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Conserved domains on  [gi|530403352|ref|XP_005267511|]
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nesprin-2 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
28-138 8.65e-69

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409091  Cd Length: 111  Bit Score: 228.18  E-value: 8.65e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTFQCRINIEHALTFLRNRSIK 107
Cdd:cd21242     1 EQEQTQKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530403352  108 LINIHVTDIIDGNPSIILGLIWTIILHFHIE 138
Cdd:cd21242    81 LINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
178-286 6.02e-65

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


:

Pssm-ID: 409093  Cd Length: 109  Bit Score: 217.01  E-value: 6.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  178 RWQMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPR 257
Cdd:cd21244     1 RWKMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPR 80
                          90       100
                  ....*....|....*....|....*....
gi 530403352  258 LLEPEDVDVVDPDEKSIMTYVAQFLQYSK 286
Cdd:cd21244    81 LLEPEDVDVVNPDEKSIMTYVAQFLQYSK 109
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6137-6350 1.87e-18

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 87.50  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6137 LWQKFLDDYSRFEDWLKSAERTAACPNSSEVLyTSAKEELKRFEAFQRQIHERLTQLELINKQYRRLARENRTDtASRLK 6216
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6217 QMVHEGNQRWDNLQRRVTAVLRRLRHFTNQREEFEGTREsILVWLTEMDLQLTNVEHF-SESDADDKMRQLNGFQQEITL 6295
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGkDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530403352 6296 NTNKIDQLIVFGEQLIQKSEPLDAVLIEDELEELHRYCQEVFGRVSRFHRRLTSC 6350
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5919-6133 2.37e-16

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 81.72  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5919 WVVFNEKNKELCAWLVQMENKVLQTADISIEEMIEKLQKDC---MEEINLFSENKLQLKQMGDQLIKaSNKSRAAEIDDK 5995
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHealEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5996 LNKINDRWQHLFDVIGSRVKKLKETFAFIQQLDKnMSNLRTWLARIESELSKPVVYDvcDDQEIQKRLAEQQDLQRDIEQ 6075
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530403352 6076 HSAGVESVFNICDVLLHDsdacANETECDSIQQTTRSLDRRWRNICAMSMERRMKIEE 6133
Cdd:cd00176   158 HEPRLKSLNELAEELLEE----GHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
KASH pfam10541
Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS ...
6891-6922 3.02e-16

Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS domain is a highly hydrophobic nuclear envelope localization domain of approximately 60 amino acids comprising a 20-amino-acid transmembrane region and a 30-35-residue C-terminal region that lies between the inner and the outer nuclear membranes. During meiotic prophase, telomeres cluster to form a bouquet arrangement of chromosomes. SUN and KASH domain proteins form complexes that span both membranes of the nuclear envelope. The KASH domain links the dynein motor complex of the microtubules, through the outer nuclear membrane to the Sad1 domain in the inner nuclear membrane which then interacts with the bouquet proteins Bqt1 and Bqt2 that are complexed with Bqt4, Rap1 and Taz1 and attached to the telomere. SUN domain-containing proteins are essential for recruiting KASH domain proteins at the outer nuclear membrane, and KASH domains provide a generic NE tethering device for functionally distinct proteins whose cytoplasmic domains mediate nuclear positioning, maintain physical connections with other cellular organelles, and possibly even influence chromosome dynamics.


:

Pssm-ID: 463142  Cd Length: 58  Bit Score: 76.09  E-value: 3.02e-16
                           10        20        30
                   ....*....|....*....|....*....|..
gi 530403352  6891 PSSEEDYSCTQANNFARSFYPMLRYTNGPPPT 6922
Cdd:pfam10541   27 PAGEEDYSCTLANNFARSFHPMLRYVNGPPPT 58
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5063-5276 2.24e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 72.86  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5063 KAITEMISWMNNVEHQTSDEDSVHSPSSasqVKHLLQKHKEFRMEMDYKQWIVDFVNQSLLQLstcdVESKRYERTEFAE 5142
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDYGDDLES---VEALLKKHEALEAELAAHEERVEALNELGEQL----IEEGHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5143 HLGEMNRQWHRVHGMLNRKIQHLEQLLESITESENKIQILnNWLEAQEERLKTLQKPESVISVQKLLLDCQDIENQLAIK 5222
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530403352 5223 SKALDELKQSYLTLESGAVPL-LEDTASRIDELFQKRSSVLTQVNQLKTSMQSVL 5276
Cdd:cd00176   159 EPRLKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6576-6799 4.11e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 69.01  E-value: 4.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6576 LQQLNSDISAITTWLKKTEaelEMLKMAKPPSDIQEIELRVKRLQEILKAFDTYKALVVSVNVSSKEFLQTESPESTELQ 6655
Cdd:cd00176     2 LQQFLRDADELEAWLSEKE---ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6656 SRLRQLSLLWEAAQGAVDSWRGGLRQSLMQCQgsktrprsdvlffkdFHQLSQNLLLWLASAKNRRQKahvTDPKADPRA 6735
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQ---------------FFRDADDLEQWLEEKEAALAS---EDLGKDLES 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530403352 6736 LLECRRELMQLEKELVERQPQVDMLQEISNSLLIKGHGEDCIEAEEKVHVIEKKLKQLREQVSQ 6799
Cdd:cd00176   141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEE 204
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4945-5169 6.03e-11

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


:

Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 65.93  E-value: 6.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 4945 HLLSYNRDSDQLTKWLESSQHTLnywkeQSLNVSQDLDTIRSNINNFFEFSKEVDEKSSLKTAVISIGNQLLHLKETDTA 5024
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELL-----SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5025 TLRASLAQFEQKWTMLITQLPDIQEKLHQLQMEKLPSRKAiTEMISWMNNVEHQTSDEDSVHSPSSasqVKHLLQKHKEF 5104
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGKDLES---VEELLKKHKEL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530403352 5105 RMEMD-YKQWIVDFVN--QSLLQLSTCDVESKRYERTEfaehlgEMNRQWHRVHGMLNRKIQHLEQLL 5169
Cdd:cd00176   152 EEELEaHEPRLKSLNElaEELLEEGHPDADEEIEEKLE------ELNERWEELLELAEERQKKLEEAL 213
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
1868-2417 9.86e-07

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 9.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1868 KKSVEQKLQKLSDflTLEGRNSKIKQVDSVLKHVKKHLPKAH----VKELISWLVGQEFELEKMESICQARAKELEDSLQ 1943
Cdd:PRK03918  254 KRKLEEKIRELEE--RIEELKKEIEELEEKVKELKELKEKAEeyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1944 QLlrlQDDHRNLRKWLTNQEEKWKGMEEPGEKTELFCQALARKreqfesvAQLNNSLKEYGFTEEEEIIMEATCLMDRYQ 2023
Cdd:PRK03918  332 EL---EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK-------EELERLKKRLTGLTPEKLEKELEELEKAKE 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2024 TLLRQLSEIEEEDKLLPTEdqsfndlahdvihwIKEIKESLMVLNSSEGKMPL-------EERiqkiKEIILLKPEGDAR 2096
Cdd:PRK03918  402 EIEEEISKITARIGELKKE--------------IKELKKAIEELKKAKGKCPVcgrelteEHR----KELLEEYTAELKR 463
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2097 IETIMKQAESSEAPLvQKTLTDIsnqwDNTLHLASTYLSHQE--KLLLEGEKYLQSkedlrLMLIELKKKQEAGFALQHG 2174
Cdd:PRK03918  464 IEKELKEIEEKERKL-RKELREL----EKVLKKESELIKLKElaEQLKELEEKLKK-----YNLEELEKKAEEYEKLKEK 533
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2175 LQEKKAQLKIYKKFLKKAQDLTSLLKELKSQGNYLLEctknpsfseepwlEIKHLHESLLQQLQDSVQNLDGHVREhdsy 2254
Cdd:PRK03918  534 LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE-------------ELAELLKELEELGFESVEELEERLKE---- 596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2255 qvcvtdlnttLDNFSKEFVSFSDKPVDqiaVEEKLQKLQELENRLSLQDGTLKKILALAKSVKQNTSSVGQKIIKDDIKS 2334
Cdd:PRK03918  597 ----------LEPFYNEYLELKDAEKE---LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE 663
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2335 LQCKQKDLENRLASAKQEMEcCLNSILKSKRSTEKKGKFTLPGREKqATSDVQESTQESAAVEKLEEDWEINKDSAVEMA 2414
Cdd:PRK03918  664 LREEYLELSRELAGLRAELE-ELEKRREEIKKTLEKLKEELEEREK-AKKELEKLEKALERVEELREKVKKYKALLKERA 741

                  ...
gi 530403352 2415 MSK 2417
Cdd:PRK03918  742 LSK 744
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5178-5384 1.13e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 53.22  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5178 KIQILNNWLEAQEERLKTLQKPESVISVQKLLLDCQDIENQLAIKSKALDELKQSYLTLESGAVPLLEDTASRIDELFQK 5257
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5258 RSSVLTQVNQLKTSMQSVLQEWKIYDQLYDEVNMMTIRFWYCMehSKPVVLSLETLRCQVENLQSLQDEAESSEGSWEKL 5337
Cdd:cd00176    88 WEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA--SEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 530403352 5338 QEVIGKLKGLC-PSVAEIIEEKCQNTHKRWTQVNQAIADQLQKAQSLL 5384
Cdd:cd00176   166 NELAEELLEEGhPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
2338-2712 1.31e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 52.38  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2338 KQKDLENRLASAKQEMECCLNSILKSKRSTEKkgkftlpgREKQATSDVQESTQESAAVEK----LEEDWEINK----DS 2409
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIEN--------RLDELSQELSDASRKIGEIEKeieqLEQEEEKLKerleEL 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2410 AVEMAMSKQLSLNAQESMKNTED-----ERKVNELQNQPLELDTMLRNEQLEEIEKLYTQLEAKKAAIKpleqteclnkt 2484
Cdd:TIGR02169  743 EEDLSSLEQEIENVKSELKELEArieelEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE----------- 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2485 etgaLVLHNIGYSAQHLDNLLQALITLKKNKESQycvLRDFQEYLAAVESSMKALLTDKESLKvgpldsvTYLDKIKKFI 2564
Cdd:TIGR02169  812 ----ARLREIEQKLNRLTLEKEYLEKEIQELQEQ---RIDLKEQIKSIEKEIENLNGKKEELE-------EELEELEAAL 877
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2565 ASIEKEkdsLGNLKIKWENLSNHVTDMDKKL--LESQIKQLEHGWEQVEQQIQKKySQQVVEYDEfttlmNKVQDTEISL 2642
Cdd:TIGR02169  878 RDLESR---LGDLKKERDELEAQLRELERKIeeLEAQIEKKRKRLSELKAKLEAL-EEELSEIED-----PKGEDEEIPE 948
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530403352  2643 QQQQQHLQLRLKSPEERAgnqsMIAL-TTDLQATKHGFSVLKGQAELQMKRIWGEKEKKNLEDGINNLKKQ 2712
Cdd:TIGR02169  949 EELSLEDVQAELQRVEEE----IRALePVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
CCDC158 super family cl37899
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2805-3389 1.80e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


The actual alignment was detected with superfamily member pfam15921:

Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 52.04  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2805 NNTLEDLRNQYQMLVLKSTQRSQQLEFKLEERSNFFAIIRKFQL----MVQESETLIIPRVETAATEAelkHHHVTLeaS 2880
Cdd:pfam15921  137 SQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLshegVLQEIRSILVDFEEASGKKI---YEHDSM--S 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2881 QKELQEIDSGISTHLQELTNiyeELNVFE-RLF-LEDQLKNLKIRT-NRIQRFIQNTCNEVE-----HKIKFCrQFHEKT 2952
Cdd:pfam15921  212 TMHFRSLGSAISKILRELDT---EISYLKgRIFpVEDQLEALKSESqNKIELLLQQHQDRIEqliseHEVEIT-GLTEKA 287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2953 SALQEEADSIQRNELLLNQEVNKGVKEEIYNLKDRLTAIKCCILQVLKLKKVFDyiglnwdfSQLDQLQTQVFEKEKELE 3032
Cdd:pfam15921  288 SSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE--------DKIEELEKQLVLANSELT 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3033 EKIKQLDTFEEEHGKYQALLSKM------RAIDLQIKKMTEVVLKAPDSSP-----------ESRRLNAQILSQRIEKAK 3095
Cdd:pfam15921  360 EARTERDQFSQESGNLDDQLQKLladlhkREKELSLEKEQNKRLWDRDTGNsitidhlrrelDDRNMEVQRLEALLKAMK 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3096 CLCD-EIIKKLNENKTFDDSFKEKEILQIKLNAEEnDKLYKVLQ-----NMVLELSPKELDE--KNCQDKlETSLHVLNQ 3167
Cdd:pfam15921  440 SECQgQMERQMAAIQGKNESLEKVSSLTAQLESTK-EMLRKVVEeltakKMTLESSERTVSDltASLQEK-ERAIEATNA 517
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3168 IKSQLQQPLLINL-EIKHIQNEKDNCEAFQEQVWA---EMCSIKAVTAIEKQREEN----------------------SS 3221
Cdd:pfam15921  518 EITKLRSRVDLKLqELQHLKNEGDHLRNVQTECEAlklQMAEKDKVIEILRQQIENmtqlvgqhgrtagamqvekaqlEK 597
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3222 EASDVETKLREFEDLQMQLNTSI---DLRTNVLNDAYENLTRYKEAVTRAVESIT----SLEAIIIPYRVDVGNPEESLE 3294
Cdd:pfam15921  598 EINDRRLELQEFKILKDKKDAKIrelEARVSDLELEKVKLVNAGSERLRAVKDIKqerdQLLNEVKTSRNELNSLSEDYE 677
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3295 MPLR----KQEELESTvahiqdlTEKLGM-ISSPEAKL-QLQYTLQELV-SKNSAMKEAFKAQE--TEAERYLENYKCYR 3365
Cdd:pfam15921  678 VLKRnfrnKSEEMETT-------TNKLKMqLKSAQSELeQTRNTLKSMEgSDGHAMKVAMGMQKqiTAKRGQIDALQSKI 750
                          650       660
                   ....*....|....*....|....
gi 530403352  3366 KMEEDIYTNLSKMETVLGQSMSSL 3389
Cdd:pfam15921  751 QFLEEAMTNANKEKHFLKEEKNKL 774
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
3656-3950 5.62e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 5.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3656 EIESQVEECRKALEDIDEKIsnEVLKSSPSYAMRRKIEEINNGLHNVEKMLQQKSKNIEKAQEIQKKMWDELDLWHSKLN 3735
Cdd:TIGR02169  262 ELEKRLEEIEQLLEELNKKI--KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3736 ELDSEVQDI-VEQDPGQA--QEWMDNLMIPFQQYQQVSQRAECRTSQLNKATVKMEEYSDllksteawiENTSHLLANPA 3812
Cdd:TIGR02169  340 ELEREIEEErKRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR---------EINELKRELDR 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3813 DYDSLRTLSHHASTVQMALEDSEQKHNLLHSifmdlEDLSIIFETDELTQSIQELSNQVTALQQKIMESLPQIQRMADDV 3892
Cdd:TIGR02169  411 LQEELQRLSEELADLNAAIAGIEAKINELEE-----EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530403352  3893 VAIESEVKSMEKRVSKIKTillskEIFDFSPEEhlkhgEVILENIRPMKKTIAEIVSY 3950
Cdd:TIGR02169  486 SKLQRELAEAEAQARASEE-----RVRGGRAVE-----EVLKASIQGVHGTVAQLGSV 533
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
3811-4113 7.06e-05

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 7.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3811 PADYDSLRTLSHHASTVQMALEDSEQK----HNLLHSIFMDLEDLSIifETDELTQSIQELSNQVTALQQKIMESLPQIQ 3886
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSElrriENRLDELSQELSDASR--KIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3887 RMADDVVAIESEVKSMEKRVSKIKTILLSKEIFDFSPEEHLKHGEV--ILENIRPMKKTIAEIVSYQVELRlpqtgmkpl 3964
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeIQAELSKLEEEVSRIEARLREIE--------- 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3965 pvfQRTNQLLQDIKLLENVTQEQNELLKVVIKQTNEWDEEIENLKQILNNYSAQFS-LEHMSPDQADKLPQLQGEIERME 4043
Cdd:TIGR02169  819 ---QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEeLEAALRDLESRLGDLKKERDELE 895
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4044 KQILSLNQRKEDL----------LVDLKATVLNLHQHLKQEQEGVERDR--LPAVTSEEGGVAERDASERKLNRRGSMSY 4111
Cdd:TIGR02169  896 AQLRELERKIEELeaqiekkrkrLSELKAKLEALEEELSEIEDPKGEDEeiPEEELSLEDVQAELQRVEEEIRALEPVNM 975

                   ..
gi 530403352  4112 LA 4113
Cdd:TIGR02169  976 LA 977
PRK03918 super family cl35229
DNA double-strand break repair ATPase Rad50;
1418-2014 1.93e-04

DNA double-strand break repair ATPase Rad50;


The actual alignment was detected with superfamily member PRK03918:

Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1418 VQEEFTEENKLLEACIFKNNELLKNIQDVQSQISKiglkdptvpaVKHRKKSLIRLDKVLDEYEEEKRHLQEMANSLPHF 1497
Cdd:PRK03918  191 IEELIKEKEKELEEVLREINEISSELPELREELEK----------LEKEVKELEELKEEIEELEKELESLEGSKRKLEEK 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1498 KDGREKTVNQQCQNTVVLWENTKAL------VTECLEQCGRVLELLKQYQNFKSILTTLIQKEESVISLQASYMGKEN-- 1569
Cdd:PRK03918  261 IRELEERIEELKKEIEELEEKVKELkelkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEErl 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1570 --LKKRIAEIEIVKEEFNEHLEVVDKINQVCKNLQFYLNKMKTFEEPPFEKEANIIVDRWLDINEKTEDYYENLGRalaL 1647
Cdd:PRK03918  341 eeLKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE---L 417
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1648 WDKLFNLKNVIDEwTEKALQKMEL--HQLTEEDRERLKEELqvheqkTSEFSRRVAEIQfllqsseiplELQVMESSILN 1725
Cdd:PRK03918  418 KKEIKELKKAIEE-LKKAKGKCPVcgRELTEEHRKELLEEY------TAELKRIEKELK----------EIEEKERKLRK 480
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1726 KMEHVQKCLTGESNCHALSGSTAELREdldqaktqigmTESLLKALSpsdsLEiftKLEEIQQQILQQKHSMILLENQIG 1805
Cdd:PRK03918  481 ELRELEKVLKKESELIKLKELAEQLKE-----------LEEKLKKYN----LE---ELEKKAEEYEKLKEKLIKLKGEIK 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1806 CLTPELS---ELKKQYESVSDLFNTKKSVLQDHFSKLLNDQCKNFNDWFSNIKvNLKECFESSETKKSVEQKLQKLSDFL 1882
Cdd:PRK03918  543 SLKKELEkleELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLK-ELEPFYNEYLELKDAEKELEREEKEL 621
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1883 -----TLEGRNSKIKQVDSVLKHVKKHLPKAHVK---ELISWLVGQEFELEKMESICQARAKELEDSLQQLLRLQDDhrn 1954
Cdd:PRK03918  622 kkleeELDKAFEELAETEKRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK--- 698
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1955 lrkwLTNQEEKwkgMEEPGEKTELFCQALARKREQFESVAQLNNSLKEYGFTEEEEIIME 2014
Cdd:PRK03918  699 ----LKEELEE---REKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASE 751
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5123-5875 3.35e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5123 LQLSTCDVESKRYERTEFAEHLGEMNRQWHRV-----------------HGMLNRKIQHLEQLLESITeseNKIQILNNW 5185
Cdd:TIGR02168  227 LALLVLRLEELREELEELQEELKEAEEELEELtaelqeleekleelrleVSELEEEIEELQKELYALA---NEISRLEQQ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5186 LEAQEERLKTLQKPESVISVQKLLLdcqdiENQLAIKSKALDELKQSYLTLEsgavPLLEDTASRIDELFQKRSSVLTQV 5265
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEEL-----ESKLDELAEELAELEEKLEELK----EELESLEAELEELEAELEELESRL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5266 NQLKTSMQSVLQEwkiYDQLYDEVNMMTIRFWYCMEHSKPVVLSLETLRCQVENLQSLQDEAEssegswekLQEVIGKLK 5345
Cdd:TIGR02168  375 EELEEQLETLRSK---VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--------LKELQAELE 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5346 GLcpsvaEIIEEKCQNTHKRWTQVNQAIADQLQKAQSLLQLWKAYSNAHGEAAARLKQQEAKFQQL----ANISMSGNNL 5421
Cdd:TIGR02168  444 EL-----EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsegvKALLKNQSGL 518
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5422 AEILPPALQDIK---------------ELQHDVQKTKEAFLQNSSVLdrlpQPAESSTHMLLPGPLHSLQRAAYLEKMLL 5486
Cdd:TIGR02168  519 SGILGVLSELISvdegyeaaieaalggRLQAVVVENLNAAKKAIAFL----KQNELGRVTFLPLDSIKGTEIQGNDREIL 594
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5487 VKANEFEFVLSQFKDFGVRLESLkglimheeenldrlhqqekenpdsfLNHVLALTAQSPDIEHLNEVSLKLPLSDVAVk 5566
Cdd:TIGR02168  595 KNIEGFLGVAKDLVKFDPKLRKA-------------------------LSYLLGGVLVVDDLDNALELAKKLRPGYRIV- 648
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5567 TLQN--MNRQWI------RATATALERCSELqgiglnEKFLYCCEKWIQLLEKIEEALKvDVANSLPELLEQQKTYKMLE 5638
Cdd:TIGR02168  649 TLDGdlVRPGGVitggsaKTNSSILERRREI------EELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKEL 721
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5639 AEVSINQTIADSYVTQSLQlldttEIENRPEFITEFSKLTDRWQNAVQGVRQRKGDVDGLV----RQWQDFTTSVENLFR 5714
Cdd:TIGR02168  722 EELSRQISALRKDLARLEA-----EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELaeaeAEIEELEAQIEQLKE 796
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5715 FLTDTSHLLSAVKGQERfslyQTRSLIHELKNKEIHFQRRrttcaltleageklllttdlktKESVGRRISQLQDSWKDM 5794
Cdd:TIGR02168  797 ELKALREALDELRAELT----LLNEEAANLRERLESLERR----------------------IAATERRLEDLEEQIEEL 850
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5795 EPQLAEMIKQFQstvETWDQCEKKIKELKSrLQVLKAQSEDPLPELHEDLHNEKELIKELEQSLASWTQNLKELQTMKAD 5874
Cdd:TIGR02168  851 SEDIESLAAEIE---ELEELIEELESELEA-LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926

