGG------------------------------------------------------- 542
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  787 gedprrllqslslfqKPRTSFLKSKGikqkqiipknlldskslrliismtlhdrttksllHLHKKkkppsisaqfqtSLN 866
Cdd:cd14930    543 ---------------RPRRGMFRTVG----------------------------------QLYKE------------SLS 561
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  867 KLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL----LPKDVQP 942
Cdd:cd14930    562 RLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILtpnaIPKGFMD 641
                          810       820
                   ....*....|....*....|....*....
gi 1720426625  943 CREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14930    642 GKQACEKMIQALELDPNLYRVGQSKIFFR 670
MYSc_Myh6 cd14916
class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac ...
162-971 1.85e-103

class II myosin heavy chain 6, motor domain; Myosin motor domain of alpha (or fast) cardiac muscle myosin heavy chain 6. Cardiac muscle myosin is a hexamer consisting of two heavy chain subunits, two light chain subunits, and two regulatory subunits. This gene encodes the alpha heavy chain subunit of cardiac myosin. Mutations in this gene cause familial hypertrophic cardiomyopathy and atrial septal defect. Class II myosins, also called conventional myosins, are the myosin type responsible for producing actomyosin contraction in metazoan muscle and non-muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276880 [Multi-domain]  Cd Length: 670  Bit Score: 348.20  E-value: 1.85e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14916      3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNAEVVAAYRGKKRSEAPPHIFSISDNAYQYMLTDRENQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALSQKGY----------ASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVR 311
Cdd:cd14916     83 GAGKTVNTKRVIQYFASIAAIGDrskkenpnanKGTLEDQIIQANPALEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  312 GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNLNIEDGEDlKHDFERLQQAME 389
Cdd:cd14916    163 SADIETYLLEKSRVIFQLKAERNYHIFYQILSN-KKPELLDMLLvtNNPYDYAFVSQGEVSVASIDD-SEELLATDSAFD 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  390 MVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPY 469
Cdd:cd14916    241 VLGFTAEEKAGVYKLTGAIMHYGNMKFKQKQ--REEQAEPDGTEDADKSAYLMGLNSADLLKGLCHPRVKVGNEYVTKGQ 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  470 SLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEeavscLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFT 549
Cdd:cd14916    319 SVQQVYYSIGALAKSVYEKMFNWMVTRINATLETKQPRQ-----YFIGVLDIAGFEIFDFNSFEQLCINFTNEKLQQFFN 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  550 QHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTP--- 625
Cdd:cd14916    394 HHMFVLEQEEYKKEGIEWEFIDFgMDLQACIDLI-EKPMGIMSILEEECMFPKASDMTFKAKLYDNHLGKSNNFQKPrnv 472
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  626 --VLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRgsdssyvrqligmdpvavfrwavlRAAIRAMAVlreagr 703
Cdd:cd14916    473 kgKQEAHFSLVHYAGTVDYNILGWLEKNKDPLNETVVGLYQ------------------------KSSLKLMAT------ 522
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  704 LRAERAEKAAGISSpatrshmeelprgastpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkgl 783
Cdd:cd14916    523 LFSTYASADTGDSG------------------------------------------------------------------ 536
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  784 pwqgedprrllqslslfqkprtsflKSKGIKQKqiipknlldSKSLRliismtlhdrttksllhlhkkkkppSISAQFQT 863
Cdd:cd14916    537 -------------------------KGKGGKKK---------GSSFQ-------------------------TVSALHRE 557
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  864 SLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQP- 942
Cdd:cd14916    558 NLNKLMTNLKTTHPHFVRCIIPNERKAPGVMDNPLVMHQLRCNGVLEGIRICRKGFPNRILYGDFRQRYRILNPAAIPEg 637
                          810       820       830
                   ....*....|....*....|....*....|...
gi 1720426625  943 ----CREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14916    638 qfidSRKGAEKLLGSLDIDHNQYKFGHTKVFFK 670
MYSc_Myo25 cd14886
class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell ...
166-971 4.41e-102

class XXV myosin, motor domain; These myosins are MyTH-FERM myosins that play a role in cell adhesion and filopodia formation. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276851  Cd Length: 650  Bit Score: 343.41  E-value: 4.41e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  166 LKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMYE--NQQLG---KLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14886      7 LRDRFAKDKIYTYAGKLLVALNPFKQIRnLYGTEVIGRYRqaDTSRGfpsDLPPHSYAVAQSALNGLISDGISQSCIVSG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIHCLtALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd14886     87 ESGAGKTETAKQLMNFF-AYGHSTSSTDVQSLILGSNPLLESFGNAKTLRNNNSSRFGKFIKLLVGPDGGLKGGKITSYM 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVgFLPATKK 399
Cdd:cd14886    166 LELSRIEFQSTNERNYHIFYQCIKGLSPEEKKSLGFKSLESYNFLNASKCYDAPGIDDQKEFAPVRSQLEKL-FSKNEID 244
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  400 QIFSVLSAILYLGNVTYKKR-ATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITAR 478
Cdd:cd14886    245 SFYKCISGILLAGNIEFSEEgDMGVINAAKISNDEDFGKMCELLGIESSKAAQAIITKVVVINNETIISPVTQAQAEVNI 324
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  479 DSMAKSLYSALFDWIVLRINHALlnkkdMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQE 558
Cdd:cd14886    325 RAVAKDLYGALFELCVDTLNEII-----QFDADARPWIGILDIYGFEFFERNTYEQLLINYANERLQQYFINQVFKSEIQ 399
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  559 EYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVlEPAFIIQHFAG 638
Cdd:cd14886    400 EYEIEGIDHSMITFTDNSNVLAVFDKPNLSIFSFLEEQCLIQTGSSEKFTSSCKSKIKNNSFIPGKGS-QCNFTIVHTAA 478
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  639 RVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQligmdpvavfrwavlraairamavlreagrlraeraekaagissp 718
Cdd:cd14886    479 TVTYNTEEFVDKNKHKLSVDILELLMGSTNPIVNK--------------------------------------------- 513
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  719 atrshmeelprgastpseklyrctgldfsferseeldvnAFEDIMAfyESRNdlhnqiiksLKGlpwqgedprrllqsls 798
Cdd:cd14886    514 ---------------------------------------AFSDIPN--EDGN---------MKG---------------- 527
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  799 lfqkprtSFLKSKgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppsisaqFQTSLNKLLEALGKAEPF 878
Cdd:cd14886    528 -------KFLGST-------------------------------------------------FQLSIDQLMKTLSATKSH 551
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  879 FIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLL---------PKDVqpcREAIAA 949
Cdd:cd14886    552 FIRCIKTNQDKVPNKYETKSVYNQLISLSIFESIQTIHRGFAYNDTFEEFFHRNKILIshnsssqnaGEDL---VEAVKS 628
                          810       820
                   ....*....|....*....|..
gi 1720426625  950 LLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14886    629 ILENLGIPCSDYRIGKTKVFLR 650
MYSc_Myh13 cd14923
class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin ...
162-971 1.23e-100

class II myosin heavy chain 13, motor domain; Myosin motor domain of skeletal muscle myosin heavy chain 13 (also called MyHC-eo) in mammals, chicken, and green anole. Myh13 is a myosin whose expression is restricted primarily to the extrinsic eye muscles which are specialized for function in eye movement. Class II myosins, also called conventional myosins, are the myosin type responsible for producing muscle contraction in muscle cells. Myosin II contains two heavy chains made up of the head (N-terminal) and tail (C-terminal) domains with a coiled-coil morphology that holds the two heavy chains together. The intermediate neck domain is the region creating the angle between the head and tail. It also contains 4 light chains which bind the heavy chains in the "neck" region between the head and tail. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. Class-II myosins are regulated by phosphorylation of the myosin light chain or by binding of Ca2+. A cyclical interaction between myosin and actin provides the driving force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276887 [Multi-domain]  Cd Length: 671  Bit Score: 340.12  E-value: 1.23e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14923      3 VLYNLKERYAAWMIYTYSGLFCVTVNPYKWLPVYNPEVVAAYRGKKRQEAPPHIFSISDNAYQFMLTDRDNQSILITGES 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLTALS---------QKGYASG-VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVR 311
Cdd:cd14923     83 GAGKTVNTKRVIQYFATIAvtgdkkkeqQPGKMQGtLEDQIIQANPLLEAFGNAKTVRNDNSSRFGKFIRIHFGATGKLA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  312 GAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGvSEEERLEFQL--KQPQDYFYLNQHNL---NIEDGEDLKhdfeRLQQ 386
Cdd:cd14923    163 SADIETYLLEKSRVTFQLSSERSYHIFYQIMSN-KKPELIDLLLisTNPFDFPFVSQGEVtvaSIDDSEELL----ATDN 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  387 AMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRAtgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLI 466
Cdd:cd14923    238 AIDILGFSSEEKVGIYKLTGAVMHYGNMKFKQKQ--REEQAEPDGTEVADKAGYLMGLNSAEMLKGLCCPRVKVGNEYVT 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  467 LPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAvsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQY 546
Cdd:cd14923    316 KGQNVQQVTNSVGALAKAVYEKMFLWMVTRINQQLDTKQPRQYF-----IGVLDIAGFEIFDFNSLEQLCINFTNEKLQQ 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  547 YFTQHIFKLEQEEYQGEGISWHNIDY-TDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQH--EDNKYFLG 623
Cdd:cd14923    391 FFNHHMFVLEQEEYKKEGIEWEFIDFgMDLAACIELI-EKPMGIFSILEEECMFPKATDTSFKNKLYDQHlgKSNNFQKP 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  624 TPV---LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDssyvrqligmdpvavfrwavlraairamavLRE 700
Cdd:cd14923    470 KPAkgkAEAHFSLVHYAGTVDYNIAGWLDKNKDPLNETVVGLYQKSS------------------------------LKL 519
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  701 AGRLRAERAEKAAGISSpatrshmeelprGASTPSEKlyrctgldfsferseeldvnafedimafyesrndlhnqiiksl 780
Cdd:cd14923    520 LSFLFSNYAGAEAGDSG------------GSKKGGKK------------------------------------------- 544
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  781 KGLPWQgedprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAQ 860
Cdd:cd14923    545 KGSSFQ---------------------------------------------------------------------TVSAV 555
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  861 FQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDV 940
Cdd:cd14923    556 FRENLNKLMTNLRSTHPHFVRCLIPNETKTPGVMDHYLVMHQLRCNGVLEGIRICRKGFPSRILYADFKQRYRILNASAI 635
                          810       820       830
                   ....*....|....*....|....*....|....*.
gi 1720426625  941 QP-----CREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14923    636 PEgqfidSKNASEKLLNSIDVDREQYRFGHTKVFFK 671
MYSc_Myo24A cd14937
class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
160-674 3.98e-95

class XXIV A myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The function of the class XXIV myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276897  Cd Length: 637  Bit Score: 322.73  E-value: 3.98e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYnpkyVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISG 239
Cdd:cd14937      1 AEVLNMLALRYKKNYIYTIAEPMLISINPYQVIDVD----INEYKNKNTNELPPHVYSYAKDAMTDFINTKTNQSIIISG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  240 ESGSGKTQSTNFLIhcltalsqKGYASGVER------TILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGA 313
Cdd:cd14937     77 ESGSGKTEASKLVI--------KYYLSGVKEdneisnTLWDSNFILEAFGNAKTLKNNNSSRYGKYIKIELDEYQNIVSS 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  314 VVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKhDFERLqqameMVGF 393
Cdd:cd14937    149 SIEIFLLENIRVVSQEEEERGYHIFYQIFNGMSQELKNKYKIRSENEYKYIVNKNVVIPEIDDAK-DFGNL-----MISF 222
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  394 ----LPATKKQIFSVLSAILYLGNVTYKKRATGRDEG---LEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLI 466
Cdd:cd14937    223 dkmnMHDMKDDLFLTLSGLLLLGNVEYQEIEKGGKTNcseLDKNNLELVNEISNLLGINYENLKDCLVFTEKTIANQKIE 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  467 LPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQY 546
Cdd:cd14937    303 IPLSVEESVSICKSISKDLYNKIFSYITKRINNFLNNNKELNN-----YIGILDIFGFEIFSKNSLEQLLINIANEEIHS 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  547 YFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKpTGLFYLLDEESNFPHATSHTLLAKFKQQHEDN-KYFLGTP 625
Cdd:cd14937    378 IYLYIVYEKETELYKAEDILIESVKYTTNESIIDLLRGK-TSIISILEDSCLGPVKNDESIVSVYTNKFSKHeKYASTKK 456
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*....
gi 1720426625  626 VLEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQL 674
Cdd:cd14937    457 DINKNFVIKHTVSDVTYTITNFISKNKDILPSNIVRLLKVSNNKLVRSL 505
MYSc_Myo26 cd14887
class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the ...
160-971 5.96e-95

class XXVI myosin, motor domain; These MyTH-FERM myosins are thought to be related to the other myosins that have a MyTH4 domain such as class III, VII, IX, X , XV, XVI, XVII, XX, XXII, XXV, and XXXIV. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276852  Cd Length: 725  Bit Score: 325.06  E-value: 5.96e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQ--------QKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHV 231
Cdd:cd14887      1 PNLLENLYQRYNKayinkenrNCIYTYTGTLLIAVNPYRFFNLYDRQWISRFDTEANSRLVPHPFGLAEFAYCRLVRDRR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  232 NQCIVISGESGSGKTQSTNFLIHCLTALS--QKGYAS-GVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENG 308
Cdd:cd14887     81 SQSILISGESGAGKTETSKHVLTYLAAVSdrRHGADSqGLEARLLQSGPVLEAFGNAHTVLNANSSRFGKMLLLHFTGRG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  309 IVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLlgVSEEERLEFQLKQPQDYFYLnqhnlniedgedlkHDFERLQQAM 388
Cdd:cd14887    161 KLTRASVATYLLANERVVRIPSDEFSFHIFYALC--NAAVAAATQKSSAGEGDPES--------------TDLRRITAAM 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  389 EMVGFLPATKKQIFSVLSAILYLGNV---------TYKKRatgRDEGLEVGPPEVLDTLSQLLKVK-------------- 445
Cdd:cd14887    225 KTVGIGGGEQADIFKLLAAILHLGNVefttdqepeTSKKR---KLTSVSVGCEETAADRSHSSEVKclssglkvteasrk 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  446 -RETLVEVLTKRKTVTVNDKLILP------------YSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVS 512
Cdd:cd14887    302 hLKTVARLLGLPPGVEGEEMLRLAlvsrsvretrsfFDLDGAAAARDAACKNLYSRAFDAVVARINAGLQRSAKPSESDS 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  513 ---------CLSIGVLDIFGFEDFE---RNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGcih 580
Cdd:cd14887    382 dedtpsttgTQTIGILDLFGFEDLRnhsKNRLEQLCINYANERLHCFLLEQLILNEHMLYTQEGVFQNQDCSAFPFS--- 458
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  581 liskkptglFYLLDEESNFPHATSHtllakfkqqhednkyFLGTPvlepafiiqhfagrvkyQIKDFREKNMDYMRPDIV 660
Cdd:cd14887    459 ---------FPLASTLTSSPSSTSP---------------FSPTP-----------------SFRSSSAFATSPSLPSSL 497
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  661 ALLRGSDSSYVRQLIGMDPVAVFRWAVLRAAIRAMAVLREAGRLRAERAEkaagisspATRSHmeelprgastpseklYR 740
Cdd:cd14887    498 SSLSSSLSSSPPVWEGRDNSDLFYEKLNKNIINSAKYKNITPALSRENLE--------FTVSH---------------FA 554
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  741 CtgldfsferseelDVnafedimaFYESRnDLHNQIIKSLKglpwqgEDPRRLLQSLSLFqkprtsflkskgikqkqiIP 820
Cdd:cd14887    555 C-------------DV--------TYDAR-DFCRANREATS------DELERLFLACSTY------------------TR 588
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  821 KNLLDSKSLRLIISmtlhdrttksllhlhkkKKPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVL 900
Cdd:cd14887    589 LVGSKKNSGVRAIS-----------------SRRSTLSAQFASQLQQVLKALQETSCHFIRCVKPNRVQEAGIFEDAYVH 651
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426625  901 QQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQ---PCREAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd14887    652 RQLRCSGMSDLLRVMADGFPCRLPYVELWRRYETKLPMALRealTPKMFCKIVLMFLEINSNSYTFGKTKIFFR 725
MYSc_Myo37 cd14898
class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much ...
162-651 2.76e-92

class XXXVII myosin, motor domain; The class XXXVIII myosins are comprised of fungi. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276863  Cd Length: 578  Bit Score: 312.60  E-value: 2.76e-92
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKflPIYNPKYVKMYENQQlGKLEPHVFALADVAYYAMLrKHVNQCIVISGES 241
Cdd:cd14898      3 TLEILEKRYASGKIYTKSGLVFLALNPYE--TIYGAGAMKAYLKNY-SHVEPHVYDVAEASVQDLL-VHGNQTIVISGES 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCLtaLSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYleNGIVRGAVVEKYLLE 321
Cdd:cd14898     79 GSGKTENAKLVIKYL--VERTASTTSIEKLITAANLILEAFGNAKTQLNDNSSRFGKRIKLKF--DGKITGAKFETYLLE 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  322 KSRLVSQEKDERNYHVFYYlllgVSEEERLEFQlkqpQDYFYLNQHNLNIEDGEDLKHDFERLQQAMEMVGFlpATKKQI 401
Cdd:cd14898    155 KSRVTHHEKGERNFHIFYQ----FCASKRLNIK----NDFIDTSSTAGNKESIVQLSEKYKMTCSAMKSLGI--ANFKSI 224
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  402 FSVLSAILYLGNVTYKkratgrDEG-LEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDS 480
Cdd:cd14898    225 EDCLLGILYLGSIQFV------NDGiLKLQRNESFTEFCKLHNIQEEDFEESLVKFSIQVKGETIEVFNTLKQARTIRNS 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  481 MAKSLYSALFDWIVLRINHALlnkkdmeEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEY 560
Cdd:cd14898    299 MARLLYSNVFNYITASINNCL-------EGSGERSISVLDIFGFEIFESNGLDQLCINWTNEKIQNDFIKKMFRAKQGMY 371
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  561 QGEGISWHNIDYTDNVGCIHLIsKKPTGLFYLLDEESNFPHATSHTLLAKFKQQhedNKYFLGTPVlEPAFIIQHFAGRV 640
Cdd:cd14898    372 KEEGIEWPDVEFFDNNQCIRDF-EKPCGLMDLISEESFNAWGNVKNLLVKIKKY---LNGFINTKA-RDKIKVSHYAGDV 446
                          490
                   ....*....|.
gi 1720426625  641 KYQIKDFREKN 651
Cdd:cd14898    447 EYDLRDFLDKN 457
MYSc_Myo38 cd14899
class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is ...
160-674 2.43e-91

