NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1039773953|ref|XP_017176789|]
View 

oxidized low-density lipoprotein receptor 1 isoform X2 [Mus musculus]

Protein Classification

C-type lectin domain-containing protein( domain architecture ID 10132518)

C-type lectin (CTL)/C-type lectin-like (CTLD) domain-containing protein may bind carbohydrate in a calcium-dependent manner

CATH:  3.10.100.10
Gene Ontology:  GO:0030246
PubMed:  16336259|10508765
SCOP:  4002453

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 152-273 4.74e-32

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


:

Pssm-ID: 153063  Cd Length: 116  Bit Score: 114.35  E-value: 4.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 152 CPQDWLWHKENCYLFH-GPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHttSPFWIGLHRKKPGQPWLWENGTPL 230
Cdd:cd03593     1 CPKDWICYGNKCYYFSmEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSREKSEKPWKWIDGSPL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039773953 231 NFQFFKTRGVslqlySSGNCAYLQDGAVFAENCILIAFSICQK 273
Cdd:cd03593    79 NNLFNIRGST-----KSGNCAYLSSTGIYSEDCSTKKRWICEK 116
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-146 7.93e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 7.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   2 LAQQKAENTSQEskKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSKE 81
Cdd:COG1196   321 LEEELAELEEEL--EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773953  82 QEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 146
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
 
Name Accession Description Interval E-value
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 152-273 4.74e-32

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 114.35  E-value: 4.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 152 CPQDWLWHKENCYLFH-GPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHttSPFWIGLHRKKPGQPWLWENGTPL 230
Cdd:cd03593     1 CPKDWICYGNKCYYFSmEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSREKSEKPWKWIDGSPL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039773953 231 NFQFFKTRGVslqlySSGNCAYLQDGAVFAENCILIAFSICQK 273
Cdd:cd03593    79 NNLFNIRGST-----KSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 152-272 3.65e-24

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 94.20  E-value: 3.65e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  152 CPQDWLWHKENCYLFHG-PFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSP--FWIGLHRKKPGQPWLWENGT 228
Cdd:smart00034   1 CPSGWISYGGKCYKFSTeKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039773953  229 PL-NFQFFKTRGVSlqlYSSGNCAYLQ--DGAVFAENCILIAFSICQ 272
Cdd:smart00034  81 GPvSYSNWAPGEPN---NSSGDCVVLStsGGKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 171-273 2.29e-14

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 67.50  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 171 SWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSPFWIGLHRKKPGQPWLWENGTPLNFQFFKTRGVSLQlySSGNC 250
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNG--ENEDC 80

                          90       100
                  ....*....|....*....|....*
gi 1039773953 251 AYLQ--DGAVFAENCILIAFSICQK 273
Cdd:pfam00059  81 VELSssSGKWNDENCNSKNPFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 152-280 6.60e-11

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 60.51  E-value: 6.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 152 CPQDWLWHKENCYLF-HGPFSWEKNRQTCQSLGGQLLQINGADDLTFILQaiSHTTSPFWIGLHRKKPGQPWLWENGTPL 230
Cdd:PHA02642   88 CPKGWIGFGYKCFYFsEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKR--YKDSSDHWIGLNRESSNHPWKWADNSNY 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039773953 231 NFQFFKTrgvslqlySSGNCAYLQDGAVFAENCILIAFSICQKKTNHLQI 280
Cdd:PHA02642  166 NASFVIT--------GTGECAYLNDIRISSSRVYANRKWICSKTYTNIYI 207
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-146 7.93e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 7.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   2 LAQQKAENTSQEskKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSKE 81
Cdd:COG1196   321 LEEELAELEEEL--EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773953  82 QEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 146
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-147 1.64e-09

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: 58.53  E-value: 1.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    3 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAAN---SSEESQRELKGKIDTITRKLDEKS 79
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisRLEQQKQILRERLANLERQLEELE 322

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039773953   80 KEQEELLQMIQNLQEALqraaNSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 147
Cdd:TIGR02168  323 AQLEELESKLDELAEEL----AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
PRK12704 PRK12704
phosphodiesterase; Provisional
 3-128 4.23e-09

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 56.71  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   3 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQN--LQ--EALQRAANSSEESQRELKGKIDTITRKLDEK 78
Cdd:PRK12704   47 AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKrlLQkeENLDRKLELLEKREEELEKKEKELEQKQQEL 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039773953  79 SKEQEELLQMIQNLQEALQRAAN-SSEESQRELkgkIDtltlKLNEKSKEQ 128
Cdd:PRK12704  127 EKKEEELEELIEEQLQELERISGlTAEEAKEIL---LE----KVEEEARHE 170
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 16-145 7.60e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 42.59  E-value: 7.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  16 KELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQREL-------------KGKIDTITRKLDEKSKEQ 82
Cdd:pfam13851  29 KSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLenyekdkqslknlKARLKVLEKELKDLKWEH 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039773953  83 EELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEK-SKEQEELLQKNQNLQEALQRA 145
Cdd:pfam13851 109 EVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEKKlQALGETLEKKEAQLNEVLAAA 172
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 2-117 2.70e-04

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 41.50  E-value: 2.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    2 LAQQkaentSQESKKELKGKIDTLTQKLN------EKSKEQ-EELLQKNQNLQEALQRAANSSEEsqreLKGKIDTITRK 74
Cdd:smart00283 138 LAER-----SAESAKEIESLIKEIQEETNeavaamEESSSEvEEGVELVEETGDALEEIVDSVEE----IADLVQEIAAA 208

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1039773953   75 LDEKSKEQEELLQMIQNLQEALQRAANSSEESQR---ELKGKIDTL 117
Cdd:smart00283 209 TDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAaaeELSGLAEEL 254
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 2-145 1.71e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.28  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   2 LAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEqeeLLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSKE 81
Cdd:cd22656    99 LIDDLADATDDEELEEAKKTIKALLDDLLKEAKK---YQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGA 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039773953  82 --QEELLQMIQNLQEALQRAAnsseesqRELKGKIDtltlKLNEKSKEQEELLQKNQNLQEALQRA 145
Cdd:cd22656   176 iaRKEIKDLQKELEKLNEEYA-------AKLKAKID----ELKALIADDEAKLAAALRLIADLTAA 230
 
Name Accession Description Interval E-value
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 152-273 4.74e-32

C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); CLECT_NK_receptors_like: C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs), including proteins similar to oxidized low density lipoprotein (OxLDL) receptor (LOX-1), CD94, CD69, NKG2-A and -D, osteoclast inhibitory lectin (OCIL), dendritic cell-associated C-type lectin-1 (dectin-1), human myeloid inhibitory C-type lectin-like receptor (MICL), mast cell-associated functional antigen (MAFA), killer cell lectin-like receptors: subfamily F, member 1 (KLRF1) and subfamily B, member 1 (KLRB1), and lys49 receptors. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. NKRs are variously associated with activation or inhibition of natural killer (NK) cells. Activating NKRs stimulate cytolysis by NK cells of virally infected or transformed cells; inhibitory NKRs block cytolysis upon recognition of markers of healthy self cells. Most Lys49 receptors are inhibitory; some are stimulatory. OCIL inhibits NK cell function via binding to the receptor NKRP1D. Murine OCIL in addition to inhibiting NK cell function inhibits osteoclast differentiation. MAFA clusters with the type I Fc epsilon receptor (FcepsilonRI) and inhibits the mast cells secretory response to FcepsilonRI stimulus. CD72 is a negative regulator of B cell receptor signaling. NKG2D is an activating receptor for stress-induced antigens; human NKG2D ligands include the stress induced MHC-I homologs, MICA, MICB, and ULBP family of glycoproteins Several NKRs have a carbohydrate-binding capacity which is not mediated through calcium ions (e.g. OCIL binds a range of high molecular weight sulfated glycosaminoglycans including dextran sulfate, fucoidan, and gamma-carrageenan sugars). Dectin-1 binds fungal beta-glucans and in involved in the innate immune responses to fungal pathogens. MAFA binds saccharides having terminal alpha-D mannose residues in a calcium-dependent manner. LOX-1 is the major receptor for OxLDL in endothelial cells and thought to play a role in the pathology of atherosclerosis. Some NKRs exist as homodimers (e.g.Lys49, NKG2D, CD69, LOX-1) and some as heterodimers (e.g. CD94/NKG2A). Dectin-1 can function as a monomer in vitro.