                   .
gi 530403352  5875 L 5875
Cdd:TIGR02168  927 L 927
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4496-5321 1.23e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4496 EELKTYTTQLEDLRQEASNLQTQENMTEEAYINLDKKLFEL----------FLTLSQCLSSVEEMLEMPRLYREDGSGQQ 4565
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELeeeieelqkeLYALANEISRLEQQKQILRERLANLERQL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4566 VHYETlalelkklYLALSDKKGDLLKamtwpgENTNLLLECFDNLQVCLEhtqaaavcrskSLKAGLDYNRSYQNEIKRL 4645
Cdd:TIGR02168  319 EELEA--------QLEELESKLDELA------EELAELEEKLEELKEELE-----------SLEAELEELEAELEELESR 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4646 YHQLIKSKTSLQQSLNEISgqsvaEQLQKADAytvELENAESRVAKLRDEGERLHlpyallQEVYKLEDVLdsmwgmlra 4725
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLE-----LQIASLNN---EIERLEARLERLEDRRERLQ------QEIEELLKKL--------- 430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4726 rytelsspfvtESQQDALLQGMVELVKIGKEKLAHGHLKQTKSKVALQAQIENHKVFFQKLVADMLLIQAySAKILPSLL 4805
Cdd:TIGR02168  431 -----------EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-RLDSLERLQ 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4806 QNRETFWAeqvtEVKILEEKSRQCGMKLQSLLQKWeEFDENY-ASLEKDLEILIStlpsvSLVEETEERLVERISFyqqI 4884
Cdd:TIGR02168  499 ENLEGFSE----GVKALLKNQSGLSGILGVLSELI-SVDEGYeAAIEAALGGRLQ-----AVVVENLNAAKKAIAF---L 565
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4885 KRNIGGKHARLYQTLNEGKQLVASvscpelEGQIAKLEEQWLSLNKKIDHELHRLQALLKHLLSYNRDSDQltkwLESSQ 4964
Cdd:TIGR02168  566 KQNELGRVTFLPLDSIKGTEIQGN------DREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD----LDNAL 635
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4965 HTLNYWKEQSLNVSQDLDTIR----------SNINNFFEFSKEVDEKSSLKTAVISignqLLHLKETDTATLRASLAQFE 5034
Cdd:TIGR02168  636 ELAKKLRPGYRIVTLDGDLVRpggvitggsaKTNSSILERRREIEELEEKIEELEE----KIAELEKALAELRKELEELE 711
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5035 QKWTMLITQLPDIQEKLHQLQMEKLPSRKAItemiswmNNVEHQTSDEDSVHSPSSASQVKHLLQKHKEFRMEMDYKQWI 5114
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEV-------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5115 VDfVNQSLLQLSTcDVESKRYERTEFAEHLGEMNRQWHRVHGMLNRKIQHLEQLLESITESENKIQILNNWLEAQEERLK 5194
Cdd:TIGR02168  785 EE-LEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5195 TLQKPESvisvqKLLLDCQDIENQLAIKSKALDELKQSYLTLESGavplLEDTASRIDELFQKRSSVLTQVNQLKTSMQS 5274
Cdd:TIGR02168  863 ELEELIE-----ELESELEALLNERASLEEALALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELRLEG 933
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*...
gi 530403352  5275 VLQEWK-IYDQLYDEVNMMtirFWYCMEHSKPVVLSLETLRCQVENLQ 5321
Cdd:TIGR02168  934 LEVRIDnLQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLE 978
 
Name Accession Description Interval E-value
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
28-138 8.65e-69

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409091  Cd Length: 111  Bit Score: 228.18  E-value: 8.65e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTFQCRINIEHALTFLRNRSIK 107
Cdd:cd21242     1 EQEQTQKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530403352  108 LINIHVTDIIDGNPSIILGLIWTIILHFHIE 138
Cdd:cd21242    81 LINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
178-286 6.02e-65

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409093  Cd Length: 109  Bit Score: 217.01  E-value: 6.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  178 RWQMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPR 257
Cdd:cd21244     1 RWKMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPR 80
                          90       100
                  ....*....|....*....|....*....
gi 530403352  258 LLEPEDVDVVDPDEKSIMTYVAQFLQYSK 286
Cdd:cd21244    81 LLEPEDVDVVNPDEKSIMTYVAQFLQYSK 109
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
28-279 2.35e-31

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 134.30  E-value: 2.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQLARHTSPSvISDLFTDIKKGHVLLDLLEVLSGQQLPR-DKGSNTF-QCRINIEHALTFLRNRS 105
Cdd:COG5069     5 KWQKVQKKTFTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEyNETPETRiHVMENVSGRLEFIKGKG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  106 IKLINIHVTDIIDGNPSIILGLIWTIILHFHIEKLAQtlscnynqpslddvsvvdsspassppakkcskvqaRWQMSARK 185
Cdd:COG5069    84 VKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINE-----------------------------------EGELTKHI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  186 ALLLWAQEQCATYE-SVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSV-KHRSNKD-NLREAFRIAEQELKIPRLLEPE 262
Cdd:COG5069   129 NLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLdLQKKNKAlNNFQAFENANKVIGIARLIGVE 208
                         250
                  ....*....|....*...
gi 530403352  263 DV-DVVDPDEKSIMTYVA 279
Cdd:COG5069   209 DIvNVSIPDERSIMTYVS 226
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
181-281 1.17e-23

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 98.90  E-value: 1.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   181 MSARKALLLWAQEQCATY-ESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHR--SNKDNLREAFRIAEQELKIPR 257
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPK 80
                           90       100
                   ....*....|....*....|....*
gi 530403352   258 -LLEPEdvDVVDPDEKSIMTYVAQF 281
Cdd:pfam00307   81 vLIEPE--DLVEGDNKSVLTYLASL 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6137-6350 1.87e-18

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 87.50  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6137 LWQKFLDDYSRFEDWLKSAERTAACPNSSEVLyTSAKEELKRFEAFQRQIHERLTQLELINKQYRRLARENRTDtASRLK 6216
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6217 QMVHEGNQRWDNLQRRVTAVLRRLRHFTNQREEFEGTREsILVWLTEMDLQLTNVEHF-SESDADDKMRQLNGFQQEITL 6295
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGkDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530403352 6296 NTNKIDQLIVFGEQLIQKSEPLDAVLIEDELEELHRYCQEVFGRVSRFHRRLTSC 6350
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5919-6133 2.37e-16

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 81.72  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5919 WVVFNEKNKELCAWLVQMENKVLQTADISIEEMIEKLQKDC---MEEINLFSENKLQLKQMGDQLIKaSNKSRAAEIDDK 5995
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHealEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5996 LNKINDRWQHLFDVIGSRVKKLKETFAFIQQLDKnMSNLRTWLARIESELSKPVVYDvcDDQEIQKRLAEQQDLQRDIEQ 6075
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530403352 6076 HSAGVESVFNICDVLLHDsdacANETECDSIQQTTRSLDRRWRNICAMSMERRMKIEE 6133
Cdd:cd00176   158 HEPRLKSLNELAEELLEE----GHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
185-281 2.66e-16

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 77.74  E-value: 2.66e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352    185 KALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVK----HRSNKDNLREAFRIAEQELKIPRLLE 260
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAaslsRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 530403352    261 PEDVDVVDPDEKSIMTYVAQF 281
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
KASH pfam10541
Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS ...
6891-6922 3.02e-16

Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS domain is a highly hydrophobic nuclear envelope localization domain of approximately 60 amino acids comprising a 20-amino-acid transmembrane region and a 30-35-residue C-terminal region that lies between the inner and the outer nuclear membranes. During meiotic prophase, telomeres cluster to form a bouquet arrangement of chromosomes. SUN and KASH domain proteins form complexes that span both membranes of the nuclear envelope. The KASH domain links the dynein motor complex of the microtubules, through the outer nuclear membrane to the Sad1 domain in the inner nuclear membrane which then interacts with the bouquet proteins Bqt1 and Bqt2 that are complexed with Bqt4, Rap1 and Taz1 and attached to the telomere. SUN domain-containing proteins are essential for recruiting KASH domain proteins at the outer nuclear membrane, and KASH domains provide a generic NE tethering device for functionally distinct proteins whose cytoplasmic domains mediate nuclear positioning, maintain physical connections with other cellular organelles, and possibly even influence chromosome dynamics.


Pssm-ID: 463142  Cd Length: 58  Bit Score: 76.09  E-value: 3.02e-16
                           10        20        30
                   ....*....|....*....|....*....|..
gi 530403352  6891 PSSEEDYSCTQANNFARSFYPMLRYTNGPPPT 6922
Cdd:pfam10541   27 PAGEEDYSCTLANNFARSFHPMLRYVNGPPPT 58
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
31-137 2.53e-15

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 75.40  E-value: 2.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352    31 DTQKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDK-GSNTFQCRINIEHALTFLRNR-SIKL 108
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*....
gi 530403352   109 INIHVTDIIDGNPSIILGLIWTIILHFHI 137
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
35-134 2.38e-14

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 72.35  E-value: 2.38e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352     35 KAFTCWINSQLArHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDK---GSNTFQCRINIEHALTFLRNRSIKLINI 111
Cdd:smart00033    1 KTLLRWVNSLLA-EYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLF 79
                            90       100
                    ....*....|....*....|...
gi 530403352    112 HVTDIIDGNPsIILGLIWTIILH 134
Cdd:smart00033   80 EPEDLVEGPK-LILGVIWTLISL 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5063-5276 2.24e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 72.86  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5063 KAITEMISWMNNVEHQTSDEDSVHSPSSasqVKHLLQKHKEFRMEMDYKQWIVDFVNQSLLQLstcdVESKRYERTEFAE 5142
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDYGDDLES---VEALLKKHEALEAELAAHEERVEALNELGEQL----IEEGHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5143 HLGEMNRQWHRVHGMLNRKIQHLEQLLESITESENKIQILnNWLEAQEERLKTLQKPESVISVQKLLLDCQDIENQLAIK 5222
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530403352 5223 SKALDELKQSYLTLESGAVPL-LEDTASRIDELFQKRSSVLTQVNQLKTSMQSVL 5276
Cdd:cd00176   159 EPRLKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6576-6799 4.11e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 69.01  E-value: 4.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6576 LQQLNSDISAITTWLKKTEaelEMLKMAKPPSDIQEIELRVKRLQEILKAFDTYKALVVSVNVSSKEFLQTESPESTELQ 6655
Cdd:cd00176     2 LQQFLRDADELEAWLSEKE---ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6656 SRLRQLSLLWEAAQGAVDSWRGGLRQSLMQCQgsktrprsdvlffkdFHQLSQNLLLWLASAKNRRQKahvTDPKADPRA 6735
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQ---------------FFRDADDLEQWLEEKEAALAS---EDLGKDLES 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530403352 6736 LLECRRELMQLEKELVERQPQVDMLQEISNSLLIKGHGEDCIEAEEKVHVIEKKLKQLREQVSQ 6799
Cdd:cd00176   141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEE 204
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4945-5169 6.03e-11

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 65.93  E-value: 6.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 4945 HLLSYNRDSDQLTKWLESSQHTLnywkeQSLNVSQDLDTIRSNINNFFEFSKEVDEKSSLKTAVISIGNQLLHLKETDTA 5024
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELL-----SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5025 TLRASLAQFEQKWTMLITQLPDIQEKLHQLQMEKLPSRKAiTEMISWMNNVEHQTSDEDSVHSPSSasqVKHLLQKHKEF 5104
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGKDLES---VEELLKKHKEL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530403352 5105 RMEMD-YKQWIVDFVN--QSLLQLSTCDVESKRYERTEfaehlgEMNRQWHRVHGMLNRKIQHLEQLL 5169
Cdd:cd00176   152 EEELEaHEPRLKSLNElaEELLEEGHPDADEEIEEKLE------ELNERWEELLELAEERQKKLEEAL 213
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1868-2417 9.86e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 9.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1868 KKSVEQKLQKLSDflTLEGRNSKIKQVDSVLKHVKKHLPKAH----VKELISWLVGQEFELEKMESICQARAKELEDSLQ 1943
Cdd:PRK03918  254 KRKLEEKIRELEE--RIEELKKEIEELEEKVKELKELKEKAEeyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1944 QLlrlQDDHRNLRKWLTNQEEKWKGMEEPGEKTELFCQALARKreqfesvAQLNNSLKEYGFTEEEEIIMEATCLMDRYQ 2023
Cdd:PRK03918  332 EL---EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK-------EELERLKKRLTGLTPEKLEKELEELEKAKE 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2024 TLLRQLSEIEEEDKLLPTEdqsfndlahdvihwIKEIKESLMVLNSSEGKMPL-------EERiqkiKEIILLKPEGDAR 2096
Cdd:PRK03918  402 EIEEEISKITARIGELKKE--------------IKELKKAIEELKKAKGKCPVcgrelteEHR----KELLEEYTAELKR 463
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2097 IETIMKQAESSEAPLvQKTLTDIsnqwDNTLHLASTYLSHQE--KLLLEGEKYLQSkedlrLMLIELKKKQEAGFALQHG 2174
Cdd:PRK03918  464 IEKELKEIEEKERKL-RKELREL----EKVLKKESELIKLKElaEQLKELEEKLKK-----YNLEELEKKAEEYEKLKEK 533
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2175 LQEKKAQLKIYKKFLKKAQDLTSLLKELKSQGNYLLEctknpsfseepwlEIKHLHESLLQQLQDSVQNLDGHVREhdsy 2254
Cdd:PRK03918  534 LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE-------------ELAELLKELEELGFESVEELEERLKE---- 596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2255 qvcvtdlnttLDNFSKEFVSFSDKPVDqiaVEEKLQKLQELENRLSLQDGTLKKILALAKSVKQNTSSVGQKIIKDDIKS 2334
Cdd:PRK03918  597 ----------LEPFYNEYLELKDAEKE---LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE 663
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2335 LQCKQKDLENRLASAKQEMEcCLNSILKSKRSTEKKGKFTLPGREKqATSDVQESTQESAAVEKLEEDWEINKDSAVEMA 2414
Cdd:PRK03918  664 LREEYLELSRELAGLRAELE-ELEKRREEIKKTLEKLKEELEEREK-AKKELEKLEKALERVEELREKVKKYKALLKERA 741

                  ...
gi 530403352 2415 MSK 2417
Cdd:PRK03918  742 LSK 744
SPEC smart00150
Spectrin repeats;
6139-6240 1.12e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.41  E-value: 1.12e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   6139 QKFLDDYSRFEDWLKSAERTAACPNSSEVLyTSAKEELKRFEAFQRQIHERLTQLELINKQYRRLARENRTDtASRLKQM 6218
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL-ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 530403352   6219 VHEGNQRWDNLQRRVTAVLRRL 6240
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5178-5384 1.13e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 53.22  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5178 KIQILNNWLEAQEERLKTLQKPESVISVQKLLLDCQDIENQLAIKSKALDELKQSYLTLESGAVPLLEDTASRIDELFQK 5257
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5258 RSSVLTQVNQLKTSMQSVLQEWKIYDQLYDEVNMMTIRFWYCMehSKPVVLSLETLRCQVENLQSLQDEAESSEGSWEKL 5337
Cdd:cd00176    88 WEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA--SEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 530403352 5338 QEVIGKLKGLC-PSVAEIIEEKCQNTHKRWTQVNQAIADQLQKAQSLL 5384
Cdd:cd00176   166 NELAEELLEEGhPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC smart00150
Spectrin repeats;
5063-5166 4.65e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.48  E-value: 4.65e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   5063 KAITEMISWMNNVEHQTSDEDSVHSPSSasqVKHLLQKHKEFRMEMDYKQWIVDFVNQSLLQLstcdVESKRYERTEFAE 5142
Cdd:smart00150    5 RDADELEAWLEEKEQLLASEDLGKDLES---VEALLKKHEAFEAELEAHEERVEALNELGEQL----IEEGHPDAEEIEE 77
                            90       100
                    ....*....|....*....|....
gi 530403352   5143 HLGEMNRQWHRVHGMLNRKIQHLE 5166
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKLE 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
5774-6081 9.44e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.76  E-value: 9.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5774 LKTKESVGRRISQLQDSWKDMEPQLAEMIKQFQSTVETWDQCEKKIKELKSRLqvlKAQSEDPLPELHEDLHNEKELIKE 5853
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAEIAS 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5854 LEQSLASWTQNLKEL--QTMKADLTRHVLVEDVMVLKEQIEHLHRQWEDLCLRVAIRKQEIEDRLNTwvvFNEKNKELCA 5931
Cdd:TIGR02169  306 LERSIAEKERELEDAeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE---LEEVDKEFAE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5932 WLVQMEnkvlqtadiSIEEMIEKLQKDcMEEINLFSENKLQLKQMGDQLIkASNKSRAAEIDDKLNKINDRWQHLFDVIG 6011
Cdd:TIGR02169  383 TRDELK---------DYREKLEKLKRE-INELKRELDRLQEELQRLSEEL-ADLNAAIAGIEAKINELEEEKEDKALEIK 451
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  6012 SRVKKLKETFAFIQQLDKNMSNLRTWLARIESELSKPvvydvcdDQEIQKRLAEQQDLQRDIEQHSAGVE 6081
Cdd:TIGR02169  452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL-------QRELAEAEAQARASEERVRGGRAVEE 514
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2338-2712 1.31e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.38  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2338 KQKDLENRLASAKQEMECCLNSILKSKRSTEKkgkftlpgREKQATSDVQESTQESAAVEK----LEEDWEINK----DS 2409
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIEN--------RLDELSQELSDASRKIGEIEKeieqLEQEEEKLKerleEL 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2410 AVEMAMSKQLSLNAQESMKNTED-----ERKVNELQNQPLELDTMLRNEQLEEIEKLYTQLEAKKAAIKpleqteclnkt 2484
Cdd:TIGR02169  743 EEDLSSLEQEIENVKSELKELEArieelEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE----------- 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2485 etgaLVLHNIGYSAQHLDNLLQALITLKKNKESQycvLRDFQEYLAAVESSMKALLTDKESLKvgpldsvTYLDKIKKFI 2564
Cdd:TIGR02169  812 ----ARLREIEQKLNRLTLEKEYLEKEIQELQEQ---RIDLKEQIKSIEKEIENLNGKKEELE-------EELEELEAAL 877
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2565 ASIEKEkdsLGNLKIKWENLSNHVTDMDKKL--LESQIKQLEHGWEQVEQQIQKKySQQVVEYDEfttlmNKVQDTEISL 2642
Cdd:TIGR02169  878 RDLESR---LGDLKKERDELEAQLRELERKIeeLEAQIEKKRKRLSELKAKLEAL-EEELSEIED-----PKGEDEEIPE 948
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530403352  2643 QQQQQHLQLRLKSPEERAgnqsMIAL-TTDLQATKHGFSVLKGQAELQMKRIWGEKEKKNLEDGINNLKKQ 2712
Cdd:TIGR02169  949 EELSLEDVQAELQRVEEE----IRALePVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2805-3389 1.80e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 52.04  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2805 NNTLEDLRNQYQMLVLKSTQRSQQLEFKLEERSNFFAIIRKFQL----MVQESETLIIPRVETAATEAelkHHHVTLeaS 2880
Cdd:pfam15921  137 SQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLshegVLQEIRSILVDFEEASGKKI---YEHDSM--S 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2881 QKELQEIDSGISTHLQELTNiyeELNVFE-RLF-LEDQLKNLKIRT-NRIQRFIQNTCNEVE-----HKIKFCrQFHEKT 2952
Cdd:pfam15921  212 TMHFRSLGSAISKILRELDT---EISYLKgRIFpVEDQLEALKSESqNKIELLLQQHQDRIEqliseHEVEIT-GLTEKA 287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2953 SALQEEADSIQRNELLLNQEVNKGVKEEIYNLKDRLTAIKCCILQVLKLKKVFDyiglnwdfSQLDQLQTQVFEKEKELE 3032
Cdd:pfam15921  288 SSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE--------DKIEELEKQLVLANSELT 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3033 EKIKQLDTFEEEHGKYQALLSKM------RAIDLQIKKMTEVVLKAPDSSP-----------ESRRLNAQILSQRIEKAK 3095
Cdd:pfam15921  360 EARTERDQFSQESGNLDDQLQKLladlhkREKELSLEKEQNKRLWDRDTGNsitidhlrrelDDRNMEVQRLEALLKAMK 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3096 CLCD-EIIKKLNENKTFDDSFKEKEILQIKLNAEEnDKLYKVLQ-----NMVLELSPKELDE--KNCQDKlETSLHVLNQ 3167
Cdd:pfam15921  440 SECQgQMERQMAAIQGKNESLEKVSSLTAQLESTK-EMLRKVVEeltakKMTLESSERTVSDltASLQEK-ERAIEATNA 517
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3168 IKSQLQQPLLINL-EIKHIQNEKDNCEAFQEQVWA---EMCSIKAVTAIEKQREEN----------------------SS 3221
Cdd:pfam15921  518 EITKLRSRVDLKLqELQHLKNEGDHLRNVQTECEAlklQMAEKDKVIEILRQQIENmtqlvgqhgrtagamqvekaqlEK 597
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3222 EASDVETKLREFEDLQMQLNTSI---DLRTNVLNDAYENLTRYKEAVTRAVESIT----SLEAIIIPYRVDVGNPEESLE 3294
Cdd:pfam15921  598 EINDRRLELQEFKILKDKKDAKIrelEARVSDLELEKVKLVNAGSERLRAVKDIKqerdQLLNEVKTSRNELNSLSEDYE 677
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3295 MPLR----KQEELESTvahiqdlTEKLGM-ISSPEAKL-QLQYTLQELV-SKNSAMKEAFKAQE--TEAERYLENYKCYR 3365
Cdd:pfam15921  678 VLKRnfrnKSEEMETT-------TNKLKMqLKSAQSELeQTRNTLKSMEgSDGHAMKVAMGMQKqiTAKRGQIDALQSKI 750
                          650       660
                   ....*....|....*....|....
gi 530403352  3366 KMEEDIYTNLSKMETVLGQSMSSL 3389
Cdd:pfam15921  751 QFLEEAMTNANKEKHFLKEEKNKL 774
SPEC smart00150
Spectrin repeats;
6025-6132 2.51e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.55  E-value: 2.51e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   6025 QQLDKNMSNLRTWLARIESELSKPVVYDvcDDQEIQKRLAEQQDLQRDIEQHSAGVESVFNICDVLLHDSDAcanetECD 6104
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGK--DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-----DAE 73
                            90       100
                    ....*....|....*....|....*...
gi 530403352   6105 SIQQTTRSLDRRWRNICAMSMERRMKIE 6132
Cdd:smart00150   74 EIEERLEELNERWEELKELAEERRQKLE 101
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6574-6681 4.08e-05

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.16  E-value: 4.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  6574 QNLQQLNSDISAITTWLKKTEAELEMLKMAKppsDIQEIELRVKRLQEILKAFDTYKALVVSVNVSSKEFLQTESPESTE 6653
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGK---DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 530403352  6654 LQSRLRQLSLLWEAAQGAVDSWRGGLRQ 6681
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3656-3950 5.62e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 5.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3656 EIESQVEECRKALEDIDEKIsnEVLKSSPSYAMRRKIEEINNGLHNVEKMLQQKSKNIEKAQEIQKKMWDELDLWHSKLN 3735
Cdd:TIGR02169  262 ELEKRLEEIEQLLEELNKKI--KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3736 ELDSEVQDI-VEQDPGQA--QEWMDNLMIPFQQYQQVSQRAECRTSQLNKATVKMEEYSDllksteawiENTSHLLANPA 3812
Cdd:TIGR02169  340 ELEREIEEErKRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR---------EINELKRELDR 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3813 DYDSLRTLSHHASTVQMALEDSEQKHNLLHSifmdlEDLSIIFETDELTQSIQELSNQVTALQQKIMESLPQIQRMADDV 3892
Cdd:TIGR02169  411 LQEELQRLSEELADLNAAIAGIEAKINELEE-----EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530403352  3893 VAIESEVKSMEKRVSKIKTillskEIFDFSPEEhlkhgEVILENIRPMKKTIAEIVSY 3950
Cdd:TIGR02169  486 SKLQRELAEAEAQARASEE-----RVRGGRAVE-----EVLKASIQGVHGTVAQLGSV 533
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3811-4113 7.06e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 7.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3811 PADYDSLRTLSHHASTVQMALEDSEQK----HNLLHSIFMDLEDLSIifETDELTQSIQELSNQVTALQQKIMESLPQIQ 3886
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSElrriENRLDELSQELSDASR--KIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3887 RMADDVVAIESEVKSMEKRVSKIKTILLSKEIFDFSPEEHLKHGEV--ILENIRPMKKTIAEIVSYQVELRlpqtgmkpl 3964
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeIQAELSKLEEEVSRIEARLREIE--------- 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3965 pvfQRTNQLLQDIKLLENVTQEQNELLKVVIKQTNEWDEEIENLKQILNNYSAQFS-LEHMSPDQADKLPQLQGEIERME 4043
Cdd:TIGR02169  819 ---QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEeLEAALRDLESRLGDLKKERDELE 895
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4044 KQILSLNQRKEDL----------LVDLKATVLNLHQHLKQEQEGVERDR--LPAVTSEEGGVAERDASERKLNRRGSMSY 4111
Cdd:TIGR02169  896 AQLRELERKIEELeaqiekkrkrLSELKAKLEALEEELSEIEDPKGEDEeiPEEELSLEDVQAELQRVEEEIRALEPVNM 975