class XXXVIII myosin; The class XXXVIII myosins are comprised of Stramenopiles. Not much is known about this myosin class. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276864 [Multi-domain]  Cd Length: 717  Bit Score: 314.34  E-value: 2.43e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPKYVKMY---ENQQLGK-------LEPHVFALADVAYYAMLR 228
Cdd:cd14899      1 ASILNALRLRYERHAIYTHIGDILISINPFQDLPqLYGDEILRGYaydHNSQFGDrvtstdpREPHLFAVARAAYIDIVQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  229 KHVNQCIVISGESGSGKTQSTN-----FLIHCLTALSQKGYASG-----------VERTILGAGPVLEAFGNAKTAHNNN 292
Cdd:cd14899     81 NGRSQSILISGESGAGKTEATKiimtyFAVHCGTGNNNLTNSESisppaspsrttIEEQVLQSNPILEAFGNARTVRNDN 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  293 SSRFGKFIQVNYL-ENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLG----VSEEERLEFQLKQ-PQDYFYLNQ 366
Cdd:cd14899    161 SSRFGKFIELRFRdERRRLAGARIRTYLLEKIRVIKQAPHERNFHIFYELLSAdnncVSKEQKQVLALSGgPQSFRLLNQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  367 HNLNIE-DGEDLKHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDT-------- 437
Cdd:cd14899    241 SLCSKRrDGVKDGVQFRATKRAMQQLGMSEGEIGGVLEIVAAVLHMGNVDFEQIPHKGDDTVFADEARVMSSttgafdhf 320
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  438 --LSQLLKVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHAL----------LNKK 505
Cdd:cd14899    321 tkAAELLGVSTEALDHALTKRWLHASNETLVVGVDVAHARNTRNALTMECYRLLFEWLVARVNNKLqrqasapwgaDESD 400
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  506 DMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKK 585
Cdd:cd14899    401 VDDEEDATDFIGLLDIFGFEDMAENSFEQLCINYANEALQHQFNQYIFEEEQRLYRDEGIRWSFVDFPNNRACLELFEHR 480
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  586 PTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNK---YFLGTPVLEPA--FIIQHFAGRVKYQIKDFREKNMDYMRPDIV 660
Cdd:cd14899    481 PIGIFSLTDQECVFPQGTDRALVAKYYLEFEKKNshpHFRSAPLIQRTtqFVVAHYAGCVTYTIDGFLAKNKDSFCESAA 560
                          570
                   ....*....|....
gi 1720426625  661 ALLRGSDSSYVRQL 674
Cdd:cd14899    561 QLLAGSSNPLIQAL 574
MYSc_Myo16 cd14878
class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal ...
160-971 3.00e-88

class XVI myosin, motor domain; These XVI type myosins are also known as Neuronal tyrosine-phosphorylated phosphoinositide-3-kinase adapter 3/NYAP3. Myo16 is thought to play a regulatory role in cell cycle progression and has been recently implicated in Schizophrenia. Class XVI myosins are characterized by an N-terminal ankyrin repeat domain and some with chitin synthase domains that arose independently from the ones in the class XVII fungal myosins. They bind protein phosphatase 1 catalytic subunits 1alpha/PPP1CA and 1gamma/PPP1CC. Human Myo16 interacts with ACOT9, ARHGAP26 and PIK3R2 and with components of the WAVE1 complex, CYFIP1 and NCKAP1. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276844 [Multi-domain]  Cd Length: 656  Bit Score: 303.28  E-value: 3.00e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYEN---QQLGKLEPHVFALADVAYYAMLRKHVNQCIV 236
Cdd:cd14878      1 SSLLYEIQKRFGNNQIYTFIGDILLLVNPYKELPIYSTMVSQLYLSssgQLCSSLPPHLFSCAERAFHQLFQERRPQCFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  237 ISGESGSGKTQSTNFLIHCLTAlsqkgyASGVERTILG-----AGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE-NGIV 310
Cdd:cd14878     81 LSGERGSGKTEASKQIMKHLTC------RASSSRTTFDsrfkhVNCILEAFGHAKTTLNDLSSCFIKYFELQFCErKKHL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  311 RGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLniEDGEDLKHDFER-----LQ 385
Cdd:cd14878    155 TGARIYTYMLEKSRLVSQPPGQSNFLIFYLLMDGLSAEEKYGLHLNNLCAHRYLNQTMR--EDVSTAERSLNReklavLK 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  386 QAMEMVGFLPATKKQIFSVLSAILYLGNVTYKkrATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKL 465
Cdd:cd14878    233 QALNVVGFSSLEVENLFVILSAILHLGDIRFT--ALTEADSAFVSDLQLLEQVAGMLQVSTDELASALTTDIQYFKGDMI 310
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  466 ILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKkDMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQ 545
Cdd:cd14878    311 IRRHTIQIAEFYRDLLAKSLYSRLFSFLVNTVNCCLQSQ-DEQKSMQTLDIGILDIFGFEEFQKNEFEQLCVNMTNEKMH 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  546 YYFTQHIFKLEQEEYQGEGISWHNIDYTDN-VGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHED---NKYF 621
Cdd:cd14878    390 HYINEVLFLQEQTECVQEGVTMETAYSPGNqTGVLDFFFQKPSGFLSLLDEESQMIWSVEPNLPKKLQSLLESsntNAVY 469
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  622 L------GTPVLE---PAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVallrgsdssyvrqligmdpvavfrwavlraai 692
Cdd:cd14878    470 SpmkdgnGNVALKdqgTAFTVMHYAGRVMYEIVGAIEKNKDSLSQNLL-------------------------------- 517
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  693 ramavlreagrlraeraekaagisspatrshmeelprgastpseklyrctgldFSFERSEELDVNafedimafyesrndl 772
Cdd:cd14878    518 -----------------------------------------------------FVMKTSENVVIN--------------- 529
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  773 hnqiikslkglpwqgedprrllqslSLFQkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkK 852
Cdd:cd14878    530 -------------------------HLFQ--------------------------------------------------S 534
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  853 KPPSISAQFQTSLNKLLEALGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQF 932
Cdd:cd14878    535 KLVTIASQLRKSLADIIGKLQKCTPHFIHCIKPNNSKLPDTFDNFYVSAQLQYIGVLEMVKIFRYGYPVRLSFSDFLSRY 614
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....
gi 1720426625  933 QVLLpkDVQPCREAIAALLEK-----LQVDRQNYQIGKTKVFLK 971
Cdd:cd14878    615 KPLA--DTLLGEKKKQSAEERcrlvlQQCKLQGWQMGVRKVFLK 656
MYSc_Myo12 cd14874
class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They ...
160-971 9.44e-81

class XXXIII myosin, motor domain; Little is known about the XXXIII class of myosins. They are found predominately in nematodes. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276841 [Multi-domain]  Cd Length: 628  Bit Score: 280.60  E-value: 9.44e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYenqqlgklepHVFALADVAYYAMLRKHVN-QCIVIS 238
Cdd:cd14874      1 AGIAQNLHERFKKGQTYTKASNVLVFVNDFNKLSIQDQLVIKKC----------HISGVAENALDRIKSMSSNaESIVFG 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  239 GESGSGKTQSTNFLIHCLTALSQKGYASGVERTIlgaGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKY 318
Cdd:cd14874     71 GESGSGKSYNAFQVFKYLTSQPKSKVTTKHSSAI---ESVFKSFGCAKTLKNDEATRFGCSIDLLYKRNVLTGLNLKYTV 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQHNLNIEDGEDLKHdFERLQQAMEMVGFLPATK 398
Cdd:cd14874    148 PLEVPRVISQKPGERNFNVFYEVYHGLNDEMKAKFGIKGLQKFFYINQGNSTENIQSDVNH-FKHLEDALHVLGFSDDHC 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  399 KQIFSVLSAILYLGNVTYKKRATGRDEG--LEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVndklilPYSLSEAIT 476
Cdd:cd14874    227 ISIYKIISTILHIGNIYFRTKRNPNVEQdvVEIGNMSEVKWVAFLLEVDFDQLVNFLLPKSEDGT------TIDLNAALD 300
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  477 ARDSMAKSLYSALFDWIVLRINHALlnKKDMEEAVsclsIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLE 556
Cdd:cd14874    301 NRDSFAMLIYEELFKWVLNRIGLHL--KCPLHTGV----ISILDHYGFEKYNNNGVEEFLINSVNERIENLFVKHSFHDQ 374
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  557 QEEYQGEGISwhnIDYT-----DNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPVLEP-A 630
Cdd:cd14874    375 LVDYAKDGIS---VDYKvpnsiENGKTVELLFKKPYGLLPLLTDECKFPKGSHESYLEHCNLNHTDRSSYGKARNKERlE 451
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  631 FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairamavlreagrlraerae 710
Cdd:cd14874    452 FGVRHCIGTTWYNVTDFFSRNKRIISLSAVQLLRSSKNPIIGLLF----------------------------------- 496
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  711 kaagisspatRSHmeelprgastpseklyrctgldfSFERSEELdvnafedimafyesrndlhnqiikslkglpwqgedp 790
Cdd:cd14874    497 ----------ESY-----------------------SSNTSDMI------------------------------------ 507
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  791 rrllqslslfqkprtsflkskgIKQKQIIPKNlldskslrliiSMTLHDRTTKSLLHlhkkkkppsisaqfqtslnklle 870
Cdd:cd14874    508 ----------------------VSQAQFILRG-----------AQEIADKINGSHAH----------------------- 531
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  871 algkaepfFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPC---REAI 947
Cdd:cd14874    532 --------FVRCIKSNNERQPKKFDIPLVNRQIKNLLLAELLSFRIKGYPVKISKTTFARQYRCLLPGDIAMCqneKEII 603
                          810       820
                   ....*....|....*....|....*
gi 1720426625  948 AALLEKLQVDRQN-YQIGKTKVFLK 971
Cdd:cd14874    604 QDILQGQGVKYENdFKIGTEYVFLR 628
MYSc_Myo20 cd14881
class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such ...
163-664 3.97e-79

class XX myosin, motor domain; These class 20 myosins are primarily insect myosins with such members as Drosophila, Daphnia, and mosquitoes. These myosins contain a single IQ motif in the neck region. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276847 [Multi-domain]  Cd Length: 633  Bit Score: 275.84  E-value: 3.97e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  163 LQNLKLRFMQQKIYTYAGSILVAINPFKFLPiyNPKYVKMYENQQLGKLephvfaLADVAYYAMlRKHVN----QCIVIS 238
Cdd:cd14881      4 MKCLQARFYAKEFFTNVGPILLSVNPYRDVG--NPLTLTSTRSSPLAPQ------LLKVVQEAV-RQQSEtgypQAIILS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  239 GESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVvEKY 318
Cdd:cd14881     75 GTSGSGKTYASMLLLRQLFDVAGGGPETDAFKHLAAAFTVLRSLGSAKTATNSESSRIGHFIEVQVTDGALYRTKI-HCY 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  319 LLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLK--QPQDYFYLNQHnlniEDGEDLKHDFERLQQAMEMVGFLPA 396
Cdd:cd14881    154 FLDQTRVIRPLPGEKNYHIFYQMLAGLSQEERVKLHLDgySPANLRYLSHG----DTRQNEAEDAARFQAWKACLGILGI 229
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  397 TKKQIFSVLSAILYLGNVTYKKRATGrdeGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRktvTVNDKLILPYSLSEAIT 476
Cdd:cd14881    230 PFLDVVRVLAAVLLLGNVQFIDGGGL---EVDVKGETELKSVAALLGVSGAALFRGLTTR---THNARGQLVKSVCDANM 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  477 A---RDSMAKSLYSALFDWIVLRIN-----HALLNKKDMEEavsclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14881    304 SnmtRDALAKALYCRTVATIVRRANslkrlGSTLGTHATDG-----FIGILDMFGFEDPKPSQLEHLCINLCAETMQHFY 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  549 TQHIFKLEQEEYQGEGISWH-NIDYTDNVGCIHLISKKPTGLFYLLDEESNfPHATSHTLLAKFKQQHEDNKYFLGT-PV 626
Cdd:cd14881    379 NTHIFKSSIESCRDEGIQCEvEVDYVDNVPCIDLISSLRTGLLSMLDVECS-PRGTAESYVAKIKVQHRQNPRLFEAkPQ 457
                          490       500       510
                   ....*....|....*....|....*....|....*...
gi 1720426625  627 LEPAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLR 664
Cdd:cd14881    458 DDRMFGIRHFAGRVVYDASDFLDTNRDVVPDDLVAVFY 495
MYSc_Myo44 cd14905
class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV ...
162-671 6.08e-78

class XLIV myosin, motor domain; There is little known about the function of the myosin XLIV class. Members here include cellular slime mold Polysphondylium and soil-living amoeba Dictyostelium. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276870  Cd Length: 673  Bit Score: 273.51  E-value: 6.08e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGkLEPHVFALADVAYYAMLRKHVNQCIVISGES 241
Cdd:cd14905      3 LINIIQARYKKEIIYTYIGPILVSVNPLRYLPFLHSQELVRNYNQRRG-LPPHLFALAAKAISDMQDFRRDQLIFIGGES 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  242 GSGKTQSTNFLIHCL--TALSQKGYasgVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd14905     82 GSGKSENTKIIIQYLltTDLSRSKY---LRDYILESGIILESFGHASTDSNHNSSRWGKYFEMFYSLYGEIQGAKLYSYF 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYFYLNQ-HNLNIEDGEDlKHDFERLQQAMEMVGFLPATK 398
Cdd:cd14905    159 LDENRVTYQNKGERNFHIFYQFLKGITDEEKAAYQLGDINSYHYLNQgGSISVESIDD-NRVFDRLKMSFVFFDFPSEKI 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  399 KQIFSVLSAILYLGNVTYKKratgRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNdklilpyslsEAITAR 478
Cdd:cd14905    238 DLIFKTLSFIIILGNVTFFQ----KNGKTEVKDRTLIESLSHNITFDSTKLENILISDRSMPVN----------EAVENR 303
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  479 DSMAKSLYSALFDWIVlrinhALLNKKdMEEAVSCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQE 558
Cdd:cd14905    304 DSLARSLYSALFHWII-----DFLNSK-LKPTQYSHTLGILDLFGQESSQLNGYEQFSINFLEERLQQIYLQTVLKQEQR 377
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  559 EYQGEGISWHN-IDYTDNVGCIHLISKkptgLFYLLDEESNFPHATSHTLLAKFKQQHEDNKYFLGTPvlePAFIIQHFA 637
Cdd:cd14905    378 EYQTERIPWMTpISFKDNEESVEMMEK----IINLLDQESKNINSSDQIFLEKLQNFLSRHHLFGKKP---NKFGIEHYF 450
                          490       500       510
                   ....*....|....*....|....*....|....
gi 1720426625  638 GRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYV 671
Cdd:cd14905    451 GQFYYDVRGFIIKNRDEILQRTNVLHKNSITKYL 484
MYSc_Myo21 cd14882
class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class ...
161-971 5.72e-74

class XXI myosin, motor domain; The myosins here are comprised of insects. Leishmania class XXI myosins do not group with them. Myo21, unlike other myosin proteins, contains UBA-like protein domains and has no structural or functional relationship with the myosins present in other organisms possessing cilia or flagella. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. They have diverse tails with IQ, WW, PX, and Tub domains. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276848  Cd Length: 642  Bit Score: 261.21  E-value: 5.72e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  161 NLLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGE 240
Cdd:cd14882      2 NILEELRHRYLMGESYTFIGDILLSLNPNEIKQEYPQEFHAKYRCKSRSDNAPHIFSVADSAYQDMLHHEEPQHIILSGE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  241 SGSGKTqsTNFLiHCLTALSQKGYA-SGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYL 319
Cdd:cd14882     82 SYSGKT--TNAR-LLIKHLCYLGDGnRGATGRVESSIKAILALVNAGTPLNADSTRCILQYQLTFGSTGKMSGAIFWMYQ 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  320 LEKSRLVSQEKDERNYHVFYYLLLGVSEEERL-EFQLKQPQDYFYLNQHNLNIEDG-----EDLKHDFERLQQAMEMVGF 393
Cdd:cd14882    159 LEKLRVSTTDGNQSNFHIFYYFYDFIEAQNRLkEYNLKAGRNYRYLRIPPEVPPSKlkyrrDDPEGNVERYKEFEEILKD 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  394 LPATKKQ---IFSVLSAILYLGNVTYKKratGRDEGlEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTVNDKLILPYS 470
Cdd:cd14882    239 LDFNEEQletVRKVLAAILNLGEIRFRQ---NGGYA-ELENTEIASRVAELLRLDEKKFMWALTNYCLIKGGSAERRKHT 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  471 LSEAITARDSMAKSLYSALFDWIVLRINHALLnkkdMEEAV--SCLSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYF 548
Cdd:cd14882    315 TEEARDARDVLASTLYSRLVDWIINRINMKMS----FPRAVfgDKYSISIHDMFGFECFHRNRLEQLMVNTLNEQMQYHY 390
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  549 TQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLDEESNFPHATSHTLlakfKQQHEDNKYFLgTPVLE 628
Cdd:cd14882    391 NQRIFISEMLEMEEEDIPTINLRFYDNKTAVDQLMTKPDGLFYIIDDASRSCQDQNYIM----DRIKEKHSQFV-KKHSA 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  629 PAFIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLIgmdpvavfrwavlraairamavlreagrlraer 708
Cdd:cd14882    466 HEFSVAHYTGRIIYDAREFADKNRDFVPPEMIETMRSSLDESVKLMF--------------------------------- 512
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  709 aekaagisspaTRSHMEELPRGASTpseklYRCTGLdfsferseeldvnafedimafyesrndlhnQIIKSLkglpwqge 788
Cdd:cd14882    513 -----------TNSQVRNMRTLAAT-----FRATSL------------------------------ELLKML-------- 538
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  789 dprrllqslslfqkprtsflkskgikqkqiipknlldskslrliismtlhdrttksllhlhkkkkppSISAqfqtslnkl 868
Cdd:cd14882    539 -------------------------------------------------------------------SIGA--------- 542
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  869 lealGKAEPFFIRCIRSNAEKKELCFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVL---LPKDVQPCRE 945
Cdd:cd14882    543 ----NSGGTHFVRCIRSDLEYKPRGFHSEVVRQQMRALAVLDTAKARQKGFSYRIPFQEFLRRYQFLafdFDETVEMTKD 618
                          810       820
                   ....*....|....*....|....*.
gi 1720426625  946 AIAALLEKLQVdrQNYQIGKTKVFLK 971
Cdd:cd14882    619 NCRLLLIRLKM--EGWAIGKTKVFLK 642
MYSc_Myo23 cd14884
class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 ...
160-673 2.74e-72