Pssm-ID: 153063  Cd Length: 116  Bit Score: 114.35  E-value: 4.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 152 CPQDWLWHKENCYLFH-GPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHttSPFWIGLHRKKPGQPWLWENGTPL 230
Cdd:cd03593     1 CPKDWICYGNKCYYFSmEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSREKSEKPWKWIDGSPL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039773953 231 NFQFFKTRGVslqlySSGNCAYLQDGAVFAENCILIAFSICQK 273
Cdd:cd03593    79 NNLFNIRGST-----KSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 152-272 3.65e-24

C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function as calcium-dependent carbohydrate binding modules.


Pssm-ID: 214480 [Multi-domain]  Cd Length: 124  Bit Score: 94.20  E-value: 3.65e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  152 CPQDWLWHKENCYLFHG-PFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSP--FWIGLHRKKPGQPWLWENGT 228
Cdd:smart00034   1 CPSGWISYGGKCYKFSTeKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039773953  229 PL-NFQFFKTRGVSlqlYSSGNCAYLQ--DGAVFAENCILIAFSICQ 272
Cdd:smart00034  81 GPvSYSNWAPGEPN---NSSGDCVVLStsGGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 162-273 9.14e-19

C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type lectin-like (CTLD) domain; protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. This group is chiefly comprised of eukaryotic CTLDs, but contains some, as yet functionally uncharacterized, bacterial CTLDs. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces, including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. For example: mannose-binding lectin and lung surfactant proteins A and D bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, and apoptotic cells) and mediate functions associated with killing and phagocytosis; P (platlet)-, E (endothelial)-, and L (leukocyte)- selectins (sels) mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. Several CTLDs bind to protein ligands, and only some of these binding interactions are Ca2+-dependent; including the CTLDs of Coagulation Factors IX/X (IX/X) and Von Willebrand Factor (VWF) binding proteins, and natural killer cell receptors. C-type lectins, such as lithostathine, and some type II antifreeze glycoproteins function in a Ca2+-independent manner to bind inorganic surfaces. Many proteins in this group contain a single CTLD; these CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers, from which ligand-binding sites project in different orientations. Various vertebrate type 1 transmembrane proteins including macrophage mannose receptor, endo180, phospholipase A2 receptor, and dendritic and epithelial cell receptor (DEC205) have extracellular domains containing 8 or more CTLDs; these CTLDs remain in the parent model. In some members (IX/X and VWF binding proteins), a loop extends to the adjoining domain to form a loop-swapped dimer. A similar conformation is seen in the macrophage mannose receptor CRD4's putative non-sugar bound form of the domain in the acid environment of the endosome. Lineage specific expansions of CTLDs have occurred in several animal lineages including Drosophila melanogaster and Caenorhabditis elegans; these CTLDs also remain in the parent model.


Pssm-ID: 153057 [Multi-domain]  Cd Length: 116  Bit Score: 79.59  E-value: 9.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 162 NCYLFH-GPFSWEKNRQTCQSLGGQLLQINGADDLTFIL-QAISHTTSPFWIGLHRKKPGQPWLWENGTPLnFQFFKTRG 239
Cdd:cd00037     1 SCYKFStEKLTWEEAQEYCRSLGGHLASIHSEEENDFLAsLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPL-VDYTNWAP 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039773953 240 VSLQLYSSGNCAYL---QDGAVFAENCILIAFSICQK 273
Cdd:cd00037    80 GEPNPGGSEDCVVLsssSDGKWNDVSCSSKLPFICEK 116
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 152-263 5.85e-15

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 69.71  E-value: 5.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 152 CPQDWLWHKENCY-LFHGPFSWEKNRQTCQSL--GGQLLQINGADDLTFILQAIS---HTTSPFWIGLHRKKPGQPWLWE 225
Cdd:cd03594     1 CPKGWLPYKGNCYgYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISsyqKAYQPVWIGLHDPQQSRGWEWS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039773953 226 NGTPLNFqFFKTRGVSLQlySSGNCAYLQDGAVF----AENC 263
Cdd:cd03594    81 DGSKLDY-RSWDRNPPYA--RGGYCAELSRSTGFlkwnDANC 119
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 171-273 2.29e-14

Lectin C-type domain; This family includes both long and short form C-type


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 67.50  E-value: 2.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 171 SWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSPFWIGLHRKKPGQPWLWENGTPLNFQFFKTRGVSLQlySSGNC 250
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNG--ENEDC 80

                          90       100
                  ....*....|....*....|....*
gi 1039773953 251 AYLQ--DGAVFAENCILIAFSICQK 273
Cdd:pfam00059  81 VELSssSGKWNDENCNSKNPFVCEK 105
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 152-231 1.78e-13

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 65.79  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 152 CPQDWLWHKENCYLF-HGPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSpFWIGLHRKKPGQPWLWENGTPL 230
Cdd:cd03590     1 CPTNWKSFQSSCYFFsTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS-YWIGLSDEETEGEWKWVDGTPL 79


                  .
gi 1039773953 231 N 231
Cdd:cd03590    80 N 80
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 152-280 6.60e-11

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 60.51  E-value: 6.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 152 CPQDWLWHKENCYLF-HGPFSWEKNRQTCQSLGGQLLQINGADDLTFILQaiSHTTSPFWIGLHRKKPGQPWLWENGTPL 230
Cdd:PHA02642   88 CPKGWIGFGYKCFYFsEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKR--YKDSSDHWIGLNRESSNHPWKWADNSNY 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039773953 231 NFQFFKTrgvslqlySSGNCAYLQDGAVFAENCILIAFSICQKKTNHLQI 280
Cdd:PHA02642  166 NASFVIT--------GTGECAYLNDIRISSSRVYANRKWICSKTYTNIYI 207
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-146 7.93e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 7.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   2 LAQQKAENTSQEskKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSKE 81
Cdd:COG1196   321 LEEELAELEEEL--EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773953  82 QEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 146
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-147 1.64e-09

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: 58.53  E-value: 1.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    3 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAAN---SSEESQRELKGKIDTITRKLDEKS 79
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisRLEQQKQILRERLANLERQLEELE 322

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039773953   80 KEQEELLQMIQNLQEALqraaNSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 147
Cdd:TIGR02168  323 AQLEELESKLDELAEEL----AELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 152-232 1.78e-09

C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina; CLECT_CEL-1_like: C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and Echinoidin from Anthocidaris crassispina. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CEL-1 CTLD binds three calcium ions and has a high specificity for N-acteylgalactosamine (GalNAc). CEL-1 exhibits strong cytotoxicity which is inhibited by GalNAc. This protein may play a role as a toxin defending against predation. Echinoidin is found in the coelomic fluid of the sea urchin and is specific for GalBeta1-3GalNAc. Echinoidin has a cell adhesive activity towards human cancer cells which is not mediated through the CTLD. Both CEL-1 and Echinoidin are multimeric proteins comprised of multiple dimers linked by disulfide bonds.