                   ..
gi 530403352  4112 LA 4113
Cdd:TIGR02169  976 LA 977
SPEC smart00150
Spectrin repeats;
6577-6679 1.09e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.63  E-value: 1.09e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   6577 QQLNSDISAITTWLKKTEaelEMLKMAKPPSDIQEIELRVKRLQEILKAFDTYKALVVSVNVSSKEFLQTESPESTELQS 6656
Cdd:smart00150    1 QQFLRDADELEAWLEEKE---QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEE 77
                            90       100
                    ....*....|....*....|...
gi 530403352   6657 RLRQLSLLWEAAQGAVDSWRGGL 6679
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKL 100
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1418-2014 1.93e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1418 VQEEFTEENKLLEACIFKNNELLKNIQDVQSQISKiglkdptvpaVKHRKKSLIRLDKVLDEYEEEKRHLQEMANSLPHF 1497
Cdd:PRK03918  191 IEELIKEKEKELEEVLREINEISSELPELREELEK----------LEKEVKELEELKEEIEELEKELESLEGSKRKLEEK 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1498 KDGREKTVNQQCQNTVVLWENTKAL------VTECLEQCGRVLELLKQYQNFKSILTTLIQKEESVISLQASYMGKEN-- 1569
Cdd:PRK03918  261 IRELEERIEELKKEIEELEEKVKELkelkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEErl 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1570 --LKKRIAEIEIVKEEFNEHLEVVDKINQVCKNLQFYLNKMKTFEEPPFEKEANIIVDRWLDINEKTEDYYENLGRalaL 1647
Cdd:PRK03918  341 eeLKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE---L 417
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1648 WDKLFNLKNVIDEwTEKALQKMEL--HQLTEEDRERLKEELqvheqkTSEFSRRVAEIQfllqsseiplELQVMESSILN 1725
Cdd:PRK03918  418 KKEIKELKKAIEE-LKKAKGKCPVcgRELTEEHRKELLEEY------TAELKRIEKELK----------EIEEKERKLRK 480
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1726 KMEHVQKCLTGESNCHALSGSTAELREdldqaktqigmTESLLKALSpsdsLEiftKLEEIQQQILQQKHSMILLENQIG 1805
Cdd:PRK03918  481 ELRELEKVLKKESELIKLKELAEQLKE-----------LEEKLKKYN----LE---ELEKKAEEYEKLKEKLIKLKGEIK 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1806 CLTPELS---ELKKQYESVSDLFNTKKSVLQDHFSKLLNDQCKNFNDWFSNIKvNLKECFESSETKKSVEQKLQKLSDFL 1882
Cdd:PRK03918  543 SLKKELEkleELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLK-ELEPFYNEYLELKDAEKELEREEKEL 621
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1883 -----TLEGRNSKIKQVDSVLKHVKKHLPKAHVK---ELISWLVGQEFELEKMESICQARAKELEDSLQQLLRLQDDhrn 1954
Cdd:PRK03918  622 kkleeELDKAFEELAETEKRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK--- 698
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1955 lrkwLTNQEEKwkgMEEPGEKTELFCQALARKREQFESVAQLNNSLKEYGFTEEEEIIME 2014
Cdd:PRK03918  699 ----LKEELEE---REKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASE 751
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5123-5875 3.35e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5123 LQLSTCDVESKRYERTEFAEHLGEMNRQWHRV-----------------HGMLNRKIQHLEQLLESITeseNKIQILNNW 5185
Cdd:TIGR02168  227 LALLVLRLEELREELEELQEELKEAEEELEELtaelqeleekleelrleVSELEEEIEELQKELYALA---NEISRLEQQ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5186 LEAQEERLKTLQKPESVISVQKLLLdcqdiENQLAIKSKALDELKQSYLTLEsgavPLLEDTASRIDELFQKRSSVLTQV 5265
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEEL-----ESKLDELAEELAELEEKLEELK----EELESLEAELEELEAELEELESRL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5266 NQLKTSMQSVLQEwkiYDQLYDEVNMMTIRFWYCMEHSKPVVLSLETLRCQVENLQSLQDEAEssegswekLQEVIGKLK 5345
Cdd:TIGR02168  375 EELEEQLETLRSK---VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--------LKELQAELE 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5346 GLcpsvaEIIEEKCQNTHKRWTQVNQAIADQLQKAQSLLQLWKAYSNAHGEAAARLKQQEAKFQQL----ANISMSGNNL 5421
Cdd:TIGR02168  444 EL-----EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsegvKALLKNQSGL 518
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5422 AEILPPALQDIK---------------ELQHDVQKTKEAFLQNSSVLdrlpQPAESSTHMLLPGPLHSLQRAAYLEKMLL 5486
Cdd:TIGR02168  519 SGILGVLSELISvdegyeaaieaalggRLQAVVVENLNAAKKAIAFL----KQNELGRVTFLPLDSIKGTEIQGNDREIL 594
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5487 VKANEFEFVLSQFKDFGVRLESLkglimheeenldrlhqqekenpdsfLNHVLALTAQSPDIEHLNEVSLKLPLSDVAVk 5566
Cdd:TIGR02168  595 KNIEGFLGVAKDLVKFDPKLRKA-------------------------LSYLLGGVLVVDDLDNALELAKKLRPGYRIV- 648
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5567 TLQN--MNRQWI------RATATALERCSELqgiglnEKFLYCCEKWIQLLEKIEEALKvDVANSLPELLEQQKTYKMLE 5638
Cdd:TIGR02168  649 TLDGdlVRPGGVitggsaKTNSSILERRREI------EELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKEL 721
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5639 AEVSINQTIADSYVTQSLQlldttEIENRPEFITEFSKLTDRWQNAVQGVRQRKGDVDGLV----RQWQDFTTSVENLFR 5714
Cdd:TIGR02168  722 EELSRQISALRKDLARLEA-----EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELaeaeAEIEELEAQIEQLKE 796
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5715 FLTDTSHLLSAVKGQERfslyQTRSLIHELKNKEIHFQRRrttcaltleageklllttdlktKESVGRRISQLQDSWKDM 5794
Cdd:TIGR02168  797 ELKALREALDELRAELT----LLNEEAANLRERLESLERR----------------------IAATERRLEDLEEQIEEL 850
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5795 EPQLAEMIKQFQstvETWDQCEKKIKELKSrLQVLKAQSEDPLPELHEDLHNEKELIKELEQSLASWTQNLKELQTMKAD 5874
Cdd:TIGR02168  851 SEDIESLAAEIE---ELEELIEELESELEA-LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926

                   .
gi 530403352  5875 L 5875
Cdd:TIGR02168  927 L 927
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5747-6047 4.33e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5747 KEIHFQRRRTTCALTLEAGEKLLLTTDLKTKESVGRRISQLQDSwkdmEPQLAEMIKQFQSTVETWDqcekKIKELKSRL 5826
Cdd:PRK03918  172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE----LPELREELEKLEKEVKELE----ELKEEIEEL 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5827 QVLKAQSEDPLPELHEDLHNEKELIKELEQSLASWTQNLKELQTMKADLTRHVLVEDVMV---------------LKEQI 5891
Cdd:PRK03918  244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEeyldelreiekrlsrLEEEI 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5892 EHLHRQWEDLCLRVA------IRKQEIEDRLNTWVVFNEKNKELCAWLVQMENKVLQTADISIEEMIEKLQ------KDC 5959
Cdd:PRK03918  324 NGIEERIKELEEKEErleelkKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEelekakEEI 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5960 MEEINLFSENKLQLKQMGDQLIKASNKSRAAEIDDKLNKINDRWQHLFDVIGSRVKKLKETFAFIQQLDKNMSNLRTWLA 6039
Cdd:PRK03918  404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483

                  ....*...
gi 530403352 6040 RIESELSK 6047
Cdd:PRK03918  484 ELEKVLKK 491
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1660-2352 7.20e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.65  E-value: 7.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1660 EWTEKALQKMElHQLTEEDReRLKEELQVHEQKTSEFSRRVAEIQFLLQssEIPLELQVMeSSILNKMEHVQKCLTGE-- 1737
Cdd:pfam15921   74 EHIERVLEEYS-HQVKDLQR-RLNESNELHEKQKFYLRQSVIDLQTKLQ--EMQMERDAM-ADIRRRESQSQEDLRNQlq 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1738 SNCHALSGSTAeLRED-LDQAKTQIGMTESLLkaLSPSDSLE----IFTKLEEIQQQILQQKHSMILLE-NQIGC----- 1806
Cdd:pfam15921  149 NTVHELEAAKC-LKEDmLEDSNTQIEQLRKMM--LSHEGVLQeirsILVDFEEASGKKIYEHDSMSTMHfRSLGSaiski 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1807 ---LTPELSELKKQYESVSDLFNTKKSVLQDHFSKLLNDQCKNFNDWFSNIKVNLKECFESSETKKSVEQKLQKLSDFLT 1883
Cdd:pfam15921  226 lreLDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1884 LEGRN-------------SKIKQVDSVLKHVKKhLPKAHVKELISWLVGQEFELEKMESICQARAKE---LEDSLQQLlr 1947
Cdd:pfam15921  306 EQARNqnsmymrqlsdleSTVSQLRSELREAKR-MYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKL-- 382
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1948 LQDDHRNlRKWLTNQEEKWKGMEEPGEKTELFCQALARKRE----QFESVAQLNNSLKE-------------YGFTEEEE 2010
Cdd:pfam15921  383 LADLHKR-EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDdrnmEVQRLEALLKAMKSecqgqmerqmaaiQGKNESLE 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2011 IIMEATCLMDRYQTLLRQ-LSEIEEEDKLLPTEDQSFNDLAHDvihwIKEIKESLMVLNSSEGKmpLEERIQ-KIKEIIL 2088
Cdd:pfam15921  462 KVSSLTAQLESTKEMLRKvVEELTAKKMTLESSERTVSDLTAS----LQEKERAIEATNAEITK--LRSRVDlKLQELQH 535
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2089 LKPEGDaRIETIMKQAESSEAPLVQ--KTLTDISNQWDNTLHLASTYLSHQEKLLLEGEKYLQSKEDLRLMLIELKKkqe 2166
Cdd:pfam15921  536 LKNEGD-HLRNVQTECEALKLQMAEkdKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI--- 611
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2167 agfalqhgLQEKKaQLKIyKKFLKKAQDLTSLLKELKSQGNYLLECTKnpsfseepwlEIKHLHESLLQQLQDSVQNLDG 2246
Cdd:pfam15921  612 --------LKDKK-DAKI-RELEARVSDLELEKVKLVNAGSERLRAVK----------DIKQERDQLLNEVKTSRNELNS 671
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2247 HVREhdsYQVcvtdLNTTLDNFSKEFVSFSDKPVDQIAVEEklQKLQELENRLSLQDGTLKKILALAKSV-KQNTSSVGQ 2325
Cdd:pfam15921  672 LSED---YEV----LKRNFRNKSEEMETTTNKLKMQLKSAQ--SELEQTRNTLKSMEGSDGHAMKVAMGMqKQITAKRGQ 742
                          730       740
                   ....*....|....*....|....*..
gi 530403352  2326 kiikddIKSLQCKQKDLENRLASAKQE 2352
Cdd:pfam15921  743 ------IDALQSKIQFLEEAMTNANKE 763
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5701-5916 9.53e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 44.36  E-value: 9.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5701 QWQDFTTSVENLFRFLTDTSHLLSAvkGQERFSLYQTRSLIHELKN--KEIHFQRRRttcALTLEAGEKLLLTTDLKTKE 5778
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEAleAELAAHEER---VEALNELGEQLIEEGHPDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5779 SVGRRISQLQDSWKDMEPQLAEMIKQFQSTVETW---DQCEKKIKELKSRLQVLKAQSEDPLPELHEDLHNEkelIKELE 5855
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQqffRDADDLEQWLEEKEAALASEDLGKDLESVEELLKK---HKELE 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530403352 5856 QSLASWTQNLKELQTMKADLTRHVLVEDVMVLKEQIEHLHRQWEDLCLRVAIRKQEIEDRL 5916
Cdd:cd00176   153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4496-5321 1.23e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4496 EELKTYTTQLEDLRQEASNLQTQENMTEEAYINLDKKLFEL----------FLTLSQCLSSVEEMLEMPRLYREDGSGQQ 4565
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELeeeieelqkeLYALANEISRLEQQKQILRERLANLERQL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4566 VHYETlalelkklYLALSDKKGDLLKamtwpgENTNLLLECFDNLQVCLEhtqaaavcrskSLKAGLDYNRSYQNEIKRL 4645
Cdd:TIGR02168  319 EELEA--------QLEELESKLDELA------EELAELEEKLEELKEELE-----------SLEAELEELEAELEELESR 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4646 YHQLIKSKTSLQQSLNEISgqsvaEQLQKADAytvELENAESRVAKLRDEGERLHlpyallQEVYKLEDVLdsmwgmlra 4725
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLE-----LQIASLNN---EIERLEARLERLEDRRERLQ------QEIEELLKKL--------- 430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4726 rytelsspfvtESQQDALLQGMVELVKIGKEKLAHGHLKQTKSKVALQAQIENHKVFFQKLVADMLLIQAySAKILPSLL 4805
Cdd:TIGR02168  431 -----------EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-RLDSLERLQ 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4806 QNRETFWAeqvtEVKILEEKSRQCGMKLQSLLQKWeEFDENY-ASLEKDLEILIStlpsvSLVEETEERLVERISFyqqI 4884
Cdd:TIGR02168  499 ENLEGFSE----GVKALLKNQSGLSGILGVLSELI-SVDEGYeAAIEAALGGRLQ-----AVVVENLNAAKKAIAF---L 565
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4885 KRNIGGKHARLYQTLNEGKQLVASvscpelEGQIAKLEEQWLSLNKKIDHELHRLQALLKHLLSYNRDSDQltkwLESSQ 4964
Cdd:TIGR02168  566 KQNELGRVTFLPLDSIKGTEIQGN------DREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD----LDNAL 635
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4965 HTLNYWKEQSLNVSQDLDTIR----------SNINNFFEFSKEVDEKSSLKTAVISignqLLHLKETDTATLRASLAQFE 5034
Cdd:TIGR02168  636 ELAKKLRPGYRIVTLDGDLVRpggvitggsaKTNSSILERRREIEELEEKIEELEE----KIAELEKALAELRKELEELE 711
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5035 QKWTMLITQLPDIQEKLHQLQMEKLPSRKAItemiswmNNVEHQTSDEDSVHSPSSASQVKHLLQKHKEFRMEMDYKQWI 5114
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEV-------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5115 VDfVNQSLLQLSTcDVESKRYERTEFAEHLGEMNRQWHRVHGMLNRKIQHLEQLLESITESENKIQILNNWLEAQEERLK 5194
Cdd:TIGR02168  785 EE-LEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5195 TLQKPESvisvqKLLLDCQDIENQLAIKSKALDELKQSYLTLESGavplLEDTASRIDELFQKRSSVLTQVNQLKTSMQS 5274
Cdd:TIGR02168  863 ELEELIE-----ELESELEALLNERASLEEALALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELRLEG 933
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*...
gi 530403352  5275 VLQEWK-IYDQLYDEVNMMtirFWYCMEHSKPVVLSLETLRCQVENLQ 5321
Cdd:TIGR02168  934 LEVRIDnLQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLE 978
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6024-6133 1.74e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 41.54  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  6024 IQQLDKNMSNLRTWLARIESELSKPVVYDvcDDQEIQKRLAEQQDLQRDIEQHSAGVESVFNICDVLLHDSDACAnetec 6103
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGK--DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYAS----- 75
                           90       100       110
                   ....*....|....*....|....*....|
gi 530403352  6104 DSIQQTTRSLDRRWRNICAMSMERRMKIEE 6133
Cdd:pfam00435   76 EEIQERLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3037-3371 1.77e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3037 QLDTFEEEHGK---YQALLSKMRAIdlqikKMTEVVLKAPDSSPESRRLNAQI--LSQRIEKAKCLCDEIIKKLNenktf 3111
Cdd:TIGR02169  199 QLERLRREREKaerYQALLKEKREY-----EGYELLKEKEALERQKEAIERQLasLEEELEKLTEEISELEKRLE----- 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3112 ddsfkEKEILQIKLNAEENDKL---YKVLQNMVLELspkELDEKNCQDKLETSLHVLNQIKSQLQQpllINLEIKHIQNE 3188
Cdd:TIGR02169  269 -----EIEQLLEELNKKIKDLGeeeQLRVKEKIGEL---EAEIASLERSIAEKERELEDAEERLAK---LEAEIDKLLAE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3189 KDNCEAFQEQVWAEMCSIKA-VTAIEKQREENSSEASDVETKLREFEDLQMQLNTSIDLRTNVLNDAYENLTRYKEAVTR 3267
Cdd:TIGR02169  338 IEELEREIEEERKRRDKLTEeYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3268 AVESITSLEAIIIPYRVDVGNPEESLEmplRKQEELESTVAHIQDLTEKLGMISspEAKLQLQYTLQELVSKNSAMKEAF 3347
Cdd:TIGR02169  418 LSEELADLNAAIAGIEAKINELEEEKE---DKALEIKKQEWKLEQLAADLSKYE--QELYDLKEEYDRVEKELSKLQREL 492
                          330       340
                   ....*....|....*....|....
gi 530403352  3348 KAQETEAeRYLENYKCYRKMEEDI 3371
Cdd:TIGR02169  493 AEAEAQA-RASEERVRGGRAVEEV 515
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3690-3880 2.97e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 42.82  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 3690 RKIEEINNGLHNVEKMLQQKS-----KNIEKAQEIQKKMWDELDLWHSKLNELDSEVQDIVEQDPGQA---QEWMDNLMi 3761
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDygddlESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 3762 pfQQYQQVSQRAECRTSQLNKATVKMEEYSDLLKsTEAWIENTSHLLAN---PADYDSLRTLSHHASTVQMALEDSEQKH 3838
Cdd:cd00176    86 --QRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASedlGKDLESVEELLKKHKELEEELEAHEPRL 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 530403352 3839 NLLHSIFMDLEDLSIIFETDELTQSIQELSNQVTALQQKIME 3880
Cdd:cd00176   163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEE 204
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3232-4049 3.78e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3232 EFEDLQMQL-NTSIDLRTNVLNDAYENLTRYKEAVTRAVESITSLEAIIIPY-------RVDVGNPEESLEmplRKQEEL 3303
Cdd:TIGR02168  214 RYKELKAELrELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELeekleelRLEVSELEEEIE---ELQKEL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3304 ESTVAHIQDLTEKLGMISSPEAKL-----QLQYTLQELVSKN-----------------SAMKEAFKAQETEAERYLENY 3361
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLerqleELEAQLEELESKLdelaeelaeleekleelKEELESLEAELEELEAELEEL 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3362 KCYRKMEEDIYTNLSKMETVLGQSMSSLPLSYREALERLEQSKALVSNLISTKEELMKLRQILRllrlrctendgicLLK 3441
Cdd:TIGR02168  371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-------------LKE 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3442 IVSALWEKWLSLLEAAKEWEMWCEELKQewkfVSEEIEREAIILDNLQEELPEISKTKEAatTEELSELLDCLCQYGENV 3521
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEE----LREELEEAEQALDAAERELAQLQARLDS--LERLQENLEGFSEGVKAL 511
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3522 EKQQLLLTLLLQRIRSIQNVPES-SGAVETV--PAFQEITSMKERCNKLLQKVQKNKELVQTEIQERHSFT-KEIIALKN 3597
Cdd:TIGR02168  512 LKNQSGLSGILGVLSELISVDEGyEAAIEAAlgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKgTEIQGNDR 591
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3598 FFQQTTTSFQNMAfQDHPEKSEQFEELQSILKKGKLTFENIMEKLRI--KYSEMYTIV----------------PAEIES 3659
Cdd:TIGR02168  592 EILKNIEGFLGVA-KDLVKFDPKLRKALSYLLGGVLVVDDLDNALELakKLRPGYRIVtldgdlvrpggvitggSAKTNS 670
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3660 QVEECRKALEDIDEKISnevlksspsyAMRRKIEEINNGLHNVEKMLQQKSKNIEKAQEIQKKMWDELDLWHSKLNELDS 3739
Cdd:TIGR02168  671 SILERRREIEELEEKIE----------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3740 EVQdiveqdpgQAQEWMDNLMIPFQQYQQvsQRAEcRTSQLNKATVKMEEYSDLLKSTEAWIENTS-HLLANPADYDSLR 3818
Cdd:TIGR02168  741 EVE--------QLEERIAQLSKELTELEA--EIEE-LEERLEEAEEELAEAEAEIEELEAQIEQLKeELKALREALDELR 809
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3819 ----TLSHHASTVQMALEDSEQKHNLLHSIFMDLED---------LSIIFETDELTQSIQELSNQVTALQQKIMESLPQI 3885
Cdd:TIGR02168  810 aeltLLNEEAANLRERLESLERRIAATERRLEDLEEqieelsediESLAAEIEELEELIEELESELEALLNERASLEEAL 889
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3886 QRMADDVVAIESEVKSMEKRVSKIKTILLSKeifdfspEEHLKHGEVILENIRPMKKTIAEIVS--YQVELRLPQTgmKP 3963
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEEL-------REKLAQLELRLEGLEVRIDNLQERLSeeYSLTLEEAEA--LE 960
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3964 LPVFQRTNQLLQDIKLLENvtqEQNELLKV---VIkqtnewdEEIENLKQILNNYSAQFSlehmspDQADKLPQLQGEIE 4040
Cdd:TIGR02168  961 NKIEDDEEEARRRLKRLEN---KIKELGPVnlaAI-------EEYEELKERYDFLTAQKE------DLTEAKETLEEAIE 1024