class XXIII myosin, motor domain; These myosins are predicted to have a neck region with 1-2 IQ motifs and a single MyTH4 domain in its C-terminal tail. The lack of a FERM domain here is odd since MyTH4 domains are usually found alongside FERM domains where they bind to microtubules. At any rate these Class XXIII myosins are still proposed to function in the apicomplexan microtubule cytoskeleton. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276850 [Multi-domain]  Cd Length: 685  Bit Score: 257.14  E-value: 2.74e-72
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  160 ANLLQNLKLRFMQQKIYTYAGSILVAINPFKFLP-IYNPK----YVKMYENQQLGK---LEPHVFALADVAYYAMLRKHV 231
Cdd:cd14884      1 PNVLQNLKNRYLKNKIYTFHASLLLALNPYKPLKeLYDQDvmnvYLHKKSNSAASAapfPKAHIYDIANMAYKNMRGKLK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  232 NQCIVISGESGSGKTQSTNFLIHCLTALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLE----- 306
Cdd:cd14884     81 RQTIVVSGHSGSGKTENCKFLFKYFHYIQTDSQMTERIDKLIYINNILESMSNATTIKNNNSSRCGRINLLIFEEventq 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  307 ----NGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEE----RL--------------EFQLKQPQDYFYL 364
Cdd:cd14884    161 knmfNGCFRNIKIKILLLEINRCIAHNFGERNFHVFYQVLRGLSDEDlarrNLvrncgvygllnpdeSHQKRSVKGTLRL 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  365 NQHNLNIEDGEDLKHD--FERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKkratgrdeglevgppevldTLSQLL 442
Cdd:cd14884    241 GSDSLDPSEEEKAKDEknFVALLHGLHYIKYDERQINEFFDIIAGILHLGNRAYK-------------------AAAECL 301
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  443 KVKRETLVEVLTKRKTVTVNDKLILPYSLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEEAVSCLS------- 515
Cdd:cd14884    302 QIEEEDLENVIKYKNIRVSHEVIRTERRKENATSTRDTLIKFIYKKLFNKIIEDINRNVLKCKEKDESDNEDIysineai 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  516 IGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKkptgLFYLLDE 595
Cdd:cd14884    382 ISILDIYGFEELSGNDFDQLCINLANEKLNNYYINNEIEKEKRIYARENIICCSDVAPSYSDTLIFIAK----IFRRLDD 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  596 ESNFpHATSHT---------LLAKFKQQHEDNKYFLG-------------TPVLEPAFIIQHFAGRVKYQIKDFREKNMD 653
Cdd:cd14884    458 ITKL-KNQGQKktddhffryLLNNERQQQLEGKVSYGfvlnhdadgtakkQNIKKNIFFIRHYAGLVTYRINNWIDKNSD 536
                          570       580
                   ....*....|....*....|
gi 1720426625  654 YMRPDIVALLRGSDSSYVRQ 673
Cdd:cd14884    537 KIETSIETLISCSSNRFLRE 556
MYSc_Myo18 cd01386
class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain ...
163-971 4.53e-70

class XVIII myosin, motor domain; Many members of this class contain a N-terminal PDZ domain which is commonly found in proteins establishing molecular complexes. The motor domain itself does not exhibit ATPase activity, suggesting that it functions as an actin tether protein. It also has two IQ domains that probably bind light chains or related calmodulins and a C-terminal tail with two sections of coiled-coil domains, which are thought to mediate homodimerization. The function of these myosins are largely unknown. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276837 [Multi-domain]  Cd Length: 689  Bit Score: 250.69  E-value: 4.53e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  163 LQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGESG 242
Cdd:cd01386      4 LHTLRQRYGANLIHTYAGPSLIVINPRHPLAVYSEKVAKMFKGCRREDMPPHIYASAQSAYRAMLMSRRDQSIVLLGRSG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  243 SGKTQSTNFLIH--CLTALSQKGYASgVERtILGAGPVLEAFGNAKTAHNNNSSRFGKFIQVNYLENGIVRGAVVEKYLL 320
Cdd:cd01386     84 SGKTTNCRHILEylVTAAGSVGGVLS-VEK-LNAALTVLEAFGNVRTALNGNATRFSQLFSLDFDQAGQLASASIQTLLL 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  321 EKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQ--PQDYFYLNQHnLNIEDGEDLKHDFERLQQAMEMVGFLPATK 398
Cdd:cd01386    162 ERSRVARRPEGESNFNVFYYLLAGADAALRTELHLNQlaESNSFGIVPL-QKPEDKQKAAAAFSKLQAAMKTLGISEEEQ 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  399 KQIFSVLSAILYLGnvtykkrATGRDEGLEVGPPEVLDTLS-----QLLKVKRETLVEVLTK--------RKTVTVNDKL 465
Cdd:cd01386    241 RAIWSILAAIYHLG-------AAGATKAASAGRKQFARPEWaqraaYLLGCTLEELSSAIFKhhlsggpqQSTTSSGQES 313
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  466 ILPYSLSE----AITARDSMAKSLYSALFDWIVlrinhALLNKKDMEEAVSCLSIGVLDIFGFED-----FERNS-FEQF 535
Cdd:cd01386    314 PARSSSGGpkltGVEALEGFAAGLYSELFAAVV-----SLINRSLSSSHHSTSSITIVDTPGFQNpahsgSQRGAtFEDL 388
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  536 CINYANEQLQYYFTQHIFKLEQEEYQGEGIswhNIDYTDNVGCIH----LISKKPT--------------GLFYLLDEES 597
Cdd:cd01386    389 CHNYAQERLQLLFHERTFVAPLERYKQENV---EVDFDLPELSPGalvaLIDQAPQqalvrsdlrdedrrGLLWLLDEEA 465
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  598 NFPHATSHTLLAKFKQQHEDNKYFLGTPVLEPA-----FIIQHfagrvkyqikdfreknmdymrpdivallrgsdssyvr 672
Cdd:cd01386    466 LYPGSSDDTFLERLFSHYGDKEGGKGHSLLRRSegplqFVLGH------------------------------------- 508
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  673 qLIGMDPVavfRWAVlraairamavlreAGRLRAERaekaagiSSPATRshmeelprgastpseklyrctgldfsferse 752
Cdd:cd01386    509 -LLGTNPV---EYDV-------------SGWLKAAK-------ENPSAQ------------------------------- 533
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  753 eldvNAfedimafyesrndlhnqiikslkglpwqgedpRRLLQSlslfqkprtSFLKSKGIKQKqiipknlldskslrli 832
Cdd:cd01386    534 ----NA--------------------------------TQLLQE---------SQKETAAVKRK---------------- 552
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  833 ismtlhdrttksllhlhkkkkppSISAQFQTSLNKLLEALGKAEPFFIRCI--RSNAEKKE----LCFDDELVLQ----- 901
Cdd:cd01386    553 -----------------------SPCLQIKFQVDALIDTLRRTGLHFVHCLlpQHNAGKDErstsSPAAGDELLDvpllr 609
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  902 -QLRYTGMLETVRIRRSGYSAKYTFQDFTEQFQVLLPKDVQPC---------REAIAALLEKLQVDRQNYQIGKTKVFLK 971
Cdd:cd01386    610 sQLRGSQLLDALRLYRQGFPDHMPLGEFRRRFQVLAPPLTKKLglnsevadeRKAVEELLEELDLEKSSYRIGLSQVFFR 689
RhoGAP_myosin_IXA cd04406
RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1700-1885 9.12e-70

RhoGAP_myosin_IXA: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in myosins IXA. Class IX myosins contain a characteristic head domain, a neck domain and a tail domain which contains a C6H2-zinc binding motif and a Rho-GAP domain. Class IX myosins are single-headed, processive myosins that are partly cytoplasmic, and partly associated with membranes and the actin cytoskeleton. Class IX myosins are implicated in the regulation of neuronal morphogenesis and function of sensory systems, like the inner ear. There are two major isoforms, myosin IXA and IXB with several splice variants, which are both expressed in developing neurons. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239871  Cd Length: 186  Bit Score: 232.58  E-value: 9.12e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRE 1779
Cdd:cd04406      1 FGVELSRLTSEDRSVPLVVEKLINYIEMHGLYTEGIYRKSGSTNKIKELRQGLDTDANSVNLDDYNIHVIASVFKQWLRD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1780 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1859
Cdd:cd04406     81 LPNPLMTFELYEEFLRAMGLQERRETVRGVYSVIDQLSRTHLNTLERLIFHLVRIALQEETNRMSANALAIVFAPCILRC 160
                          170       180
                   ....*....|....*....|....*.
gi 1720426625 1860 PDNSDPLTSMKDVLKITTCVEMLIKE 1885
Cdd:cd04406    161 PDTTDPLQSVQDISKTTTCVELIVCE 186
RhoGAP smart00324
GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac ...
1713-1886 3.85e-58

GTPase-activator protein for Rho-like GTPases; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases. etter domain limits and outliers.


Pssm-ID: 214618  Cd Length: 174  Bit Score: 198.64  E-value: 3.85e-58
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  1713 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVK-LEDFPIHAITGVLKQWLRELPEPLMTFAQYG 1791
Cdd:smart00324    2 PIPIIVEKCIEYLEKRGLDTEGIYRVSGSKSRVKELRDAFDSGPDPDLdLSEYDVHDVAGLLKLFLRELPEPLITYELYE 81
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  1792 DFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDPltSMKD 1871
Cdd:smart00324   82 EFIEAAKLEDETERLRALRELLSLLPPANRATLRYLLAHLNRVAEHSEENKMTARNLAIVFGPTLLRPPDGEVA--SLKD 159
                           170
                    ....*....|....*
gi 1720426625  1872 VLKITTCVEMLIKEQ 1886
Cdd:smart00324  160 IRHQNTVIEFLIENA 174
MYSc_Myo32 cd14893
class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but ...
162-970 6.01e-58

class XXXII myosin, motor domain; Class XXXII myosins do not contain any IQ motifs, but possess tandem MyTH4 and FERM domains. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276858  Cd Length: 741  Bit Score: 215.99  E-value: 6.01e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMYENQQ----------LGKLEPHVFALADVAYYAMLRKHV 231
Cdd:cd14893      3 ALYTLRARYRMEQVYTWVDRVLVGVNPVTPLPIYTPDHMQAYNKSReqtplyekdtVNDAPPHVFALAQNALRCMQDAGE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  232 NQCIVISGESGSGKTQSTNFLIHCLT-----------ALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRFGKFI 300
Cdd:cd14893     83 DQAVILLGGMGAGKSEAAKLIVQYLCeigdeteprpdSEGASGVLHPIGQQILHAFTILEAFGNAATRQNRNSSRFAKMI 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  301 QVNYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQL---KQPQDYFYLNQHNLNIEDGEDL 377
Cdd:cd14893    163 SVEFSKHGHVIGGGFTTHYFEKSRVIDCRSHERNFHVFYQVLAGVQHDPTLRDSLemnKCVNEFVMLKQADPLATNFALD 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  378 KHDFERLQQAMEMVGFLPATKKQIFSVLSAILYLGNVTYKKRATGRDEGLEVGPPEVLDTLSQLLKVKRE-TLVEVLTKR 456
Cdd:cd14893    243 ARDYRDLMSSFSALRIRKNQRVEIVRIVAALLHLGNVDFVPDPEGGKSVGGANSTTVSDAQSCALKDPAQiLLAAKLLEV 322
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  457 KTVTV-------------NDKLILPY---SLSEAITARDSMAKSLYSALFDWIVLRINHALLNKKDMEE----AVSCLSI 516
Cdd:cd14893    323 EPVVLdnyfrtrqffskdGNKTVSSLkvvTVHQARKARDTFVRSLYESLFNFLVETLNGILGGIFDRYEksniVINSQGV 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  517 GVLDIFGFEDFE--RNSFEQFCINYANEQLQYYFTQHIFK-----LEQEEYQGEG-ISWH-NIDYT-DNVGCIHLISKKP 586
Cdd:cd14893    403 HVLDMVGFENLTpsQNSFDQLCFNYWSEKVHHFYVQNTLAinfsfLEDESQQVENrLTVNsNVDITsEQEKCLQLFEDKP 482
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  587 TGLFYLLDEESNFPHATSHTLLAKFKQQHED---------NKYFLGTPVLEPA-----FIIQHFAGRVKYQIKDFREKNM 652
Cdd:cd14893    483 FGIFDLLTENCKVRLPNDEDFVNKLFSGNEAvgglsrpnmGADTTNEYLAPSKdwrllFIVQHHCGKVTYNGKGLSSKNM 562
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  653 DYMRPDIVALLRGSDSsyvrqligmdpvavfrwAVLRAAiramavlrEAGRLRAERAEKAAGISSPATRShmeelprgas 732
Cdd:cd14893    563 LSISSTCAAIMQSSKN-----------------AVLHAV--------GAAQMAAASSEKAAKQTEERGST---------- 607
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  733 tpseklyrctgldfsferseeldvnafedimafyesrndlhnqiikslkglpwqgedprrllqslslfqkpRTSFLKSKG 812
Cdd:cd14893    608 -----------------------------------------------------------------------SSKFRKSAS 616
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  813 IKQKQiipKNLLDSKSLRLiismtlhdrttksllhlhkkkkppsisaqfQTSLNKLLEALGKAEPFFIRCIRSNAEKKEL 892
Cdd:cd14893    617 SARES---KNITDSAATDV------------------------------YNQADALLHALNHTGKNFLVCIKPNETLEEG 663
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  893 CFDDELVLQQLRYTGMLETVRIRRSGYSAKYTFQDFTEQFqvllpKDVQPCREAIAALLEKLQ----VDRQNYQIGKTKV 968
Cdd:cd14893    664 VFDSAYVMKQIRMNHLVELMQASRSIFTVHLTYGHFFRRY-----KNVCGHRGTLESLLRSLSaigvLEEEKFVVGKTKV 738

                   ..
gi 1720426625  969 FL 970
Cdd:cd14893    739 YL 740
RhoGAP pfam00620
RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.
1715-1861 6.71e-56

RhoGAP domain; GTPase activator proteins towards Rho/Rac/Cdc42-like small GTPases.


Pssm-ID: 459875  Cd Length: 148  Bit Score: 191.22  E-value: 6.71e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1715 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPA-AVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1793
Cdd:pfam00620    1 PLIVRKCVEYLEKRGLDTEGIFRVSGSASRIKELREAFDRGPDvDLDLEEEDVHVVASLLKLFLRELPEPLLTFELYEEF 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720426625 1794 LRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPD 1861
Cdd:pfam00620   81 IEAAKLPDEEERLEALRELLRKLPPANRDTLRYLLAHLNRVAQNSDVNKMNAHNLAIVFGPTLLRPPD 148
RA_Myosin-IXb cd17217
Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is ...
16-112 1.78e-55

Ras-associating (RA) domain found in Myosin-IXb; Myosin-IXb, also termed myosin-9b (Myo9b), is a motor protein with a Rho GTPase activating domain (RhoGAP); it is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen and in several immune cells including dendritic cells, macrophages and CD4+ T. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a RhoGAP domain. Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells.


Pssm-ID: 340737  Cd Length: 96  Bit Score: 188.08  E-value: 1.78e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   16 TYHLHIYPQLSSAgSQTSCRVTATKDSTTSDVIQDVVASLHLDGSKHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRA 95
Cdd:cd17217      1 VYALQIYPQLSAE-SSTCCIVLATKEATASDVIKDAVATLGLDSSKPYVLAEVKESGGEEWVLDANDSPVQRVLLWPRKA 79
                           90
                   ....*....|....*..
gi 1720426625   96 QDEHPQEDGYYFLLQER 112
Cdd:cd17217     80 QDDHPQSDGYYFLLQER 96
RhoGAP cd00159
RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like ...
1715-1885 1.96e-53

RhoGAP: GTPase-activator protein (GAP) for Rho-like GTPases; GAPs towards Rho/Rac/Cdc42-like small GTPases. Small GTPases (G proteins) cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when bound to GDP. The Rho family of small G proteins, which includes Cdc42Hs, activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. G proteins generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude. The RhoGAPs are one of the major classes of regulators of Rho G proteins.


Pssm-ID: 238090 [Multi-domain]  Cd Length: 169  Bit Score: 185.20  E-value: 1.96e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1715 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFL 1794
Cdd:cd00159      1 PLIIEKCIEYLEKNGLNTEGIFRVSGSASKIEELKKKFDRGEDIDDLEDYDVHDVASLLKLYLRELPEPLIPFELYDEFI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1795 RAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDplTSMKDVLK 1874
Cdd:cd00159     81 ELAKIEDEEERIEALKELLKSLPPENRDLLKYLLKLLHKISQNSEVNKMTASNLAIVFAPTLLRPPDSDD--ELLEDIKK 158
                          170
                   ....*....|.
gi 1720426625 1875 ITTCVEMLIKE 1885
Cdd:cd00159    159 LNEIVEFLIEN 169
MYSc_Myo24B cd14938
class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a ...
162-674 4.69e-52

class XXIV B myosin, motor domain; These myosins have a 1-2 IQ motifs in their neck and a coiled-coil region in their C-terminal tail. The functions of these myosins remain elusive. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276898 [Multi-domain]  Cd Length: 713  Bit Score: 197.37  E-value: 4.69e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  162 LLQNLKLRFMQQKIYTYAGSILVAINPFKFLPIYNPKYVKMY---ENQQLGKLEPHVFALADVAYYAMLRKhvNQCIVIS 238
Cdd:cd14938      3 VLYHLKERFKNNKFYTKMGPLLIFINPKINNNINNEETIEKYkciDCIEDLSLNEYHVVHNALKNLNELKR--NQSIIIS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  239 GESGSGKTQSTNFLIHCL----------------------TALSQKGYASGVERTILGAGPVLEAFGNAKTAHNNNSSRF 296
Cdd:cd14938     81 GESGSGKSEIAKNIINFIayqvkgsrrlptnlndqeedniHNEENTDYQFNMSEMLKHVNVVMEAFGNAKTVKNNNSSRF 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  297 GKFIQVnYLENGIVRGAVVEKYLLEKSRLVSQEKDERNYHVFYYLLLGVSEEERLEFQLKQPQDYfylnqHNLNIEDGED 376
Cdd:cd14938    161 SKFCTI-HIENEEIKSFHIKKFLLDKERLINRKANENSFNIFYYIINGSSDKFKKMYFLKNIENY-----SMLNNEKGFE 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  377 LKHDFE-RLQQAMEMVGFLPATKKQI---FSVLSAILYLGNV----TYKKRAT---GRDEGLEVGPPEVLDTLS------ 439
Cdd:cd14938    235 KFSDYSgKILELLKSLNYIFDDDKEIdfiFSVLSALLLLGNTeivkAFRKKSLlmgKNQCGQNINYETILSELEnsedig 314
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  440 ------------QLLKVKRETLVEVLTKRktVTVNDKLILPYSLSEAITAR-DSMAKSLYSALFDWIVLRINHALLNKKD 506
Cdd:cd14938    315 ldenvknlllacKLLSFDIETFVKYFTTN--YIFNDSILIKVHNETKIQKKlENFIKTCYEELFNWIIYKINEKCTQLQN 392
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  507 MEEAVSclSIGVLDIFGFEDFERNSFEQFCINYANEQLQYYFTQHIFKLEQEEYQGEGISW-HNIDYTDNVG-CIHLISK 584
Cdd:cd14938    393 ININTN--YINVLDMAYFENSKDNSLEQLLINTTNEEIIKIKNDCLYKKRVLSYNEDGIFCeYNSENIDNEPlYNLLVGP 470
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  585 KPTGLFYLLDEESN---FPHATSHTL-LAKFKQqheDNKYFLGTPVLE--PAFIIQHFAGRVKYQIKDFREKNMDYMRPD 658
Cdd:cd14938    471 TEGSLFSLLENVSTktiFDKSNLHSSiIRKFSR---NSKYIKKDDITGnkKTFVITHSCGDIIYNAENFVEKNIDILTNR 547
                          570
                   ....*....|....*.
gi 1720426625  659 IVALLRGSDSSYVRQL 674
Cdd:cd14938    548 FIDMVKQSENEYMRQF 563
RhoGAP_ARAP cd04385
RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1707-1857 2.34e-38

RhoGAP_ARAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in ARAPs. ARAPs (also known as centaurin deltas) contain, besides the RhoGAP domain, an Arf GAP, ankyrin repeat ras-associating, and PH domains. Since their ArfGAP activity is PIP3-dependent, ARAPs are considered integration points for phosphoinositide, Arf and Rho signaling. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239850  Cd Length: 184  Bit Score: 142.45  E-value: 2.34e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1707 LTSDkaSVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKL---EDFPiHAITGVLKQWLRELPEP 1783
Cdd:cd04385     10 LTDN--DIPVIVDKCIDFITQHGLMSEGIYRKNGKNSSVKKLLEAFRKDARSVQLregEYTV-HDVADVLKRFLRDLPDP 86
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426625 1784 LMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLL 1857
Cdd:cd04385     87 LLTSELHAEWIEAAELENKDERIARYKELIRRLPPINRATLKVLIGHLYRVQKHSDENQMSVHNLALVFGPTLF 160
C1_Myosin-IXb cd20884
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar ...
1630-1687 1.89e-36

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXb and similar proteins; Myosin-IXb, also called unconventional myosin-9b (Myo9b), is an actin-dependent motor protein of the unconventional myosin IX class. It is expressed abundantly in tissues of the immune system, like lymph nodes, thymus, and spleen, and in several immune cells including dendritic cells, macrophages and CD4+ T cells. Myosin-IXb contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating (RhoGAP) domain. Myosin-IXb acts as a motorized signaling molecule that links Rho signaling to the dynamic actin cytoskeleton. It regulates leukocyte migration by controlling RhoA signaling. Myosin-IXb is also involved in the development of autoimmune diseases, including rheumatoid arthritis, systemic lupus erythematosus, and type 1 diabetes. Moreover, Myosin-IXb is a ROBO-interacting protein that suppresses RhoA activity in lung cancer cells. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410434  Cd Length: 58  Bit Score: 132.29  E-value: 1.89e-36
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720426625 1630 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1687
Cdd:cd20884      1 EEYNGHVFTSYQVNIMQSCEQCSSYIWAMEKALLCSVCKMTCHKKCLSKIQSHCSSTC 58
RA_Myosin-IX cd01779
Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor ...
18-112 3.84e-36

Ras-associating (RA) domain found in Myosin-IX; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains and a C-terminal tail containing a Rho-GTPase activating protein (RhoGAP) domain. The RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis and IXb is expressed abundantly in tissues of the immune system.