Pssm-ID: 153059  Cd Length: 137  Bit Score: 55.06  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 152 CPQDWLWHKENCYLFHGP-FSWEKNRQTCQSLG-----GQLLQINGADDLTFILQ-----AISHTTSPFWIGLHRKKPGQ 220
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDrLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDlfessRGPDTPYGLWIGLHDRTSEG 80

                          90
                  ....*....|..
gi 1039773953 221 PWLWENGTPLNF 232
Cdd:cd03589    81 PFEWTDGSPVDF 92
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-147 2.59e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   3 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEE---SQRELKGKIDTITRKLDEKS 79
Cdd:COG1196   264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEleeELAELEEELEELEEELEELE 343

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039773953  80 KEQEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 147
Cdd:COG1196   344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 2-147 3.60e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.25  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   2 LAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAanssEESQRELKGKIDTITRKLDEKSKE 81
Cdd:COG1196   277 EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAEL----EEELEELEEELEELEEELEEAEEE 352

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039773953  82 QEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 147
Cdd:COG1196   353 LEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
PRK12704 PRK12704
phosphodiesterase; Provisional
 3-128 4.23e-09

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 56.71  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   3 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQN--LQ--EALQRAANSSEESQRELKGKIDTITRKLDEK 78
Cdd:PRK12704   47 AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKrlLQkeENLDRKLELLEKREEELEKKEKELEQKQQEL 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039773953  79 SKEQEELLQMIQNLQEALQRAAN-SSEESQRELkgkIDtltlKLNEKSKEQ 128
Cdd:PRK12704  127 EKKEEELEELIEEQLQELERISGlTAEEAKEIL---LE----KVEEEARHE 170
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 164-235 4.30e-09

A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_VCBS: A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Bacterial CTLDs within this group are functionally uncharacterized. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153073 [Multi-domain]  Cd Length: 118  Bit Score: 53.20  E-value: 4.30e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039773953 164 YLF-HGPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAIShTTSPFWIGLHRKKPGQPWLWENGTPLNFQFF 235
Cdd:cd03603     3 YKFvDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFG-GYGASWIGASDAATEGTWKWSDGEESTYTNW 74
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 12-146 1.12e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  12 QESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQ---RELKGKIDTITRKLDEKSKEQEELLQM 88
Cdd:COG1196   238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQaeeYELLAELARLEQDIARLEERRRELEER 317

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039773953  89 IQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 146
Cdd:COG1196   318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 3-147 1.26e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   3 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQREL---KGKIDTITRKLDEKS 79
Cdd:COG1196   243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIarlEERRRELEERLEELE 322

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039773953  80 KEQEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 147
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 4-148 8.85e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.02  E-value: 8.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   4 QQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKsKEQE 83
Cdd:COG1196   241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE-ERLE 319

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773953  84 ELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAANF 148
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-147 2.24e-07

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: 51.30  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   2 LAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQE---ALQRAANSSEESQRELKGKIDTITRKLDEK 78
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERriaALARRIRALEQELAALEAELAELEKEIAEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  79 SKEQEELLQMIQNLQEALQR-----------AANSSEESQR----------ELKGKIDTLTLKLNEKSKEQEELLQKNQN 137
Cdd:COG4942    96 RAELEAQKEELAELLRALYRlgrqpplalllSPEDFLDAVRrlqylkylapARREQAEELRADLAELAALRAELEAERAE 175

                         170
                  ....*....|
gi 1039773953 138 LQEALQRAAN 147
Cdd:COG4942   176 LEALLAELEE 185
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1-142 2.79e-07

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: 51.61  E-value: 2.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    1 MLAQQKAENTSQESKK------ELKGKIDTLTQKLNEKSKEQEELLQKNQNLQE---ALQRAANSSEESQRELKGKIDTI 71
Cdd:TIGR02169  787 RLSHSRIPEIQAELSKleeevsRIEARLREIEQKLNRLTLEKEYLEKEIQELQEqriDLKEQIKSIEKEIENLNGKKEEL 866

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039773953   72 TRKLDEKSKEQEELLQMIQNLQEALQRAanssEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEAL 142
Cdd:TIGR02169  867 EEELEELEAALRDLESRLGDLKKERDEL----EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-146 3.38e-07

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: 51.21  E-value: 3.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    1 MLAQQKAENTSQESKKEL---KGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQR----------ELKGK 67
Cdd:TIGR02168  273 RLEVSELEEEIEELQKELyalANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEelaeleekleELKEE 352

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   68 IDTITRKLDEKSKEQEELLQMIQNLQEALQRAAN---SSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQR 144
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432


                   ..
gi 1039773953  145 AA 146
Cdd:TIGR02168  433 AE 434
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 12-147 6.11e-07

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: 6.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   12 QESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQE---ALQRAANSSEESQRELKGKIDTITRKLDEKSKEQEELLQM 88
Cdd:TIGR02169  293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039773953   89 IQNLQEALQRaansSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 147
Cdd:TIGR02169  373 LEEVDKEFAE----TRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 6-145 1.76e-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: 48.91  E-value: 1.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    6 KAENTSQESKKELKGKIDTLTQKLnEKSKEQ-----EELLQKNQNLQEALQRAANSSEESQ-------RELKGKIDTITR 73
Cdd:TIGR02169  230 KEKEALERQKEAIERQLASLEEEL-EKLTEEiseleKRLEEIEQLLEELNKKIKDLGEEEQlrvkekiGELEAEIASLER 308

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773953   74 KLDEKSKEQEELLQMIQNLQE---ALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRA 145
Cdd:TIGR02169  309 SIAEKERELEDAEERLAKLEAeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAET 383
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 2-140 2.33e-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: 48.91  E-value: 2.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    2 LAQQKAENTSQESK-KELKGKIDTLTQKLNEKSKEQEELLQ---KNQNLQEALQRAANSSEESQRELKGKIDTITRKLDE 77
Cdd:TIGR02169  690 LSSLQSELRRIENRlDELSQELSDASRKIGEIEKEIEQLEQeeeKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039773953   78 K----SKEQEELLQMIQNLQEA----LQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQE 140
Cdd:TIGR02169  770 LeedlHKLEEALNDLEARLSHSripeIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-141 2.91e-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: 48.53  E-value: 2.91e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    4 QQKAENTSQESKKEL---KGKIDTLTQKLNEKSKEQEELLQKNQNLQ---EALQRAANSSEESQRELKGKIDTITRKLDE 77
Cdd:TIGR02169  317 LEDAEERLAKLEAEIdklLAEIEELEREIEEERKRRDKLTEEYAELKeelEDLRAELEEVDKEFAETRDELKDYREKLEK 396

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039773953   78 KSKEQEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEA 141
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQL 460
PRK09039 PRK09039
peptidoglycan -binding protein;
12-139 3.79e-06

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 47.65  E-value: 3.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  12 QESKKELKGKIDTLTQKLNEKSKEQEELlqknQNLQEALQRAANSSEESQRELKGKIDTiTRKLDEKSKEQEELL-QMIQ 90
Cdd:PRK09039   73 RQGNQDLQDSVANLRASLSAAEAERSRL----QALLAELAGAGAAAEGRAGELAQELDS-EKQVSARALAQVELLnQQIA 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039773953  91 NLQE---ALQRAANSSEESQRELKGKIDTLTLKLNEKskeqeeLLQKNQNLQ 139
Cdd:PRK09039  148 ALRRqlaALEAALDASEKRDRESQAKIADLGRRLNVA------LAQRVQELN 193
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 12-142 4.10e-06

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: 48.13  E-value: 4.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   12 QESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAAN---SSEESQRELKGKIDTITRKLDEKSKE---QEEL 85
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELIEELESELEALLNErasLEEA 888

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039773953   86 LQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEAL 142
Cdd:TIGR02168  889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 17-131 4.26e-06