                   ....*....
gi 530403352  4041 RMEKQILSL 4049
Cdd:TIGR02168 1025 EIDREARER 1033
SPEC smart00150
Spectrin repeats;
4949-5051 3.81e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.39  E-value: 3.81e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   4949 YNRDSDQLTKWLESSQHTLnywkeQSLNVSQDLDTIRSNINNFFEFSKEVDEKSSLKTAVISIGNQLLHLKETDTATLRA 5028
Cdd:smart00150    3 FLRDADELEAWLEEKEQLL-----ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEE 77
                            90       100
                    ....*....|....*....|...
gi 530403352   5029 SLAQFEQKWTMLITQLPDIQEKL 5051
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKL 100
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4913-5198 6.93e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 6.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4913 ELEGQIAKLEEQ------WLSLNKKIDHelHRLQALLKHLLSYNRDSDQLTKWLESSQHTLNYWKEQSLNVSQDLDTIRS 4986
Cdd:TIGR02168  197 ELERQLKSLERQaekaerYKELKAELRE--LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4987 NINN-----------FFEFSKEVDEksslKTAVISIGNQLLHLKETDTATLRASLAQFEQKWTMLITQLPDIQEKLHQLQ 5055
Cdd:TIGR02168  275 EVSEleeeieelqkeLYALANEISR----LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5056 MEKLPSRKAITEMISWMNNVEhQTSDEDSVHSPSSASQVKHLLQKHKEFRMEMDY----KQWIVDFVNQSLLQLSTCDVE 5131
Cdd:TIGR02168  351 EELESLEAELEELEAELEELE-SRLEELEEQLETLRSKVAQLELQIASLNNEIERlearLERLEDRRERLQQEIEELLKK 429
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530403352  5132 SKRYERTEFAEHLGEMNRQWHRVHGMLNRKIQHLEQLLESITESENKIQILNNWLEAQEERLKTLQK 5198
Cdd:TIGR02168  430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
3858-4110 7.88e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 3858 DELTQSIQELSNQVTALQQKIMESLPQIQRMADDVVAIESEVKSMEKRVSKIKTIL--LSKEIfdfspeehlkhgEVILE 3935
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeLEKEI------------AELRA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 3936 NIRPMKKTIAEIVSYQVELRLpQTGMKPLPVFQRTNQLLQDIKLLENVTQEQNELLKVVIKQTnewdEEIENLKQILNNy 4015
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGR-QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEA- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 4016 saqfslehmspdQADKLPQLQGEIERMEKQILSLNQRKEDLLVDLKATVLNLHQHLKQEQEGVER--DRLPAVTSEEGGV 4093
Cdd:COG4942   172 ------------ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEleALIARLEAEAAAA 239
                         250
                  ....*....|....*..
gi 530403352 4094 AERDASERKLNRRGSMS 4110
Cdd:COG4942   240 AERTPAAGFAALKGKLP 256
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
1868-2635 9.29e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 9.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1868 KKSVEQKLQKLSDFLTLEgrnsKIKQVDSVLKHVKKHLpKAHVKELISWLVGQEFELEKMESICQARAKELEDSLQQLLR 1947
Cdd:TIGR00618  159 KAKSKEKKELLMNLFPLD----QYTQLALMEFAKKKSL-HGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1948 LQDDHRNLRKWLTNQEEKwkgMEEPGEKTELFCQALARKREqfesvaqLNNSLKEYGFTEEEeiiMEATCLMDRYQTLLR 2027
Cdd:TIGR00618  234 ALQQTQQSHAYLTQKREA---QEEQLKKQQLLKQLRARIEE-------LRAQEAVLEETQER---INRARKAAPLAAHIK 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2028 QLSEIEEEDKLLPTEDQS-FNDLAHDVIHWIKEIKESLmvlnSSEGKMPLEERIQKIKEIILLKPEGDARIETIMKQAES 2106
Cdd:TIGR00618  301 AVTQIEQQAQRIHTELQSkMRSRAKLLMKRAAHVKQQS----SIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2107 SEAPLvqKTLTDISNQWDNTLHLASTYLSHQEKLLLEGEKYLQSKEDLRLMLIELKKKQEA---GFALQHGLQEKKAQLK 2183
Cdd:TIGR00618  377 LTQHI--HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELqqrYAELCAAAITCTAQCE 454
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2184 IYKKFL--KKAQDLTSLLKELKSQGNYLLECTknpsfseepwlEIKHLHESLLQQLQDSVQNLDG-----HVREHDSYQV 2256
Cdd:TIGR00618  455 KLEKIHlqESAQSLKEREQQLQTKEQIHLQET-----------RKKAVVLARLLELQEEPCPLCGscihpNPARQDIDNP 523
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2257 CVTDLNTTLDNFSKEFVSFSDKPVDQIAVEEkLQKLQELENRLSLQDGTLKKILALAKSVKQNTSSVGQkiIKDDIKSLQ 2336
Cdd:TIGR00618  524 GPLTRRMQRGEQTYAQLETSEEDVYHQLTSE-RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN--ITVRLQDLT 600
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2337 CKQKDLENRLASAKQEMECCLNSILKSKRSTEKKGKFTlpgREKQATSDVQESTQESAAVEKLEEDWEINKDSAVEMAMS 2416
Cdd:TIGR00618  601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS---QELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS 677
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2417 KQLSLNAQESMKN--TEDERKVNELQNQPLELDTML------RNEQLEEIEKLYTQLEAKKAAIKPLEQT-ECLNKTETG 2487
Cdd:TIGR00618  678 RQLALQKMQSEKEqlTYWKEMLAQCQTLLRELETHIeeydreFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLK 757
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2488 ALVLHNIGYSAQHLDNL--LQALITLKKNKESQYCVLRDFQEYLAAVESSMKALLTDKESLKVgpLDSVTYLDKIKKFIA 2565
Cdd:TIGR00618  758 ARTEAHFNNNEEVTAALqtGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILN--LQCETLVQEEEQFLS 835
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530403352  2566 SIEKEKDSLGNLKIKWENLSNHVTDMDKKLLES-QIKQLEHGWEQVEQQIQKKYSQQVVEYDEFTTLMNKV 2635
Cdd:TIGR00618  836 RLEEKSATLGEITHQLLKYEECSKQLAQLTQEQaKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANV 906
 
Name Accession Description Interval E-value
CH_SYNE2_rpt1 cd21242
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ...
28-138 8.65e-69

first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409091  Cd Length: 111  Bit Score: 228.18  E-value: 8.65e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTFQCRINIEHALTFLRNRSIK 107
Cdd:cd21242     1 EQEQTQKRTFTNWINSQLAKHSPPSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530403352  108 LINIHVTDIIDGNPSIILGLIWTIILHFHIE 138
Cdd:cd21242    81 LINIHVPDIIEGKPSIILGLIWTIILHFHIE 111
CH_SYNE2_rpt2 cd21244
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ...
178-286 6.02e-65

second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409093  Cd Length: 109  Bit Score: 217.01  E-value: 6.02e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  178 RWQMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPR 257
Cdd:cd21244     1 RWKMSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPR 80
                          90       100
                  ....*....|....*....|....*....
gi 530403352  258 LLEPEDVDVVDPDEKSIMTYVAQFLQYSK 286
Cdd:cd21244    81 LLEPEDVDVVNPDEKSIMTYVAQFLQYSK 109
CH_SYNE-like_rpt1 cd21190
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ...
28-138 1.45e-60

first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409039  Cd Length: 113  Bit Score: 204.73  E-value: 1.45e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKG--SNTFQCRINIEHALTFLRNRS 105
Cdd:cd21190     1 EQERVQKKTFTNWINSHLAKLSQPIVINDLFVDIKDGTALLRLLEVLSGQKLPIESGrvLQRAHKLSNIRNALDFLTKRC 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 530403352  106 IKLINIHVTDIIDGNPSIILGLIWTIILHFHIE 138
Cdd:cd21190    81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_SYNE-like_rpt2 cd21192
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ...
180-286 2.39e-58

second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409041  Cd Length: 107  Bit Score: 198.03  E-value: 2.39e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  180 QMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLL 259
Cdd:cd21192     1 QGSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLL 80
                          90       100
                  ....*....|....*....|....*..
gi 530403352  260 EPEDVDVVDPDEKSIMTYVAQFLQYSK 286
Cdd:cd21192    81 EVEDVLVDKPDERSIMTYVSQFLRMFP 107
CH_SYNE1_rpt2 cd21243
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ...
178-283 3.49e-51

second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409092  Cd Length: 109  Bit Score: 177.51  E-value: 3.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  178 RWQMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPR 257
Cdd:cd21243     1 KFKGGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPR 80
                          90       100
                  ....*....|....*....|....*.
gi 530403352  258 LLEPEDVDVVDPDEKSIMTYVAQFLQ 283
Cdd:cd21243    81 LLDPEDVDVDKPDEKSIMTYVAQFLK 106
CH_PLEC-like_rpt2 cd21189
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
182-279 1.26e-46

second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409038  Cd Length: 105  Bit Score: 164.49  E-value: 1.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21189     1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
                          90
                  ....*....|....*...
gi 530403352  262 EDVDVVDPDEKSIMTYVA 279
Cdd:cd21189    81 EDVDVPEPDEKSIITYVS 98
CH_beta_spectrin_rpt2 cd21194
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
182-284 1.51e-43

second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409043  Cd Length: 105  Bit Score: 155.65  E-value: 1.51e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21194     2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
                          90       100
                  ....*....|....*....|...
gi 530403352  262 EDVDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21194    82 EDVDVARPDEKSIMTYVASYYHY 104
CH_SYNE1_rpt1 cd21241
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ...
28-138 2.45e-42

first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409090  Cd Length: 113  Bit Score: 152.53  E-value: 2.45e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNT--FQCRINIEHALTFLRNRS 105
Cdd:cd21241     1 EQERVQKKTFTNWINSYLAKRKPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRLkrVHFLSNINTALKFLESKK 80
                          90       100       110
                  ....*....|....*....|....*....|...
gi 530403352  106 IKLINIHVTDIIDGNPSIILGLIWTIILHFHIE 138
Cdd:cd21241    81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQIE 113
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
32-135 4.42e-39

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 142.93  E-value: 4.42e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   32 TQKKAFTCWINSQLARHTSPsvISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTFQCRINIEHALTFLRNRSIKLINI 111
Cdd:cd21188     3 VQKKTFTKWVNKHLIKARRR--VVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
                          90       100
                  ....*....|....*....|....
gi 530403352  112 HVTDIIDGNPSIILGLIWTIILHF 135
Cdd:cd21188    81 RAEDIVDGNPKLTLGLIWTIILHF 104
CH_SPTB_like_rpt2 cd21248
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
182-284 4.53e-39

second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409097  Cd Length: 105  Bit Score: 142.92  E-value: 4.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21248     2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
                          90       100
                  ....*....|....*....|...
gi 530403352  262 EDVDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21248    82 EDVNVEQPDEKSIITYVVTYYHY 104
CH_SPTBN5_rpt2 cd21249
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
180-284 4.55e-38

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409098  Cd Length: 109  Bit Score: 140.00  E-value: 4.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  180 QMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLL 259
Cdd:cd21249     2 LRSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLL 81
                          90       100
                  ....*....|....*....|....*
gi 530403352  260 EPEDVDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21249    82 DPEDVAVPHPDERSIMTYVSLYYHY 106
CH_CLMN_rpt2 cd21245
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
180-283 2.61e-37

second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409094  Cd Length: 106  Bit Score: 138.00  E-value: 2.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  180 QMSARKALLLWAQEQCATYeSVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLL 259
Cdd:cd21245     1 QRKAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLL 79
                          90       100
                  ....*....|....*....|....
gi 530403352  260 EPEDVDVVDPDEKSIMTYVAQFLQ 283
Cdd:cd21245    80 EPEDVMVDSPDEQSIMTYVAQFLE 103
CH_ACTN_rpt2 cd21216
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ...
180-281 5.84e-36

second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409065  Cd Length: 115  Bit Score: 134.41  E-value: 5.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  180 QMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLL 259
Cdd:cd21216     8 ELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDVAEKHLDIPKML 87
                          90       100
                  ....*....|....*....|...
gi 530403352  260 EPED-VDVVDPDEKSIMTYVAQF 281
Cdd:cd21216    88 DAEDiVNTPRPDERSVMTYVSCY 110
CH_SPTB_rpt2 cd21319
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ...
182-284 7.11e-36

second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409168  Cd Length: 112  Bit Score: 133.98  E-value: 7.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21319     5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
                          90       100
                  ....*....|....*....|...
gi 530403352  262 EDVDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21319    85 EDVFTENPDEKSIITYVVAFYHY 107
CH_DMD-like_rpt1 cd21186
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
31-137 7.68e-35

first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409035  Cd Length: 107  Bit Score: 130.96  E-value: 7.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   31 DTQKKAFTCWINSQLARHTSPSvISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTFQCRINIEHALTFLRNRSIKLIN 110
Cdd:cd21186     1 DVQKKTFTKWINSQLSKANKPP-IKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVN 79
                          90       100
                  ....*....|....*....|....*..
gi 530403352  111 IHVTDIIDGNPSIILGLIWTIILHFHI 137
Cdd:cd21186    80 ISSNDIVDGNPKLTLGLVWSIILHWQV 106
CH_MICALL2 cd21253
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ...
182-284 1.25e-34

calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409102  Cd Length: 106  Bit Score: 130.16  E-value: 1.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKhrsnKDNLRE----AFRIAEQELKIPR 257
Cdd:cd21253     1 AGIKALQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLS----KENVYEnnklAFTVAEKELGIPA 76
                          90       100
                  ....*....|....*....|....*...
gi 530403352  258 LLEPED-VDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21253    77 LLDAEDmVALKVPDKLSILTYVSQYYNY 104
CH_SPTB-like_rpt1 cd21246
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ...
25-133 6.58e-33

first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409095  Cd Length: 117  Bit Score: 125.56  E-value: 6.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   25 LQAEQEDTQKKAFTCWINSQLARHTSPsvISDLFTDIKKGHVLLDLLEVLSGQQLPR-DKGSNTFQCRINIEHALTFLRN 103
Cdd:cd21246     9 LADEREAVQKKTFTKWVNSHLARVGCR--INDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKE 86
                          90       100       110
                  ....*....|....*....|....*....|
gi 530403352  104 RSIKLINIHVTDIIDGNPSIILGLIWTIIL 133
Cdd:cd21246    87 QRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
CH_SPTBN2_rpt2 cd21321
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
182-284 1.01e-32

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409170  Cd Length: 119  Bit Score: 125.17  E-value: 1.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21321     5 SAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTKLLDP 84
                          90       100
                  ....*....|....*....|...
gi 530403352  262 EDVDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21321    85 EDVNVDQPDEKSIITYVATYYHY 107
CH_SpAIN1-like_rpt2 cd21291
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
181-281 1.62e-32

second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409140  Cd Length: 115  Bit Score: 124.56  E-value: 1.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  181 MSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLE 260
Cdd:cd21291     9 LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDIASKEIGIPQLLD 88
                          90       100
                  ....*....|....*....|..
gi 530403352  261 PEDV-DVVDPDEKSIMTYVAQF 281
Cdd:cd21291    89 VEDVcDVAKPDERSIMTYVAYY 110
SAC6 COG5069
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
28-279 2.35e-31

Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];


Pssm-ID: 227401 [Multi-domain]  Cd Length: 612  Bit Score: 134.30  E-value: 2.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQLARHTSPSvISDLFTDIKKGHVLLDLLEVLSGQQLPR-DKGSNTF-QCRINIEHALTFLRNRS 105
Cdd:COG5069     5 KWQKVQKKTFTKWTNEKLISGGQKE-FGDLDTDLKDGVKLAQLLEALQKDNAGEyNETPETRiHVMENVSGRLEFIKGKG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  106 IKLINIHVTDIIDGNPSIILGLIWTIILHFHIEKLAQtlscnynqpslddvsvvdsspassppakkcskvqaRWQMSARK 185
Cdd:COG5069    84 VKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINE-----------------------------------EGELTKHI 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  186 ALLLWAQEQCATYE-SVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSV-KHRSNKD-NLREAFRIAEQELKIPRLLEPE 262
Cdd:COG5069   129 NLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALIHDSRPDTLDPNVLdLQKKNKAlNNFQAFENANKVIGIARLIGVE 208
                         250
                  ....*....|....*...
gi 530403352  263 DV-DVVDPDEKSIMTYVA 279
Cdd:COG5069   209 DIvNVSIPDERSIMTYVS 226
CH_DYST_rpt2 cd21239
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
182-279 2.75e-31

second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409088  Cd Length: 104  Bit Score: 120.48  E-value: 2.75e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQeLKIPRLLEP 261
Cdd:cd21239     1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
                          90
                  ....*....|....*...
gi 530403352  262 EDVDVVDPDEKSIMTYVA 279
Cdd:cd21239    80 EDVDVSSPDEKSVITYVS 97
CH_MICAL_EHBP-like cd22198
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ...
185-281 6.81e-31

calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409188  Cd Length: 105  Bit Score: 119.31  E-value: 6.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  185 KALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEPEDV 264
Cdd:cd22198     3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEM 82
                          90
                  ....*....|....*...
gi 530403352  265 DVVD-PDEKSIMTYVAQF 281
Cdd:cd22198    83 ASLAvPDKLSMVSYLSQF 100
CH_MICALL cd21197
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ...
183-284 2.00e-30

calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409046  Cd Length: 105  Bit Score: 118.02  E-value: 2.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  183 ARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEPE 262
Cdd:cd21197     1 KIQALLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAE 80
                          90       100
                  ....*....|....*....|...
gi 530403352  263 D-VDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21197    81 DmVTMHVPDRLSIITYVSQYYNH 103
CH_DYST_rpt1 cd21236
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ...
28-140 6.22e-30

first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409085  Cd Length: 128  Bit Score: 117.78  E-value: 6.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQLARHTSPsvISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTFQCRINIEHALTFLRNRSIK 107
Cdd:cd21236    13 ERDKVQKKTFTKWINQHLMKVRKH--VNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVK 90
                          90       100       110
                  ....*....|....*....|....*....|...
gi 530403352  108 LINIHVTDIIDGNPSIILGLIWTIILHFHIEKL 140
Cdd:cd21236    91 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 123
CH_PLEC_rpt2 cd21238
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
181-279 1.02e-29

second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409087  Cd Length: 106  Bit Score: 116.27  E-value: 1.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  181 MSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLE 260
Cdd:cd21238     1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
                          90
                  ....*....|....*....
gi 530403352  261 PEDVDVVDPDEKSIMTYVA 279
Cdd:cd21238    81 PEDVDVPQPDEKSIITYVS 99
CH_MACF1_rpt2 cd21240
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
181-279 1.89e-29

second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409089  Cd Length: 107  Bit Score: 115.52  E-value: 1.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  181 MSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQeLKIPRLLE 260
Cdd:cd21240     3 MSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLLD 81
                          90
                  ....*....|....*....
gi 530403352  261 PEDVDVVDPDEKSIMTYVA 279
Cdd:cd21240    82 AEDVDVPSPDEKSVITYVS 100
CH_DMD_rpt1 cd21231
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
28-138 2.72e-29

first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.


Pssm-ID: 409080  Cd Length: 111  Bit Score: 115.02  E-value: 2.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQLARhTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTFQCRINIEHALTFLRNRSIK 107
Cdd:cd21231     2 EREDVQKKTFTKWINAQFAK-FGKPPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530403352  108 LINIHVTDIIDGNPSIILGLIWTIILHFHIE 138
Cdd:cd21231    81 LVNIGSADIVDGNHKLTLGLIWSIILHWQVK 111
CH_SPTBN4_rpt2 cd21322
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
178-284 3.54e-29

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409171  Cd Length: 130  Bit Score: 115.54  E-value: 3.54e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  178 RWQMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPR 257
Cdd:cd21322    13 RETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQAFNTAEQHLGLTK 92
                          90       100
                  ....*....|....*....|....*..
gi 530403352  258 LLEPEDVDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21322    93 LLDPEDVNMEAPDEKSIITYVVSFYHY 119
CH_SPTBN1_rpt2 cd21320
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
182-284 4.81e-29

second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409169  Cd Length: 108  Bit Score: 114.43  E-value: 4.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21320     2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
                          90       100
                  ....*....|....*....|...
gi 530403352  262 EDVDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21320    82 EDISVDHPDEKSIITYVVTYYHY 104
CH_DMD-like_rpt2 cd21187
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ...
185-283 5.26e-29

second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409036  Cd Length: 104  Bit Score: 114.06  E-value: 5.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  185 KALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEPEDV 264
Cdd:cd21187     3 KTLLAWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPEDV 82
                          90
                  ....*....|....*....
gi 530403352  265 DVVDPDEKSIMTYVAQFLQ 283
Cdd:cd21187    83 NVEQPDKKSILMYVTSLFQ 101
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
25-133 6.19e-29

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409042  Cd Length: 116  Bit Score: 114.32  E-value: 6.19e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   25 LQAEQEDTQKKAFTCWINSQLARHtsPSVISDLFTDIKKGHVLLDLLEVLSGQQLPR-DKGSNTFQCRINIEHALTFLRn 103
Cdd:cd21193     9 LQEERINIQKKTFTKWINSFLEKA--NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFLK- 85
                          90       100       110
                  ....*....|....*....|....*....|
gi 530403352  104 RSIKLINIHVTDIIDGNPSIILGLIWTIIL 133
Cdd:cd21193    86 TKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
CH_PLEC_rpt1 cd21235
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ...
28-137 7.25e-28

first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409084  Cd Length: 119  Bit Score: 111.27  E-value: 7.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQLARhtSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTFQCRINIEHALTFLRNRSIK 107
Cdd:cd21235     2 ERDRVQKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 530403352  108 LINIHVTDIIDGNPSIILGLIWTIILHFHI 137
Cdd:cd21235    80 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 109
CH_EHBP cd21198
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ...
182-280 1.23e-27

calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409047  Cd Length: 105  Bit Score: 110.21  E-value: 1.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQeLKIPRLLEP 261
Cdd:cd21198     1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
                          90       100
                  ....*....|....*....|
gi 530403352  262 EDVDVVD-PDEKSIMTYVAQ 280
Cdd:cd21198    80 ADMVLLSvPDKLSVMTYLHQ 99
CH_SPTBN2_rpt1 cd21317
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ...
24-133 1.36e-27

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409166  Cd Length: 132  Bit Score: 111.30  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   24 SLQAEQEDTQKKAFTCWINSQLARHTSPsvISDLFTDIKKGHVLLDLLEVLSGQQLPR-DKGSNTFQCRINIEHALTFLR 102
Cdd:cd21317    23 ALADEREAVQKKTFTKWVNSHLARVTCR--IGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLK 100
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530403352  103 NRSIKLINIHVTDIIDGNPSIILGLIWTIIL 133
Cdd:cd21317   101 EQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
CH_MICALL1 cd21252
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ...
183-284 3.33e-27

calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409101  Cd Length: 107  Bit Score: 109.19  E-value: 3.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  183 ARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEPE 262
Cdd:cd21252     1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
                          90       100
                  ....*....|....*....|...
gi 530403352  263 D-VDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21252    81 DmVSMKVPDCLSIMTYVSQYYNH 103
CH_SPTBN4_rpt1 cd21318
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ...
4-133 3.67e-27

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409167  Cd Length: 139  Bit Score: 110.12  E-value: 3.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352    4 SPELPTEDEQGSWGIDDLH--ISLQAEQEDTQKKAFTCWINSQLARhtSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPR 81
Cdd:cd21318     8 STERPWDEPAATAKLFECSriKALADEREAVQKKTFTKWVNSHLAR--VPCRINDLYTDLRDGYVLTRLLEVLSGEQLPK 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530403352   82 -DKGSNTFQCRINIEHALTFLRNRSIKLINIHVTDIIDGNPSIILGLIWTIIL 133
Cdd:cd21318    86 pTRGRMRIHSLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
CH_CLMN_rpt1 cd21191
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ...
28-139 9.13e-27

first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409040  Cd Length: 114  Bit Score: 108.05  E-value: 9.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSntFQCRI----NIEHALTFLRN 103
Cdd:cd21191     1 ERENVQKRTFTRWINLHLEKCNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEYKP--SSHRIfrlnNIAKALKFLED 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 530403352  104 RSIKLINIHVTDIIDGNPSIILGLIWTIILHFHIEK 139
Cdd:cd21191    79 SNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
CH_MACF1_rpt1 cd21237
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ...
28-140 5.35e-26

first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409086  Cd Length: 118  Bit Score: 106.27  E-value: 5.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQLARHTSPsvISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTFQCRINIEHALTFLRNRSIK 107
Cdd:cd21237     2 ERDRVQKKTFTKWVNKHLMKVRKH--INDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVK 79
                          90       100       110
                  ....*....|....*....|....*....|...
gi 530403352  108 LINIHVTDIIDGNPSIILGLIWTIILHFHIEKL 140
Cdd:cd21237    80 LVNIRNDDITDGNPKLTLGLIWTIILHFQISDI 112
CH_UTRN_rpt1 cd21232
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
31-138 3.39e-25

first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.


Pssm-ID: 409081  Cd Length: 107  Bit Score: 103.55  E-value: 3.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   31 DTQKKAFTCWINSQLARHTSPSvISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTFQCRINIEHALTFLRNRSIKLIN 110
Cdd:cd21232     1 DVQKKTFTKWINARFSKSGKPP-IKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVN 79
                          90       100
                  ....*....|....*....|....*...
gi 530403352  111 IHVTDIIDGNPSIILGLIWTIILHFHIE 138
Cdd:cd21232    80 IGGTDIVDGNHKLTLGLLWSIILHWQVK 107
CH_EHBP1L1 cd21255
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ...
182-284 6.53e-24

calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409104  Cd Length: 105  Bit Score: 99.48  E-value: 6.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQeLKIPRLLEP 261
Cdd:cd21255     1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
                          90       100
                  ....*....|....*....|....
gi 530403352  262 EDVDVVD-PDEKSIMTYVAQFLQY 284
Cdd:cd21255    80 ADMVLLPiPDKLIVMTYLCQLRAH 103
CH_FLN-like_rpt2 cd21184
second calponin homology (CH) domain found in the filamin family; The filamin family includes ...
182-284 8.25e-24

second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409033  Cd Length: 103  Bit Score: 99.23  E-value: 8.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYesvNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNK-DNLREAFRIAEQELKIPRLLE 260
Cdd:cd21184     1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLDKENPlENATKAMDIAEEELGIPKIIT 77
                          90       100
                  ....*....|....*....|....
gi 530403352  261 PEDVDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21184    78 PEDMVSPNVDELSVMTYLSYFRNA 101
CH_CTX_rpt2 cd21226
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
185-281 8.47e-24

second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409075  Cd Length: 103  Bit Score: 99.08  E-value: 8.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  185 KALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEPEDV 264
Cdd:cd21226     3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
                          90
                  ....*....|....*..
gi 530403352  265 DVVDPDEKSIMTYVAQF 281
Cdd:cd21226    83 MTGNPDERSIVLYTSLF 99
CH_ACTN1_rpt2 cd21287
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ...
180-281 9.63e-24

second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409136  Cd Length: 124  Bit Score: 99.77  E-value: 9.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  180 QMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLL 259
Cdd:cd21287     8 ETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKML 87
                          90       100
                  ....*....|....*....|...
gi 530403352  260 EPED-VDVVDPDEKSIMTYVAQF 281
Cdd:cd21287    88 DAEDiVGTARPDEKAIMTYVSSF 110
CH_DMD_rpt2 cd21233
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ...
183-283 9.88e-24

second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.