Pssm-ID: 340477  Cd Length: 97  Bit Score: 132.83  E-value: 3.84e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   18 HLHIYPQLSSAgSQTSCRVTATKDSTTSDVIQDVVASLHLDGSKHYVLVEVKESGG---EEWVLDASDSPVHRVLLWPRR 94
Cdd:cd01779      1 MVRVYPGALSP-ETEFLSVEATKQTTASEVIECLVAKLRLDKAECYELAEVCGSGGqgcKERRLGPSENPVQVQLLWPKM 79
                           90
                   ....*....|....*...
gi 1720426625   95 AQDEHPQEDGYYFLLQER 112
Cdd:cd01779     80 AGDSDNQVTSYRFFLREK 97
RhoGAP_nadrin cd04386
RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1700-1885 1.44e-35

RhoGAP_nadrin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Nadrin-like proteins. Nadrin, also named Rich-1, has been shown to be involved in the regulation of Ca2+-dependent exocytosis in neurons and recently has been implicated in tight junction maintenance in mammalian epithelium. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239851  Cd Length: 203  Bit Score: 135.28  E-value: 1.44e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCV-DSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDF---PiHAITGVLKQ 1775
Cdd:cd04386      5 FGTPLeEHLKRTGREIALPIEACVMCLLETGMNEEGLFRVGGGASKLKRLKAALDAGTFSLPLDEFysdP-HAVASALKS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1776 WLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPC 1855
Cdd:cd04386     84 YLRELPDPLLTYNLYEDWVQAANKPDEDERLQAIWRILNKLPRENRDNLRYLIKFLSKLAQKSDENKMSPSNIAIVLAPN 163
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720426625 1856 LLRCP-DNSDPLTSMKDVLKITTCVEMLIKE 1885
Cdd:cd04386    164 LLWAKnEGSLAEMAAGTSVHVVAIVELIISH 194
RhoGAP_fRGD1 cd04398
RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1700-1869 2.51e-35

RhoGAP_fRGD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD1-like proteins. Yeast Rgd1 is a GAP protein for Rho3 and Rho4 and plays a role in low-pH response. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239863  Cd Length: 192  Bit Score: 134.07  E-value: 2.51e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTS-DKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKL---EDF--PIHAITGVL 1773
Cdd:cd04398      1 FGVPLEDLILrEGDNVPNIVYQCIQAIENFGLNLEGIYRLSGNVSRVNKLKELFDKDPLNVLLispEDYesDIHSVASLL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1774 KQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFA 1853
Cdd:cd04398     81 KLFFRELPEPLLTKALSREFIEAAKIEDESRRRDALHGLINDLPDANYATLRALMFHLARIKEHESVNRMSVNNLAIIWG 160
                          170
                   ....*....|....*.
gi 1720426625 1854 PCLLrcPDNSDPLTSM 1869
Cdd:cd04398    161 PTLM--NAAPDNAADM 174
RhoGAP_ARHGAP27_15_12_9 cd04403
RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1700-1869 3.22e-34

RhoGAP_ARHGAP27_15_12_9: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP27 (also called CAMGAP1), ARHGAP15, 12 and 9-like proteins; This subgroup of ARHGAPs are multidomain proteins that contain RhoGAP, PH, SH3 and WW domains. Most members that are studied show GAP activity towards Rac1, some additionally show activity towards Cdc42. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239868 [Multi-domain]  Cd Length: 187  Bit Score: 130.59  E-value: 3.22e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTS-DKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAA----VKLEDfpIHAITGVLK 1774
Cdd:cd04403      1 FGCHLEALCQrENSTVPKFVRLCIEAVEKRGLDVDGIYRVSGNLAVIQKLRFAVDHDEKLdlddSKWED--IHVITGALK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1775 QWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1854
Cdd:cd04403     79 LFFRELPEPLFPYSLFNDFVAAIKLSDYEQRVSAVKDLIKSLPKPNHDTLKMLFRHLCRVIEHGEKNRMTTQNLAIVFGP 158
                          170
                   ....*....|....*..
gi 1720426625 1855 CLLRcP--DNSDPLTSM 1869
Cdd:cd04403    159 TLLR-PeqETGNIAVHM 174
RhoGAP_chimaerin cd04372
RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1707-1884 5.47e-33

RhoGAP_chimaerin: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of chimaerins. Chimaerins are a family of phorbolester- and diacylglycerol-responsive GAPs specific for the Rho-like GTPase Rac. Chimaerins exist in two alternative splice forms that each contain a C-terminal GAP domain, and a central C1 domain which binds phorbol esters, inducing a conformational change that activates the protein; one splice form is lacking the N-terminal Src homology-2 (SH2) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239837 [Multi-domain]  Cd Length: 194  Bit Score: 127.25  E-value: 5.47e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1707 LTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTD--PAAVKLEDFP-IHAITGVLKQWLRELPEP 1783
Cdd:cd04372      9 VKAHNTQRPMVVDMCIREIEARGLQSEGLYRVSGFAEEIEDVKMAFDRDgeKADISATVYPdINVITGALKLYFRDLPIP 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1784 LMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDnS 1863
Cdd:cd04372     89 VITYDTYPKFIDAAKISNPDERLEAVHEALMLLPPAHYETLRYLMEHLKRVTLHEKDNKMNAENLGIVFGPTLMRPPE-D 167
                          170       180
                   ....*....|....*....|.
gi 1720426625 1864 DPLTSMKDVLKITTCVEMLIK 1884
Cdd:cd04372    168 SALTTLNDMRYQILIVQLLIT 188
MYSc_Myo33 cd14894
class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 ...
272-675 5.30e-31

class myosin, motor domain; Class XXXIII myosins have variable numbers of IQ domain and 2 tandem ANK repeats that are separated by a PH domain. The myosin classes XXX to XXXIV contain members from Phytophthora species and Hyaloperonospora parasitica. The catalytic (head) domain has ATPase activity and belongs to the larger group of P-loop NTPases. Myosins are actin-dependent molecular motors that play important roles in muscle contraction, cell motility, and organelle transport. The head domain is a molecular motor, which utilizes ATP hydrolysis to generate directed movement toward the plus end along actin filaments. A cyclical interaction between myosin and actin provides the driving force. Rates of ATP hydrolysis and consequently the speed of movement along actin filaments vary widely, from about 0.04 micrometer per second for myosin I to 4.5 micrometer per second for myosin II in skeletal muscle. Myosin II moves in discrete steps about 5-10 nm long and generates 1-5 piconewtons of force. Upon ATP binding, the myosin head dissociates from an actin filament. ATP hydrolysis causes the head to pivot and associate with a new actin subunit. The release of Pi causes the head to pivot and move the filament (power stroke). Release of ADP completes the cycle. CyMoBase classifications were used to confirm and identify the myosins in this hierarchy.


Pssm-ID: 276859 [Multi-domain]  Cd Length: 871  Bit Score: 133.33  E-value: 5.30e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  272 ILGAGPVLEAFGNAKTAHNNNSSRFGKF--IQVNYlenGI------VRGAVVEKYLLEKSRLVSQ------EKDERNYHV 337
Cdd:cd14894    249 VLDSNIVLEAFGHATTSMNLNSSRFGKMttLQVAF---GLhpwefqICGCHISPFLLEKSRVTSErgresgDQNELNFHI 325
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  338 FYYLLLGVSEEERLEFQLKQPQ---------DYFYLNQHNLN--IEDGEDLKHDFERLQQAMEMVGFL---PATKKQIFS 403
Cdd:cd14894    326 LYAMVAGVNAFPFMRLLAKELHldgidcsalTYLGRSDHKLAgfVSKEDTWKKDVERWQQVIDGLDELnvsPDEQKTIFK 405
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  404 VLSAILYLGNVTYKKR-ATGRDEGLEVGPPEVLDTLSQLLKVKRETLVEVLTKRKTVTV---NDKLILPYSLSEAITARD 479
Cdd:cd14894    406 VLSAVLWLGNIELDYReVSGKLVMSSTGALNAPQKVVELLELGSVEKLERMLMTKSVSLqstSETFEVTLEKGQVNHVRD 485
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  480 SMAKSLYSALFDWIVLRINHALL--------NKKDME------EAVSCLSIgvLDIFGFEDFERNSFEQFCINYANEQLq 545
Cdd:cd14894    486 TLARLLYQLAFNYVVFVMNEATKmsalstdgNKHQMDsnasapEAVSLLKI--VDVFGFEDLTHNSLDQLCINYLSEKL- 562
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  546 yyftqhiFKLEQEEYQGEGISWHNIDYTDNVGCIHLISKKPTGLFYLLdEESNFPHATSHTllaKFKQQHEDNKYFL--- 622
Cdd:cd14894    563 -------YAREEQVIAVAYSSRPHLTARDSEKDVLFIYEHPLGVFASL-EELTILHQSENM---NAQQEEKRNKLFVrni 631
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720426625  623 --------------------GTPVLEPA--FIIQHFAGRVKYQIKDFREKNMDYMRPDIVALLRGSDSSYVRQLI 675
Cdd:cd14894    632 ydrnssrlpepprvlsnakrHTPVLLNVlpFVIPHTRGNVIYDANDFVKKNSDFVYANLLVGLKTSNSSHFCRML 706
RhoGAP_SYD1 cd04379
RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1700-1867 9.16e-31

RhoGAP_SYD1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in SYD-1_like proteins. Syd-1, first identified and best studied in C.elegans, has been shown to play an important role in neuronal development by specifying axonal properties. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239844  Cd Length: 207  Bit Score: 121.42  E-value: 9.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLT---SDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKL--EDFP-IHAITGVL 1773
Cdd:cd04379      1 FGVPLSRLVereGESRDVPIVLQKCVQEIERRGLDVIGLYRLCGSAAKKKELRDAFERNSAAVELseELYPdINVITGVL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1774 KQWLRELPEPLMTFAQYGDFLRA--VELP-EKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAI 1850
Cdd:cd04379     81 KDYLRELPEPLITPQLYEMVLEAlaVALPnDVQTNTHLTLSIIDCLPLSAKATLLLLLDHLSLVLSNSERNKMTPQNLAV 160
                          170
                   ....*....|....*..
gi 1720426625 1851 IFAPCLLRCPDNSDPLT 1867
Cdd:cd04379    161 CFGPVLMFCSQEFSRYG 177
Motor_domain cd01363
Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the ...
182-302 1.20e-30

Myosin and Kinesin motor domain; Myosin and Kinesin motor domain. These ATPases belong to the P-loop NTPase family and provide the driving force in myosin and kinesin mediated processes. Some of the names do not match with what is given in the sequence list. This is because they are based on the current nomenclature by Kollmar/Sebe-Pedros.


Pssm-ID: 276814 [Multi-domain]  Cd Length: 170  Bit Score: 119.76  E-value: 1.20e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625  182 ILVAINPFKFLPIYNP-KYVKMYENQQLGKLEPHVFALADVAYYAMLRKHVNQCIVISGESGSGKTQSTNFLIHCLTALS 260
Cdd:cd01363      1 VLVRVNPFKELPIYRDsKIIVFYRGFRRSESQPHVFAIADPAYQSMLDGYNNQSIFAYGESGAGKTETMKGVIPYLASVA 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426625  261 QKGYASG--------------VERTILGAGPVLEAFGNAKTAHNNNSSRFGKFIQV 302
Cdd:cd01363     81 FNGINKGetegwvylteitvtLEDQILQANPILEAFGNAKTTRNENSSRFGKFIEI 136
RhoGAP_ARHGAP20 cd04402
RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1700-1883 1.14e-29

RhoGAP_ARHGAP20: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP20-like proteins. ArhGAP20, also known as KIAA1391 and RA-RhoGAP, contains a RhoGAP, a RA, and a PH domain, and ANXL repeats. ArhGAP20 is activated by Rap1 and induces inactivation of Rho, which in turn leads to neurite outgrowth. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239867  Cd Length: 192  Bit Score: 117.78  E-value: 1.14e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTSDkASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDpAAVKLEDFPIHAITGVLKQWLRE 1779
Cdd:cd04402      2 FGQPLSNICED-DNLPKPILDMLSLLYQKGPSTEGIFRRSANAKACKELKEKLNSG-VEVDLKAEPVLLLASVLKDFLRN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1780 LPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRC 1859
Cdd:cd04402     80 IPGSLLSSDLYEEWMSALDQENEEEKIAELQRLLDKLPRPNVLLLKHLICVLHNISQNSETNKMDAFNLAVCIAPSLLWP 159
                          170       180
                   ....*....|....*....|....
gi 1720426625 1860 PDNSDPLtsMKDVLKITTCVEMLI 1883
Cdd:cd04402    160 PASSELQ--NEDLKKVTSLVQFLI 181
RhoGAP_ARHGAP21 cd04395
RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1700-1883 1.81e-29

RhoGAP_ARHGAP21: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP21-like proteins. ArhGAP21 is a multi-domain protein, containing RhoGAP, PH and PDZ domains, and is believed to play a role in the organization of the cell-cell junction complex. It has been shown to function as a GAP of Cdc42 and RhoA, and to interact with alpha-catenin and Arf6. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239860  Cd Length: 196  Bit Score: 117.50  E-value: 1.81e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDS--LTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLED---FPIHAITGVLK 1774
Cdd:cd04395      2 FGVPLDDcpPSSENPYVPLIVEVCCNIVEARGLETVGIYRVPGNNAAISALQEELNRGGFDIDLQDprwRDVNVVSSLLK 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1775 QWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1854
Cdd:cd04395     82 SFFRKLPEPLFTNELYPDFIEANRIEDPVERLKELRRLIHSLPDHHYETLKHLIRHLKTVADNSEVNKMEPRNLAIVFGP 161
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1720426625 1855 CLLRCPDNS--DPLTSMKDVLKIttcVEMLI 1883
Cdd:cd04395    162 TLVRTSDDNmeTMVTHMPDQCKI---VETLI 189
RhoGAP_GMIP_PARG1 cd04378
RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1713-1884 8.12e-29

RhoGAP_GMIP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein) and PARG1 (PTPL1-associated RhoGAP1). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239843  Cd Length: 203  Bit Score: 115.60  E-value: 8.12e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1713 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGD 1792
Cdd:cd04378     15 EVPFIIKKCTSEIENRALGVQGIYRVSGSKARVEKLCQAFENGKDLVELSELSPHDISSVLKLFLRQLPEPLILFRLYND 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1793 FL----RAVELPEKQEQL-------SAIYAV---LDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLR 1858
Cdd:cd04378     95 FIalakEIQRDTEEDKAPntpievnRIIRKLkdlLRQLPASNYNTLQHLIAHLYRVAEQFEENKMSPNNLGIVFGPTLIR 174
                          170       180
                   ....*....|....*....|....*...
gi 1720426625 1859 CPDNSDP--LTSMKDVLKITTCVEMLIK 1884
Cdd:cd04378    175 PRPGDADvsLSSLVDYGYQARLVEFLIT 202
C1_Myosin-IX cd20818
protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; ...
1632-1687 1.75e-28

protein kinase C conserved region 1 (C1 domain) found in the unconventional myosin-IX family; Myosins IX (Myo9) is a class of unique motor proteins with a common structure of an N-terminal extension preceding a myosin head homologous to the Ras-association (RA) domain, a head (motor) domain, a neck with IQ motifs that bind light chains, and a C-terminal tail containing cysteine-rich zinc binding (C1) and Rho-GTPase activating protein (RhoGAP) domains. There are two genes for myosins IX in humans, IXa and IXb, that are different in their expression and localization. IXa is expressed abundantly in brain and testis, and IXb is expressed abundantly in tissues of the immune system. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410368  Cd Length: 56  Bit Score: 109.31  E-value: 1.75e-28
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426625 1632 HNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1687
Cdd:cd20818      1 HNGHKFATVQFNIPTYCEVCNSFIWLMEKGLVCQVCKFTCHKKCYSKITAPCKGNS 56
RhoGAP-p50rhoGAP cd04404
RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1700-1887 6.89e-28

RhoGAP-p50rhoGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p50RhoGAP-like proteins; p50RhoGAP, also known as RhoGAP-1, contains a C-terminal RhoGAP domain and an N-terminal Sec14 domain which binds phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3). It is ubiquitously expressed and preferentially active on Cdc42. This subgroup also contains closely related ARHGAP8. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239869 [Multi-domain]  Cd Length: 195  Bit Score: 112.82  E-value: 6.89e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTS---DKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQAL-QTDPaaVKLEDFP-IHAITGVLK 1774
Cdd:cd04404      6 FGVSLQFLKEknpEQEPIPPVVRETVEYLQAHALTTEGIFRRSANTQVVKEVQQKYnMGEP--VDFDQYEdVHLPAVILK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1775 QWLRELPEPLMTFAQYGDFLRAVELPeKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1854
Cdd:cd04404     84 TFLRELPEPLLTFDLYDDIVGFLNVD-KEERVERVKQLLQTLPEENYQVLKYLIKFLVQVSAHSDQNKMTNSNLAVVFGP 162
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1720426625 1855 CLLRCPDNSdplTSMKDVLKITTCVEMLIKEQM 1887
Cdd:cd04404    163 NLLWAKDAS---MSLSAINPINTFTKFLLDHQD 192
RhoGAP_MgcRacGAP cd04382
RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1701-1872 2.16e-27

RhoGAP_MgcRacGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in MgcRacGAP proteins. MgcRacGAP plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling. ii) after phosphorylation by aurora B MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain a N-terminal C1-like domain, and a C-terminal RhoGAP domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239847  Cd Length: 193  Bit Score: 111.23  E-value: 2.16e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1701 GVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLREL 1780
Cdd:cd04382      4 GELADFDPSTSPMIPALIVHCVNEIEARGLTEEGLYRVSGSEREVKALKEKFLRGKTVPNLSKVDIHVICGCLKDFLRSL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1781 PEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDvNRMSPGALAIIFAPCLLRCP 1860
Cdd:cd04382     84 KEPLITFALWKEFMEAAEILDEDNSRAALYQAISELPQPNRDTLAFLILHLQRVAQSPE-CKMDINNLARVFGPTIVGYS 162
                          170
                   ....*....|...
gi 1720426625 1861 D-NSDPLTSMKDV 1872
Cdd:cd04382    163 VpNPDPMTILQDT 175
RhoGAP_GMIP cd04408
RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP ...
1700-1883 5.16e-27

RhoGAP_GMIP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of GMIP (Gem interacting protein). GMIP plays important roles in neurite growth and axonal guidance, and interacts with Gem, a member of the RGK subfamily of the Ras small GTPase superfamily, through the N-terminal half of the protein. GMIP contains a C-terminal RhoGAP domain. GMIP inhibits RhoA function, but is inactive towards Rac1 and Cdc41. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239873  Cd Length: 200  Bit Score: 110.29  E-value: 5.16e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTSD-KASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLR 1778
Cdd:cd04408      1 FGVDFSQLPRDfPEEVPFVVVRCTAEIENRALGVQGIYRISGSKARVEKLCQAFENGRDLVDLSGHSPHDITSVLKHFLK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1779 ELPEPLMTFAQYGDFL-----------RAVELPE-KQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPG 1846
Cdd:cd04408     81 ELPEPVLPFQLYDDFIalakelqrdseKAAESPSiVENIIRSLKELLGRLPVSNYNTLRHLMAHLYRVAERFEDNKMSPN 160
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1720426625 1847 ALAIIFAPCLLRCPDNSD-PLTSMKDVLKITTCVEMLI 1883
Cdd:cd04408    161 NLGIVFGPTLLRPLVGGDvSMICLLDTGYQAQLVEFLI 198
RA_Myosin-IXa cd17216
Ras-associating (RA) domain found in Myosin-IXa; Myosin-IXa, also termed myosin-9a (Myo9a), is ...
19-112 2.00e-26

Ras-associating (RA) domain found in Myosin-IXa; Myosin-IXa, also termed myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Its RA domain is located at its head domain and has the beta-grasp ubiquitin-like fold with unknown function. Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function.