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 47.90  E-value: 4.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  17 ELKGKIDTLTQKLNEKSKEQ-------EELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRK-LDEKSKEQEELLQM 88
Cdd:PRK00409  513 EDKEKLNELIASLEELERELeqkaeeaEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQaIKEAKKEADEIIKE 592

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1039773953  89 IQNLQEALQRAANSSE--ESQRELKGKIDTLTLKLNEKSKEQEEL 131
Cdd:PRK00409  593 LRQLQKGGYASVKAHEliEARKRLNKANEKKEKKKKKQKEKQEEL 637
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 3-145 6.60e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.75  E-value: 6.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   3 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDE--KSK 80
Cdd:COG3883    20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAlyRSG 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039773953  81 EQEELLQMI---QNLQEALQRAANSSE---------ESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRA 145
Cdd:COG3883   100 GSVSYLDVLlgsESFSDFLDRLSALSKiadadadllEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 16-114 6.61e-06

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: 46.68  E-value: 6.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  16 KELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSKEQEELLQMIQNLQEA 95
Cdd:COG4942   156 RADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235

                          90       100
                  ....*....|....*....|
gi 1039773953  96 LQRAANSSEESQ-RELKGKI 114
Cdd:COG4942   236 AAAAAERTPAAGfAALKGKL 255
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
2-144 8.25e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 8.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   2 LAQQKAENTSQesKKELKGKIDTLTQKLNEKSKEQEELLQkNQNLQEALQRAANS----SEESQR---------ELKGKI 68
Cdd:COG3206   224 LESQLAEARAE--LAEAEARLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELeaelAELSARytpnhpdviALRAQI 300

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  69 DTITRKLDEkskEQEELLQMIQNLQEALQRAANSSEESQRELKGKIDTltlkLNEKSKEQEELLQ----KNQNLQEALQR 144
Cdd:COG3206   301 AALRAQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLERevevARELYESLLQR 373
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 12-142 9.51e-06

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.69  E-value: 9.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  12 QESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEE-----SQRELKG---KIDTITRKLDEKSKEQE 83
Cdd:COG1579    34 AELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKEYEAlqkEIESLKRRISDLEDEIL 113

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039773953  84 ELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEAL 142
Cdd:COG1579   114 ELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2-144 1.24e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.60  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   2 LAQQKAENTSQE-SKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEAlqraaNSSEESQRELKGKIDTITRKLDEKSK 80
Cdd:PRK03918  240 IEELEKELESLEgSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-----KEKAEEYIKLSEFYEEYLDELREIEK 314

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039773953  81 EQEELLQMIQNLQEALQRaANSSEESQRELKGKIDTLTLKLNEkSKEQEELLQKNQNLQEALQR 144
Cdd:PRK03918  315 RLSRLEEEINGIEERIKE-LEEKEERLEELKKKLKELEKRLEE-LEERHELYEEAKAKKEELER 376
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-141 1.24e-05

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: 46.59  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    1 MLAQQKAENTSQESKKELKGKIDTLTQKLNEkskeQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSK 80
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEAQIEQ----LKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039773953   81 EQEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEA 141
Cdd:TIGR02168  839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
PHA02867 PHA02867
C-type lectin protein; Provisional
 147-278 1.44e-05

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 44.29  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 147 NFSGPCPQDWLWHKENCYLFH-GPFSWEKNRQTCQSLGGQLLQINGADDLTFILQaisHTTSPFWIglHRKKpgqpwlWE 225
Cdd:PHA02867   44 YFSKVCPDEWIGYNSKCYYFTiNETNWNDSKKLCDVMDSSLIRFDNIETLNFVSR---YGKGSYWI--DINQ------NR 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039773953 226 NgtplnfqffkTRGVSLQLYSSGN----CAYLQDGAVFAENCILIAFSICQKKTNHL 278
Cdd:PHA02867  113 K----------IPGINFSLYYEQGvndiCLLFDTSNIIEMSCIFHERTICVKEDRYT 159
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
17-147 1.58e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 1.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   17 ELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEEsqrELKGKIDTITRKLDEKSKEQEELLQMIQNLQEAL 96
Cdd:COG4913    299 ELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLE---QLEREIERLERELEERERRRARLEALLAALGLPL 375

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039773953   97 QRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 147
Cdd:COG4913    376 PASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
PRK12704 PRK12704
phosphodiesterase; Provisional
 46-149 1.60e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 45.92  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  46 LQEALQRAANSSEESQRELKGKIDTITRKLDEKSKEQEELLQMIQN--LQ--EALQRAANSSEESQRELKGKIDTLTLKL 121
Cdd:PRK12704   44 LEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKrlLQkeENLDRKLELLEKREEELEKKEKELEQKQ 123

                          90       100
                  ....*....|....*....|....*...
gi 1039773953 122 NEKSKEQEELLQKNQNLQEALQRAANFS 149
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERISGLT 151
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
17-153 2.12e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  17 ELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAaNSSEESQRELKGKIDTITRKLdEKSKEQEELLQMIQNLQEAL 96
Cdd:PRK03918  297 KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKEL-EEKEERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEEL 374

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773953  97 QR-----AANSSEESQRELK---GKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAANFSGPCP 153
Cdd:PRK03918  375 ERlkkrlTGLTPEKLEKELEeleKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 4-147 4.78e-05

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: 44.66  E-value: 4.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    4 QQKAENTSQESKKELKGKIDTLTQKLNEKS---KEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSK 80
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   81 EQEELLQMIQNLQEALQRAANSSEESQREL---------------KGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRA 145
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRRerlqqeieellkkleEAELKELQAELEELEEELEELQEELERLEEALEEL 466


                   ..
gi 1039773953  146 AN 147
Cdd:TIGR02168  467 RE 468
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
4-147 5.69e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   4 QQKAENTSQeSKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLqeALQRAANSSEESQRELKGKIDTITRKLDEKSKEQE 83
Cdd:COG3206   167 ELRREEARK-ALEFLEEQLPELRKELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAELAEAEARLA 243

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039773953  84 ELLQMIQNLQEALQRAANSSEESQ-----RELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 147
Cdd:COG3206   244 ALRAQLGSGPDALPELLQSPVIQQlraqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ 312
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 16-146 5.72e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 5.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  16 KELKGKIDTLtqKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELkgkiDTITRKLDEKSKEQEELLQMIQNLQEA 95
Cdd:COG1196   216 RELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAEL----AELEAELEELRLELEELELELEEAQAE 289

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039773953  96 LQRAANSSEESQREL---KGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 146
Cdd:COG1196   290 EYELLAELARLEQDIarlEERRRELEERLEELEEELAELEEELEELEEELEELE 343
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 13-92 7.29e-05

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 43.52  E-value: 7.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  13 ESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAansseesqRELKGKIDTITRKLDEKSKEQEELLQMIQNL 92
Cdd:PRK05431   35 EERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEV--------KELKEEIKALEAELDELEAELEELLLRIPNL 106
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5-140 7.46e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 7.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   5 QKAENTSQESKKELKGKIDTLtQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSKEQEE 84
Cdd:PRK03918  161 ENAYKNLGEVIKEIKRRIERL-EKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039773953  85 LlqmiqnlqEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQE 140
Cdd:PRK03918  240 I--------EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE 287
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 16-145 7.60e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 42.59  E-value: 7.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  16 KELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQREL-------------KGKIDTITRKLDEKSKEQ 82
Cdd:pfam13851  29 KSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLenyekdkqslknlKARLKVLEKELKDLKWEH 108

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039773953  83 EELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEK-SKEQEELLQKNQNLQEALQRA 145
Cdd:pfam13851 109 EVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEKKlQALGETLEKKEAQLNEVLAAA 172
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 3-147 7.76e-05