Pssm-ID: 409082  Cd Length: 111  Bit Score: 99.23  E-value: 9.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  183 ARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSV-KHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21233     1 SEKILLSWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVvSQQSATERLDHAFNIARQHLGIEKLLDP 80
                          90       100
                  ....*....|....*....|..
gi 530403352  262 EDVDVVDPDEKSIMTYVAQFLQ 283
Cdd:cd21233    81 EDVATAHPDKKSILMYVTSLFQ 102
CH_EHBP1 cd21254
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ...
182-280 1.10e-23

calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409103  Cd Length: 107  Bit Score: 99.16  E-value: 1.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEqELKIPRLLEP 261
Cdd:cd21254     1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEP 79
                          90       100
                  ....*....|....*....|
gi 530403352  262 EDVDVVD-PDEKSIMTYVAQ 280
Cdd:cd21254    80 SDMVLLAvPDKLTVMTYLYQ 99
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
181-281 1.17e-23

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 98.90  E-value: 1.17e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   181 MSARKALLLWAQEQCATY-ESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHR--SNKDNLREAFRIAEQELKIPR 257
Cdd:pfam00307    1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSefDKLENINLALDVAEKKLGVPK 80
                           90       100
                   ....*....|....*....|....*
gi 530403352   258 -LLEPEdvDVVDPDEKSIMTYVAQF 281
Cdd:pfam00307   81 vLIEPE--DLVEGDNKSVLTYLASL 103
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
30-135 1.34e-23

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 98.63  E-value: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   30 EDTQKKAFTCWINSQLARHTSPsvISDLFTDIKKGHVLLDLLEVLSGQQLPR--DKGSNTFQCRINIEHALTFLRNRSIK 107
Cdd:cd21215     2 VDVQKKTFTKWLNTKLSSRGLS--ITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVK 79
                          90       100
                  ....*....|....*....|....*...
gi 530403352  108 LINIHVTDIIDGNPSIILGLIWTIILHF 135
Cdd:cd21215    80 LTNIGAEDIVDGNLKLILGLLWTLILRF 107
CH_ACTN3_rpt2 cd21289
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ...
180-281 1.51e-23

second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409138  Cd Length: 124  Bit Score: 99.41  E-value: 1.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  180 QMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLL 259
Cdd:cd21289     8 ETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEVAEKYLDIPKML 87
                          90       100
                  ....*....|....*....|...
gi 530403352  260 EPED-VDVVDPDEKSIMTYVAQF 281
Cdd:cd21289    88 DAEDiVNTPKPDEKAIMTYVSCF 110
CH_ACTN4_rpt2 cd21290
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ...
180-281 1.99e-23

second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409139  Cd Length: 125  Bit Score: 99.00  E-value: 1.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  180 QMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLL 259
Cdd:cd21290    11 ETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKML 90
                          90       100
                  ....*....|....*....|...
gi 530403352  260 EPED-VDVVDPDEKSIMTYVAQF 281
Cdd:cd21290    91 DAEDiVNTARPDEKAIMTYVSSF 113
CH_MICAL2_3-like cd21195
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ...
187-287 1.35e-21

calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409044 [Multi-domain]  Cd Length: 110  Bit Score: 93.18  E-value: 1.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  187 LLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLE-PEDVD 265
Cdd:cd21195     9 LLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMAS 88
                          90       100
                  ....*....|....*....|..
gi 530403352  266 VVDPDEKSIMTYVAQFLQYSKD 287
Cdd:cd21195    89 AQEPDKLSMVMYLSKFYELFRG 110
CH_ACTN2_rpt2 cd21288
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ...
180-281 1.66e-21

second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409137  Cd Length: 124  Bit Score: 93.60  E-value: 1.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  180 QMSARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLL 259
Cdd:cd21288     8 ETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEIAEKHLDIPKML 87
                          90       100
                  ....*....|....*....|...
gi 530403352  260 EPED-VDVVDPDEKSIMTYVAQF 281
Cdd:cd21288    88 DAEDiVNTPKPDERAIMTYVSCF 110
CH_SPTBN1_rpt1 cd21316
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ...
24-133 2.73e-21

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409165  Cd Length: 154  Bit Score: 93.95  E-value: 2.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   24 SLQAEQEDTQKKAFTCWINSQLARHTSPsvISDLFTDIKKGHVLLDLLEVLSGQQLPR-DKGSNTFQCRINIEHALTFLR 102
Cdd:cd21316    45 ALADEREAVQKKTFTKWVNSHLARVSCR--ITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLK 122
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530403352  103 NRSIKLINIHVTDIIDGNPSIILGLIWTIIL 133
Cdd:cd21316   123 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
30-133 2.76e-21

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 92.07  E-value: 2.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   30 EDTQKKAFTCWINSQLaRHTSPSvISDLFTDIKKGHVLLDLLEVLSGQQLPR-DKGSNTFQCRINIEHALTFLRNRSIKL 108
Cdd:cd21214     3 EKQQRKTFTAWCNSHL-RKAGTQ-IENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKL 80
                          90       100
                  ....*....|....*....|....*
gi 530403352  109 INIHVTDIIDGNPSIILGLIWTIIL 133
Cdd:cd21214    81 VSIGAEEIVDGNLKMTLGMIWTIIL 105
CH_SPTBN5_rpt1 cd21247
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ...
19-137 9.96e-21

first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409096  Cd Length: 125  Bit Score: 91.36  E-value: 9.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   19 DDLHI-SLQAEQEDTQKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPR-DKGSNTFQCRINIEH 96
Cdd:cd21247     6 EKGHIrKLQEQRMTMQKKTFTKWMNNVFSKNGAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSK 85
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 530403352   97 ALTFLRNRsIKLINIHVTDIIDGNPSIILGLIWTIILHFHI 137
Cdd:cd21247    86 AITFLKTK-VPVKLIGPENIVDGDRTLILGLIWIIILRFQI 125
CH_MICAL3 cd21251
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ...
187-287 2.02e-20

calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409100 [Multi-domain]  Cd Length: 111  Bit Score: 90.01  E-value: 2.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  187 LLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKI-PRLLEPEDVD 265
Cdd:cd21251    10 LLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGIsPIMTGKEMAS 89
                          90       100
                  ....*....|....*....|..
gi 530403352  266 VVDPDEKSIMTYVAQFLQYSKD 287
Cdd:cd21251    90 VGEPDKLSMVMYLTQFYEMFKD 111
CH_UTRN_rpt2 cd21234
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ...
183-283 6.72e-20

second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.


Pssm-ID: 409083 [Multi-domain]  Cd Length: 104  Bit Score: 88.09  E-value: 6.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  183 ARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEPE 262
Cdd:cd21234     1 SEKILLSWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPE 80
                          90       100
                  ....*....|....*....|.
gi 530403352  263 DVDVVDPDEKSIMTYVAQFLQ 283
Cdd:cd21234    81 DVAVQLPDKKSIIMYLTSLFE 101
CH_CYTS cd21199
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ...
182-284 1.58e-19

calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409048  Cd Length: 112  Bit Score: 87.42  E-value: 1.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEqELKIPRLLEP 261
Cdd:cd21199     8 SKRNALLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTI 86
                          90       100
                  ....*....|....*....|....
gi 530403352  262 EDVDVVD-PDEKSIMTYVAQFLQY 284
Cdd:cd21199    87 DEMVSMErPDWQSVMSYVTAIYKH 110
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
33-137 4.70e-19

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409076  Cd Length: 109  Bit Score: 85.80  E-value: 4.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   33 QKKAFTCWINSQLarHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPR--DKGSNTFQCRINIEHALTFLRNRSIKLIN 110
Cdd:cd21227     5 QKNTFTNWVNEQL--KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVN 82
                          90       100
                  ....*....|....*....|....*..
gi 530403352  111 IHVTDIIDGNPSIILGLIWTIILHFHI 137
Cdd:cd21227    83 IGNEDIVNGNLKLILGLIWHLILRYQI 109
CH_MICAL2 cd21250
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ...
187-281 5.80e-19

calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409099 [Multi-domain]  Cd Length: 110  Bit Score: 85.70  E-value: 5.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  187 LLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEPEDVDV 266
Cdd:cd21250     9 LLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTGKEMAS 88
                          90
                  ....*....|....*.
gi 530403352  267 V-DPDEKSIMTYVAQF 281
Cdd:cd21250    89 AeEPDKLSMVMYLSKF 104
CH_SMTN-like cd21200
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ...
182-278 7.57e-19

calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409049  Cd Length: 107  Bit Score: 85.09  E-value: 7.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21200     1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
                          90
                  ....*....|....*....
gi 530403352  262 EDVDVV--DPDEKSIMTYV 278
Cdd:cd21200    81 EDMVRMgnRPDWKCVFTYV 99
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
33-135 1.60e-18

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409032  Cd Length: 108  Bit Score: 84.45  E-value: 1.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   33 QKKAFTCWINSQLarHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRD---KGSNTFQCRINIEHALTFLRNRSIKLI 109
Cdd:cd21183     5 QANTFTRWCNEHL--KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRSynrRPAFQQHYLENVSTALKFIEADHIKLV 82
                          90       100
                  ....*....|....*....|....*.
gi 530403352  110 NIHVTDIIDGNPSIILGLIWTIILHF 135
Cdd:cd21183    83 NIGSGDIVNGNIKLILGLIWTLILHY 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6137-6350 1.87e-18

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 87.50  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6137 LWQKFLDDYSRFEDWLKSAERTAACPNSSEVLyTSAKEELKRFEAFQRQIHERLTQLELINKQYRRLARENRTDtASRLK 6216
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDL-ESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPD-AEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6217 QMVHEGNQRWDNLQRRVTAVLRRLRHFTNQREEFEGTREsILVWLTEMDLQLTNVEHF-SESDADDKMRQLNGFQQEITL 6295
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGkDLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530403352 6296 NTNKIDQLIVFGEQLIQKSEPLDAVLIEDELEELHRYCQEVFGRVSRFHRRLTSC 6350
Cdd:cd00176   158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
CH_dFLNA-like_rpt1 cd21311
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
33-137 2.15e-18

first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409160  Cd Length: 124  Bit Score: 84.43  E-value: 2.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   33 QKKAFTCWINSQLarHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTF--QCRINIEHALTFLRN-RSIKLI 109
Cdd:cd21311    16 QQNTFTRWANEHL--KTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRPTFrsQKLENVSVALKFLEEdEGIKIV 93
                          90       100
                  ....*....|....*....|....*...
gi 530403352  110 NIHVTDIIDGNPSIILGLIWTIILHFHI 137
Cdd:cd21311    94 NIDSSDIVDGKLKLILGLIWTLILHYSI 121
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
33-135 2.85e-18

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 83.40  E-value: 2.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   33 QKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPR--DKGSNTFQCRINIEHALTFLRNRSIKLIN 110
Cdd:cd21212     1 EIEIYTDWANHYLEKGGHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGihSRPKTRAQKLENIQACLQFLAALGVDVQG 80
                          90       100
                  ....*....|....*....|....*
gi 530403352  111 IHVTDIIDGNPSIILGLIWTIILHF 135
Cdd:cd21212    81 ITAEDIVDGNLKAILGLFFSLSRYK 105
CH_SMTNB cd21259
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ...
182-281 2.06e-17

calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409108  Cd Length: 112  Bit Score: 81.19  E-value: 2.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21259     1 SIKQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDV 80
                          90       100
                  ....*....|....*....|.
gi 530403352  262 ED-VDVVDPDEKSIMTYVAQF 281
Cdd:cd21259    81 EDmVRMREPDWKCVYTYIQEF 101
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5919-6133 2.37e-16

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 81.72  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5919 WVVFNEKNKELCAWLVQMENKVLQTADISIEEMIEKLQKDC---MEEINLFSENKLQLKQMGDQLIKaSNKSRAAEIDDK 5995
Cdd:cd00176     2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHealEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5996 LNKINDRWQHLFDVIGSRVKKLKETFAFIQQLDKnMSNLRTWLARIESELSKPVVYDvcDDQEIQKRLAEQQDLQRDIEQ 6075
Cdd:cd00176    81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRD-ADDLEQWLEEKEAALASEDLGK--DLESVEELLKKHKELEEELEA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530403352 6076 HSAGVESVFNICDVLLHDsdacANETECDSIQQTTRSLDRRWRNICAMSMERRMKIEE 6133
Cdd:cd00176   158 HEPRLKSLNELAEELLEE----GHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
CH_SMTNL1 cd21260
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ...
184-281 2.38e-16

calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409109  Cd Length: 116  Bit Score: 78.59  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  184 RKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEPED 263
Cdd:cd21260     3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
                          90
                  ....*....|....*....
gi 530403352  264 -VDVVDPDEKSIMTYVAQF 281
Cdd:cd21260    83 mVRMSVPDSKCVYTYIQEL 101
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
185-281 2.66e-16

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 77.74  E-value: 2.66e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352    185 KALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVK----HRSNKDNLREAFRIAEQELKIPRLLE 260
Cdd:smart00033    1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAaslsRFKKIENINLALSFAEKLGGKVVLFE 80
                            90       100
                    ....*....|....*....|.
gi 530403352    261 PEDVDVVDPDEKSIMTYVAQF 281
Cdd:smart00033   81 PEDLVEGPKLILGVIWTLISL 101
KASH pfam10541
Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS ...
6891-6922 3.02e-16

Nuclear envelope localization domain; The KASH (for Klarsicht/ANC-1/Syne-1 homology) or KLS domain is a highly hydrophobic nuclear envelope localization domain of approximately 60 amino acids comprising a 20-amino-acid transmembrane region and a 30-35-residue C-terminal region that lies between the inner and the outer nuclear membranes. During meiotic prophase, telomeres cluster to form a bouquet arrangement of chromosomes. SUN and KASH domain proteins form complexes that span both membranes of the nuclear envelope. The KASH domain links the dynein motor complex of the microtubules, through the outer nuclear membrane to the Sad1 domain in the inner nuclear membrane which then interacts with the bouquet proteins Bqt1 and Bqt2 that are complexed with Bqt4, Rap1 and Taz1 and attached to the telomere. SUN domain-containing proteins are essential for recruiting KASH domain proteins at the outer nuclear membrane, and KASH domains provide a generic NE tethering device for functionally distinct proteins whose cytoplasmic domains mediate nuclear positioning, maintain physical connections with other cellular organelles, and possibly even influence chromosome dynamics.


Pssm-ID: 463142  Cd Length: 58  Bit Score: 76.09  E-value: 3.02e-16
                           10        20        30
                   ....*....|....*....|....*....|..
gi 530403352  6891 PSSEEDYSCTQANNFARSFYPMLRYTNGPPPT 6922
Cdd:pfam10541   27 PAGEEDYSCTLANNFARSFHPMLRYVNGPPPT 58
CH_SMTNA cd21258
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ...
182-278 4.22e-16

calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409107  Cd Length: 111  Bit Score: 77.40  E-value: 4.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21258     1 SIKQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEV 80
                          90
                  ....*....|....*....
gi 530403352  262 EDVDVV--DPDEKSIMTYV 278
Cdd:cd21258    81 EDMMIMgkKPDSKCVFTYV 99
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
33-135 6.67e-16

first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409077  Cd Length: 108  Bit Score: 76.76  E-value: 6.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   33 QKKAFTCWINSQLArhTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPR--DKGSNTFQCRI-NIEHALTFLRNRSIKLI 109
Cdd:cd21228     5 QQNTFTRWCNEHLK--CVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkyNKRPTFRQMKLeNVSVALEFLERESIKLV 82
                          90       100
                  ....*....|....*....|....*.
gi 530403352  110 NIHVTDIIDGNPSIILGLIWTIILHF 135
Cdd:cd21228    83 SIDSSAIVDGNLKLILGLIWTLILHY 108
CH_CYTSB cd21257
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ...
182-284 7.08e-16

calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409106  Cd Length: 112  Bit Score: 76.99  E-value: 7.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21257     8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAESVGIKPSLELS 87
                          90       100
                  ....*....|....*....|...
gi 530403352  262 EDVDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21257    88 EMMYTDRPDWQSVMQYVAQIYKY 110
CH pfam00307
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ...
31-137 2.53e-15

Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.


Pssm-ID: 425596 [Multi-domain]  Cd Length: 109  Bit Score: 75.40  E-value: 2.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352    31 DTQKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDK-GSNTFQCRINIEHALTFLRNR-SIKL 108
Cdd:pfam00307    1 LELEKELLRWINSHLAEYGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKlNKSEFDKLENINLALDVAEKKlGVPK 80
                           90       100
                   ....*....|....*....|....*....
gi 530403352   109 INIHVTDIIDGNPSIILGLIWTIILHFHI 137
Cdd:pfam00307   81 VLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
CH_SMTNL2 cd21261
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ...
182-278 2.84e-15

calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409110  Cd Length: 107  Bit Score: 75.00  E-value: 2.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21261     1 SIKQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEV 80
                          90
                  ....*....|....*....
gi 530403352  262 EDVDVV--DPDEKSIMTYV 278
Cdd:cd21261    81 EDMMVMgrKPDPMCVFTYV 99
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
33-135 1.24e-14

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 73.10  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   33 QKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGS--NTFQCRINIEHALTFLRNRSIKLIN 110
Cdd:cd21213     1 QLQAYVAWVNSQLKKRPGIRPVQDLRRDLRDGVALAQLIEILAGEKLPGIDWNptTDAERKENVEKVLQFMASKRIRMHQ 80
                          90       100
                  ....*....|....*....|....*
gi 530403352  111 IHVTDIIDGNPSIILGLIWTIILHF 135
Cdd:cd21213    81 TSAKDIVDGNLKAIMRLILALAAHF 105
CH smart00033
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ...
35-134 2.38e-14

Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.


Pssm-ID: 214479 [Multi-domain]  Cd Length: 101  Bit Score: 72.35  E-value: 2.38e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352     35 KAFTCWINSQLArHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDK---GSNTFQCRINIEHALTFLRNRSIKLINI 111
Cdd:smart00033    1 KTLLRWVNSLLA-EYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLF 79
                            90       100
                    ....*....|....*....|...
gi 530403352    112 HVTDIIDGNPsIILGLIWTIILH 134
Cdd:smart00033   80 EPEDLVEGPK-LILGVIWTLISL 101
CH_FLN_rpt2 cd21230
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
182-281 9.30e-14

second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409079  Cd Length: 103  Bit Score: 70.49  E-value: 9.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCatyESVNVTDFKSSWRNGMAFLAIIHALRPDLI-DMKSVKHRSNKDNLREAFRIAEQELKIPRLLE 260
Cdd:cd21230     1 TPKQRLLGWIQNKI---PQLPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
                          90       100
                  ....*....|....*....|...
gi 530403352  261 PEDVdvVDP--DEKSIMTYVAQF 281
Cdd:cd21230    78 PEEI--INPnvDEMSVMTYLSQF 98
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6025-6240 1.10e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 73.63  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6025 QQLDKNMSNLRTWLARIESELSKPVVydVCDDQEIQKRLAEQQDLQRDIEQHSAGVESVFNICDVLLHdsdacANETECD 6104
Cdd:cd00176     3 QQFLRDADELEAWLSEKEELLSSTDY--GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-----EGHPDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6105 SIQQTTRSLDRRWRNICAMSMERRMKIEETWRLWQkFLDDYSRFEDWLKSAERTAAcPNSSEVLYTSAKEELKRFEAFQR 6184
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQ-FFRDADDLEQWLEEKEAALA-SEDLGKDLESVEELLKKHKELEE 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530403352 6185 QIHERLTQLELINKQYRRLARENRTDTASRLKQMVHEGNQRWDNLQRRVTAVLRRL 6240
Cdd:cd00176   154 ELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKL 209
CH_jitterbug-like_rpt2 cd21229
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
184-283 1.46e-13

second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409078  Cd Length: 105  Bit Score: 70.11  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  184 RKALLLWAQeqcATYESVNVTDFKSSWRNGMAFLAIIHALRPDLI-DMKSVkHRSNK-DNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21229     5 KKLMLAWLQ---AVLPELKITNFSTDWNDGIALSALLDYCKPGLCpNWRKL-DPSNSlENCRRAMDLAKREFNIPMVLSP 80
                          90       100
                  ....*....|....*....|..
gi 530403352  262 EDVDVVDPDEKSIMTYVAQFLQ 283
Cdd:cd21229    81 EDLSSPHLDELSGMTYLSYFMK 102
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
34-133 1.99e-13

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 69.67  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   34 KKAFTCWINSQLARHtSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRD--KGSNTFQCRINIEHALTFLRNRSI-KLIN 110
Cdd:cd00014     1 EEELLKWINEVLGEE-LPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDL 79
                          90       100
                  ....*....|....*....|....
gi 530403352  111 IHVTDII-DGNPSIILGLIWTIIL 133
Cdd:cd00014    80 FEPEDLYeKGNLKKVLGTLWALAL 103
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5063-5276 2.24e-13

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 72.86  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5063 KAITEMISWMNNVEHQTSDEDSVHSPSSasqVKHLLQKHKEFRMEMDYKQWIVDFVNQSLLQLstcdVESKRYERTEFAE 5142
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDYGDDLES---VEALLKKHEALEAELAAHEERVEALNELGEQL----IEEGHPDAEEIQE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5143 HLGEMNRQWHRVHGMLNRKIQHLEQLLESITESENKIQILnNWLEAQEERLKTLQKPESVISVQKLLLDCQDIENQLAIK 5222
Cdd:cd00176    80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLE-QWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAH 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530403352 5223 SKALDELKQSYLTLESGAVPL-LEDTASRIDELFQKRSSVLTQVNQLKTSMQSVL 5276
Cdd:cd00176   159 EPRLKSLNELAEELLEEGHPDaDEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_MICAL1 cd21196
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ...
182-281 4.70e-13

calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409045  Cd Length: 106  Bit Score: 68.53  E-value: 4.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQELKIPRLLEP 261
Cdd:cd21196     3 GTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSA 82
                          90       100
                  ....*....|....*....|
gi 530403352  262 EDVdVVDPDEKSIMTYVAQF 281
Cdd:cd21196    83 QAV-VAGSDPLGLIAYLSHF 101
CH_SF cd00014
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
184-281 7.19e-13

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


Pssm-ID: 409031 [Multi-domain]  Cd Length: 103  Bit Score: 68.13  E-value: 7.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  184 RKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSN---KDNLREAFRIAEQE-LKIPRLL 259
Cdd:cd00014     1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLgLPELDLF 80
                          90       100
                  ....*....|....*....|..
gi 530403352  260 EPEDVdVVDPDEKSIMTYVAQF 281
Cdd:cd00014    81 EPEDL-YEKGNLKKVLGTLWAL 101
CH_FLNC_rpt1 cd21310
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ...
33-137 7.41e-13

first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409159  Cd Length: 125  Bit Score: 68.90  E-value: 7.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   33 QKKAFTCWINSQLArhTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGS--NTFQCRI-NIEHALTFLRNRSIKLI 109
Cdd:cd21310    17 QQNTFTRWCNEHLK--CVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKYHPrpNFRQMKLeNVSVALEFLDREHIKLV 94
                          90       100
                  ....*....|....*....|....*...
gi 530403352  110 NIHVTDIIDGNPSIILGLIWTIILHFHI 137
Cdd:cd21310    95 SIDSKAIVDGNLKLILGLIWTLILHYSI 122
CH_CYTSA cd21256
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ...
182-284 1.06e-12

calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409105  Cd Length: 119  Bit Score: 68.18  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEQeLKIPRLLEP 261
Cdd:cd21256    14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAES-VGIKSTLDI 92
                          90       100
                  ....*....|....*....|....
gi 530403352  262 ED-VDVVDPDEKSIMTYVAQFLQY 284
Cdd:cd21256    93 NEmVRTERPDWQSVMTYVTAIYKY 116
CH_PLS_FIM_rpt1 cd21217
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
34-132 2.48e-12

first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409066 [Multi-domain]  Cd Length: 114  Bit Score: 66.83  E-value: 2.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   34 KKAFTCWINSQLAR--HTSPSVI-----SDLFTDIKKGHVLLDLLE-VLSG----QQLPRDKGSNTFQCRINIEHALTFL 101
Cdd:cd21217     3 KEAFVEHINSLLADdpDLKHLLPidpdgDDLFEALRDGVLLCKLINkIVPGtideRKLNKKKPKNIFEATENLNLALNAA 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530403352  102 RNRSIKLINIHVTDIIDGNPSIILGLIWTII 132
Cdd:cd21217    83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6576-6799 4.11e-12