Pssm-ID: 340736  Cd Length: 96  Bit Score: 105.01  E-value: 2.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   19 LHIYPQLSSAGSqTSCRVTATKDSTTSDVIQDVVASLHLDGSKHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRAQDE 98
Cdd:cd17216      4 LRIYPGNIAEGT-IYCPVPARKNTTAAEVIESLINKLQLDKTKCYVLAEVKEFGGEEWILNPTDCPVQRMMLWPRMALEN 82
                           90
                   ....*....|....
gi 1720426625   99 HPQEDGYYFLLQER 112
Cdd:cd17216     83 RFSGEDYRFLLREK 96
RhoGAP_Graf cd04374
RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase ...
1710-1883 2.10e-26

RhoGAP_Graf: GTPase-activator protein (GAP) domain for Rho-like GTPases found in GRAF (GTPase regulator associated with focal adhesion kinase); Graf is a multi-domain protein, containing SH3 and PH domains, that binds focal adhesion kinase and influences cytoskeletal changes mediated by Rho proteins. Graf exhibits GAP activity toward RhoA and Cdc42, but only weakly activates Rac1. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239839  Cd Length: 203  Bit Score: 108.63  E-value: 2.10e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1710 DKASVPIVlEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQAL----QTDPAAVKLE--DFPIHAITGVLKQWLRELPEP 1783
Cdd:cd04374     25 DDIGFKFV-RKCIEAVETRGINEQGLYRVVGVNSKVQKLLSLGldpkTSTPGDVDLDnsEWEIKTITSALKTYLRNLPEP 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1784 LMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNS 1863
Cdd:cd04374    104 LMTYELHNDFINAAKSENLESRVNAIHSLVHKLPEKNREMLELLIKHLTNVSDHSKKNLMTVSNLGVVFGPTLLRPQEET 183
                          170       180
                   ....*....|....*....|
gi 1720426625 1864 dpLTSMKDVLKITTCVEMLI 1883
Cdd:cd04374    184 --VAAIMDIKFQNIVVEILI 201
RhoGAP_p190 cd04373
RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1700-1883 2.65e-26

RhoGAP_p190: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of p190-like proteins. p190, also named RhoGAP5, plays a role in neuritogenesis and axon branch stability. p190 shows a preference for Rho, over Rac and Cdc42, and consists of an N-terminal GTPase domain and a C-terminal GAP domain. The central portion of p190 contains important regulatory phosphorylation sites. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239838  Cd Length: 185  Bit Score: 107.93  E-value: 2.65e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTREL-RQALQTDPAAVKLEDFPIHAITGVLKQWLR 1778
Cdd:cd04373      1 FGVPLANVVTSEKPIPIFLEKCVEFIEATGLETEGIYRVSGNKTHLDSLqKQFDQDHNLDLVSKDFTVNAVAGALKSFFS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1779 ELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLR 1858
Cdd:cd04373     81 ELPDPLIPYSMHLELVEAAKINDREQRLHALKELLKKFPPENFDVFKYVITHLNKVSQNSKVNLMTSENLSICFWPTLMR 160
                          170       180
                   ....*....|....*....|....*..
gi 1720426625 1859 cPD--NSDPLTSMKDVlkiTTCVEMLI 1883
Cdd:cd04373    161 -PDftSMEALSATRIY---QTIIETFI 183
RhoGAP_Bcr cd04387
RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr ...
1700-1871 3.63e-26

RhoGAP_Bcr: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of Bcr (breakpoint cluster region protein)-like proteins. Bcr is a multidomain protein with a variety of enzymatic functions. It contains a RhoGAP and a Rho GEF domain, a Ser/Thr kinase domain, an N-terminal oligomerization domain, and a C-terminal PDZ binding domain, in addition to PH and C2 domains. Bcr is a negative regulator of: i) RacGTPase, via the Rho GAP domain, ii) the Ras-Raf-MEK-ERK pathway, via phosphorylation of the Ras binding protein AF-6, and iii) the Wnt signaling pathway through binding beta-catenin. Bcr can form a complex with beta-catenin and Tcf1. The Wnt signaling pathway is involved in cell proliferation, differentiation, and cell renewal. Bcr was discovered as a fusion partner of Abl. The Bcr-Abl fusion is characteristic for a large majority of chronic myelogenous leukemias (CML). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239852 [Multi-domain]  Cd Length: 196  Bit Score: 107.71  E-value: 3.63e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTSDKAS-VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTD--PAAVKLEDFPIHAITGVLKQW 1776
Cdd:cd04387      1 FGVKISTVTKRERSkVPYIVRQCVEEVERRGMEEVGIYRISGVATDIQALKAAFDTNnkDVSVMLSEMDVNAIAGTLKLY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1777 LRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCL 1856
Cdd:cd04387     81 FRELPEPLFTDELYPNFAEGIALSDPVAKESCMLNLLLSLPDPNLVTFLFLLHHLKRVAEREEVNKMSLHNLATVFGPTL 160
                          170
                   ....*....|....*..
gi 1720426625 1857 LRCP--DNSDPLTSMKD 1871
Cdd:cd04387    161 LRPSekESKIPTNTMTD 177
RhoGAP_CdGAP cd04384
RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1714-1860 2.58e-24

RhoGAP_CdGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of CdGAP-like proteins; CdGAP contains an N-terminal RhoGAP domain and a C-terminal proline-rich region, and it is active on both Cdc42 and Rac1 but not RhoA. CdGAP is recruited to focal adhesions via the interaction with the scaffold protein actopaxin (alpha-parvin). Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239849 [Multi-domain]  Cd Length: 195  Bit Score: 102.58  E-value: 2.58e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1714 VPIVLEKLLEHVEMHGLYTeGLYRKSGAANRTRELRQALQTDpAAVKLEDFP----IHAITGVLKQWLRELPEPLMTFAQ 1789
Cdd:cd04384     18 VPQVLKSCTEFIEKHGIVD-GIYRLSGIASNIQRLRHEFDSE-QIPDLTKDVyiqdIHSVSSLCKLYFRELPNPLLTYQL 95
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720426625 1790 YGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCP 1860
Cdd:cd04384     96 YEKFSEAVSAASDEERLEKIHDVIQQLPPPHYRTLEFLMRHLSRLAKYCSITNMHAKNLAIVWAPNLLRSK 166
RhoGAP_ARHGAP18 cd04391
RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1700-1886 5.10e-24

RhoGAP_ARHGAP18: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP18-like proteins. The function of ArhGAP18 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239856  Cd Length: 216  Bit Score: 102.42  E-value: 5.10e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSL------TSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTD--PAAVKLEDFPIHAITG 1771
Cdd:cd04391      2 FGVPLSTLlerdqkKVPGSKVPLIFQKLINKLEERGLETEGILRIPGSAQRVKFLCQELEAKfyEGTFLWDQVKQHDAAS 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1772 VLKQWLRELPEPLMTfAQYGDFLRAVE-LPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAI 1850
Cdd:cd04391     82 LLKLFIRELPQPLLT-VEYLPAFYSVQgLPSKKDQLQALNLLVLLLPEANRDTLKALLEFLQKVVDHEEKNKMNLWNVAM 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1720426625 1851 IFAPCLLRC--PDNSDPLTSMKDVLKITTC---VEMLIKEQ 1886
Cdd:cd04391    161 IMAPNLFPPrgKHSKDNESLQEEVNMAAGCaniMRLLIRYQ 201
RhoGAP-ARHGAP11A cd04394
RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1700-1883 2.36e-23

RhoGAP-ARHGAP11A: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP11A-like proteins. The mouse homolog of human ArhGAP11A has been detected as a gene exclusively expressed in immature ganglion cells, potentially playing a role in retinal development. The exact function of ArhGAP11A is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239859 [Multi-domain]  Cd Length: 202  Bit Score: 99.85  E-value: 2.36e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLT----SDKASVPIVLEKLLEHVEMHgLYTEGLYRKSGAANRTRELRqaLQTDPAAVKLEDFPIHAITGVLKQ 1775
Cdd:cd04394      2 FGVPLHSLPhstvPEYGNVPKFLVDACTFLLDH-LSTEGLFRKSGSVVRQKELK--AKLEGGEACLSSALPCDVAGLLKQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1776 WLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPC 1855
Cdd:cd04394     79 FFRELPEPLLPYDLHEALLKAQELPTDEERKSATLLLTCLLPDEHVNTLRYFFSFLYDVAQRCSENKMDSSNLAVIFAPN 158
                          170       180       190
                   ....*....|....*....|....*....|
gi 1720426625 1856 LLRCPDNSDPLTS--MKDVLKITTCVEMLI 1883
Cdd:cd04394    159 LFQSEEGGEKMSSstEKRLRLQAAVVQTLI 188
RhoGAP_ARHGAP22_24_25 cd04390
RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1714-1885 3.37e-23

RhoGAP_ARHGAP22_24_25: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ARHGAP22, 24 and 25-like proteins; longer isoforms of these proteins contain an additional N-terminal pleckstrin homology (PH) domain. ARHGAP25 (KIA0053) has been identified as a GAP for Rac1 and Cdc42. Short isoforms (without the PH domain) of ARHGAP24, called RC-GAP72 and p73RhoGAP, and of ARHGAP22, called p68RacGAP, has been shown to be involved in angiogenesis and endothelial cell capillary formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239855 [Multi-domain]  Cd Length: 199  Bit Score: 99.44  E-value: 3.37e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1714 VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1793
Cdd:cd04390     22 VPILVEQCVDFIREHGLKEEGLFRLPGQANLVKQLQDAFDAGERPSFDSDTDVHTVASLLKLYLRELPEPVIPWAQYEDF 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1794 LRAVELPEKQEQ--LSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRcPDNSDPLTSMKD 1871
Cdd:cd04390    102 LSCAQLLSKDEEkgLGELMKQVSILPKVNYNLLSYICRFLDEVQSNSSVNKMSVQNLATVFGPNILR-PKVEDPATIMEG 180
                          170
                   ....*....|....
gi 1720426625 1872 VLKITTCVEMLIKE 1885
Cdd:cd04390    181 TPQIQQLMTVMISK 194
RhoGAP_PARG1 cd04409
RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1714-1884 2.86e-22

RhoGAP_PARG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of PARG1 (PTPL1-associated RhoGAP1). PARG1 was originally cloned as an interaction partner of PTPL1, an intracellular protein-tyrosine phosphatase. PARG1 interacts with Rap2, also a member of the Ras small GTPase superfamily whose exact function is unknown, and shows strong preference for Rho. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239874  Cd Length: 211  Bit Score: 97.19  E-value: 2.86e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1714 VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDF 1793
Cdd:cd04409     16 IPFIIKKCTSEIESRALCLKGIYRVNGAKSRVEKLCQAFENGKDLVELSELSPHDISNVLKLYLRQLPEPLILFRLYNEF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1794 L-------------RAVELPEKQEQ---------LSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAII 1851
Cdd:cd04409     96 IglakesqhvnetqEAKKNSDKKWPnmctelnriLLKSKDLLRQLPAPNYNTLQFLIVHLHRVSEQAEENKMSASNLGII 175
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1720426625 1852 FAPCLLRcPDNSDP---LTSMKDVLKITTCVEMLIK 1884
Cdd:cd04409    176 FGPTLIR-PRPTDAtvsLSSLVDYPHQARLVELLIT 210
RhoGAP_ARHGAP6 cd04376
RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1713-1883 1.66e-21

RhoGAP_ARHGAP6: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP6-like proteins. ArhGAP6 shows GAP activity towards RhoA, but not towards Cdc42 and Rac1. ArhGAP6 is often deleted in microphthalmia with linear skin defects syndrome (MLS); MLS is a severe X-linked developmental disorder. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239841  Cd Length: 206  Bit Score: 94.81  E-value: 1.66e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1713 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGD 1792
Cdd:cd04376      8 QVPRLVESCCQHLEKHGLQTVGIFRVGSSKKRVRQLREEFDRGIDVVLDENHSVHDVAALLKEFFRDMPDPLLPRELYTA 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1793 FLRAVELpEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVAL-LEDV----------NRMSPGALAIIFAPCLLRCPD 1861
Cdd:cd04376     88 FIGTALL-EPDEQLEALQLLIYLLPPCNCDTLHRLLKFLHTVAEhAADSidedgqevsgNKMTSLNLATIFGPNLLHKQK 166
                          170       180
                   ....*....|....*....|....*..
gi 1720426625 1862 NSDPLTS-----MKDVLKITTCVEMLI 1883
Cdd:cd04376    167 SGEREFVqaslrIEESTAIINVVQTMI 193
RhoGAP_FAM13A1a cd04393
RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1700-1876 4.07e-21

RhoGAP_FAM13A1a: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of FAM13A1, isoform a-like proteins. The function of FAM13A1a is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by up several orders of magnitude.


Pssm-ID: 239858 [Multi-domain]  Cd Length: 189  Bit Score: 92.91  E-value: 4.07e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLTSD---KASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQW 1776
Cdd:cd04393      3 FGVPLQELQQAgqpENGVPAVVRHIVEYLEQHGLEQEGLFRVNGNAETVEWLRQRLDSGEEVDLSKEADVCSAASLLRLF 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1777 LRELPEPLMTFAQYGDFLRAV-ELPEKQEQLSAIYAVLDHLPEANHtSLERLIFH-LVKVALLEDVNRMSPGALAIIFAP 1854
Cdd:cd04393     83 LQELPEGLIPASLQIRLMQLYqDYNGEDEFGRKLRDLLQQLPPVNY-SLLKFLCHfLSNVASQHHENRMTAENLAAVFGP 161
                          170       180
                   ....*....|....*....|..
gi 1720426625 1855 CLLRCPDNSDPLTSMKDVLKIT 1876
Cdd:cd04393    162 DVFHVYTDVEDMKEQEICSRIM 183
RhoGAP_ARHGAP19 cd04392
RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1720-1891 6.33e-21

RhoGAP_ARHGAP19: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ArhGAP19-like proteins. The function of ArhGAP19 is unknown. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239857  Cd Length: 208  Bit Score: 93.29  E-value: 6.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1720 KLLEHVEMHgLYTEGLYRKSGAANRTRELRQALQTD-PAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFLRAVE 1798
Cdd:cd04392     15 QLIEYLEKN-LRVEGLFRKPGNSARQQELRDLLNSGtDLDLESGGFHAHDCATVLKGFLGELPEPLLTHAHYPAHLQIAD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1799 L------------PEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLrCPDNSDPL 1866
Cdd:cd04392     94 LcqfdekgnktsaPDKERLLEALQLLLLLLPEENRNLLKLILDLLYQTAKHEDKNKMSADNLALLFTPHLI-CPRNLTPE 172
                          170       180
                   ....*....|....*....|....*
gi 1720426625 1867 TSMKDVLKITTCVEMLIKEQMRKYK 1891
Cdd:cd04392    173 DLHENAQKLNSIVTFMIKHSQKLFK 197
RhoGAP_fBEM3 cd04400
RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of ...
1713-1856 3.41e-20

RhoGAP_fBEM3: RhoGAP (GTPase-activator [GAP] protein for Rho-like small GTPases) domain of fungal BEM3-like proteins. Bem3 is a GAP protein of Cdc42, and is specifically involved in the control of the initial assembly of the septin ring in yeast bud formation. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239865 [Multi-domain]  Cd Length: 190  Bit Score: 90.50  E-value: 3.41e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1713 SVPIVLEKLLEHVEMHG-LYTEGLYRKSGAANRTRELRQALQTDPAAVKLED---FPIHAITGVLKQWLRELPEPLMTFA 1788
Cdd:cd04400     21 DLPSVVYRCIEYLDKNRaIYEEGIFRLSGSASVIKQLKERFNTEYDVDLFSSslyPDVHTVAGLLKLYLRELPTLILGGE 100
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720426625 1789 QYGDFLRAVELPEKQEQLSAIYAVL-DHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCL 1856
Cdd:cd04400    101 LHNDFKRLVEENHDRSQRALELKDLvSQLPQANYDLLYVLFSFLRKIIEHSDVNKMNLRNVCIVFSPTL 169
RhoGAP_KIAA1688 cd04389
RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in ...
1714-1884 2.30e-19