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: 43.60  E-value: 7.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   3 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQ------------------------EALQRAANSSE 58
Cdd:COG4942    73 ALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGrqpplalllspedfldavrrlqylKYLAPARREQA 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  59 ESQRELKGKIDTITRKLDEKSKEQEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNL 138
Cdd:COG4942   153 EELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARL 232


                  ....*....
gi 1039773953 139 QEALQRAAN 147
Cdd:COG4942   233 EAEAAAAAE 241
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 2-146 9.20e-05

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 42.25  E-value: 9.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   2 LAQQKAENTSQES---KKELKGKIDTLTQKLNEKSKEQEELLQknQNLQEALQRAANSSEESQRELKGKIDTITRKLDEK 78
Cdd:pfam01442  23 VAQELVDRLEKETealRERLQKDLEEVRAKLEPYLEELQAKLG--QNVEELRQRLEPYTEELRKRLNADAEELQEKLAPY 100

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039773953  79 SKEQEEllQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKE-QEELLQKNQNLQEALQRAA 146
Cdd:pfam01442 101 GEELRE--RLEQNVDALRARLAPYAEELRQKLAERLEELKESLAPYAEEvQAQLSQRLQELREKLEPQA 167
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 12-123 1.41e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.22  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  12 QESKKELKGKIDTLTQKLnEKSKEQEELLQKN---QNLQ---EALQRAANSSEESQRELKGKIDTITRKLDEKSKEQEEL 85
Cdd:COG1579    58 EKEIKRLELEIEEVEARI-KKYEEQLGNVRNNkeyEALQkeiESLKRRISDLEDEILELMERIEELEEELAELEAELAEL 136

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1039773953  86 LQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNE 123
Cdd:COG1579   137 EAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 194-271 1.58e-04

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Many CTLDs are calcium-dependent carbohydrate binding modules; other CTLDs bind protein ligands, lipids, and inorganic surfaces including CaCO3 and ice. Animal C-type lectins are involved in such functions as extracellular matrix organization, endocytosis, complement activation, pathogen recognition, and cell-cell interactions. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 40.05  E-value: 1.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039773953 194 DLTFILQAISHTTSPFWIGLHRKKpgQPWLWENGTPLNFQFFKTrgvsLQLYSSGNCAYL-QDGAVFAENCILIAFSIC 271
Cdd:cd03602    34 DNALLSNLSRVSNSAAWIGLYRDV--DSWRWSDGSESSFRNWNT----FQPFGQGDCATMySSGRWYAALCSALKPFIC 106
PRK11281 PRK11281
mechanosensitive channel MscK;
2-142 1.65e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.98  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    2 LAQQKAENTSQESKKELKGKIDTLTQKLNEKSKE----QEELLQKNQ---NLQEALQRAANS-SEESQRelkgkIDTITR 73
Cdd:PRK11281   103 LEALKDDNDEETRETLSTLSLRQLESRLAQTLDQlqnaQNDLAEYNSqlvSLQTQPERAQAAlYANSQR-----LQQIRN 177

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039773953   74 KLDEKSKEQEELLQMIQNLQEALQRAANSSEESQR-ELKGK---IDTLTLKLNEKSKEQEELLQKNQNLQEAL 142
Cdd:PRK11281   178 LLKGGKVGGKALRPSQRVLLQAEQALLNAQNDLQRkSLEGNtqlQDLLQKQRDYLTARIQRLEHQLQLLQEAI 250
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
26-146 1.89e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   26 TQKLNEKSKEQEELLQKNQNLQEALQRAanssEESQRELKGKIDTITR--KLDEKSKEQEELLQMIQNLQEALQRAANSS 103
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEAL----EAELDALQERREALQRlaEYSWDEIDVASAEREIAELEAELERLDASS 684

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1039773953  104 ------EESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 146
Cdd:COG4913    685 ddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ 733
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
16-145 2.25e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  16 KELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQR--------ELKGKIDTITRKLDEKSKEQEELLQ 87
Cdd:COG4717    74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlekllqllPLYQELEALEAELAELPERLEELEE 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039773953  88 MIQNLQEALQRAANSSEEsQRELKGKIDTLTLKLNEKSKEQ-EELLQKNQNLQEALQRA 145
Cdd:COG4717   154 RLEELRELEEELEELEAE-LAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAEL 211
DUF5930 pfam19353
Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. ...
 29-146 2.40e-04

Family of unknown function (DUF5930); This family of proteins is functionally uncharacterized. This family of proteins is found in rhodobacteria. Proteins in this family are typically between 411 and 445 amino acids in length. The family is found to the N-terminus of pfam01551.


Pssm-ID: 466052 [Multi-domain]  Cd Length: 320  Bit Score: 41.70  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  29 LNEKSKEQEELLQknqnlqealqraansSEESQRELKGKIDTITRKLDEKSKEQEELLQMIQNLQEALQRAANSSEESQR 108
Cdd:pfam19353 111 LEQVSVMQSELLA---------------SEERRRELETGIEVIQSTLRRTMKERDAARAELAALQAELEGGGAAAAARAA 175

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1039773953 109 ELKGKIDTLTLKLNEKSKEQEELLqknQNLQEALQRAA 146
Cdd:pfam19353 176 DADATLDFLTAALAETAAERDQIA---ADAQDALAEAD 210
PTZ00121 PTZ00121
MAEBL; Provisional
 5-144 2.69e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 2.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    5 QKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKnqnlQEALQRAANSSEESQrELKGKIDTITRKLDEKSKEQEE 84
Cdd:PTZ00121  1653 KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA----AEALKKEAEEAKKAE-ELKKKEAEEKKKAEELKKAEEE 1727

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   85 LLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQR 144
Cdd:PTZ00121  1728 NKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
MA smart00283
Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo ...
 2-117 2.70e-04

Methyl-accepting chemotaxis-like domains (chemotaxis sensory transducer); Thought to undergo reversible methylation in response to attractants or repellants during bacterial chemotaxis.


Pssm-ID: 214599 [Multi-domain]  Cd Length: 262  Bit Score: 41.50  E-value: 2.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    2 LAQQkaentSQESKKELKGKIDTLTQKLN------EKSKEQ-EELLQKNQNLQEALQRAANSSEEsqreLKGKIDTITRK 74
Cdd:smart00283 138 LAER-----SAESAKEIESLIKEIQEETNeavaamEESSSEvEEGVELVEETGDALEEIVDSVEE----IADLVQEIAAA 208

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1039773953   75 LDEKSKEQEELLQMIQNLQEALQRAANSSEESQR---ELKGKIDTL 117
Cdd:smart00283 209 TDEQAAGSEEVNAAIDEIAQVTQETAAMSEEISAaaeELSGLAEEL 254
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1-133 2.80e-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: 42.35  E-value: 2.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    1 MLAQQKAENtsQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRA---ANSSEESQRELKGKIDTITRKLDE 77
Cdd:TIGR02168  842 DLEEQIEEL--SEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLrseLEELSEELRELESKRSELRRELEE 919

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039773953   78 KSKE-------QEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQ 133
Cdd:TIGR02168  920 LREKlaqlelrLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 17-145 3.08e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  17 ELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAanssEESQRELKGKIDTITRKLDEKSKEQEEL-----LQMIQN 91
Cdd:COG1579    21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDL----EKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeYEALQK 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039773953  92 LQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRA 145
Cdd:COG1579    97 EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
16-147 3.12e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  16 KELKGKIDTLTQKLNEKSKEQEELlQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSKEQEELLQMIQNLQEa 95
Cdd:PRK03918  210 NEISSELPELREELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKE- 287