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 69.01  E-value: 4.11e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6576 LQQLNSDISAITTWLKKTEaelEMLKMAKPPSDIQEIELRVKRLQEILKAFDTYKALVVSVNVSSKEFLQTESPESTELQ 6655
Cdd:cd00176     2 LQQFLRDADELEAWLSEKE---ELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6656 SRLRQLSLLWEAAQGAVDSWRGGLRQSLMQCQgsktrprsdvlffkdFHQLSQNLLLWLASAKNRRQKahvTDPKADPRA 6735
Cdd:cd00176    79 ERLEELNQRWEELRELAEERRQRLEEALDLQQ---------------FFRDADDLEQWLEEKEAALAS---EDLGKDLES 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530403352 6736 LLECRRELMQLEKELVERQPQVDMLQEISNSLLIKGHGEDCIEAEEKVHVIEKKLKQLREQVSQ 6799
Cdd:cd00176   141 VEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEE 204
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
30-131 1.66e-11

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409074  Cd Length: 111  Bit Score: 64.47  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   30 EDTQKKAFTCWINSQLARHTSPSvISDLFTDIKKGHVLLDLLEVLSGQQLPRD---KGSNTFQCRINIEHALTFLRNR-S 105
Cdd:cd21225     2 EKVQIKAFTAWVNSVLEKRGIPK-ISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlK 80
                          90       100
                  ....*....|....*....|....*.
gi 530403352  106 IKLINIHVTDIIDGNPSIILGLIWTI 131
Cdd:cd21225    81 IRVQGIGAEDFVDNNKKLILGLLWTL 106
CH_dFLNA-like_rpt2 cd21315
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ...
182-281 2.54e-11

second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409164  Cd Length: 118  Bit Score: 64.03  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQeqcATYESVNVTDFKSSWRNGMAFLAIIHALRPDLI-DMKSVKHRSNKDNLREAFRIAEQELKIPRLLE 260
Cdd:cd21315    16 TPKQRLLGWIQ---SKVPDLPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
                          90       100
                  ....*....|....*....|...
gi 530403352  261 PEDVdvVDP--DEKSIMTYVAQF 281
Cdd:cd21315    93 PEEM--VNPkvDELSMMTYLSQF 113
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4945-5169 6.03e-11

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 65.93  E-value: 6.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 4945 HLLSYNRDSDQLTKWLESSQHTLnywkeQSLNVSQDLDTIRSNINNFFEFSKEVDEKSSLKTAVISIGNQLLHLKETDTA 5024
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELL-----SSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5025 TLRASLAQFEQKWTMLITQLPDIQEKLHQLQMEKLPSRKAiTEMISWMNNVEHQTSDEDSVHSPSSasqVKHLLQKHKEF 5104
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASEDLGKDLES---VEELLKKHKEL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530403352 5105 RMEMD-YKQWIVDFVN--QSLLQLSTCDVESKRYERTEfaehlgEMNRQWHRVHGMLNRKIQHLEQLL 5169
Cdd:cd00176   152 EEELEaHEPRLKSLNElaEELLEEGHPDADEEIEEKLE------ELNERWEELLELAEERQKKLEEAL 213
CH_FLNB_rpt1 cd21309
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ...
27-137 9.38e-11

first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409158  Cd Length: 131  Bit Score: 63.18  E-value: 9.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   27 AEQEDTQKKAFTCWINSQLArhTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSN-TF-QCRI-NIEHALTFLRN 103
Cdd:cd21309    12 APWKKIQQNTFTRWCNEHLK--CVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRKYHQRpTFrQMQLeNVSVALEFLDR 89
                          90       100       110
                  ....*....|....*....|....*....|....
gi 530403352  104 RSIKLINIHVTDIIDGNPSIILGLIWTIILHFHI 137
Cdd:cd21309    90 ESIKLVSIDSKAIVDGNLKLILGLVWTLILHYSI 123
CH_FLNB_rpt2 cd21313
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ...
182-281 1.01e-10

second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409162  Cd Length: 110  Bit Score: 62.03  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  182 SARKALLLWAQEQCAtyeSVNVTDFKSSWRNGMAFLAIIHALRPDLI-DMKSVKHRSNKDNLREAFRIAEQELKIPRLLE 260
Cdd:cd21313     8 TPKQRLLGWIQNKIP---YLPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGVPQVIT 84
                          90       100
                  ....*....|....*....|.
gi 530403352  261 PEDVDVVDPDEKSIMTYVAQF 281
Cdd:cd21313    85 PEEIIHPDVDEHSVMTYLSQF 105
CH_FLNA_rpt1 cd21308
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ...
27-137 2.23e-10

first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409157  Cd Length: 129  Bit Score: 62.03  E-value: 2.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   27 AEQEDTQKKAFTCWINSQLarHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTFQCRINIEH---ALTFLRN 103
Cdd:cd21308    15 APWKKIQQNTFTRWCNEHL--KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRKHNQRPTFRQMQLENvsvALEFLDR 92
                          90       100       110
                  ....*....|....*....|....*....|....
gi 530403352  104 RSIKLINIHVTDIIDGNPSIILGLIWTIILHFHI 137
Cdd:cd21308    93 ESIKLVSIDSKAIVDGNLKLILGLIWTLILHYSI 126
CH_FLNC_rpt2 cd21314
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ...
180-281 2.85e-10

second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409163  Cd Length: 115  Bit Score: 61.24  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  180 QMSARKALLLWAQEQCAtyeSVNVTDFKSSWRNGMAFLAIIHALRPDLI-DMKSVKHRSNKDNLREAFRIAEQELKIPRL 258
Cdd:cd21314     9 KQTPKQRLLGWIQNKVP---QLPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQV 85
                          90       100
                  ....*....|....*....|....*
gi 530403352  259 LEPEDVdvVDP--DEKSIMTYVAQF 281
Cdd:cd21314    86 IAPEEI--VDPnvDEHSVMTYLSQF 108
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5830-6019 5.06e-09

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 60.15  E-value: 5.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5830 KAQSEDPlPELHEDLHNEKELIKELEQSLASWTQNLKELQTMKADLTRHvLVEDVMVLKEQIEHLHRQWEDLCLRVAIRK 5909
Cdd:cd00176    22 LLSSTDY-GDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEE-GHPDAEEIQERLEELNQRWEELRELAEERR 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5910 QEIEDRLNTWVvFNEKNKELCAWLVQMENKVLQTADISIEEMIEKLQKDC---MEEINLFSENKLQLKQMGDQLIKASNK 5986
Cdd:cd00176   100 QRLEEALDLQQ-FFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHkelEEELEAHEPRLKSLNELAEELLEEGHP 178
                         170       180       190
                  ....*....|....*....|....*....|...
gi 530403352 5987 SRAAEIDDKLNKINDRWQHLFDVIGSRVKKLKE 6019
Cdd:cd00176   179 DADEEIEEKLEELNERWEELLELAEERQKKLEE 211
CH_PLS_FIM_rpt3 cd21219
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
30-137 1.03e-08

third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409068  Cd Length: 113  Bit Score: 56.52  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   30 EDTQ-KKAFTCWINSqLARhtsPSVISDLFTDIKKGHVLLDLLE-----VLSGQQLPRDKGSNTFQCRINIEHALTFLRN 103
Cdd:cd21219     1 EGSReERAFRMWLNS-LGL---DPLINNLYEDLRDGLVLLQVLDkiqpgCVNWKKVNKPKPLNKFKKVENCNYAVDLAKK 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 530403352  104 RSIKLINIHVTDIIDGNPSIILGLIWTIIlHFHI 137
Cdd:cd21219    77 LGFSLVGIGGKDIADGNRKLTLALVWQLM-RYHV 109
CH_ASPM_rpt2 cd21224
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ...
185-282 5.49e-08

second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409073 [Multi-domain]  Cd Length: 138  Bit Score: 55.38  E-value: 5.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  185 KALLLWAQEQCATYeSVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSN-------------------------- 238
Cdd:cd21224     3 SLLLKWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTqtvdraqdeaedfwvaefspstgdsg 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530403352  239 -----KDNLREAFRIAEQELK----IPRLLEPEDVDVVDPDEKSIMTYVAqFL 282
Cdd:cd21224    82 lsselLANEKRNFKLVQQAVAelggVPALLRASDMSNTIPDEKVVILFLS-YL 133
CH_FLNA_rpt2 cd21312
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ...
180-281 8.42e-08

second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409161  Cd Length: 114  Bit Score: 54.04  E-value: 8.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  180 QMSARKALLLWAQEQCAtyeSVNVTDFKSSWRNGMAFLAIIHALRPDLI-DMKSVKHRSNKDNLREAFRIAEQELKIPRL 258
Cdd:cd21312    10 KQTPKQRLLGWIQNKLP---QLPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGIPQV 86
                          90       100
                  ....*....|....*....|....*
gi 530403352  259 LEPEDVdvVDP--DEKSIMTYVAQF 281
Cdd:cd21312    87 ITPEEI--VDPnvDEHSVMTYLSQF 109
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
35-131 7.72e-07

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409135  Cd Length: 105  Bit Score: 50.80  E-value: 7.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   35 KAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKGSNTFQCRI--NIEHALTFLRNRSIKLINIH 112
Cdd:cd21286     3 KIYTDWANHYLAKSGHKRLIKDLQQDIADGVLLAEIIQIIANEKVEDINGCPRSQSQMieNVDVCLSFLAARGVNVQGLS 82
                          90
                  ....*....|....*....
gi 530403352  113 VTDIIDGNPSIILGLIWTI 131
Cdd:cd21286    83 AEEIRNGNLKAILGLFFSL 101
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1868-2417 9.86e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.84  E-value: 9.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1868 KKSVEQKLQKLSDflTLEGRNSKIKQVDSVLKHVKKHLPKAH----VKELISWLVGQEFELEKMESICQARAKELEDSLQ 1943
Cdd:PRK03918  254 KRKLEEKIRELEE--RIEELKKEIEELEEKVKELKELKEKAEeyikLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1944 QLlrlQDDHRNLRKWLTNQEEKWKGMEEPGEKTELFCQALARKreqfesvAQLNNSLKEYGFTEEEEIIMEATCLMDRYQ 2023
Cdd:PRK03918  332 EL---EEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK-------EELERLKKRLTGLTPEKLEKELEELEKAKE 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2024 TLLRQLSEIEEEDKLLPTEdqsfndlahdvihwIKEIKESLMVLNSSEGKMPL-------EERiqkiKEIILLKPEGDAR 2096
Cdd:PRK03918  402 EIEEEISKITARIGELKKE--------------IKELKKAIEELKKAKGKCPVcgrelteEHR----KELLEEYTAELKR 463
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2097 IETIMKQAESSEAPLvQKTLTDIsnqwDNTLHLASTYLSHQE--KLLLEGEKYLQSkedlrLMLIELKKKQEAGFALQHG 2174
Cdd:PRK03918  464 IEKELKEIEEKERKL-RKELREL----EKVLKKESELIKLKElaEQLKELEEKLKK-----YNLEELEKKAEEYEKLKEK 533
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2175 LQEKKAQLKIYKKFLKKAQDLTSLLKELKSQGNYLLEctknpsfseepwlEIKHLHESLLQQLQDSVQNLDGHVREhdsy 2254
Cdd:PRK03918  534 LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEE-------------ELAELLKELEELGFESVEELEERLKE---- 596
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2255 qvcvtdlnttLDNFSKEFVSFSDKPVDqiaVEEKLQKLQELENRLSLQDGTLKKILALAKSVKQNTSSVGQKIIKDDIKS 2334
Cdd:PRK03918  597 ----------LEPFYNEYLELKDAEKE---LEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE 663
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 2335 LQCKQKDLENRLASAKQEMEcCLNSILKSKRSTEKKGKFTLPGREKqATSDVQESTQESAAVEKLEEDWEINKDSAVEMA 2414
Cdd:PRK03918  664 LREEYLELSRELAGLRAELE-ELEKRREEIKKTLEKLKEELEEREK-AKKELEKLEKALERVEELREKVKKYKALLKERA 741

                  ...
gi 530403352 2415 MSK 2417
Cdd:PRK03918  742 LSK 744
SPEC smart00150
Spectrin repeats;
6139-6240 1.12e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 50.41  E-value: 1.12e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   6139 QKFLDDYSRFEDWLKSAERTAACPNSSEVLyTSAKEELKRFEAFQRQIHERLTQLELINKQYRRLARENRTDtASRLKQM 6218
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGKDL-ESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEER 78
                            90       100
                    ....*....|....*....|..
gi 530403352   6219 VHEGNQRWDNLQRRVTAVLRRL 6240
Cdd:smart00150   79 LEELNERWEELKELAEERRQKL 100
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5178-5384 1.13e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 53.22  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5178 KIQILNNWLEAQEERLKTLQKPESVISVQKLLLDCQDIENQLAIKSKALDELKQSYLTLESGAVPLLEDTASRIDELFQK 5257
Cdd:cd00176     8 DADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5258 RSSVLTQVNQLKTSMQSVLQEWKIYDQLYDEVNMMTIRFWYCMehSKPVVLSLETLRCQVENLQSLQDEAESSEGSWEKL 5337
Cdd:cd00176    88 WEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALA--SEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 530403352 5338 QEVIGKLKGLC-PSVAEIIEEKCQNTHKRWTQVNQAIADQLQKAQSLL 5384
Cdd:cd00176   166 NELAEELLEEGhPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_FIMB_rpt3 cd21300
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
29-137 1.29e-06

third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409149  Cd Length: 119  Bit Score: 50.89  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   29 QEDTQKKAFTCWINSQlarhTSPSVISDLFTDIKKGHVLLDLLEVLSG--------QQLPRDKGSNTFQCRINIEHALTF 100
Cdd:cd21300     4 EGEREARVFTLWLNSL----DVEPAVNDLFEDLRDGLILLQAYDKVIPgsvnwkkvNKAPASAEISRFKAVENTNYAVEL 79
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 530403352  101 LRNRSIKLINIHVTDIIDGNPSIILGLIWTiILHFHI 137
Cdd:cd21300    80 GKQLGFSLVGIQGADITDGSRTLTLALVWQ-LMRFHI 115
SPEC smart00150
Spectrin repeats;
5063-5166 4.65e-06

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 48.48  E-value: 4.65e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   5063 KAITEMISWMNNVEHQTSDEDSVHSPSSasqVKHLLQKHKEFRMEMDYKQWIVDFVNQSLLQLstcdVESKRYERTEFAE 5142
Cdd:smart00150    5 RDADELEAWLEEKEQLLASEDLGKDLES---VEALLKKHEAFEAELEAHEERVEALNELGEQL----IEEGHPDAEEIEE 77
                            90       100
                    ....*....|....*....|....
gi 530403352   5143 HLGEMNRQWHRVHGMLNRKIQHLE 5166
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKLE 101
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
5774-6081 9.44e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.76  E-value: 9.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5774 LKTKESVGRRISQLQDSWKDMEPQLAEMIKQFQSTVETWDQCEKKIKELKSRLqvlKAQSEDPLPELHEDLHNEKELIKE 5853
Cdd:TIGR02169  229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKI---KDLGEEEQLRVKEKIGELEAEIAS 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5854 LEQSLASWTQNLKEL--QTMKADLTRHVLVEDVMVLKEQIEHLHRQWEDLCLRVAIRKQEIEDRLNTwvvFNEKNKELCA 5931
Cdd:TIGR02169  306 LERSIAEKERELEDAeeRLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE---LEEVDKEFAE 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5932 WLVQMEnkvlqtadiSIEEMIEKLQKDcMEEINLFSENKLQLKQMGDQLIkASNKSRAAEIDDKLNKINDRWQHLFDVIG 6011
Cdd:TIGR02169  383 TRDELK---------DYREKLEKLKRE-INELKRELDRLQEELQRLSEEL-ADLNAAIAGIEAKINELEEEKEDKALEIK 451
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  6012 SRVKKLKETFAFIQQLDKNMSNLRTWLARIESELSKPvvydvcdDQEIQKRLAEQQDLQRDIEQHSAGVE 6081
Cdd:TIGR02169  452 KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKL-------QRELAEAEAQARASEERVRGGRAVEE 514
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
2338-2712 1.31e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.38  E-value: 1.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2338 KQKDLENRLASAKQEMECCLNSILKSKRSTEKkgkftlpgREKQATSDVQESTQESAAVEK----LEEDWEINK----DS 2409
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIEN--------RLDELSQELSDASRKIGEIEKeieqLEQEEEKLKerleEL 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2410 AVEMAMSKQLSLNAQESMKNTED-----ERKVNELQNQPLELDTMLRNEQLEEIEKLYTQLEAKKAAIKpleqteclnkt 2484
Cdd:TIGR02169  743 EEDLSSLEQEIENVKSELKELEArieelEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE----------- 811
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2485 etgaLVLHNIGYSAQHLDNLLQALITLKKNKESQycvLRDFQEYLAAVESSMKALLTDKESLKvgpldsvTYLDKIKKFI 2564
Cdd:TIGR02169  812 ----ARLREIEQKLNRLTLEKEYLEKEIQELQEQ---RIDLKEQIKSIEKEIENLNGKKEELE-------EELEELEAAL 877
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2565 ASIEKEkdsLGNLKIKWENLSNHVTDMDKKL--LESQIKQLEHGWEQVEQQIQKKySQQVVEYDEfttlmNKVQDTEISL 2642
Cdd:TIGR02169  878 RDLESR---LGDLKKERDELEAQLRELERKIeeLEAQIEKKRKRLSELKAKLEAL-EEELSEIED-----PKGEDEEIPE 948
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530403352  2643 QQQQQHLQLRLKSPEERAgnqsMIAL-TTDLQATKHGFSVLKGQAELQMKRIWGEKEKKNLEDGINNLKKQ 2712
Cdd:TIGR02169  949 EELSLEDVQAELQRVEEE----IRALePVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
2805-3389 1.80e-05

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 52.04  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2805 NNTLEDLRNQYQMLVLKSTQRSQQLEFKLEERSNFFAIIRKFQL----MVQESETLIIPRVETAATEAelkHHHVTLeaS 2880
Cdd:pfam15921  137 SQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLshegVLQEIRSILVDFEEASGKKI---YEHDSM--S 211
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2881 QKELQEIDSGISTHLQELTNiyeELNVFE-RLF-LEDQLKNLKIRT-NRIQRFIQNTCNEVE-----HKIKFCrQFHEKT 2952
Cdd:pfam15921  212 TMHFRSLGSAISKILRELDT---EISYLKgRIFpVEDQLEALKSESqNKIELLLQQHQDRIEqliseHEVEIT-GLTEKA 287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2953 SALQEEADSIQRNELLLNQEVNKGVKEEIYNLKDRLTAIKCCILQVLKLKKVFDyiglnwdfSQLDQLQTQVFEKEKELE 3032
Cdd:pfam15921  288 SSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYE--------DKIEELEKQLVLANSELT 359
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3033 EKIKQLDTFEEEHGKYQALLSKM------RAIDLQIKKMTEVVLKAPDSSP-----------ESRRLNAQILSQRIEKAK 3095
Cdd:pfam15921  360 EARTERDQFSQESGNLDDQLQKLladlhkREKELSLEKEQNKRLWDRDTGNsitidhlrrelDDRNMEVQRLEALLKAMK 439
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3096 CLCD-EIIKKLNENKTFDDSFKEKEILQIKLNAEEnDKLYKVLQ-----NMVLELSPKELDE--KNCQDKlETSLHVLNQ 3167
Cdd:pfam15921  440 SECQgQMERQMAAIQGKNESLEKVSSLTAQLESTK-EMLRKVVEeltakKMTLESSERTVSDltASLQEK-ERAIEATNA 517
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3168 IKSQLQQPLLINL-EIKHIQNEKDNCEAFQEQVWA---EMCSIKAVTAIEKQREEN----------------------SS 3221
Cdd:pfam15921  518 EITKLRSRVDLKLqELQHLKNEGDHLRNVQTECEAlklQMAEKDKVIEILRQQIENmtqlvgqhgrtagamqvekaqlEK 597
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3222 EASDVETKLREFEDLQMQLNTSI---DLRTNVLNDAYENLTRYKEAVTRAVESIT----SLEAIIIPYRVDVGNPEESLE 3294
Cdd:pfam15921  598 EINDRRLELQEFKILKDKKDAKIrelEARVSDLELEKVKLVNAGSERLRAVKDIKqerdQLLNEVKTSRNELNSLSEDYE 677
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3295 MPLR----KQEELESTvahiqdlTEKLGM-ISSPEAKL-QLQYTLQELV-SKNSAMKEAFKAQE--TEAERYLENYKCYR 3365
Cdd:pfam15921  678 VLKRnfrnKSEEMETT-------TNKLKMqLKSAQSELeQTRNTLKSMEgSDGHAMKVAMGMQKqiTAKRGQIDALQSKI 750
                          650       660
                   ....*....|....*....|....
gi 530403352  3366 KMEEDIYTNLSKMETVLGQSMSSL 3389
Cdd:pfam15921  751 QFLEEAMTNANKEKHFLKEEKNKL 774
SPEC smart00150
Spectrin repeats;
6025-6132 2.51e-05

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 46.55  E-value: 2.51e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   6025 QQLDKNMSNLRTWLARIESELSKPVVYDvcDDQEIQKRLAEQQDLQRDIEQHSAGVESVFNICDVLLHDSDAcanetECD 6104
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGK--DLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-----DAE 73
                            90       100
                    ....*....|....*....|....*...
gi 530403352   6105 SIQQTTRSLDRRWRNICAMSMERRMKIE 6132
Cdd:smart00150   74 EIEERLEELNERWEELKELAEERRQKLE 101
CH_AtFIM_like_rpt3 cd21299
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ...
29-140 2.72e-05

third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409148  Cd Length: 114  Bit Score: 46.73  E-value: 2.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   29 QEDTQKKAFTCWINSQlarhTSPSVISDLFTDIKKGHVLLDLLEVLSGQ------------QLPRDKGSNTFQCrINIEH 96
Cdd:cd21299     1 ETSREERCFRLWINSL----GIDTYVNNVFEDVRDGWVLLEVLDKVSPGsvnwkhankppiKMPFKKVENCNQV-VKIGK 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 530403352   97 ALTFlrnrsiKLINIHVTDIIDGNPSIILGLIWTiILHFHIEKL 140
Cdd:cd21299    76 QLKF------SLVNVAGNDIVQGNKKLILALLWQ-LMRYHMLQL 112
CH_PLS_rpt3 cd21298
third calponin homology (CH) domain found in the plastin family; The plastin family includes ...
28-131 2.91e-05

third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409147  Cd Length: 117  Bit Score: 46.84  E-value: 2.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   28 EQEDTQKKAFTCWINSQlarHTSPSViSDLFTDIKKGHVLLDLLEVL-------SGQQLPRDKGSNTFQCRINIEHALTF 100
Cdd:cd21298     2 IEETREEKTYRNWMNSL---GVNPFV-NHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVEL 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530403352  101 LRNRSIKLINIHVTDIIDGNPSIILGLIWTI 131
Cdd:cd21298    78 GKKLKFSLVGIGGKDIYDGNRTLTLALVWQL 108
CH_jitterbug-like_rpt3 cd21185
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
185-281 3.09e-05

third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409034  Cd Length: 98  Bit Score: 46.14  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  185 KALLLWAQEQCAtyeSVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSNKDNLREAFRIAEqELKIPRLLEPEdv 264
Cdd:cd21185     4 KATLRWVRQLLP---DVDVNNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGK-SLGVEPVLTAE-- 77
                          90
                  ....*....|....*....
gi 530403352  265 DVVDPD--EKSIMTYVAQF 281
Cdd:cd21185    78 EMADPEveHLGIMAYAAQL 96
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
4839-5053 3.78e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 48.60  E-value: 3.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 4839 KWEEFDENYASLE---KDLEILISTLPSVSLVEETEERLVErisfYQQIKRNIGGKHARLYQTLNEGKQLVASVSC--PE 4913
Cdd:cd00176     1 KLQQFLRDADELEawlSEKEELLSSTDYGDDLESVEALLKK----HEALEAELAAHEERVEALNELGEQLIEEGHPdaEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 4914 LEGQIAKLEEQWLSLNKKIDHELHRLQALLKhLLSYNRDSDQLTKWLESSQHTLnywkeQSLNVSQDLDTIRSNINNFFE 4993
Cdd:cd00176    77 IQERLEELNQRWEELRELAEERRQRLEEALD-LQQFFRDADDLEQWLEEKEAAL-----ASEDLGKDLESVEELLKKHKE 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530403352 4994 FSKEVDEKSSLKTAVISIGNQLLHLK-ETDTATLRASLAQFEQKWTMLITQLPDIQEKLHQ 5053
Cdd:cd00176   151 LEEELEAHEPRLKSLNELAEELLEEGhPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6574-6681 4.08e-05