RhoGAP_KIAA1688: GTPase-activator protein (GAP) domain for Rho-like GTPases found in KIAA1688-like proteins; KIAA1688 is a protein of unknown function that contains a RhoGAP domain and a myosin tail homology 4 (MyTH4) domain. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239854  Cd Length: 187  Bit Score: 87.83  E-value: 2.30e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1714 VPIVLEKLLEHV-EMHGLYTEGLYRKSGAANRTRELRqaLQTDPAAV---KLEDfpIHAITGVLKQWLRELPEPLMTFAQ 1789
Cdd:cd04389     21 LPWILTFLSEKVlALGGFQTEGIFRVPGDIDEVNELK--LRVDQWDYplsGLED--PHVPASLLKLWLRELEEPLIPDAL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1790 YGDFLRAVELPEKqeqlsaIYAVLDHLPEANHTSLERLIfHLVKVALLEDV---NRMSPGALAIIFAPCLLRCpDNSDPL 1866
Cdd:cd04389     97 YQQCISASEDPDK------AVEIVQKLPIINRLVLCYLI-NFLQVFAQPENvahTKMDVSNLAMVFAPNILRC-TSDDPR 168
                          170
                   ....*....|....*...
gi 1720426625 1867 TSMKDVLKITTCVEMLIK 1884
Cdd:cd04389    169 VIFENTRKEMSFLRTLIE 186
C1_Myosin-IXa cd20883
protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar ...
1630-1684 2.55e-19

protein kinase C conserved region 1 (C1 domain) found in unconventional myosin-IXa and similar proteins; Myosin-IXa, also called unconventional myosin-9a (Myo9a), is a single-headed, actin-dependent motor protein of the unconventional myosin IX class. It is expressed in several tissues and is enriched in the brain and testes. Myosin-IXa contains a Ras-associating (RA) domain, a motor domain, a protein kinase C conserved region 1 (C1), and a Rho GTPase activating domain (RhoGAP). Myosin-IXa binds the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor (AMPAR) GluA2 subunit, and plays a key role in controlling the molecular structure and function of hippocampal synapses. Moreover, Myosin-IXa functions in epithelial cell morphology and differentiation, such that its knockout mice develop hydrocephalus and kidney dysfunction. Myosin-IXa regulates collective epithelial cell migration by targeting RhoGAP activity to cell-cell junctions. Myosin-IXa negatively regulates Rho GTPase signaling, and functions as a regulator of kidney tubule function. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410433  Cd Length: 58  Bit Score: 83.48  E-value: 2.55e-19
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720426625 1630 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20883      1 EEHNGHIFKSTQYSIPTYCEYCSSLIWMMDRAYVCKLCRYACHKKCCLKTTTKCS 55
RhoGap_RalBP1 cd04381
RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1700-1856 9.44e-19

RhoGap_RalBP1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in RalBP1 proteins, also known as RLIP, RLIP76 or cytocentrin. RalBP1 plays an important role in endocytosis during interphase. During mitosis, RalBP1 transiently associates with the centromere and has been shown to play an essential role in the proper assembly of the mitotic apparatus. RalBP1 is an effector of the Ral GTPase which itself is an effector of Ras. RalBP1 contains a RhoGAP domain, which shows weak activity towards Rac1 and Cdc42, but not towards Ral, and a Ral effector domain binding motif. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239846 [Multi-domain]  Cd Length: 182  Bit Score: 85.95  E-value: 9.44e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVD-----SLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRqALQTDPAAVKLEDFPIHAITGVLK 1774
Cdd:cd04381      1 FGASLSlaverSRCHDGIDLPLVFRECIDYVEKHGMKCEGIYKVSGIKSKVDELK-AAYNRRESPNLEEYEPPTVASLLK 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1775 QWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAP 1854
Cdd:cd04381     80 QYLRELPEPLLTKELMPRFEEACGRPTEAEREQELQRLLKELPECNRLLLAWLIVHMDHVIAQELETKMNIQNISIVLSP 159

                   ..
gi 1720426625 1855 CL 1856
Cdd:cd04381    160 TV 161
RhoGAP_DLC1 cd04375
RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1700-1856 2.76e-18

RhoGAP_DLC1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of DLC1-like proteins. DLC1 shows in vitro GAP activity towards RhoA and CDC42. Beside its C-terminal GAP domain, DLC1 also contains a SAM (sterile alpha motif) and a START (StAR-related lipid transfer action) domain. DLC1 has tumor suppressor activity in cell culture. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239840  Cd Length: 220  Bit Score: 85.93  E-value: 2.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVD-SLTSDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVKLEDFPIHAITGVLKQWLR 1778
Cdd:cd04375      5 FGVPLLvNLQRTGQPLPRSIQQAMRWLRNNALDQVGLFRKSGVKSRIQKLRSMIESSTDNVNYDGQQAYDVADMLKQYFR 84
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720426625 1779 ELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCL 1856
Cdd:cd04375     85 DLPEPLLTNKLSETFIAIFQYVPKEQRLEAVQCAILLLPDENREVLQTLLYFLSDVAANSQENQMTATNLAVCLAPSL 162
RhoGAP_p85 cd04388
RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present ...
1715-1865 4.80e-18

RhoGAP_p85: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in the p85 isoforms of the regulatory subunit of the class IA PI3K (phosphatidylinositol 3'-kinase). This domain is also called Bcr (breakpoint cluster region protein) homology (BH) domain. Class IA PI3Ks are heterodimers, containing a regulatory subunit (p85) and a catalytic subunit (p110) and are activated by growth factor receptor tyrosine kinases (RTKs); this activation is mediated by the p85 subunit. p85 isoforms, alpha and beta, contain a C-terminal p110-binding domain flanked by two SH2 domains, an N-terminal SH3 domain, and a RhoGAP domain flanked by two proline-rich regions. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239853  Cd Length: 200  Bit Score: 84.54  E-value: 4.80e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1715 PIVLEKLLEHVEMHGLYTEGLYRKSGAANRTrELRQALQTDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYGDFL 1794
Cdd:cd04388     16 PPLLIKLVEAIEKKGLESSTLYRTQSSSSLT-ELRQILDCDAASVDLEQFDVAALADALKRYLLDLPNPVIPAPVYSEMI 94
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426625 1795 RA---VELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDP 1865
Cdd:cd04388     95 SRaqeVQSSDEYAQLLRKLIRSPNLPHQYWLTLQYLLKHFFRLCQSSSKNLLSARALAEIFSPLLFRFQPASSD 168
RhoGAP_srGAP cd04383
RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1714-1865 7.42e-17

RhoGAP_srGAP: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in srGAPs. srGAPs are components of the intracellular part of Slit-Robo signalling pathway that is important for axon guidance and cell migration. srGAPs contain an N-terminal FCH domain, a central RhoGAP domain and a C-terminal SH3 domain; this SH3 domain interacts with the intracellular proline-rich-tail of the Roundabout receptor (Robo). This interaction with Robo then activates the rhoGAP domain which in turn inhibits Cdc42 activity. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239848  Cd Length: 188  Bit Score: 80.93  E-value: 7.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1714 VPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQ--TDPAAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQYG 1791
Cdd:cd04383     18 IPLVVESCIRFINLYGLQHQGIFRVSGSQVEVNDIKNAFErgEDPLADDQNDHDINSVAGVLKLYFRGLENPLFPKERFE 97
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720426625 1792 DFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNSDP 1865
Cdd:cd04383     98 DLMSCVKLENPTERVHQIREILSTLPRSVIIVMRYLFAFLNHLSQFSDENMMDPYNLAICFGPTLMPVPEGQDQ 171
RA pfam00788
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-114 1.40e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Recent evidence (not yet in MEDLINE) shows that some RA domains do NOT bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase.


Pssm-ID: 425871  Cd Length: 93  Bit Score: 73.91  E-value: 1.40e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   15 ATYHLHIYPQLSSAGSqTSCRVTATKDSTTSDVIQDVVASLHLDGSK-HYVLVEVKESGGEEWVLDASDSPVHRVLLWPR 93
Cdd:pfam00788    1 DDGVLKVYTEDGKPGT-TYKTILVSSSTTAEEVIEALLEKFGLEDDPrDYVLVEVLERGGGERRLPDDECPLQIQLQWPR 79
                           90       100
                   ....*....|....*....|.
gi 1720426625   94 RAQDehpqedgYYFLLQERNA 114
Cdd:pfam00788   80 DASD-------SRFLLRKRDD 93
RA smart00314
Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); ...
15-113 7.24e-15

Ras association (RalGDS/AF-6) domain; RasGTP effectors (in cases of AF6, canoe and RalGDS); putative RasGTP effectors in other cases. Kalhammer et al. have shown that not all RA domains bind RasGTP. Predicted structure similar to that determined, and that of the RasGTP-binding domain of Raf kinase. Predicted RA domains in PLC210 and nore1 found to bind RasGTP. Included outliers (Grb7, Grb14, adenylyl cyclases etc.)


Pssm-ID: 214612  Cd Length: 90  Bit Score: 71.95  E-value: 7.24e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625    15 ATYHLHIYPQLSSagSQTSCRVTATKDSTTSDVIQDVVASLHLDGS-KHYVLVEVKEsGGEEWVLDASDSPVHRVLLWPR 93
Cdd:smart00314    1 DTFVLRVYVDDLP--GGTYKTLRVSSRTTARDVIQQLLEKFHLTDDpEEYVLVEVLP-DGKERVLPDDENPLQLQKLWPR 77
                            90       100
                    ....*....|....*....|
gi 1720426625    94 RaqdehpqEDGYYFLLQERN 113
Cdd:smart00314   78 R-------GPNLRFVLRKRD 90
RhoGAP_fLRG1 cd04397
RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1691-1883 1.73e-13

RhoGAP_fLRG1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal LRG1-like proteins. Yeast Lrg1p is required for efficient cell fusion, and mother-daughter cell separation, possibly through acting as a RhoGAP specifically regulating 1,3-beta-glucan synthesis. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239862  Cd Length: 213  Bit Score: 71.63  E-value: 1.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1691 SELGAEPGHFgvcvdsltsdkaSVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDPAAVK--LEDFPIHa 1768
Cdd:cd04397     16 STLGVGPGKL------------RIPALIDDIISAMRQMDMSVEGVFRKNGNIRRLKELTEEIDKNPTEVPdlSKENPVQ- 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1769 ITGVLKQWLRELPEPLMTFAQYGDFLRAVELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKVALLEDV-----NRM 1843
Cdd:cd04397     83 LAALLKKFLRELPDPLLTFKLYRLWISSQKIEDEEERKRVLHLVYCLLPKYHRDTMEVLFSFLKWVSSFSHIdeetgSKM 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1720426625 1844 SPGALAIIFAPCLLRcPDNSDPLTSMKDVLKITTcVEMLI 1883
Cdd:cd04397    163 DIHNLATVITPNILY-SKTDNPNTGDEYFLAIEA-VNYLI 200
RhoGAP_fSAC7_BAG7 cd04396
RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1713-1861 6.11e-13

RhoGAP_fSAC7_BAG7: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal SAC7 and BAG7-like proteins. Both proteins are GTPase activating proteins of Rho1, but differ functionally in vivo: SAC7, but not BAG7, is involved in the control of Rho1-mediated activation of the PKC-MPK1 pathway. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239861  Cd Length: 225  Bit Score: 70.52  E-value: 6.11e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1713 SVPIVLEKLLEHVEMHGLYTEGLYRKSGAANRTRELRQALQTDP---AAVKLEDFPIHAITGVLKQWLRELPEPLMTFAQ 1789
Cdd:cd04396     31 YIPVVVAKCGVYLKENATEVEGIFRVAGSSKRIRELQLIFSTPPdygKSFDWDGYTVHDAASVLRRYLNNLPEPLVPLDL 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1790 YGDFLRAVE----------------LPEKQEQLSAIY-AVLDHLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIF 1852
Cdd:cd04396    111 YEEFRNPLRkrprilqymkgrinepLNTDIDQAIKEYrDLITRLPNLNRQLLLYLLDLLAVFARNSDKNLMTASNLAAIF 190

                   ....*....
gi 1720426625 1853 APCLLRCPD 1861
Cdd:cd04396    191 QPGILSHPD 199
C1 smart00109
Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol ...
1635-1683 2.10e-12

Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains); Some bind phorbol esters and diacylglycerol. Some bind RasGTP. Zinc-binding domains.


Pssm-ID: 197519  Cd Length: 50  Bit Score: 63.64  E-value: 2.10e-12
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|
gi 1720426625  1635 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:smart00109    1 HKHVFRTFTKPTFCCVCRKSIWGSFKqGLRCSECKVKCHKKCADKVPKAC 50
C1 cd00029
protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich ...
1635-1683 8.28e-12

protein kinase C conserved region 1 (C1 domain) superfamily; The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains. It contains the motif HX12CX2CXnCX2CX4HX2CX7C, where C and H are cysteine and histidine, respectively; X represents other residues; and n is either 13 or 14. C1 has a globular fold with two separate Zn(2+)-binding sites. It was originally discovered as lipid-binding modules in protein kinase C (PKC) isoforms. C1 domains that bind and respond to phorbol esters (PE) and diacylglycerol (DAG) are referred to as typical, and those that do not respond to PE and DAG are deemed atypical. A C1 domain may also be referred to as PKC or non-PKC C1, based on the parent protein's activity. Most C1 domain-containing non-PKC proteins act as lipid kinases and scaffolds, except PKD which acts as a protein kinase. PKC C1 domains play roles in membrane translocation and activation of the enzyme.


Pssm-ID: 410341  Cd Length: 50  Bit Score: 61.76  E-value: 8.28e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd00029      1 HRFVPTTFSSPTFCDVCGKLIWgLFKQGLKCSDCGLVCHKKCLDKAPSPC 50
C1_PDZD8 cd20825
protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 ...
1632-1685 2.65e-11

protein kinase C conserved region 1 (C1 domain) found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZD8, also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondrial membranes. PDZD8-dependent ER-mitochondria membrane tethering is essential for ER-mitochondria Ca2+ transfer. In neurons, it is involved in the regulation of dendritic Ca2+ dynamics by regulating mitochondrial Ca2+ uptake. PDZD8 also plays an indirect role in the regulation of cell morphology and cytoskeletal organization. It contains a PDZ domain and a C1 domain. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410375  Cd Length: 55  Bit Score: 60.37  E-value: 2.65e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426625 1632 HNGHVFASYQVNIPQSCEQCLSYIWLMDkALLCSVCKMTCHKKCVHKIQ--SYCSY 1685
Cdd:cd20825      1 EGKHDFVLTQFQNATYCDFCKKKIWLKE-AFQCRLCGMICHKKCLDKCQaeTLCTR 55
RA cd17043
Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA ...
19-99 9.71e-10

Ras-associating (RA) domain, structurally similar to a beta-grasp ubiquitin-like fold; RA domain-containing proteins function by interacting with Ras proteins directly or indirectly and are involved in various functions ranging from tumor suppression to being oncoproteins. Ras proteins are small GTPases that are involved in cellular signal transduction. The RA domain has the beta-grasp ubiquitin-like (Ubl) fold with low sequence similarity to ubiquitin (Ub); Ub is a protein modifier in eukaryotes that is involved in various cellular processes, including transcriptional regulation, cell cycle control, and DNA repair. RA-containing proteins include RalGDS, AF6, RIN, RASSF1, SNX27, CYR1, STE50, and phospholipase C epsilon.


Pssm-ID: 340563  Cd Length: 87  Bit Score: 56.94  E-value: 9.71e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625   19 LHIYPQlSSAGSQTSCRVTATKDSTTSDVIQDVVASLHLDGS-KHYVLVEVKESGGEEWVLDASDSPVHRVLLWPRRAQD 97
Cdd:cd17043      2 LKVYDD-DLAPGSAYKSILVSSTTTAREVVQLLLEKYGLEEDpEDYSLYEVSEKQETERVLHDDECPLLIQLEWGPQGTE 80

                   ..
gi 1720426625   98 EH 99
Cdd:cd17043     81 FR 82
C1_TNS2-like cd20826
protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; ...
1634-1684 1.54e-09

protein kinase C conserved region 1 (C1 domain) found in tensin-2 like (TNS2-like) proteins; The TNS2-like group includes TNS2, and variants of TNS1 and TNS3. Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity and interferes with AKT1 signaling. Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. Typical TNS1 and TNS3 do not contain C1 domains, but some isoforms/variants do. Members of this family contain an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410376  Cd Length: 52  Bit Score: 55.47  E-value: 1.54e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720426625 1634 GHVFASYQVNIPQSCEQCLSYIWlmDKALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20826      2 SHSFKEKSFRKPRTCDVCKQIIW--NEGSSCRVCKYACHRKCEPKVTAACS 50
RhoGAP_OCRL1 cd04380
RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain ...
1713-1863 1.28e-08

RhoGAP_OCRL1: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain present in OCRL1-like proteins. OCRL1 (oculocerebrorenal syndrome of Lowe 1)-like proteins contain two conserved domains: a central inositol polyphosphate 5-phosphatase domain and a C-terminal Rho GAP domain, this GAP domain lacks the catalytic residue and therefore maybe inactive. OCRL-like proteins are type II inositol polyphosphate 5-phosphatases that can hydrolyze lipid PI(4,5)P2 and PI(3,4,5)P3 and soluble Ins(1,4,5)P3 and Ins(1,3,4,5)P4, but their individual specificities vary. The functionality of the RhoGAP domain is still unclear. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239845  Cd Length: 220  Bit Score: 57.35  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1713 SVPIVLEKLLEHVEMHGLYTEGLYRKSG----AANRTRELRQALQTDPAAVKLedFPIHAITGVLKQWLRELPEPLMTFA 1788
Cdd:cd04380     49 SIPKEIWRLVDYLYTRGLAQEGLFEEPGlpsePGELLAEIRDALDTGSPFNSP--GSAESVAEALLLFLESLPDPIIPYS 126
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426625 1789 QYGDFLRAVELPEKQeqlsaIYAVLD-HLPEANHTSLERLIFHLVKVALLEDVNRMSPGALAIIFAPCLLRCPDNS 1863
Cdd:cd04380    127 LYERLLEAVANNEED-----KRQVIRiSLPPVHRNVFVYLCSFLRELLSESADRGLDENTLATIFGRVLLRDPPRA 197
C1_SpBZZ1-like cd20824
protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein ...
1635-1684 1.13e-07

protein kinase C conserved region 1 (C1 domain) found in Schizosaccharomyces pombe protein BZZ1 and similar proteins; BZZ1 is a syndapin-like F-BAR protein that plays a role in endocytosis and trafficking to the vacuole. It functions with type I myosins to restore polarity of the actin cytoskeleton after NaCl stress. BZZ1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. Schizosaccharomyces pombe BZZ1 also harbors a C1 domain, but Saccharomyces cerevisiae BZZ1 doesn't have any. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410374  Cd Length: 53  Bit Score: 50.01  E-value: 1.13e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20824      2 HNFKPHSFSIPTKCDYCGEKIWgLSKKGLSCKDCGFNCHIKCELKVPPECP 52
C1_DEF8 cd20819
protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 ...
1633-1683 1.24e-07

protein kinase C conserved region 1 (C1 domain) found in differentially expressed in FDCP 8 (DEF-8) and similar proteins; DEF-8 positively regulates lysosome peripheral distribution and ruffled border formation in osteoclasts. It is involved in bone resorption. DEF-8 contains a protein kinase C conserved region 1 (C1) domain followed by a putative zinc-RING and/or ribbon. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410369  Cd Length: 62  Bit Score: 50.36  E-value: 1.24e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720426625 1633 NGHVFASYQVNIP--QSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20819      4 LGHHFVLQKSKSSskQYCDKCCGIIWgLLQTWYRCTDCGYRCHSKCLNSITRTC 57
C1_1 pfam00130
Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the ...
1635-1683 2.34e-07

Phorbol esters/diacylglycerol binding domain (C1 domain); This domain is also known as the Protein kinase C conserved region 1 (C1) domain.