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039773953  96 lqraANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 147
Cdd:PRK03918  288 ----LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 3-150 3.75e-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: 41.97  E-value: 3.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    3 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQREL---------------KGK 67
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRerlqqeieellkkleEAE 434

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   68 IDTITRKLDEKSKEQEELLQMIQNLQEALQRAANSSEESQREL---KGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQR 144
Cdd:TIGR02168  435 LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALdaaERELAQLQARLDSLERLQENLEGFSEGVKALLKN 514


                   ....*.
gi 1039773953  145 AANFSG 150
Cdd:TIGR02168  515 QSGLSG 520
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 2-140 4.33e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.54  E-value: 4.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   2 LAQQKAENTSQESKKELKG---KIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGK---IDTITRKL 75
Cdd:TIGR04523 300 LNNQKEQDWNKELKSELKNqekKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKqneIEKLKKEN 379

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773953  76 DEKSKEQEELLQMIQNLQEALQRAanssEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQE 140
Cdd:TIGR04523 380 QSYKQEIKNLESQINDLESKIQNQ----EKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNS 440
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
8-147 5.06e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   8 ENTSQESKKELKGKIDTLTQKLNEKSKEQEEL-LQKNQNLQEALQRAANSSEESQRelkgkidtitRKLDEKSKEQEELL 86
Cdd:COG4717   332 PDLSPEELLELLDRIEELQELLREAEELEEELqLEELEQEIAALLAEAGVEDEEEL----------RAALEQAEEYQELK 401

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039773953  87 QMIQNLQEALQRAANSSEESQR-----ELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 147
Cdd:COG4717   402 EELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
16-145 5.56e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 5.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  16 KELKGKIDTLT-QKLNEKSKEQEELLQKNQNLqEALQRAANSSEESQRELKGKIDTITRKLDEKSKEQEELLQMIQNL-- 92
Cdd:PRK03918  506 KELEEKLKKYNlEELEKKAEEYEKLKEKLIKL-KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgf 584

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039773953  93 --QEALQRAANSSEESQR---ELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRA 145
Cdd:PRK03918  585 esVEELEERLKELEPFYNeylELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
3-111 5.79e-04

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   3 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKgKIDTITRKLDEKSKEQ 82
Cdd:COG2433   389 ELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELS-EARSEERREIRKDREI 467

                          90       100
                  ....*....|....*....|....*....
gi 1039773953  83 EELLQMIQNLQEALQRAANSSEESQRELK 111
Cdd:COG2433   468 SRLDREIERLERELEEERERIEELKRKLE 496
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 13-92 6.18e-04

Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.


Pssm-ID: 426757 [Multi-domain]  Cd Length: 108  Bit Score: 38.34  E-value: 6.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  13 ESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAansseesqRELKGKIDTITRKLDEKSKEQEELLQMIQNL 92
Cdd:pfam02403  36 EKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEV--------KELKDELKALEAELKELEAELDKLLLTIPNI 107
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
31-147 6.21e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 6.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   31 EKSKEQEELLQKNQNLQEALQRAANSSEESQRELKG-KIDTITRKLDEKSKEQEELLQMIQNLQEALQRAanssEESQRE 109
Cdd:COG4913    245 EDAREQIELLEPIRELAERYAAARERLAELEYLRAAlRLWFAQRRLELLEAELEELRAELARLEAELERL----EARLDA 320

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1039773953  110 LKGKIDTLTLKLNEKSKEQEELLQK-NQNLQEALQRAAN 147
Cdd:COG4913    321 LREELDELEAQIRGNGGDRLEQLEReIERLERELEERER 359
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 5-117 6.27e-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: 41.20  E-value: 6.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    5 QKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALqraaNSSEESQRELKGKIDTITRKLDEkskEQEE 84
Cdd:TIGR02168  879 LNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEVRIDNLQERLSE---EYSL 951

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1039773953   85 LLQMIQNLQEALQRAANSSEESQRELKGKIDTL 117
Cdd:TIGR02168  952 TLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 8-151 6.87e-04

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 40.81  E-value: 6.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   8 ENTSQESKKELKGKIDTLTQKLNEKS-----KEQEELLQKNQNLQEALQRAANSSEE--SQ-RELKGKIDTITRKLD--E 77
Cdd:pfam05911 657 DNLSSDPEIPSDGPLVSGSNDLKTEEnkrlkEEFEQLKSEKENLEVELASCTENLEStkSQlQESEQLIAELRSELAslK 736

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773953  78 KSKEQ-EELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAANFSGP 151
Cdd:pfam05911 737 ESNSLaETQLKCMAESYEDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESS 811
PTZ00121 PTZ00121
MAEBL; Provisional
 3-141 6.98e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 6.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    3 AQQKAEntSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEAlQRAANSSEESQR--ELKGKIDTiTRKLDEKSK 80
Cdd:PTZ00121  1376 AKKKAD--AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKA-DEAKKKAEEKKKadEAKKKAEE-AKKADEAKK 1451

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039773953   81 EQEElLQMIQNLQEALQRAANSSEESQR-ELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEA 141
Cdd:PTZ00121  1452 KAEE-AKKAEEAKKKAEEAKKADEAKKKaEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKA 1512
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 4-151 8.24e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.71  E-value: 8.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    4 QQKAENTSQESKKELKGKIDTLTqklnekskEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSKEQE 83
Cdd:COG3096    531 QQNAERLLEEFCQRIGQQLDAAE--------ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAP 602

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039773953   84 ELLQmiqnLQEALQRAANSSEE---SQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAANFSGP 151
Cdd:COG3096    603 AWLA----AQDALERLREQSGEalaDSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGA 669
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
3-145 8.66e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 8.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   3 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNL----QEALQRAANSSEESQR---ELKGKIDTITRKL 75
Cdd:PRK03918  539 GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPFYNeylELKDAEKELEREE 618

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  76 DEKSKEQEELLQMIQNLQEALQRAansseesqRELKGKIDTLTLKLNEksKEQEELLQKNQNLQEALQRA 145
Cdd:PRK03918  619 KELKKLEEELDKAFEELAETEKRL--------EELRKELEELEKKYSE--EEYEELREEYLELSRELAGL 678
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
12-146 1.38e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  12 QESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQraansseesqrELKGKIDTITRKLDEKSKEQEELLQMIQN 91
Cdd:COG1340   152 AKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQ-----------ELHEEMIELYKEADELRKEADELHKEIVE 220

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1039773953  92 LQEALqraansseesqRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 146
Cdd:COG1340   221 AQEKA-----------DELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEE 264
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 3-148 1.41e-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: 39.75  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   3 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQR------------------AANSSEESQREL 64
Cdd:COG4942    59 ALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEllralyrlgrqpplalllSPEDFLDAVRRL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  65 K------GKIDTITRKLDEKSKEQEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNL 138
Cdd:COG4942   139 QylkylaPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218

                         170
                  ....*....|
gi 1039773953 139 QEALQRAANF 148
Cdd:COG4942   219 QQEAEELEAL 228
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 10-141 1.43e-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: 40.05  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   10 TSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANsseesqrELKGKIDTITRKLDEKSKEQEELLQMI 89
Cdd:TIGR02169  382 ETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA-------AIAGIEAKINELEEEKEDKALEIKKQE 454

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039773953   90 QNLQEAlqRAANSSEESQ-RELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEA 141
Cdd:TIGR02169  455 WKLEQL--AADLSKYEQElYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
HlpA COG2825
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ...
 22-114 1.62e-03

Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442073 [Multi-domain]  Cd Length: 171  Bit Score: 38.28  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  22 IDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRklDEKSKEQEELLQMIQNLQEALQRAAN 101
Cdd:COG2825    31 VQRILQESPEGKAAQKKLEKEFKKRQAELQKLEKELQALQEKLQKEAATLSE--EERQKKERELQKKQQELQRKQQEAQQ 108