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 46.16  E-value: 4.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  6574 QNLQQLNSDISAITTWLKKTEAELEMLKMAKppsDIQEIELRVKRLQEILKAFDTYKALVVSVNVSSKEFLQTESPESTE 6653
Cdd:pfam00435    1 LLLQQFFRDADDLESWIEEKEALLSSEDYGK---DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEE 77
                           90       100
                   ....*....|....*....|....*...
gi 530403352  6654 LQSRLRQLSLLWEAAQGAVDSWRGGLRQ 6681
Cdd:pfam00435   78 IQERLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3656-3950 5.62e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 5.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3656 EIESQVEECRKALEDIDEKIsnEVLKSSPSYAMRRKIEEINNGLHNVEKMLQQKSKNIEKAQEIQKKMWDELDLWHSKLN 3735
Cdd:TIGR02169  262 ELEKRLEEIEQLLEELNKKI--KDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3736 ELDSEVQDI-VEQDPGQA--QEWMDNLMIPFQQYQQVSQRAECRTSQLNKATVKMEEYSDllksteawiENTSHLLANPA 3812
Cdd:TIGR02169  340 ELEREIEEErKRRDKLTEeyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKR---------EINELKRELDR 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3813 DYDSLRTLSHHASTVQMALEDSEQKHNLLHSifmdlEDLSIIFETDELTQSIQELSNQVTALQQKIMESLPQIQRMADDV 3892
Cdd:TIGR02169  411 LQEELQRLSEELADLNAAIAGIEAKINELEE-----EKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL 485
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 530403352  3893 VAIESEVKSMEKRVSKIKTillskEIFDFSPEEhlkhgEVILENIRPMKKTIAEIVSY 3950
Cdd:TIGR02169  486 SKLQRELAEAEAQARASEE-----RVRGGRAVE-----EVLKASIQGVHGTVAQLGSV 533
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3811-4113 7.06e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.07  E-value: 7.06e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3811 PADYDSLRTLSHHASTVQMALEDSEQK----HNLLHSIFMDLEDLSIifETDELTQSIQELSNQVTALQQKIMESLPQIQ 3886
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSElrriENRLDELSQELSDASR--KIGEIEKEIEQLEQEEEKLKERLEELEEDLS 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3887 RMADDVVAIESEVKSMEKRVSKIKTILLSKEIFDFSPEEHLKHGEV--ILENIRPMKKTIAEIVSYQVELRlpqtgmkpl 3964
Cdd:TIGR02169  748 SLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpeIQAELSKLEEEVSRIEARLREIE--------- 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3965 pvfQRTNQLLQDIKLLENVTQEQNELLKVVIKQTNEWDEEIENLKQILNNYSAQFS-LEHMSPDQADKLPQLQGEIERME 4043
Cdd:TIGR02169  819 ---QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEeLEAALRDLESRLGDLKKERDELE 895
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4044 KQILSLNQRKEDL----------LVDLKATVLNLHQHLKQEQEGVERDR--LPAVTSEEGGVAERDASERKLNRRGSMSY 4111
Cdd:TIGR02169  896 AQLRELERKIEELeaqiekkrkrLSELKAKLEALEEELSEIEDPKGEDEeiPEEELSLEDVQAELQRVEEEIRALEPVNM 975

                   ..
gi 530403352  4112 LA 4113
Cdd:TIGR02169  976 LA 977
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
6556-6683 7.36e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 47.83  E-value: 7.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 6556 DRWEMIQ--AQELHNKLKIKQNLQQLNSDISAITTWLKKTEAELEMLkmaKPPSDIQEIELRVKRLQEILKAFDTYKALV 6633
Cdd:cd00176    86 QRWEELRelAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE---DLGKDLESVEELLKKHKELEEELEAHEPRL 162
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 530403352 6634 VSVNVSSKEFLQTESPEST-ELQSRLRQLSLLWEAAQGAVDSWRGGLRQSL 6683
Cdd:cd00176   163 KSLNELAEELLEEGHPDADeEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CH_FIMB_rpt1 cd21294
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ...
33-132 8.16e-05

first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409143  Cd Length: 125  Bit Score: 45.90  E-value: 8.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   33 QKKAFTCWINSQLA-------RHTSPSVISDLFTDIKKGHVLLDLL---------EVLSGQQLPRDKGSNTFQCRINIEH 96
Cdd:cd21294     7 ERREFTKHINAVLAgdpdvgsRLPFPTDTFQLFDECKDGLVLSKLIndsvpdtidERVLNKPPRKNKPLNNFQMIENNNI 86
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 530403352   97 ALTFLRNRSIKLINIHVTDIIDGNPSIILGLIWTII 132
Cdd:cd21294    87 VINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
SPEC smart00150
Spectrin repeats;
6577-6679 1.09e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.63  E-value: 1.09e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   6577 QQLNSDISAITTWLKKTEaelEMLKMAKPPSDIQEIELRVKRLQEILKAFDTYKALVVSVNVSSKEFLQTESPESTELQS 6656
Cdd:smart00150    1 QQFLRDADELEAWLEEKE---QLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEE 77
                            90       100
                    ....*....|....*....|...
gi 530403352   6657 RLRQLSLLWEAAQGAVDSWRGGL 6679
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKL 100
SPEC smart00150
Spectrin repeats;
5922-6018 1.57e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 44.24  E-value: 1.57e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   5922 FNEKNKELCAWLVQMENKVLQTADISIEEMIEKLQKDC---MEEINLFSENKLQLKQMGDQLIKASNKSrAAEIDDKLNK 5998
Cdd:smart00150    3 FLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHeafEAELEAHEERVEALNELGEQLIEEGHPD-AEEIEERLEE 81
                            90       100
                    ....*....|....*....|
gi 530403352   5999 INDRWQHLFDVIGSRVKKLK 6018
Cdd:smart00150   82 LNERWEELKELAEERRQKLE 101
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
29-131 1.80e-04

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409134  Cd Length: 121  Bit Score: 44.57  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   29 QEDTQKKAFTCWINSQLARHTSPSVISDLFTDIKKGHVLLDLLEVLSGQQLPRDKG--SNTFQCRINIEHALTFLRNRSI 106
Cdd:cd21285     7 ENGFDKQIYTDWANHYLAKSGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGI 86
                          90       100
                  ....*....|....*....|....*
gi 530403352  107 KLINIHVTDIIDGNPSIILGLIWTI 131
Cdd:cd21285    87 NIQGLSAEEIRNGNLKAILGLFFSL 111
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1418-2014 1.93e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1418 VQEEFTEENKLLEACIFKNNELLKNIQDVQSQISKiglkdptvpaVKHRKKSLIRLDKVLDEYEEEKRHLQEMANSLPHF 1497
Cdd:PRK03918  191 IEELIKEKEKELEEVLREINEISSELPELREELEK----------LEKEVKELEELKEEIEELEKELESLEGSKRKLEEK 260
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1498 KDGREKTVNQQCQNTVVLWENTKAL------VTECLEQCGRVLELLKQYQNFKSILTTLIQKEESVISLQASYMGKEN-- 1569
Cdd:PRK03918  261 IRELEERIEELKKEIEELEEKVKELkelkekAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEErl 340
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1570 --LKKRIAEIEIVKEEFNEHLEVVDKINQVCKNLQFYLNKMKTFEEPPFEKEANIIVDRWLDINEKTEDYYENLGRalaL 1647
Cdd:PRK03918  341 eeLKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGE---L 417
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1648 WDKLFNLKNVIDEwTEKALQKMEL--HQLTEEDRERLKEELqvheqkTSEFSRRVAEIQfllqsseiplELQVMESSILN 1725
Cdd:PRK03918  418 KKEIKELKKAIEE-LKKAKGKCPVcgRELTEEHRKELLEEY------TAELKRIEKELK----------EIEEKERKLRK 480
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1726 KMEHVQKCLTGESNCHALSGSTAELREdldqaktqigmTESLLKALSpsdsLEiftKLEEIQQQILQQKHSMILLENQIG 1805
Cdd:PRK03918  481 ELRELEKVLKKESELIKLKELAEQLKE-----------LEEKLKKYN----LE---ELEKKAEEYEKLKEKLIKLKGEIK 542
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1806 CLTPELS---ELKKQYESVSDLFNTKKSVLQDHFSKLLNDQCKNFNDWFSNIKvNLKECFESSETKKSVEQKLQKLSDFL 1882
Cdd:PRK03918  543 SLKKELEkleELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLK-ELEPFYNEYLELKDAEKELEREEKEL 621
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1883 -----TLEGRNSKIKQVDSVLKHVKKHLPKAHVK---ELISWLVGQEFELEKMESICQARAKELEDSLQQLLRLQDDhrn 1954
Cdd:PRK03918  622 kkleeELDKAFEELAETEKRLEELRKELEELEKKyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK--- 698
                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 1955 lrkwLTNQEEKwkgMEEPGEKTELFCQALARKREQFESVAQLNNSLKEYGFTEEEEIIME 2014
Cdd:PRK03918  699 ----LKEELEE---REKAKKELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASE 751
CH_PLS_FIM_rpt2 cd21218
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ...
181-280 2.93e-04

second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409067  Cd Length: 114  Bit Score: 43.83  E-value: 2.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  181 MSARKALLLWAQEQC--ATYESVNVTDFKSSWRNGMAFLAIIHALRPDLIDMKSVKHRSN-KDNLREAFRIAE--QELKI 255
Cdd:cd21218     9 LPPEEILLRWVNYHLkkAGPTKKRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSeEDLEKRAEKVLQaaEKLGC 88
                          90       100
                  ....*....|....*....|....*
gi 530403352  256 PRLLEPEdvDVVDPDEKSIMTYVAQ 280
Cdd:cd21218    89 KYFLTPE--DIVSGNPRLNLAFVAT 111
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5123-5875 3.35e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5123 LQLSTCDVESKRYERTEFAEHLGEMNRQWHRV-----------------HGMLNRKIQHLEQLLESITeseNKIQILNNW 5185
Cdd:TIGR02168  227 LALLVLRLEELREELEELQEELKEAEEELEELtaelqeleekleelrleVSELEEEIEELQKELYALA---NEISRLEQQ 303
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5186 LEAQEERLKTLQKPESVISVQKLLLdcqdiENQLAIKSKALDELKQSYLTLEsgavPLLEDTASRIDELFQKRSSVLTQV 5265
Cdd:TIGR02168  304 KQILRERLANLERQLEELEAQLEEL-----ESKLDELAEELAELEEKLEELK----EELESLEAELEELEAELEELESRL 374
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5266 NQLKTSMQSVLQEwkiYDQLYDEVNMMTIRFWYCMEHSKPVVLSLETLRCQVENLQSLQDEAEssegswekLQEVIGKLK 5345
Cdd:TIGR02168  375 EELEEQLETLRSK---VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE--------LKELQAELE 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5346 GLcpsvaEIIEEKCQNTHKRWTQVNQAIADQLQKAQSLLQLWKAYSNAHGEAAARLKQQEAKFQQL----ANISMSGNNL 5421
Cdd:TIGR02168  444 EL-----EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFsegvKALLKNQSGL 518
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5422 AEILPPALQDIK---------------ELQHDVQKTKEAFLQNSSVLdrlpQPAESSTHMLLPGPLHSLQRAAYLEKMLL 5486
Cdd:TIGR02168  519 SGILGVLSELISvdegyeaaieaalggRLQAVVVENLNAAKKAIAFL----KQNELGRVTFLPLDSIKGTEIQGNDREIL 594
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5487 VKANEFEFVLSQFKDFGVRLESLkglimheeenldrlhqqekenpdsfLNHVLALTAQSPDIEHLNEVSLKLPLSDVAVk 5566
Cdd:TIGR02168  595 KNIEGFLGVAKDLVKFDPKLRKA-------------------------LSYLLGGVLVVDDLDNALELAKKLRPGYRIV- 648
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5567 TLQN--MNRQWI------RATATALERCSELqgiglnEKFLYCCEKWIQLLEKIEEALKvDVANSLPELLEQQKTYKMLE 5638
Cdd:TIGR02168  649 TLDGdlVRPGGVitggsaKTNSSILERRREI------EELEEKIEELEEKIAELEKALA-ELRKELEELEEELEQLRKEL 721
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5639 AEVSINQTIADSYVTQSLQlldttEIENRPEFITEFSKLTDRWQNAVQGVRQRKGDVDGLV----RQWQDFTTSVENLFR 5714
Cdd:TIGR02168  722 EELSRQISALRKDLARLEA-----EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELaeaeAEIEELEAQIEQLKE 796
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5715 FLTDTSHLLSAVKGQERfslyQTRSLIHELKNKEIHFQRRrttcaltleageklllttdlktKESVGRRISQLQDSWKDM 5794
Cdd:TIGR02168  797 ELKALREALDELRAELT----LLNEEAANLRERLESLERR----------------------IAATERRLEDLEEQIEEL 850
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5795 EPQLAEMIKQFQstvETWDQCEKKIKELKSrLQVLKAQSEDPLPELHEDLHNEKELIKELEQSLASWTQNLKELQTMKAD 5874
Cdd:TIGR02168  851 SEDIESLAAEIE---ELEELIEELESELEA-LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926

                   .
gi 530403352  5875 L 5875
Cdd:TIGR02168  927 L 927
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5747-6047 4.33e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5747 KEIHFQRRRTTCALTLEAGEKLLLTTDLKTKESVGRRISQLQDSwkdmEPQLAEMIKQFQSTVETWDqcekKIKELKSRL 5826
Cdd:PRK03918  172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSE----LPELREELEKLEKEVKELE----ELKEEIEEL 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5827 QVLKAQSEDPLPELHEDLHNEKELIKELEQSLASWTQNLKELQTMKADLTRHVLVEDVMV---------------LKEQI 5891
Cdd:PRK03918  244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEeyldelreiekrlsrLEEEI 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5892 EHLHRQWEDLCLRVA------IRKQEIEDRLNTWVVFNEKNKELCAWLVQMENKVLQTADISIEEMIEKLQ------KDC 5959
Cdd:PRK03918  324 NGIEERIKELEEKEErleelkKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEelekakEEI 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5960 MEEINLFSENKLQLKQMGDQLIKASNKSRAAEIDDKLNKINDRWQHLFDVIGSRVKKLKETFAFIQQLDKNMSNLRTWLA 6039
Cdd:PRK03918  404 EEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483

                  ....*...
gi 530403352 6040 RIESELSK 6047
Cdd:PRK03918  484 ELEKVLKK 491
SPEC smart00150
Spectrin repeats;
6248-6347 7.15e-04

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 42.32  E-value: 7.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   6248 EEFEGTRESILVWLTEMDLQLTNVEHF-SESDADDKMRQLNGFQQEITLNTNKIDQLIVFGEQLIQKSEPlDAVLIEDEL 6326
Cdd:smart00150    1 QQFLRDADELEAWLEEKEQLLASEDLGkDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
                            90       100
                    ....*....|....*....|.
gi 530403352   6327 EELHRYCQEVFGRVSRFHRRL 6347
Cdd:smart00150   80 EELNERWEELKELAEERRQKL 100
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1660-2352 7.20e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 46.65  E-value: 7.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1660 EWTEKALQKMElHQLTEEDReRLKEELQVHEQKTSEFSRRVAEIQFLLQssEIPLELQVMeSSILNKMEHVQKCLTGE-- 1737
Cdd:pfam15921   74 EHIERVLEEYS-HQVKDLQR-RLNESNELHEKQKFYLRQSVIDLQTKLQ--EMQMERDAM-ADIRRRESQSQEDLRNQlq 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1738 SNCHALSGSTAeLRED-LDQAKTQIGMTESLLkaLSPSDSLE----IFTKLEEIQQQILQQKHSMILLE-NQIGC----- 1806
Cdd:pfam15921  149 NTVHELEAAKC-LKEDmLEDSNTQIEQLRKMM--LSHEGVLQeirsILVDFEEASGKKIYEHDSMSTMHfRSLGSaiski 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1807 ---LTPELSELKKQYESVSDLFNTKKSVLQDHFSKLLNDQCKNFNDWFSNIKVNLKECFESSETKKSVEQKLQKLSDFLT 1883
Cdd:pfam15921  226 lreLDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQ 305
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1884 LEGRN-------------SKIKQVDSVLKHVKKhLPKAHVKELISWLVGQEFELEKMESICQARAKE---LEDSLQQLlr 1947
Cdd:pfam15921  306 EQARNqnsmymrqlsdleSTVSQLRSELREAKR-MYEDKIEELEKQLVLANSELTEARTERDQFSQEsgnLDDQLQKL-- 382
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1948 LQDDHRNlRKWLTNQEEKWKGMEEPGEKTELFCQALARKRE----QFESVAQLNNSLKE-------------YGFTEEEE 2010
Cdd:pfam15921  383 LADLHKR-EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDdrnmEVQRLEALLKAMKSecqgqmerqmaaiQGKNESLE 461
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2011 IIMEATCLMDRYQTLLRQ-LSEIEEEDKLLPTEDQSFNDLAHDvihwIKEIKESLMVLNSSEGKmpLEERIQ-KIKEIIL 2088
Cdd:pfam15921  462 KVSSLTAQLESTKEMLRKvVEELTAKKMTLESSERTVSDLTAS----LQEKERAIEATNAEITK--LRSRVDlKLQELQH 535
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2089 LKPEGDaRIETIMKQAESSEAPLVQ--KTLTDISNQWDNTLHLASTYLSHQEKLLLEGEKYLQSKEDLRLMLIELKKkqe 2166
Cdd:pfam15921  536 LKNEGD-HLRNVQTECEALKLQMAEkdKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKI--- 611
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2167 agfalqhgLQEKKaQLKIyKKFLKKAQDLTSLLKELKSQGNYLLECTKnpsfseepwlEIKHLHESLLQQLQDSVQNLDG 2246
Cdd:pfam15921  612 --------LKDKK-DAKI-RELEARVSDLELEKVKLVNAGSERLRAVK----------DIKQERDQLLNEVKTSRNELNS 671
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2247 HVREhdsYQVcvtdLNTTLDNFSKEFVSFSDKPVDQIAVEEklQKLQELENRLSLQDGTLKKILALAKSV-KQNTSSVGQ 2325
Cdd:pfam15921  672 LSED---YEV----LKRNFRNKSEEMETTTNKLKMQLKSAQ--SELEQTRNTLKSMEGSDGHAMKVAMGMqKQITAKRGQ 742
                          730       740
                   ....*....|....*....|....*..
gi 530403352  2326 kiikddIKSLQCKQKDLENRLASAKQE 2352
Cdd:pfam15921  743 ------IDALQSKIQFLEEAMTNANKE 763
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
5701-5916 9.53e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 44.36  E-value: 9.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5701 QWQDFTTSVENLFRFLTDTSHLLSAvkGQERFSLYQTRSLIHELKN--KEIHFQRRRttcALTLEAGEKLLLTTDLKTKE 5778
Cdd:cd00176     1 KLQQFLRDADELEAWLSEKEELLSS--TDYGDDLESVEALLKKHEAleAELAAHEER---VEALNELGEQLIEEGHPDAE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 5779 SVGRRISQLQDSWKDMEPQLAEMIKQFQSTVETW---DQCEKKIKELKSRLQVLKAQSEDPLPELHEDLHNEkelIKELE 5855
Cdd:cd00176    76 EIQERLEELNQRWEELRELAEERRQRLEEALDLQqffRDADDLEQWLEEKEAALASEDLGKDLESVEELLKK---HKELE 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530403352 5856 QSLASWTQNLKELQTMKADLTRHVLVEDVMVLKEQIEHLHRQWEDLCLRVAIRKQEIEDRL 5916
Cdd:cd00176   153 EELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
1986-2476 1.17e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 45.88  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1986 KREQFESVAQLNNSLKEYGFTEEEEIIMEATCLMDRYQTLLRQLSEIEEEDKLLPTEDQSFndlahdvihWIKEIKESLM 2065
Cdd:pfam15921  343 KIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRL---------WDRDTGNSIT 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2066 VlnsSEGKMPLEERIQKIKeiillkpegdaRIETIMKQAESSEAPLVQKTLTDISNQWDNTLHLAStyLSHQekllLEGE 2145
Cdd:pfam15921  414 I---DHLRRELDDRNMEVQ-----------RLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS--LTAQ----LEST 473
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2146 KYLQSK--EDLRLMLIELKKKQEAGFALQHGLQEKKAQLKIYKKFLKKAQDLTSL----LKELKSQGNYLLECTKNPSFS 2219
Cdd:pfam15921  474 KEMLRKvvEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLklqeLQHLKNEGDHLRNVQTECEAL 553
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2220 EEPWLEIKHLHESLLQQLQDSVQNLDGHVREHDSYQVCVTDLNTTLDNFSKEFVSFsdkpvdQIAVEEKLQKLQELENRL 2299
Cdd:pfam15921  554 KLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF------KILKDKKDAKIRELEARV 627
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2300 SlqDGTLKKI---------LALAKSVKQNTSSVGQ--KIIKDDIKSLQCKQKDLENRLASAKQEMECCLNSI---LKSKR 2365
Cdd:pfam15921  628 S--DLELEKVklvnagserLRAVKDIKQERDQLLNevKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLkmqLKSAQ 705
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2366 STEKKGKFTLPGREKQ--ATSDVQESTQESAAVEKLEEDWEINKDSAVEMAMSkqlSLNAQESMKNTEDERKVNELQNQP 2443
Cdd:pfam15921  706 SELEQTRNTLKSMEGSdgHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMT---NANKEKHFLKEEKNKLSQELSTVA 782
                          490       500       510
                   ....*....|....*....|....*....|...
gi 530403352  2444 LEldtmlRNEQLEEIEKLYTQLEAKKAAIKPLE 2476
Cdd:pfam15921  783 TE-----KNKMAGELEVLRSQERRLKEKVANME 810
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4496-5321 1.23e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4496 EELKTYTTQLEDLRQEASNLQTQENMTEEAYINLDKKLFEL----------FLTLSQCLSSVEEMLEMPRLYREDGSGQQ 4565
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELeeeieelqkeLYALANEISRLEQQKQILRERLANLERQL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4566 VHYETlalelkklYLALSDKKGDLLKamtwpgENTNLLLECFDNLQVCLEhtqaaavcrskSLKAGLDYNRSYQNEIKRL 4645
Cdd:TIGR02168  319 EELEA--------QLEELESKLDELA------EELAELEEKLEELKEELE-----------SLEAELEELEAELEELESR 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4646 YHQLIKSKTSLQQSLNEISgqsvaEQLQKADAytvELENAESRVAKLRDEGERLHlpyallQEVYKLEDVLdsmwgmlra 4725
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLE-----LQIASLNN---EIERLEARLERLEDRRERLQ------QEIEELLKKL--------- 430
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4726 rytelsspfvtESQQDALLQGMVELVKIGKEKLAHGHLKQTKSKVALQAQIENHKVFFQKLVADMLLIQAySAKILPSLL 4805
Cdd:TIGR02168  431 -----------EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQA-RLDSLERLQ 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4806 QNRETFWAeqvtEVKILEEKSRQCGMKLQSLLQKWeEFDENY-ASLEKDLEILIStlpsvSLVEETEERLVERISFyqqI 4884
Cdd:TIGR02168  499 ENLEGFSE----GVKALLKNQSGLSGILGVLSELI-SVDEGYeAAIEAALGGRLQ-----AVVVENLNAAKKAIAF---L 565
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4885 KRNIGGKHARLYQTLNEGKQLVASvscpelEGQIAKLEEQWLSLNKKIDHELHRLQALLKHLLSYNRDSDQltkwLESSQ 4964
Cdd:TIGR02168  566 KQNELGRVTFLPLDSIKGTEIQGN------DREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDD----LDNAL 635
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4965 HTLNYWKEQSLNVSQDLDTIR----------SNINNFFEFSKEVDEKSSLKTAVISignqLLHLKETDTATLRASLAQFE 5034
Cdd:TIGR02168  636 ELAKKLRPGYRIVTLDGDLVRpggvitggsaKTNSSILERRREIEELEEKIEELEE----KIAELEKALAELRKELEELE 711
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5035 QKWTMLITQLPDIQEKLHQLQMEKLPSRKAItemiswmNNVEHQTSDEDSVHSPSSASQVKHLLQKHKEFRMEMDYKQWI 5114
Cdd:TIGR02168  712 EELEQLRKELEELSRQISALRKDLARLEAEV-------EQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5115 VDfVNQSLLQLSTcDVESKRYERTEFAEHLGEMNRQWHRVHGMLNRKIQHLEQLLESITESENKIQILNNWLEAQEERLK 5194
Cdd:TIGR02168  785 EE-LEAQIEQLKE-ELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5195 TLQKPESvisvqKLLLDCQDIENQLAIKSKALDELKQSYLTLESGavplLEDTASRIDELFQKRSSVLTQVNQLKTSMQS 5274
Cdd:TIGR02168  863 ELEELIE-----ELESELEALLNERASLEEALALLRSELEELSEE----LRELESKRSELRRELEELREKLAQLELRLEG 933
                          810       820       830       840
                   ....*....|....*....|....*....|....*....|....*...
gi 530403352  5275 VLQEWK-IYDQLYDEVNMMtirFWYCMEHSKPVVLSLETLRCQVENLQ 5321
Cdd:TIGR02168  934 LEVRIDnLQERLSEEYSLT---LEEAEALENKIEDDEEEARRRLKRLE 978
Spectrin pfam00435
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ...
6024-6133 1.74e-03

Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.