Pssm-ID: 395079  Cd Length: 53  Bit Score: 49.36  E-value: 2.34e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:pfam00130    1 HHFVHRNFKQPTFCDHCGEFLWGLGKqGLKCSWCKLNVHKRCHEKVPPEC 50
C1_ARHGEF-like cd20832
protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine ...
1634-1684 4.97e-07

protein kinase C conserved region 1 (C1 domain) found in uncharacterized Rho guanine nucleotide exchange factor (ARHGEF)-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate Rho guanine nucleotide exchange factors ARHGEF11 and ARHGEF12, which may play a role in the regulation of RhoA GTPase by guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Unlike typical ARHGEF11 and ARHGEF12, members of this family contain a C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410382  Cd Length: 53  Bit Score: 48.14  E-value: 4.97e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720426625 1634 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20832      1 GHQFVLQHYYQVTFCNHCSGLLWgIGYQGYQCSDCEFNIHKQCIEVIEESCP 52
C1_ScPKC1-like_rpt1 cd20822
first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
1633-1683 1.31e-06

first protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410372  Cd Length: 52  Bit Score: 46.90  E-value: 1.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720426625 1633 NGHVFAS---YQVNipqSCEQCLSYiwLMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20822      1 RGHKFVQkqfYQIM---RCAVCGEF--LVNAGYQCEDCKYTCHKKCYEKVVTKC 49
C1_RASSF1-like cd20820
protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing ...
1634-1683 1.63e-06

protein kinase C conserved region 1 (C1 domain) found in the Ras association domain-containing protein 1 (RASSF1)-like family; The RASSF1-like family includes RASSF1 and RASSF5. RASSF1 and RASSF5 are members of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1; both are localized to microtubules and involved in the regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. RASSF1 and RASSF5 contain a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410370  Cd Length: 52  Bit Score: 46.67  E-value: 1.63e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720426625 1634 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20820      1 GHRFVPLELEQPTWCDLCGSVILgLFRKCLRCANCKMTCHPRCRSLVCLTC 51
C1_RASSF1 cd20885
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
1632-1684 2.34e-06

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 1 (RASSF1) and similar proteins; RASSF1 is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. RASSF1 has eight transcripts (A-H) arising from alternative splicing and differential promoter usage. RASSF1A and 1C are the most extensively studied RASSF1 with both localized to microtubules and involved in regulation of growth and migration. RASSF1 is a potential tumor suppressor that is required for death receptor-dependent apoptosis. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410435  Cd Length: 54  Bit Score: 46.49  E-value: 2.34e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720426625 1632 HNGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20885      1 GEGHDFQPCSLTNPTWCDLCGDFIWgLYKQCLRCTHCKYTCHLRCRDLVTLDCS 54
C1_nPKC_theta-like_rpt1 cd20834
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1629-1687 4.00e-06

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410384  Cd Length: 61  Bit Score: 46.16  E-value: 4.00e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1629 VQEHNGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYTG 1687
Cdd:cd20834      2 VHEVKGHEFIAKFFRQPTFCSVCKEFLWgFNKQGYQCRQCNAAVHKKCHDKILGKCPGSA 61
C1_DGKtheta_typeV_rpt1 cd20803
first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, ...
1634-1684 5.52e-06

first protein kinase C conserved region 1 (C1 domain) found in type V diacylglycerol kinase, DAG kinase theta, and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase theta, also called diglyceride kinase theta (DGK-theta), is the only isoform classified as type V; it contains a pleckstrin homology (PH)-like domain and an additional C1 domain, compared to other DGKs. It may regulate the activity of protein kinase C by controlling the balance between the two signaling lipids, diacylglycerol and phosphatidic acid. DAG kinase theta contains three copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410353  Cd Length: 56  Bit Score: 45.38  E-value: 5.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720426625 1634 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20803      1 GHSFRKKTFHKPTYCHHCTDLLWgLLNQGYQCEVCNFVSHERCLKTVVTPCS 52
C1_GMIP-like cd20816
protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP) ...
1633-1684 5.65e-06

protein kinase C conserved region 1 (C1 domain) found in the GEM-interacting protein (GMIP)-like family; The GMIP-like family includes GMIP, Rho GTPase-activating protein 29 (ARHGAP29) and Rho GTPase-activating protein 45 (ARHGAP45). GMIP is a RhoA-specific GTPase-activating protein that acts as a key factor in saltatory neuronal migration. It associates with the Rab27a effector JFC1 and modulates vesicular transport and exocytosis. ARHGAP29, also called PTPL1-associated RhoGAP protein 1 (PARG1) or Rho-type GTPase-activating protein 29, is a GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state. It has strong activity toward RHOA, and weaker activity toward RAC1 and CDC42. ARHGAP29 may act as a specific effector of RAP2A to regulate Rho. In concert with RASIP1, ARHGAP29 suppresses RhoA signaling and dampens ROCK and MYH9 activities in endothelial cells and plays an essential role in blood vessel tubulogenesis. ARHGAP45, also called minor histocompatibility antigen HA-1 (mHag HA-1), is a Rac-GAP (GTPase-Activating Protein) in endothelial cells. It acts as a novel regulator of endothelial integrity. ARHGAP45 contains a GTPase activator for the Rho-type GTPases (RhoGAP) domain that would be able to negatively regulate the actin cytoskeleton as well as cell spreading. However, it also contains N-terminally a BAR-domin which can play an autoinhibitory effect on this RhoGAP activity. Members of this family contain a zinc-binding C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410366  Cd Length: 51  Bit Score: 45.33  E-value: 5.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720426625 1633 NGHVFAsyQVNIPQSCEQCLSYIWLmdKALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20816      1 QTHRFR--RLRTPSKCRECDSYVYF--NGAECEECGLACHKKCLETLAIQCG 48
C1_MgcRacGAP cd20821
protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and ...
1635-1675 7.15e-06

protein kinase C conserved region 1 (C1 domain) found in male germ cell RacGap (MgcRacGAP) and similar proteins; MgcRacGAP, also called Rac GTPase-activating protein 1 (RACGAP1) or protein CYK4, plays an important dual role in cytokinesis: i) it is part of centralspindlin-complex, together with the mitotic kinesin MKLP1, which is critical for the structure of the central spindle by promoting microtuble bundling; and ii) after phosphorylation by aurora B, MgcRacGAP becomes an effective regulator of RhoA and plays an important role in the assembly of the contractile ring and the initiation of cytokinesis. MgcRacGAP-like proteins contain an N-terminal C1 domain, and a C-terminal RhoGAP domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410371  Cd Length: 55  Bit Score: 45.09  E-value: 7.15e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKC 1675
Cdd:cd20821      3 HRFVSKTVIKPETCVVCGKRIKFGKKALKCKDCRVVCHPDC 43
C1_nPKC_theta-like_rpt2 cd20837
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1635-1683 8.77e-06

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) theta, delta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410387  Cd Length: 50  Bit Score: 44.73  E-value: 8.77e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20837      1 HRFKVYNYMSPTFCDHCGSLLWgLFRQGLKCEECGMNVHHKCQKKVANLC 50
C1_MTMR-like cd20828
protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to ...
1635-1685 1.22e-05

protein kinase C conserved region 1 (C1 domain) found in uncharacterized proteins similar to myotubularin-related proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs), such as MTMR5 and MTMR13. MTMRs may function as guanine nucleotide exchange factors (GEFs). Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410378  Cd Length: 57  Bit Score: 44.36  E-value: 1.22e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSY 1685
Cdd:cd20828      6 HNFEPHSFVTPTNCDYCLQILWgIVKKGMKCSECGYNCHEKCQPQVPKQCSK 57
C1_cPKC_nPKC_rpt1 cd20792
first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
1634-1684 1.82e-05

first protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410342  Cd Length: 53  Bit Score: 43.77  E-value: 1.82e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720426625 1634 GHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20792      1 GHKFVATFFKQPTFCSHCKDFIWgLGKQGYQCQVCRFVVHKRCHEYVVFKCP 52
C1_dGM13116p-like cd20831
protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and ...
1632-1684 2.22e-05

protein kinase C conserved region 1 (C1 domain) found in Drosophila melanogaster GM13116p and similar proteins; This group contains uncharacterized proteins including Drosophila melanogaster GM13116p and Caenorhabditis elegans hypothetical protein R11G1.4, both of which contain C2 (a calcium-binding domain) and C1 domains. This model describes the C1 domain, a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410381  Cd Length: 58  Bit Score: 43.87  E-value: 2.22e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1720426625 1632 HNGHVFASYQVNIPQSCEQC-LSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20831      3 YNDHTFVATHFKGGPSCAVCnKLIPGRFGKqGYQCRDCGLICHKRCHVKVETHCP 57
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
1002-1031 3.35e-05

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 42.53  E-value: 3.35e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720426625 1002 ERKHFVQMKHAALTIQACWRSYRVRRALER 1031
Cdd:cd23767      1 EEEELQRMNRAATLIQALWRGYKVRKELKK 30
C1_nPKC_epsilon-like_rpt1 cd20835
first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1627-1683 3.86e-05

first protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domains. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410385  Cd Length: 64  Bit Score: 43.22  E-value: 3.86e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720426625 1627 RAVQEHNGHVFASYQVNIPQSCEQCLSYIW-LMDK-ALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20835      2 RRVHQVNGHKFMATYLRQPTYCSHCKDFIWgVIGKqGYQCQVCTCVVHKRCHQLVVTKC 60
PHA02682 PHA02682
ORF080 virion core protein; Provisional
2023-2117 4.50e-05

ORF080 virion core protein; Provisional


Pssm-ID: 177464 [Multi-domain]  Cd Length: 280  Bit Score: 47.55  E-value: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 2023 PAPALPCPISPTLSPLPEAAAPPRGRPTSFVTVRVKTPRR-TPIMPMANIKLPPGLPLHLTSWAPALQEAVVPvKRREPP 2101
Cdd:PHA02682    96 PACAPAAPAPAVTCPAPAPACPPATAPTCPPPAVCPAPARpAPACPPSTRQCPPAPPLPTPKPAPAAKPIFLH-NQLPPP 174
                           90
                   ....*....|....*.
gi 1720426625 2102 ARRQDQVHSVYIAPGA 2117
Cdd:PHA02682   175 DYPAASCPTIETAPAA 190
C1_aPKC cd20794
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
1633-1684 6.64e-05

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. Members of this family contain one C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410344  Cd Length: 55  Bit Score: 42.25  E-value: 6.64e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720426625 1633 NGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20794      1 NGHLFQAKRFNRRAVCAYCSDRIWgLGRQGYKCINCKLLVHKKCHKLVKVACG 53
C1_nPKC_epsilon-like_rpt2 cd20838
second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) ...
1635-1683 9.15e-05

second protein kinase C conserved region 1 (C1 domain) found in novel protein kinase C (nPKC) epsilon, eta, and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410388  Cd Length: 55  Bit Score: 41.87  E-value: 9.15e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20838      3 HRFSVHNYKRPTFCDHCGSLLYgLYKQGLQCKVCKMNVHKRCQKNVANNC 52
RhoGAP_fRGD2 cd04399
RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of ...
1700-1859 9.59e-05

RhoGAP_fRGD2: RhoGAP (GTPase-activator protein [GAP] for Rho-like small GTPases) domain of fungal RGD2-like proteins. Yeast Rgd2 is a GAP protein for Cdc42 and Rho5. Small GTPases cluster into distinct families, and all act as molecular switches, active in their GTP-bound form but inactive when GDP-bound. The Rho family of GTPases activates effectors involved in a wide variety of developmental processes, including regulation of cytoskeleton formation, cell proliferation and the JNK signaling pathway. GTPases generally have a low intrinsic GTPase hydrolytic activity but there are family-specific groups of GAPs that enhance the rate of GTP hydrolysis by several orders of magnitude.


Pssm-ID: 239864  Cd Length: 212  Bit Score: 45.79  E-value: 9.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1700 FGVCVDSLT-SDKASVPIVLEKLLEHVEMHGLYTEGLYRKSGA------ANRTRELRQALQT----DPAAVKLEDFPIHA 1768
Cdd:cd04399      1 FGVDLETRCrLDKKVVPLIVSAILSYLDQLYPDLINDEVRRNVwtdpvsLKETHQLRNLLNKpkkpDKEVIILKKFEPST 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1769 ITGVLKQWLRELPEPLMTfAQYGDFLRAV-------ELPEKQEQLSAIYAVLDHLPEANHTSLERLIFHLVKvalLEDVN 1841
Cdd:cd04399     81 VASVLKLYLLELPDSLIP-HDIYDLIRSLysayppsQEDSDTARIQGLQSTLSQLPKSHIATLDAIITHFYR---LIEIT 156
                          170       180
                   ....*....|....*....|....
gi 1720426625 1842 RMSPGA------LAIIFAPCLLRC 1859
Cdd:cd04399    157 KMGESEeeyadkLATSLSREILRP 180
C1_MRCKalpha cd20864
protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related ...
1635-1683 1.02e-04

protein kinase C conserved region 1 (C1 domain) found in myotonic dystrophy kinase-related Cdc42-binding kinase alpha (MRCK alpha) and similar proteins; MRCK alpha, also called Cdc42-binding protein kinase alpha, DMPK-like alpha, or myotonic dystrophy protein kinase-like alpha, is a serine/threonine-protein kinase expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK alpha is an important downstream effector of Cdc42 and plays a role in the regulation of cytoskeleton reorganization and cell migration. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410414  Cd Length: 60  Bit Score: 41.93  E-value: 1.02e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVNIPQSCEQCLS-YIWLMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20864      3 HQFVVKSFTTPTKCNQCTSlMVGLIRQGCTCEVCGFSCHVTCADKAPSVC 52
C1_ROCK2 cd20875
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1632-1673 1.02e-04

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 2 (ROCK2) and similar proteins; ROCK2 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2, also called Rho-associated protein kinase 2, Rho kinase 2, Rho-associated, coiled-coil-containing protein kinase II (ROCK-II), or p164 ROCK-2, was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410425  Cd Length: 71  Bit Score: 42.33  E-value: 1.02e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1720426625 1632 HNGHVFASYQVNIPQSCEQCLSYIWLMDK---ALLCSVCKMTCHK 1673
Cdd:cd20875      9 HKGHEFIPTLYHFPTNCEACMKPLWHMFKpppALECRRCHIKCHK 53
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1030-1052 1.22e-04

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 40.77  E-value: 1.22e-04
                            10        20
                    ....*....|....*....|...
gi 1720426625  1030 ERTQAAVYLQAAWRGYLQRQAYH 1052
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23
C1_RASSF5 cd20886
protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing ...
1634-1684 1.90e-04

protein kinase C conserved region 1 (C1 domain) found in Ras association domain-containing protein 5 (RASSF5) and similar proteins; RASSF5, also called new ras effector 1 (NORE1), or regulator for cell adhesion and polarization enriched in lymphoid tissues (RAPL), is a member of a family of RAS effectors, of which there are currently 8 members (RASSF1-8), all containing a Ras-association (RA) domain of the Ral-GDS/AF6 type. It is expressed as three transcripts (A-C) via differential promoter usage and alternative splicing. RASSF5A is a pro-apoptotic Ras effector and functions as a Ras regulated tumor suppressor. RASSF5C is regulated by Ras related protein and modulates cellular adhesion. RASSF5 is a potential tumor suppressor that seems to be involved in lymphocyte adhesion by linking RAP1A activation upon T-cell receptor or chemokine stimulation to integrin activation. It contains a C1 domain, which is descibed in this model. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410436  Cd Length: 50  Bit Score: 40.83  E-value: 1.90e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720426625 1634 GHVFASYQVnIPQSCEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20886      3 GHRFEPGAL-GPGWCDLCGRYI--LSQALRCTNCKYTCHSECRDLVQLDCN 50
C1_PKD_rpt2 cd20796
second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D ...
1635-1683 1.92e-04

second protein kinase C conserved region 1 (C1 domain) found in the family of protein kinase D (PKD); PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410346  Cd Length: 54  Bit Score: 41.12  E-value: 1.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20796      2 HTFVVHTYTKPTVCQHCKKLLKgLFRQGLQCKDCKFNCHKKCAEKVPKDC 51
C1_DGK_typeII_rpt1 cd20800
first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; ...
1648-1686 1.96e-04

first protein kinase C conserved region 1 (C1 domain) found in type II diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type II DAG kinases (DGKs) contain pleckstrin homology (PH) and sterile alpha motifs (SAM) domains, in addition to C1 and catalytic domains that are present in all DGKs. The SAM domain mediates oligomerization of type II DGKs. Three DGK isozymes (delta, eta and kappa) are classified as type II. DAG kinase delta, also called 130 kDa DAG kinase, or diglyceride kinase delta (DGK-delta), is a residential lipid kinase in the endoplasmic reticulum. It promotes lipogenesis and is involved in triglyceride biosynthesis. DAG kinase eta, also called diglyceride kinase eta (DGK-eta), plays a key role in promoting cell growth. The DAG kinase eta gene, DGKH, is a replicated risk gene of bipolar disorder (BPD). DAG kinase kappa is also called diglyceride kinase kappa (DGK-kappa) or 142 kDa DAG kinase. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410350  Cd Length: 60  Bit Score: 41.15  E-value: 1.96e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1720426625 1648 CEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYCSYT 1686
Cdd:cd20800     21 CREALSGV--TSHGLSCEVCKFKAHKRCAVKAPNNCKWT 57
C1_DGKbeta_rpt1 cd20845
first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG ...
1629-1686 2.75e-04

first protein kinase C conserved region 1 (C1 domain) found in diacylglycerol kinase beta (DAG kinase beta) and similar proteins; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. DAG kinase beta, also called 90 kDa diacylglycerol kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. It is classified as a type I DAG kinase (DGK), containing EF-hand structures that bind Ca(2+) and a recoverin homology domain, in addition to C1 and catalytic domains that are present in all DGKs. As a type I DGK, it is regulated by calcium binding. DAG kinase beta contains two copies of the C1 domain. This model corresponds to the first one. DGK-beta contains typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410395  Cd Length: 66  Bit Score: 40.99  E-value: 2.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720426625 1629 VQEHNGHVFASYQVNIPQSCEQCLSY-IWLMDKALLCSVCKMTCHKKCVHKIQSYCSYT 1686
Cdd:cd20845      2 VKDDGQHVWRLKHFNKPAYCNLCLNMlVGLGKQGLCCSFCKYTVHERCVQRAPASCIKT 60
C1_PKD_rpt1 cd20795
first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) ...
1632-1686 3.30e-04

first protein kinase C conserved region 1 (C1 domain) found in the protein kinase D (PKD) family; PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs contain N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410345  Cd Length: 56  Bit Score: 40.36  E-value: 3.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426625 1632 HNGHVfASYQVniPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYT 1686
Cdd:cd20795      4 HSLFV-HSYKS--PTFCDFCGEMLFgLVRQGLKCEGCGLNFHKRCAYKIPNNCTGS 56
C1_TNS3_v cd20889
protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar ...
1635-1683 4.03e-04

protein kinase C conserved region 1 (C1 domain) found in tensin-3 (TNS3) variant and similar proteins; Tensin-3 (TNS3), also called tensin-like SH2 domain-containing protein 1 (TENS1), or tumor endothelial marker 6 (TEM6), may play a role in actin remodeling. It is involved in the dissociation of the integrin-tensin-actin complex. This model corresponds to the C1 domain found in TNS3 variant. Typical TNS3 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410439  Cd Length: 56  Bit Score: 40.26  E-value: 4.03e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20889      3 HTFKNKTFKKPKVCSICKQVI--DSQGISCRVCKYACHKKCEAKVVTPC 49
C1_KSR cd20812
protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) ...
1635-1684 7.82e-04

protein kinase C conserved region 1 (C1 domain) found in the kinase suppressor of Ras (KSR) family; KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. KSR proteins contain a SAM-like domain, a zinc finger cysteine-rich domain (C1), and a pseudokinase domain. This model describes the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410362  Cd Length: 48  Bit Score: 39.23  E-value: 7.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVnIPQSCEQCLSYIWLmdkALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20812      3 HRFSKKLF-MRQTCDYCHKQMFF---GLKCKDCKYKCHKKCAKKAPPSCG 48
C1_TNS2 cd20887
protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; ...
1662-1684 8.01e-04