                          90
                  ....*....|...
gi 1039773953 102 SSEESQRELKGKI 114
Cdd:COG2825   109 DLQKRQQELLQPI 121
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 2-145 1.71e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 39.28  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   2 LAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEqeeLLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSKE 81
Cdd:cd22656    99 LIDDLADATDDEELEEAKKTIKALLDDLLKEAKK---YQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGA 175

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039773953  82 --QEELLQMIQNLQEALQRAAnsseesqRELKGKIDtltlKLNEKSKEQEELLQKNQNLQEALQRA 145
Cdd:cd22656   176 iaRKEIKDLQKELEKLNEEYA-------AKLKAKID----ELKALIADDEAKLAAALRLIADLTAA 230
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
16-107 2.05e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.61  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  16 KELKGKIDTLTQKLNEkskEQEELLQKNQNLQEALQRAANSSEESQRELKGKIdtitRKLDEKSKEQEELLQMIQNLQEA 95
Cdd:COG3206   294 IALRAQIAALRAQLQQ---EAQRILASLEAELEALQAREASLQAQLAQLEARL----AELPELEAELRRLEREVEVAREL 366

                          90
                  ....*....|..
gi 1039773953  96 LQRAANSSEESQ 107
Cdd:COG3206   367 YESLLQRLEEAR 378
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
22-127 2.13e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  22 IDTLTQKLnEKSKEQEELLQKNQNLQEALQRAANSSEESQR-----ELKGKIDTITRKLDEKSKEQEELLQMIQNLQEAL 96
Cdd:COG4717   384 EEELRAAL-EQAEEYQELKEELEELEEQLEELLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELEAEL 462

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039773953  97 QRAANSSEESqrELKGKIDTLTLKLNEKSKE 127
Cdd:COG4717   463 EQLEEDGELA--ELLQELEELKAELRELAEE 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 12-146 2.16e-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: 39.65  E-value: 2.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   12 QESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQ---RELKGKIDTITRKLDEKSKEQEELLQM 88
Cdd:TIGR02168  711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEaeiEELEERLEEAEEELAEAEAEIEELEAQ 790

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039773953   89 IQNLQEALQ---RAANSSEESQRELKGKIDTLTLKLN-------EKSKEQEELLQKNQNLQEALQRAA 146
Cdd:TIGR02168  791 IEQLKEELKalrEALDELRAELTLLNEEAANLRERLEslerriaATERRLEDLEEQIEELSEDIESLA 858
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 163-219 2.26e-03

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 37.41  E-value: 2.26e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773953 163 CY-LFHGPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSP-------FWIGLHRKKPG 219
Cdd:cd03600     6 CYtLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGRhgrgslrLWIGLQREPRQ 70
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
16-96 2.67e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  16 KELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQReLKGKIDTITRKLDEKSKEQEELLQMIQNLQEA 95
Cdd:COG2433   423 ERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDREISR-LDREIERLERELEEERERIEELKRKLERLKEL 501


                  .
gi 1039773953  96 L 96
Cdd:COG2433   502 W 502
mukB PRK04863
chromosome partition protein MukB;
28-123 2.71e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   28 KLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSKEQEELLQMIQNLQEALQR------AAN 101
Cdd:PRK04863   359 ELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQALERAKQLcglpdlTAD 438

                           90       100
                   ....*....|....*....|..
gi 1039773953  102 SSEESQRELKGKIDTLTLKLNE 123
Cdd:PRK04863   439 NAEDWLEEFQAKEQEATEELLS 460
PRK14150 PRK14150
heat shock protein GrpE; Provisional
 4-120 2.75e-03

heat shock protein GrpE; Provisional


Pssm-ID: 184539 [Multi-domain]  Cd Length: 193  Bit Score: 37.98  E-value: 2.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   4 QQKA--ENTSQESKKELKgkidtlTQKLNEKSKEQEELLQKN---QNLQEALQRAANSSEESQRELKGKIDTITRK--LD 76
Cdd:PRK14150    5 EQKTpqEQVSEEIEAEVE------QQEEADEAELEDELDEADariAELEAQLAEAQAEERDSVLRARAEVENIRRRaeQD 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039773953  77 -EKS------KEQEELLQMIQNLQEALQrAANSSEEsqrELKGKID--TLTLK 120
Cdd:PRK14150   79 vEKAhkfaleKFANELLPVIDNLERALQ-AADKENE---ALKALIEgvELTLK 127
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-145 3.33e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 3.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    2 LAQQKAENTSQEsKKELKGKIDTLTQKLNEKSKEQeellqknQNLQEALQRAANSSEESQRELkgkidtitrkldekske 81
Cdd:COG4913    328 LEAQIRGNGGDR-LEQLEREIERLERELEERERRR-------ARLEALLAALGLPLPASAEEF----------------- 382

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039773953   82 qEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRA 145
Cdd:COG4913    383 -AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 1-134 3.42e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 38.25  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   1 MLAQQKAENTSQESKKEL---KGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEE----------SQRELKGK 67
Cdd:pfam15905 176 MAKQEGMEGKLQVTQKNLehsKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQvekykldiaqLEELLKEK 255

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039773953  68 ---IDTITRKLDEK----SKEQEELLQMIQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQK 134
Cdd:pfam15905 256 ndeIESLKQSLEEKeqelSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 27-140 3.45e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 38.93  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  27 QKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDeKSKEQEEllqmiqnlqeALQRAANSSEES 106
Cdd:pfam05483 520 EDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLD-KSEENAR----------SIEYEVLKKEKQ 588

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039773953 107 QRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQE 140
Cdd:pfam05483 589 MKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 171-233 3.49e-03

C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin; CLECT_chondrolectin_like: C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins chondrolectin (CHODL) and layilin. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. CHODL is predominantly expressed in muscle cells and is associated with T-cell maturation. Various alternatively spliced isoforms have been of CHODL have been identified. The transmembrane form of CHODL is localized in the ER-Golgi apparatus. Layilin is widely expressed in different cell types. The extracellular CTLD of layilin binds hyaluronan (HA), a major constituent of the extracellular matrix (ECM). The cytoplasmic tail of layilin binds various members of the band 4.1/ERM superfamily (talin, radixin, and merlin). The ERM proteins are cytoskeleton-membrane linker molecules which link actin to receptors in the plasma membrane. Layilin co-localizes in with talin in membrane ruffles and may mediate signals from the ECM to the cell cytoskeleton.


Pssm-ID: 153065  Cd Length: 149  Bit Score: 37.18  E-value: 3.49e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039773953 171 SWEKNRQTCQSLGGQLLQINGADDLTFI---LQAISHTTSPFWIGLHRKKPGQP--------WLWENGTPLNFQ 233
Cdd:cd03595    26 NFEEARQACREDGGELLSIESENEQKLIerfIQTLRASDGDFWIGLRRSSQYNVtssacsslYYWLDGSISTFR 99
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 167-273 3.84e-03

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.