Pssm-ID: 395348 [Multi-domain]  Cd Length: 105  Bit Score: 41.54  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  6024 IQQLDKNMSNLRTWLARIESELSKPVVYDvcDDQEIQKRLAEQQDLQRDIEQHSAGVESVFNICDVLLHDSDACAnetec 6103
Cdd:pfam00435    3 LQQFFRDADDLESWIEEKEALLSSEDYGK--DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYAS----- 75
                           90       100       110
                   ....*....|....*....|....*....|
gi 530403352  6104 DSIQQTTRSLDRRWRNICAMSMERRMKIEE 6133
Cdd:pfam00435   76 EEIQERLEELNERWEQLLELAAERKQKLEE 105
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
3037-3371 1.77e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.44  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3037 QLDTFEEEHGK---YQALLSKMRAIdlqikKMTEVVLKAPDSSPESRRLNAQI--LSQRIEKAKCLCDEIIKKLNenktf 3111
Cdd:TIGR02169  199 QLERLRREREKaerYQALLKEKREY-----EGYELLKEKEALERQKEAIERQLasLEEELEKLTEEISELEKRLE----- 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3112 ddsfkEKEILQIKLNAEENDKL---YKVLQNMVLELspkELDEKNCQDKLETSLHVLNQIKSQLQQpllINLEIKHIQNE 3188
Cdd:TIGR02169  269 -----EIEQLLEELNKKIKDLGeeeQLRVKEKIGEL---EAEIASLERSIAEKERELEDAEERLAK---LEAEIDKLLAE 337
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3189 KDNCEAFQEQVWAEMCSIKA-VTAIEKQREENSSEASDVETKLREFEDLQMQLNTSIDLRTNVLNDAYENLTRYKEAVTR 3267
Cdd:TIGR02169  338 IEELEREIEEERKRRDKLTEeYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQR 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3268 AVESITSLEAIIIPYRVDVGNPEESLEmplRKQEELESTVAHIQDLTEKLGMISspEAKLQLQYTLQELVSKNSAMKEAF 3347
Cdd:TIGR02169  418 LSEELADLNAAIAGIEAKINELEEEKE---DKALEIKKQEWKLEQLAADLSKYE--QELYDLKEEYDRVEKELSKLQREL 492
                          330       340
                   ....*....|....*....|....
gi 530403352  3348 KAQETEAeRYLENYKCYRKMEEDI 3371
Cdd:TIGR02169  493 AEAEAQA-RASEERVRGGRAVEEV 515
CH_PLS_rpt1 cd21292
first calponin homology (CH) domain found in the plastin family; The plastin family includes ...
17-132 2.50e-03

first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409141  Cd Length: 145  Bit Score: 41.88  E-value: 2.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   17 GIDDLHISLQAEQEDTQ-------KKAFTCWINSQLA-----RHTSPSVIS--DLFTDIKKGHVLLDLLEVLSGQQLPR- 81
Cdd:cd21292     2 GIDAKGGTSEASSEGTThsyseeeKVAFVNWINKNLGddpdcKHLLPMDPNtdDLFEKVKDGILLCKMINLSVPDTIDEr 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530403352   82 ---DKGSNTFQCRINIEHALTFLRNRSIKLINIHVTDIIDGNPSIILGLIWTII 132
Cdd:cd21292    82 ainKKKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
3690-3880 2.97e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 42.82  E-value: 2.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 3690 RKIEEINNGLHNVEKMLQQKS-----KNIEKAQEIQKKMWDELDLWHSKLNELDSEVQDIVEQDPGQA---QEWMDNLMi 3761
Cdd:cd00176     7 RDADELEAWLSEKEELLSSTDygddlESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 3762 pfQQYQQVSQRAECRTSQLNKATVKMEEYSDLLKsTEAWIENTSHLLAN---PADYDSLRTLSHHASTVQMALEDSEQKH 3838
Cdd:cd00176    86 --QRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASedlGKDLESVEELLKKHKELEEELEAHEPRL 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 530403352 3839 NLLHSIFMDLEDLSIIFETDELTQSIQELSNQVTALQQKIME 3880
Cdd:cd00176   163 KSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEE 204
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3232-4049 3.78e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3232 EFEDLQMQL-NTSIDLRTNVLNDAYENLTRYKEAVTRAVESITSLEAIIIPY-------RVDVGNPEESLEmplRKQEEL 3303
Cdd:TIGR02168  214 RYKELKAELrELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELeekleelRLEVSELEEEIE---ELQKEL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3304 ESTVAHIQDLTEKLGMISSPEAKL-----QLQYTLQELVSKN-----------------SAMKEAFKAQETEAERYLENY 3361
Cdd:TIGR02168  291 YALANEISRLEQQKQILRERLANLerqleELEAQLEELESKLdelaeelaeleekleelKEELESLEAELEELEAELEEL 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3362 KCYRKMEEDIYTNLSKMETVLGQSMSSLPLSYREALERLEQSKALVSNLISTKEELMKLRQILRllrlrctendgicLLK 3441
Cdd:TIGR02168  371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE-------------LKE 437
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3442 IVSALWEKWLSLLEAAKEWEMWCEELKQewkfVSEEIEREAIILDNLQEELPEISKTKEAatTEELSELLDCLCQYGENV 3521
Cdd:TIGR02168  438 LQAELEELEEELEELQEELERLEEALEE----LREELEEAEQALDAAERELAQLQARLDS--LERLQENLEGFSEGVKAL 511
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3522 EKQQLLLTLLLQRIRSIQNVPES-SGAVETV--PAFQEITSMKERCNKLLQKVQKNKELVQTEIQERHSFT-KEIIALKN 3597
Cdd:TIGR02168  512 LKNQSGLSGILGVLSELISVDEGyEAAIEAAlgGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKgTEIQGNDR 591
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3598 FFQQTTTSFQNMAfQDHPEKSEQFEELQSILKKGKLTFENIMEKLRI--KYSEMYTIV----------------PAEIES 3659
Cdd:TIGR02168  592 EILKNIEGFLGVA-KDLVKFDPKLRKALSYLLGGVLVVDDLDNALELakKLRPGYRIVtldgdlvrpggvitggSAKTNS 670
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3660 QVEECRKALEDIDEKISnevlksspsyAMRRKIEEINNGLHNVEKMLQQKSKNIEKAQEIQKKMWDELDLWHSKLNELDS 3739
Cdd:TIGR02168  671 SILERRREIEELEEKIE----------ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA 740
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3740 EVQdiveqdpgQAQEWMDNLMIPFQQYQQvsQRAEcRTSQLNKATVKMEEYSDLLKSTEAWIENTS-HLLANPADYDSLR 3818
Cdd:TIGR02168  741 EVE--------QLEERIAQLSKELTELEA--EIEE-LEERLEEAEEELAEAEAEIEELEAQIEQLKeELKALREALDELR 809
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3819 ----TLSHHASTVQMALEDSEQKHNLLHSIFMDLED---------LSIIFETDELTQSIQELSNQVTALQQKIMESLPQI 3885
Cdd:TIGR02168  810 aeltLLNEEAANLRERLESLERRIAATERRLEDLEEqieelsediESLAAEIEELEELIEELESELEALLNERASLEEAL 889
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3886 QRMADDVVAIESEVKSMEKRVSKIKTILLSKeifdfspEEHLKHGEVILENIRPMKKTIAEIVS--YQVELRLPQTgmKP 3963
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEEL-------REKLAQLELRLEGLEVRIDNLQERLSeeYSLTLEEAEA--LE 960
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3964 LPVFQRTNQLLQDIKLLENvtqEQNELLKV---VIkqtnewdEEIENLKQILNNYSAQFSlehmspDQADKLPQLQGEIE 4040
Cdd:TIGR02168  961 NKIEDDEEEARRRLKRLEN---KIKELGPVnlaAI-------EEYEELKERYDFLTAQKE------DLTEAKETLEEAIE 1024

                   ....*....
gi 530403352  4041 RMEKQILSL 4049
Cdd:TIGR02168 1025 EIDREARER 1033
SPEC smart00150
Spectrin repeats;
4949-5051 3.81e-03

Spectrin repeats;


Pssm-ID: 197544 [Multi-domain]  Cd Length: 101  Bit Score: 40.39  E-value: 3.81e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   4949 YNRDSDQLTKWLESSQHTLnywkeQSLNVSQDLDTIRSNINNFFEFSKEVDEKSSLKTAVISIGNQLLHLKETDTATLRA 5028
Cdd:smart00150    3 FLRDADELEAWLEEKEQLL-----ASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEE 77
                            90       100
                    ....*....|....*....|...
gi 530403352   5029 SLAQFEQKWTMLITQLPDIQEKL 5051
Cdd:smart00150   78 RLEELNERWEELKELAEERRQKL 100
CH_PLS3_rpt1 cd21325
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ...
26-132 5.84e-03

first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409174  Cd Length: 148  Bit Score: 40.81  E-value: 5.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352   26 QAEQEDTQKKAFTCWINSQL-----ARHTSP--SVISDLFTDIKKGHVLLDLLEV----LSGQQLPRDKGSNTFQCRINI 94
Cdd:cd21325    18 QHSYSEEEKYAFVNWINKALendpdCRHVIPmnPNTDDLFKAVGDGIVLCKMINLsvpdTIDERAINKKKLTPFIIQENL 97
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 530403352   95 EHALTFLRNRSIKLINIHVTDIIDGNPSIILGLIWTII 132
Cdd:cd21325    98 NLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQII 135
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
3847-4077 6.26e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 6.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3847 DLEDLSIIFETDELTQ---SIQELSNQVTALQQKIMESLPQIQRMADDVVAIESEVKSMEKRVSKIKTIL--LSKEIFDF 3921
Cdd:TIGR02168  221 ELRELELALLVLRLEElreELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyaLANEISRL 300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  3922 spEEHLKHGEVILENIRpmkktiAEIVSYQVELRLpqtgmkplpVFQRTNQLLQDIKLLENVTQEQNELLKVVIKQTNEW 4001
Cdd:TIGR02168  301 --EQQKQILRERLANLE------RQLEELEAQLEE---------LESKLDELAEELAELEEKLEELKEELESLEAELEEL 363
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530403352  4002 DEEIENLKQILNNYSAQfsLEHMSPDQADKLPQ---LQGEIERMEKQILSLNQRKEDLLVDLKATVLNLHQHLKQEQEG 4077
Cdd:TIGR02168  364 EAELEELESRLEELEEQ--LETLRSKVAQLELQiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA 440
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
4913-5198 6.93e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 6.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4913 ELEGQIAKLEEQ------WLSLNKKIDHelHRLQALLKHLLSYNRDSDQLTKWLESSQHTLNYWKEQSLNVSQDLDTIRS 4986
Cdd:TIGR02168  197 ELERQLKSLERQaekaerYKELKAELRE--LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  4987 NINN-----------FFEFSKEVDEksslKTAVISIGNQLLHLKETDTATLRASLAQFEQKWTMLITQLPDIQEKLHQLQ 5055
Cdd:TIGR02168  275 EVSEleeeieelqkeLYALANEISR----LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5056 MEKLPSRKAITEMISWMNNVEhQTSDEDSVHSPSSASQVKHLLQKHKEFRMEMDY----KQWIVDFVNQSLLQLSTCDVE 5131
Cdd:TIGR02168  351 EELESLEAELEELEAELEELE-SRLEELEEQLETLRSKVAQLELQIASLNNEIERlearLERLEDRRERLQQEIEELLKK 429
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530403352  5132 SKRYERTEFAEHLGEMNRQWHRVHGMLNRKIQHLEQLLESITESENKIQILNNWLEAQEERLKTLQK 5198
Cdd:TIGR02168  430 LEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
3858-4110 7.88e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.83  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 3858 DELTQSIQELSNQVTALQQKIMESLPQIQRMADDVVAIESEVKSMEKRVSKIKTIL--LSKEIfdfspeehlkhgEVILE 3935
Cdd:COG4942    30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELaeLEKEI------------AELRA 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 3936 NIRPMKKTIAEIVSYQVELRLpQTGMKPLPVFQRTNQLLQDIKLLENVTQEQNELLKVVIKQTnewdEEIENLKQILNNy 4015
Cdd:COG4942    98 ELEAQKEELAELLRALYRLGR-QPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL----AELAALRAELEA- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352 4016 saqfslehmspdQADKLPQLQGEIERMEKQILSLNQRKEDLLVDLKATVLNLHQHLKQEQEGVER--DRLPAVTSEEGGV 4093
Cdd:COG4942   172 ------------ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEleALIARLEAEAAAA 239
                         250
                  ....*....|....*..
gi 530403352 4094 AERDASERKLNRRGSMS 4110
Cdd:COG4942   240 AERTPAAGFAALKGKLP 256
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
2140-2991 8.06e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 8.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2140 LLLEGEKYLQSKEDLRLMLIELKKKQEAGFALQHGLQEKKAQLKiyKKFLKKAQDLTSLLKELKSQGNYLLECTKnpsfs 2219
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR--LEVSELEEEIEELQKELYALANEISRLEQ----- 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2220 eepwlEIKHLHESLlQQLQDSVQNLDGHVREHDSYQVC----VTDLNTTLDNFSKEFVSFSDKpvdqiaVEEKLQKLQEL 2295
Cdd:TIGR02168  303 -----QKQILRERL-ANLERQLEELEAQLEELESKLDElaeeLAELEEKLEELKEELESLEAE------LEELEAELEEL 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2296 ENRLSLQDgtlKKILALAKSVKQntssvgqkiIKDDIKSLQCKQKDLENRLASAKQEMEcclnsILKSKRSTEkkgkftl 2375
Cdd:TIGR02168  371 ESRLEELE---EQLETLRSKVAQ---------LELQIASLNNEIERLEARLERLEDRRE-----RLQQEIEEL------- 426
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2376 pgREKQATSDVQESTQESAAVEKLEEDWEINKDSAVEMAMSKQLSLNAQESmKNTEDERKVNELQNQPLELDTMLRN-EQ 2454
Cdd:TIGR02168  427 --LKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ-ALDAAERELAQLQARLDSLERLQENlEG 503
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2455 LEEIEKLYTQLEAKKAAIKPL--EQTECLNKTETGALVLhnIGYSAQHL--DNL---LQALITLKKNKESQ--YCVLRDF 2525
Cdd:TIGR02168  504 FSEGVKALLKNQSGLSGILGVlsELISVDEGYEAAIEAA--LGGRLQAVvvENLnaaKKAIAFLKQNELGRvtFLPLDSI 581
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2526 QEylAAVESSMKALLTDKESLKVGPLDSVTYLDKIKKFIASIekekdsLGNLKIkwenlsnhVTDMDKKLleSQIKQLEH 2605
Cdd:TIGR02168  582 KG--TEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYL------LGGVLV--------VDDLDNAL--ELAKKLRP 643
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2606 GWEQVEQQIQKKYSQQVVeydefttlmnkvqdteislqqqqqhlqlrlkSPEERAGNQSMIALTTDLQATKHGFSVLKGQ 2685
Cdd:TIGR02168  644 GYRIVTLDGDLVRPGGVI-------------------------------TGGSAKTNSSILERRREIEELEEKIEELEEK 692
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2686 -AELQMKRIWGEKEKKNLEDGINNLKKQWETLEPLHLEAENQIKKCDIR-NKMKETILWAKNLLGELNPSIPLLPDDILS 2763
Cdd:TIGR02168  693 iAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEvEQLEERIAQLSKELTELEAEIEELEERLEE 772
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2764 QIRKCKVTHDGILARQQSVESLAEEVKdkvpsLTTYEGSDLNNTLEDLRNQYQmlvlKSTQRSQQLEFKLEERSNffAII 2843
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELK-----ALREALDELRAELTLLNEEAA----NLRERLESLERRIAATER--RLE 841
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2844 RKFQLMVQESETLIIPRVETAATEAELKHHHVTLEASQKELQEIDSGISTHLQELTNIYEELNVFE--RLFLEDQLKNLK 2921
Cdd:TIGR02168  842 DLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskRSELRRELEELR 921
                          810       820       830       840       850       860       870
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2922 IRTNRIQRFIQNTCNEVEHKIKfcrQFHEKTSALQEEADSIQRNELLLNQEvnkgVKEEIYNLKDRLTAI 2991
Cdd:TIGR02168  922 EKLAQLELRLEGLEVRIDNLQE---RLSEEYSLTLEEAEALENKIEDDEEE----ARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
5803-6072 8.40e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 8.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5803 KQFQSTVETWDQCEKKIKELKSRLQVLKAQSEdpLPELHEDLHNEKELIkELEQSLASWTQNLKELQTMKADLTRhvLVE 5882
Cdd:TIGR02168  179 RKLERTRENLDRLEDILNELERQLKSLERQAE--KAERYKELKAELREL-ELALLVLRLEELREELEELQEELKE--AEE 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5883 DVMVLKEQIEHLHRQWEDLCLRVAIRKQEIEDRLNTWVVFNEKNKELCAWLVQMENKV--LQTADISIEEMIEKLQKdcM 5960
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanLERQLEELEAQLEELES--K 331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  5961 EEINLFSENKLQLKQMGDQLIKASNKSRAAEIDDKLNKINDRWQHLFDVIGSRVKKLKETFAFIQQLDKNMSNLRTWLAR 6040
Cdd:TIGR02168  332 LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
                          250       260       270
                   ....*....|....*....|....*....|..
gi 530403352  6041 IESELSKpvvydvcDDQEIQKRLAEQQDLQRD 6072
Cdd:TIGR02168  412 LEDRRER-------LQQEIEELLKKLEEAELK 436
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
1868-2635 9.29e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 9.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1868 KKSVEQKLQKLSDFLTLEgrnsKIKQVDSVLKHVKKHLpKAHVKELISWLVGQEFELEKMESICQARAKELEDSLQQLLR 1947
Cdd:TIGR00618  159 KAKSKEKKELLMNLFPLD----QYTQLALMEFAKKKSL-HGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLRE 233
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  1948 LQDDHRNLRKWLTNQEEKwkgMEEPGEKTELFCQALARKREqfesvaqLNNSLKEYGFTEEEeiiMEATCLMDRYQTLLR 2027
Cdd:TIGR00618  234 ALQQTQQSHAYLTQKREA---QEEQLKKQQLLKQLRARIEE-------LRAQEAVLEETQER---INRARKAAPLAAHIK 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2028 QLSEIEEEDKLLPTEDQS-FNDLAHDVIHWIKEIKESLmvlnSSEGKMPLEERIQKIKEIILLKPEGDARIETIMKQAES 2106
Cdd:TIGR00618  301 AVTQIEQQAQRIHTELQSkMRSRAKLLMKRAAHVKQQS----SIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT 376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2107 SEAPLvqKTLTDISNQWDNTLHLASTYLSHQEKLLLEGEKYLQSKEDLRLMLIELKKKQEA---GFALQHGLQEKKAQLK 2183
Cdd:TIGR00618  377 LTQHI--HTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELqqrYAELCAAAITCTAQCE 454
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2184 IYKKFL--KKAQDLTSLLKELKSQGNYLLECTknpsfseepwlEIKHLHESLLQQLQDSVQNLDG-----HVREHDSYQV 2256
Cdd:TIGR00618  455 KLEKIHlqESAQSLKEREQQLQTKEQIHLQET-----------RKKAVVLARLLELQEEPCPLCGscihpNPARQDIDNP 523
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2257 CVTDLNTTLDNFSKEFVSFSDKPVDQIAVEEkLQKLQELENRLSLQDGTLKKILALAKSVKQNTSSVGQkiIKDDIKSLQ 2336
Cdd:TIGR00618  524 GPLTRRMQRGEQTYAQLETSEEDVYHQLTSE-RKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN--ITVRLQDLT 600
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2337 CKQKDLENRLASAKQEMECCLNSILKSKRSTEKKGKFTlpgREKQATSDVQESTQESAAVEKLEEDWEINKDSAVEMAMS 2416
Cdd:TIGR00618  601 EKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCS---QELALKLTALHALQLTLTQERVREHALSIRVLPKELLAS 677
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2417 KQLSLNAQESMKN--TEDERKVNELQNQPLELDTML------RNEQLEEIEKLYTQLEAKKAAIKPLEQT-ECLNKTETG 2487
Cdd:TIGR00618  678 RQLALQKMQSEKEqlTYWKEMLAQCQTLLRELETHIeeydreFNEIENASSSLGSDLAAREDALNQSLKElMHQARTVLK 757
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530403352  2488 ALVLHNIGYSAQHLDNL--LQALITLKKNKESQYCVLRDFQEYLAAVESSMKALLTDKESLKVgpLDSVTYLDKIKKFIA 2565
Cdd:TIGR00618  758 ARTEAHFNNNEEVTAALqtGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILN--LQCETLVQEEEQFLS 835
                          730       740       750       760       770       780       790
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530403352  2566 SIEKEKDSLGNLKIKWENLSNHVTDMDKKLLES-QIKQLEHGWEQVEQQIQKKYSQQVVEYDEFTTLMNKV 2635
Cdd:TIGR00618  836 RLEEKSATLGEITHQLLKYEECSKQLAQLTQEQaKIIQLSDKLNGINQIKIQFDGDALIKFLHEITLYANV 906
 
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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