protein kinase C conserved region 1 (C1 domain) found in tensin-2 and similar proteins; Tensin-2 (TNS2), also called C1 domain-containing phosphatase and tensin (C1-TEN), or tensin-like C1 domain-containing phosphatase (TENC1), is an essential component for the maintenance of glomerular basement membrane (GBM) structures. It regulates cell motility and proliferation. It may have phosphatase activity. TNS2 reduces AKT1 phosphorylation, lowers AKT1 kinase activity, and interferes with AKT1 signaling. It contains an N-terminal region with a zinc finger (C1 domain), a protein tyrosine phosphatase (PTP)-like domain and a protein kinase 2 (C2) domain, and a C-terminal region with SH2 and pTyr binding (PTB) domains. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410437  Cd Length: 53  Bit Score: 39.38  E-value: 8.01e-04
                           10        20
                   ....*....|....*....|...
gi 1720426625 1662 LLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20887     28 LVCRVCKVASHKKCEAKVTSACQ 50
C1_PKD1_rpt1 cd20839
first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
1635-1690 9.28e-04

first protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the first C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410389  Cd Length: 72  Bit Score: 39.62  E-value: 9.28e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYTGRRK 1690
Cdd:cd20839      8 HALFVHSYRAPAFCDHCGEMLWgLVRQGLKCEGCGLNYHKRCAFKIPNNCSGVRKRR 64
C1_cPKC_nPKC_rpt2 cd20793
second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) ...
1635-1683 9.94e-04

second protein kinase C conserved region 1 (C1 domain) found in classical (or conventional) protein kinase C (cPKC), novel protein kinase C (nPKC), and similar proteins; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. nPKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs (aPKCs) only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. This family includes classical PKCs (cPKCs) and novel PKCs (nPKCs). There are four cPKC isoforms (named alpha, betaI, betaII, and gamma) and four nPKC isoforms (delta, epsilon, eta, and theta). Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410343  Cd Length: 50  Bit Score: 38.80  E-value: 9.94e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20793      1 HKFKVHTYYSPTFCDHCGSLLYgLVRQGLKCKDCGMNVHHRCKENVPHLC 50
C1_DGK_typeI_rpt1 cd20799
first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; ...
1635-1686 1.00e-03

first protein kinase C conserved region 1 (C1 domain) found in type I diacylglycerol kinases; Diacylglycerol (DAG) kinase (EC 2.7.1.107) is a lipid kinase that phosphorylates diacylglycerol to form phosphatidic acid. Type I DAG kinases (DGKs) contain EF-hand structures that bind Ca(2+) and recoverin homology domains, in addition to C1 and catalytic domains that are present in all DGKs. Type I DGKs, regulated by calcium binding, include three DGK isozymes (alpha, beta and gamma). DAG kinase alpha, also called 80 kDa DAG kinase, or diglyceride kinase alpha (DGK-alpha), is active upon cell stimulation, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity. DAG kinase beta, also called 90 kDa DAG kinase, or diglyceride kinase beta (DGK-beta), exhibits high phosphorylation activity for long-chain diacylglycerols. DAG kinase gamma, also called diglyceride kinase gamma (DGK-gamma), reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid. Members of this family contain two copies of the C1 domain. This model corresponds to the first one. DGK-alpha contains atypical C1 domains, while DGK-beta and DGK-gamma contain typical C1 domains that bind DAG and phorbol esters. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410349  Cd Length: 62  Bit Score: 39.28  E-value: 1.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIWLMDK-ALLCSVCKMTCHKKCVHKIQSYCSYT 1686
Cdd:cd20799      6 HVWRLKHFNKPAYCNVCENMLVGLRKqGLCCTFCKYTVHERCVSRAPASCIRT 58
C1_Sbf-like cd20827
protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf ...
1635-1684 1.12e-03

protein kinase C conserved region 1 (C1 domain) found in the myotubularin-related protein Sbf and similar proteins; This group includes Drosophila melanogaster SET domain binding factor (Sbf), the single homolog of human MTMR5/MTMR13, and similar proteins, that show high sequence similarity to vertebrate myotubularin-related proteins (MTMRs) which may function as guanine nucleotide exchange factors (GEFs). Sbf is a pseudophosphatase that coordinates both phosphatidylinositol 3-phosphate (PI(3)P) turnover and Rab21 GTPase activation in an endosomal pathway that controls macrophage remodeling. It also functions as a GEF that promotes Rab21 GTPase activation associated with PI(3)P endosomes. Vertebrate MTMR5 and MTMR13 contain an N-terminal DENN domain, a PH-GRAM domain, an inactive PTP domain, a SET interaction domain, a coiled-coil domain, and a C-terminal PH domain. Members of this family contain these domains and have an additional C1 domain. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410377  Cd Length: 53  Bit Score: 38.94  E-value: 1.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20827      2 HRFEKHNFTTPTYCDYCSSLLWgLVKTGMRCADCGYSCHEKCLEHVPKNCT 52
C1_MRCK cd20809
protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related ...
1635-1685 1.43e-03

protein kinase C conserved region 1 (C1 domain) found in the Myotonic dystrophy kinase-related Cdc42-binding kinase (MRCK) family; MRCK is thought to be a coincidence detector of signaling by the small GTPase Cdc42 and phosphoinositides. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. MRCK has been shown to promote cytoskeletal reorganization, which affects many biological processes. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. MRCK consists of a serine/threonine kinase domain, a cysteine rich (C1) region, a PH domain and a p21 binding motif. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410359  Cd Length: 53  Bit Score: 38.41  E-value: 1.43e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSY 1685
Cdd:cd20809      1 HKFIVRTFSTPTKCNHCTSLMVgLVRQGLVCEVCGYACHVSCADKAPQVCPV 52
IQ pfam00612
IQ calmodulin-binding motif; Calmodulin-binding motif.
1032-1052 2.10e-03

IQ calmodulin-binding motif; Calmodulin-binding motif.


Pssm-ID: 459869  Cd Length: 21  Bit Score: 37.30  E-value: 2.10e-03
                           10        20
                   ....*....|....*....|.
gi 1720426625 1032 TQAAVYLQAAWRGYLQRQAYH 1052
Cdd:pfam00612    1 RKAAIKIQAAWRGYLARKRYK 21
C1_betaCHN cd20857
protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; ...
1635-1689 2.16e-03

protein kinase C conserved region 1 (C1 domain) found in beta-chimaerin and similar proteins; Beta-chimaerin, also called beta-chimerin (BCH) or Rho GTPase-activating protein 3 (ARHGAP3), is a GTPase-activating protein (GAP) for p21-rac. Insufficient expression of beta-2 chimaerin is expected to lead to higher Rac activity and could therefore play a role in the progression from low-grade to high-grade tumors. Beta-chimaerin contains a functional SH2 domain that can bind to phosphotyrosine motifs within receptors, a GAP domain with specificity in vitro for Rac1 and a diacylglycerol (DAG)-binding C1 domain which allows them to translocate to membranes in response to DAG signaling and anchors them in close proximity to activated Rac. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410407  Cd Length: 61  Bit Score: 38.48  E-value: 2.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYCSYTGRR 1689
Cdd:cd20857      6 HNFKVHTFRGPHWCEYCANFMWgLIAQGVRCSDCGLNVHKQCSKHVPNDCQPDLKR 61
C1_ROCK1 cd20874
protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing ...
1630-1678 2.67e-03

protein kinase C conserved region 1 (C1 domain) found in Rho-associated coiled-coil containing protein kinase 1 (ROCK1) and similar proteins; ROCK1 is a serine/threonine kinase, catalyzing the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1, also called Rho-associated protein kinase 1, renal carcinoma antigen NY-REN-35, Rho-associated, coiled-coil-containing protein kinase I (ROCK-I), p160 ROCK-1, or p160ROCK, is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK proteins contain an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD), a pleckstrin homology (PH) domain and a C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410424  Cd Length: 69  Bit Score: 38.46  E-value: 2.67e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720426625 1630 QEHNGHVFASYQVNIPQSCEQCLSYIWLMDK---ALLCSVCKMTCHKKCVHK 1678
Cdd:cd20874      3 LPHKGHEFIPTLYHFPANCEACAKPLWHVFKpppALECRRCHVKCHKDHLDK 54
C1_TNS1_v cd20888
protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar ...
1633-1684 3.47e-03

protein kinase C conserved region 1 (C1 domain) found in tensin-1 (TNS1) variant and similar proteins; Tensin-1 (TNS1) plays a role in fibrillar adhesion formation. It may be involved in cell migration, cartilage development and in linking signal transduction pathways to the cytoskeleton. This model corresponds to the C1 domain found in TNS1 variant. Typical TNS1 does not contain C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410438  Cd Length: 57  Bit Score: 37.54  E-value: 3.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1720426625 1633 NGHVFASYQVNIPQSCEQCLSYIwlMDKALLCSVCKMTCHKKCVHKIQSYCS 1684
Cdd:cd20888      4 HTHTFKVKTFKKVKSCGICKQAI--TREGSTCRVCKLSCHKKCEAKVATPCV 53
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
1926-2067 3.93e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 41.68  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1926 FSSPYEGVRIKSPRTPVVQDLELGALPEEAAGGDEDREKEI---LMERIQSIKEEKEDITYRLPELDPRGSDEENLDSET 2002
Cdd:NF040712   192 FGRPLRPLATVPRLAREPADARPEEVEPAPAAEGAPATDSDpaeAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPD 271
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720426625 2003 SASTESLLEERGVRGAVEGPPAPALPCPISPTLSPLPEAAAPPRGRPTsfVTVRVKTPRRTPIMP 2067
Cdd:NF040712   272 EATRDAGEPPAPGAAETPEAAEPPAPAPAAPAAPAAPEAEEPARPEPP--PAPKPKRRRRRASVP 334
CRIK cd20814
protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) ...
1635-1683 4.14e-03

protein kinase C conserved region 1 (C1 domain) found in citron Rho-interacting kinase (CRIK) and similar proteins; CRIK, also called serine/threonine-protein kinase 21, is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger (C1 domain), and a pleckstrin homology (PH) domain, in addition to other motifs. This model corresponds to C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410364  Cd Length: 56  Bit Score: 37.23  E-value: 4.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIWLMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20814      5 HRFTTGLNMRATKCAVCLDGVPFGRQASKCSECGIVCHPKCSSSLPNTC 53
C1_AKAP13 cd20878
protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) ...
1633-1675 4.21e-03

protein kinase C conserved region 1 (C1 domain) found in A-kinase anchor protein 13 (AKAP-13) and similar proteins; AKAP-13, also called AKAP-Lbc, breast cancer nuclear receptor-binding auxiliary protein (Brx-1), guanine nucleotide exchange factor Lbc, human thyroid-anchoring protein 31, lymphoid blast crisis oncogene (LBC oncogene), non-oncogenic Rho GTPase-specific GTP exchange factor, protein kinase A-anchoring protein 13 (PRKA13), or p47, is a scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors (GPCRs). It activates RhoA in response to GPCR signaling via its function as a Rho guanine nucleotide exchange factor. It may also activate other Rho family members. AKAP-13 plays a role in cell growth, cell development and actin fiber formation. Its Rho-GEF activity is regulated by protein kinase A (PKA), through binding and phosphorylation. Alternative splicing of this gene in humans has at least 3 transcript variants encoding different isoforms (i.e. proto-/onco-Lymphoid blast crisis, Lbc and breast cancer nuclear receptor-binding auxiliary protein, and Brx) that contain a C1 domain followed by a dbl oncogene homology (DH) domain and a PH domain which are required for full transforming activity. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410428  Cd Length: 60  Bit Score: 37.32  E-value: 4.21e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1720426625 1633 NGHVFASYQVNIPQSCEQClSYIWLMDKALLCSVCKMTCHKKC 1675
Cdd:cd20878      6 NGHVFSPVSSVGPTQCYHC-SKPLNTKDAFLCANCNVQVHKGC 47
C1_aPKC_zeta cd21095
protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) ...
1633-1675 4.99e-03

protein kinase C conserved region 1 (C1 domain) found in the atypical protein kinase C (aPKC) zeta type; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. Members of this family contain C1 domain found in aPKC isoform zeta. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410448  Cd Length: 55  Bit Score: 37.27  E-value: 4.99e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1720426625 1633 NGHVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKC 1675
Cdd:cd21095      1 NGHLFQAKRFNRRAYCGQCSERIWgLGRQGYKCINCKLLVHKRC 44
C1_PIK3R-like_rpt2 cd20830
second protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
1646-1677 5.11e-03

second protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410380  Cd Length: 52  Bit Score: 36.84  E-value: 5.11e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1720426625 1646 QSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVH 1677
Cdd:cd20830     12 QWCDKCGKFLFgLVHQGLQCQDCGLVCHRTCAA 44
C1_PKD2_rpt2 cd20843
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and ...
1635-1683 5.29e-03

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D2 (PKD2) and similar proteins; PKD2, also called PRKD2, HSPC187, or serine/threonine-protein kinase D2 (nPKC-D2), is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of cell proliferation via MAPK1/3 (ERK1/2) signaling, oxidative stress-induced NF-kappa-B activation, inhibition of HDAC7 transcriptional repression, signaling downstream of T-cell antigen receptor (TCR) and cytokine production, and plays a role in Golgi membrane trafficking, angiogenesis, secretory granule release and cell adhesion. PKD2 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410393  Cd Length: 79  Bit Score: 37.65  E-value: 5.29e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYI-WLMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20843     12 HTFVIHSYTRPTVCQFCKKLLkGLFRQGLQCKDCKFNCHKRCATRVPNDC 61
C1_PKD1_rpt2 cd20842
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and ...
1635-1683 5.34e-03

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D (PKD) and similar proteins; PKD is also called PKD1, PRKD1, protein kinase C mu type (nPKC-mu), PRKCM, serine/threonine-protein kinase D1, or nPKC-D1. It is a serine/threonine-protein kinase that converts transient diacylglycerol (DAG) signals into prolonged physiological effects downstream of PKC, and is involved in the regulation of MAPK8/JNK1 and Ras signaling, Golgi membrane integrity and trafficking, cell survival through NF-kappa-B activation, cell migration, cell differentiation by mediating HDAC7 nuclear export, cell proliferation via MAPK1/3 (ERK1/2) signaling, and plays a role in cardiac hypertrophy, VEGFA-induced angiogenesis, genotoxic-induced apoptosis and flagellin-stimulated inflammatory response. PKD contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410392  Cd Length: 94  Bit Score: 38.07  E-value: 5.34e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYI-WLMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20842     35 HTFVIHSYTRPTVCQYCKKLLkGLFRQGLQCKDCKFNCHKRCAPKVPNNC 84
C1_ScPKC1-like_rpt2 cd20823
second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae ...
1632-1683 5.59e-03

second protein kinase C conserved region 1 (C1 domain) found in Saccharomyces cerevisiae protein kinase C-like 1 (ScPKC1) and similar proteins; ScPKC1 is required for cell growth and for the G2 to M transition of the cell division cycle. It mediates a protein kinase cascade, activating BCK1 which itself activates MKK1/MKK2. The family also includes Schizosaccharomyces pombe PKC1 and PKC2, which are involved in the control of cell shape and act as targets of the inhibitor staurosporine. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410373  Cd Length: 59  Bit Score: 36.90  E-value: 5.59e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1720426625 1632 HNGHVFASYQVNIPQSCEQClSYI--WLMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20823      2 RIPHRFEPFTNLGANWCCHC-GQMlpLGRKQIRKCTECGKTAHAQCAHLVPNFC 54
IQ smart00015
Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln ...
1008-1029 5.83e-03

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.


Pssm-ID: 197470 [Multi-domain]  Cd Length: 23  Bit Score: 36.15  E-value: 5.83e-03
                            10        20
                    ....*....|....*....|..
gi 1720426625  1008 QMKHAALTIQACWRSYRVRRAL 1029
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRY 22
C1_Stac cd20817
protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich ...
1635-1684 6.03e-03

protein kinase C conserved region 1 (C1 domain) found in the SH3 and cysteine-rich domain-containing protein (Stac) family; Stac proteins are putative adaptor proteins that are important for neuronal function. There are three mammalian members (Stac1, Stac2 and Stac3) of this family. Stac1 and Stac3 contain two SH3 domains while Stac2 contains a single SH3 domain at the C-terminus. Stac1 and Stac2 have been found to be expressed differently in mature dorsal root ganglia (DRG) neurons. Stac1 is mainly expressed in peptidergic neurons while Stac2 is found in a subset of nonpeptidergic and all trkB+ neurons. Stac proteins contain a cysteine-rich C1 domain and one or two SH3 domains at the C-terminus. This model corresponds to the C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410367  Cd Length: 51  Bit Score: 36.92  E-value: 6.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIqSYCS 1684
Cdd:cd20817      1 HSFQEHTFKKPTFCDVCKELLVgLSKQGLRCKNCKMNVHHKCQEGV-PDCS 50
C1_PIK3R-like_rpt1 cd20829
first protein kinase C conserved region 1 (C1 domain) found in uncharacterized ...
1635-1676 6.92e-03

first protein kinase C conserved region 1 (C1 domain) found in uncharacterized phosphatidylinositol 3-kinase regulatory subunit-like proteins; The family includes a group of uncharacterized proteins that show high sequence similarity to vertebrate phosphatidylinositol 3-kinase regulatory subunits (PIK3Rs), which bind to activated (phosphorylated) protein-tyrosine kinases through its SH2 domain and regulate their kinase activity. Unlike typical PIK3Rs, members of this family have two C1 domains. This model corresponds to the first one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410379  Cd Length: 53  Bit Score: 36.56  E-value: 6.92e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIWLMDKAL-LCSVCKMTCHKKCV 1676
Cdd:cd20829      1 HRLVDVYFVTPILCRHCKDYIWGKGKVGvRCEDCHACFHLVCA 43
C1_cPKC_rpt2 cd20836
second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) ...
1635-1683 7.00e-03

second protein kinase C conserved region 1 (C1 domain) found in the classical (or conventional) protein kinase C (cPKC) family; PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. Members of this family contain two copies of C1 domain. This model corresponds to the second one. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410386  Cd Length: 54  Bit Score: 36.55  E-value: 7.00e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYIW-LMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20836      1 HKFKVHTYSSPTFCDHCGSLLYgLIHQGMKCDTCDMNVHKRCVKNVPSLC 50
C1_PKD3_rpt2 cd20844
second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and ...
1635-1683 9.25e-03

second protein kinase C conserved region 1 (C1 domain) found in protein kinase D3 (PKD3) and similar proteins; PKD3 is also called PRKD3, PRKCN, serine/threonine-protein kinase D3 (nPKC-D3), protein kinase C nu type (nPKC-nu), or protein kinase EPK2. It converts transient diacylglycerol (DAG) signals into prolonged physiological effects, downstream of PKC. It is involved in the regulation of the cell cycle by modulating microtubule nucleation and dynamics. PKD3 acts as a key mediator in several cancer development signaling pathways. PKD3 contains N-terminal tandem cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. This model corresponds to the second C1 domain. The C1 domain is a cysteine-rich zinc binding domain that does not bind DNA nor possess structural similarity to conventional zinc finger domains; it contains two separate Zn(2+)-binding sites.


Pssm-ID: 410394  Cd Length: 69  Bit Score: 36.91  E-value: 9.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1720426625 1635 HVFASYQVNIPQSCEQCLSYI-WLMDKALLCSVCKMTCHKKCVHKIQSYC 1683
Cdd:cd20844      6 HTFAVHSYTRPTICQYCKRLLkGLFRQGMQCKDCRFNCHKRCASKVPRDC 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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