Pssm-ID: 153062  Cd Length: 115  Bit Score: 36.58  E-value: 3.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953 167 HGPFSWEKNRQTCQSLGGQLLQINGADDLTFIL-QAISHTTSPFWIGLHRKKPGQPWLWENGTPLNFQFFktrgvslqly 245
Cdd:cd03592     7 TEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNgFALKYNLGYYWIDGNDINNEGTWVDTDKKELEYKNW---------- 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1039773953 246 SSG--------NC---AYLQDGAVFAENCILIAFSICQK 273
Cdd:cd03592    77 APGepnngrneNCleiYIKDNGKWNDEPCSKKKSAICYT 115
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
3-144 4.16e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 37.97  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   3 AQQKAENTSQESKKELKGKIDTLTQKLNEK--SKEQE-ELLQKNQNLQEALQRAansseESQRELKGKIDTITRKLDEKS 79
Cdd:COG1340    99 KELAELNKAGGSIDKLRKEIERLEWRQQTEvlSPEEEkELVEKIKELEKELEKA-----KKALEKNEKLKELRAELKELR 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773953  80 KEQEELLQMIQNLQEALQraansseesqrELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQR 144
Cdd:COG1340   174 KEAEEIHKKIKELAEEAQ-----------ELHEEMIELYKEADELRKEADELHKEIVEAQEKADE 227
DUF4175 pfam13779
Domain of unknown function (DUF4175);
35-147 4.52e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 38.43  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  35 EQEELLQKNQNLQEAL--------QRAANSSEESQRELKGKIDTITRK-----LDE-----KSKEQEELLQMIQNLQEAL 96
Cdd:pfam13779 507 SDEEIAKLMQELREALddymqalaEQAQQNPQDLQQPDDPNAQEMTQQdlqrmLDRieelaRSGRRAEAQQMLSQLQQML 586

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039773953  97 Q-----RAANSSEESQRELKGKIDtltlKLNEKSKEQEELLQKNQNLQEALQRAAN 147
Cdd:pfam13779 587 EnlqagQPQQQQQQGQSEMQQAMD----ELGDLLREQQQLLDETFRQLQQQGGQQQ 638
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
27-145 5.31e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 5.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   27 QKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKG-----------KIDTITRKLDEKSKEQEELLQMIQNLQEA 95
Cdd:COG4913    288 RRLELLEAELEELRAELARLEAELERLEARLDALREELDEleaqirgnggdRLEQLEREIERLERELEERERRRARLEAL 367

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039773953   96 LQR---AANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRA 145
Cdd:COG4913    368 LAAlglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
PRK12705 PRK12705
hypothetical protein; Provisional
 3-157 5.43e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.15  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   3 AQQKAENTSQESKKELKGKIDTLTQKLN----EKSKEQEELLQKNQNLQEALQRAANSSEESQrELKGKIDTITRKLDEK 78
Cdd:PRK12705   46 AEEKLEAALLEAKELLLRERNQQRQEARrereELQREEERLVQKEEQLDARAEKLDNLENQLE-EREKALSARELELEEL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  79 SKeqeellqmiqNLQEALQRAANSSEESQRELkgKIDTLTLKLNE---------KSKEQEELLQKNQN-LQEALQRAAN- 147
Cdd:PRK12705  125 EK----------QLDNELYRVAGLTPEQARKL--LLKLLDAELEEekaqrvkkiEEEADLEAERKAQNiLAQAMQRIASe 192

                         170
                  ....*....|....*..
gi 1039773953 148 -------FSGPCPQDWL 157
Cdd:PRK12705  193 tasdlsvSVVPIPSDAM 209
MobL pfam18555
MobL relaxases; This family includes members of relaxase enzymes. These enzymes initiate ...
 21-145 5.48e-03

MobL relaxases; This family includes members of relaxase enzymes. These enzymes initiate bacterial conjugation contributing to the spread of antibiotic resistance. These MobL relaxases are found mainly in Firmicutes. It is suggested that MobL type relaxases play a prominent role in horizontal gene transfer in Firmicutes bacteria. Family members carry a stretch of relaxase motif III 'HUH' sequence that is characteriztic of the HUH endonuclease superfamily essential for enzymatic activity.


Pssm-ID: 436573 [Multi-domain]  Cd Length: 387  Bit Score: 37.81  E-value: 5.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953  21 KIDTLTqklNEKSKEQEELLQKNQNLqEALQRAAnsseesQRELKGKIDTITRKLDEkSKEQEELLQMIQNLQEALQRAA 100
Cdd:pfam18555 193 KQKTLD---AFKSEFANALLDRKQER-AELSRLI------RRELRPQTKEKSRSICP-SPEQEELLQQIYKKLPKDKSKW 261

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1039773953 101 NSSEESQRELKGKIDTLTLKLNEKSKEQE--ELLQKNQNLQEALQRA 145
Cdd:pfam18555 262 RYGSNAMKPARPLIDELVDKYLERYHAPEmqEYYERLKDEQDEYKAL 308
Perilipin pfam03036
Perilipin family; The perilipin family includes lipid droplet-associated protein (perilipin), ...
 5-112 5.48e-03

Perilipin family; The perilipin family includes lipid droplet-associated protein (perilipin), adipose differentiation-related protein (adipophilin) and TIP47, also known as perilin-3, altogether form the PAT family of proteins. They predominantly localize to the surface of intracellular neutral lipid droplets. Perilipin is a modulator of adipocyte lipid metabolism and adipophilinis and are involved in the development and maintenance of adipose tissue. This family appears to share some similarity with pfam08618.


Pssm-ID: 460784  Cd Length: 400  Bit Score: 38.04  E-value: 5.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   5 QKAENTSQESKKELKGKID-------TLTQKLNEKskeQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDE 77
Cdd:pfam03036 234 RQAKQRTQEALSQLHSTLDlieyarkGVDQKLQEG---QEKLRQSWLEWKKGQPEGDQKEDSEAEEVESRTLSMARSLTQ 310

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039773953  78 KSKEQ-EELLQMIQNLQEALQRAANSSEESQRELKG 112
Cdd:pfam03036 311 QLQSTcLSLVSSVQGLPQAVQEQVSQVRRSAEELQA 346
PTZ00121 PTZ00121
MAEBL; Provisional
 3-141 5.53e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 5.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953    3 AQQKAENT--SQESKK---ELKGKIDTLTQKLNEKSKEQEELLQKnqnlQEALQRAANSSEESQRELKGKIDTITRKLDE 77
Cdd:PTZ00121  1307 AKKKAEEAkkADEAKKkaeEAKKKADAAKKKAEEAKKAAEAAKAE----AEAAADEAEAAEEKAEAAEKKKEEAKKKADA 1382

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039773953   78 KSKEQEEllqmiqnlqealQRAANSSEESQRELKGKIDTLTLKLNEKsKEQEELLQKNQNLQEA 141
Cdd:PTZ00121  1383 AKKKAEE------------KKKADEAKKKAEEDKKKADELKKAAAAK-KKADEAKKKAEEKKKA 1433
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 2-142 8.62e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 37.18  E-value: 8.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   2 LAQQKAENtsQESKKELKGKIDTLTQKLNEKSKEQEELLQKnqnlQEALQRAANSSEESQRELKGKIDtitrkldeksKE 81
Cdd:pfam07888 120 LLAQRAAH--EARIRELEEDIKTLTQRVLERETELERMKER----AKKAGAQRKEEEAERKQLQAKLQ----------QT 183

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039773953  82 QEELLQMIQNLQEALQRAANSSEESQReLKGKIDTLTLKLNE---KSKEQEELLQKNQNLQEAL 142
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQ-LQDTITTLTQKLTTahrKEAENEALLEELRSLQERL 246
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 9-145 9.34e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 37.04  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773953   9 NTSQESKKELKGKIDTLTQKLNE----KSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTITRKLDEKSKEQEE 84
Cdd:pfam09787  57 DLLREEIQKLRGQIQQLRTELQEleaqQQEEAESSREQLQELEEQLATERSARREAEAELERLQEELRYLEEELRRSKAT 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039773953  85 LLQMIQNLQEALQRAANS------SEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRA 145
Cdd:pfam09787 137 LQSRIKDREAEIEKLRNQltsksqSSSSQSELENRLHQLTETLIQKQTMLEALSTEKNSLVLQLERM 203
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH