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Conserved domains on  [gi|1039773951|ref|XP_017176788|]
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oxidized low-density lipoprotein receptor 1 isoform X1 [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

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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); ...
 189-310 7.62e-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: 115.12  E-value: 7.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 189 CPQDWLWHKENCYLFH-GPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHttSPFWIGLHRKKPGQPWLWENGTPL 267
Cdd:cd03593     1 CPKDWICYGNKCYYFSmEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSREKSEKPWKWIDGSPL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039773951 268 NFQFFKTRGVslqlySSGNCAYLQDGAVFAENCILIAFSICQK 310
Cdd:cd03593    79 NNLFNIRGST-----KSGNCAYLSSTGIYSEDCSTKKRWICEK 116
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 58-184 7.20e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 7.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   58 QLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKEL---KGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQ 134
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  135 RAANSSEESQR----------ELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 184
Cdd:TIGR02168  327 ELESKLDELAEelaeleekleELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
 
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); ...
 189-310 7.62e-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: 115.12  E-value: 7.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 189 CPQDWLWHKENCYLFH-GPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHttSPFWIGLHRKKPGQPWLWENGTPL 267
Cdd:cd03593     1 CPKDWICYGNKCYYFSmEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSREKSEKPWKWIDGSPL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039773951 268 NFQFFKTRGVslqlySSGNCAYLQDGAVFAENCILIAFSICQK 310
Cdd:cd03593    79 NNLFNIRGST-----KSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 189-309 3.30e-23

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: 92.66  E-value: 3.30e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  189 CPQDWLWHKENCYLFHG-PFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSP--FWIGLHRKKPGQPWLWENGT 265
Cdd:smart00034   1 CPSGWISYGGKCYKFSTeKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039773951  266 PL-NFQFFKTRGVSlqlYSSGNCAYLQ--DGAVFAENCILIAFSICQ 309
Cdd:smart00034  81 GPvSYSNWAPGEPN---NSSGDCVVLStsGGKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 208-310 4.73e-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: 67.12  E-value: 4.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 208 SWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSPFWIGLHRKKPGQPWLWENGTPLNFQFFKTRGVSLQlySSGNC 287
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNG--ENEDC 80

                          90       100
                  ....*....|....*....|....*
gi 1039773951 288 AYLQ--DGAVFAENCILIAFSICQK 310
Cdd:pfam00059  81 VELSssSGKWNDENCNSKNPFVCEK 105
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 189-317 1.40e-10

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 60.13  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 189 CPQDWLWHKENCYLF-HGPFSWEKNRQTCQSLGGQLLQINGADDLTFILQaiSHTTSPFWIGLHRKKPGQPWLWENGTPL 267
Cdd:PHA02642   88 CPKGWIGFGYKCFYFsEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKR--YKDSSDHWIGLNRESSNHPWKWADNSNY 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039773951 268 NFQFFKTrgvslqlySSGNCAYLQDGAVFAENCILIAFSICQKKTNHLQI 317
Cdd:PHA02642  166 NASFVIT--------GTGECAYLNDIRISSSRVYANRKWICSKTYTNIYI 207
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 58-184 7.20e-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: 56.99  E-value: 7.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   58 QLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKEL---KGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQ 134
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  135 RAANSSEESQR----------ELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 184
Cdd:TIGR02168  327 ELESKLDELAEelaeleekleELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
PRK12704 PRK12704
phosphodiesterase; Provisional
 39-186 1.14e-08

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 55.94  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  39 MTLVILCLVLSVTLIV-----QWTQLRQVSDLLKQYQAnltQQDRILEGqmlAQQKAENTSQESKKELKGKIDTLTQKLN 113
Cdd:PRK12704    1 MMLLIIILIALVALVVgavigYFVRKKIAEAKIKEAEE---EAKRILEE---AKKEAEAIKKEALLEAKEEIHKLRNEFE 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039773951 114 EKSKEQEELLQKNQN--LQ--EALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAANFS 186
Cdd:PRK12704   75 KELRERRNELQKLEKrlLQkeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLT 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 58-183 1.56e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  58 QLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKK---ELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQ 134
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039773951 135 RAANSSEE---SQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 183
Cdd:COG1196   313 ELEERLEEleeELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 99-177 2.05e-04

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: 41.82  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  99 KELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQREL-------------KGKIDTLTLKLNEKSKEQ 165
Cdd:pfam13851  29 KSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLenyekdkqslknlKARLKVLEKELKDLKWEH 108

                          90
                  ....*....|..
gi 1039773951 166 EELLQKNQNLQE 177
Cdd:pfam13851 109 EVLEQRFEKVER 120
GvpT NF041669
GvpT/GvpP family gas vesicle accessory protein;
97-181 1.48e-03

GvpT/GvpP family gas vesicle accessory protein;


Pssm-ID: 469551  Cd Length: 122  Bit Score: 37.94  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  97 SKKELKGKIDTLTQKLNEKSKE-QEELLQKNQNLqeaLQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNL 175
Cdd:NF041669   32 DQEELKSKGKDLGKAAKEKSKQaAGSLKSSTANL---FKKDKDSEEEEDEENETEDEEEEETEEEDSEDYEELKEENKQL 108


                  ....*.
gi 1039773951 176 QEALQR 181
Cdd:NF041669  109 QDRLQK 114
 
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); ...
 189-310 7.62e-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: 115.12  E-value: 7.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 189 CPQDWLWHKENCYLFH-GPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHttSPFWIGLHRKKPGQPWLWENGTPL 267
Cdd:cd03593     1 CPKDWICYGNKCYYFSmEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGS--SSYWIGLSREKSEKPWKWIDGSPL 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1039773951 268 NFQFFKTRGVslqlySSGNCAYLQDGAVFAENCILIAFSICQK 310
Cdd:cd03593    79 NNLFNIRGST-----KSGNCAYLSSTGIYSEDCSTKKRWICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 189-309 3.30e-23

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: 92.66  E-value: 3.30e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  189 CPQDWLWHKENCYLFHG-PFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSP--FWIGLHRKKPGQPWLWENGT 265
Cdd:smart00034   1 CPSGWISYGGKCYKFSTeKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSdyYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039773951  266 PL-NFQFFKTRGVSlqlYSSGNCAYLQ--DGAVFAENCILIAFSICQ 309
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 ...
 199-310 5.01e-18

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: 78.43  E-value: 5.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 199 NCYLFH-GPFSWEKNRQTCQSLGGQLLQINGADDLTFIL-QAISHTTSPFWIGLHRKKPGQPWLWENGTPLnFQFFKTRG 276
Cdd:cd00037     1 SCYKFStEKLTWEEAQEYCRSLGGHLASIHSEEENDFLAsLLKKSSSSDVWIGLNDLSSEGTWKWSDGSPL-VDYTNWAP 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1039773951 277 VSLQLYSSGNCAYL---QDGAVFAENCILIAFSICQK 310
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 ...
 189-300 2.19e-14

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: 68.94  E-value: 2.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 189 CPQDWLWHKENCY-LFHGPFSWEKNRQTCQSL--GGQLLQINGADDLTFILQAIS---HTTSPFWIGLHRKKPGQPWLWE 262
Cdd:cd03594     1 CPKGWLPYKGNCYgYFRQPLSWSDAELFCQKYgpGAHLASIHSPAEAAAIASLISsyqKAYQPVWIGLHDPQQSRGWEWS 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1039773951 263 NGTPLNFqFFKTRGVSLQlySSGNCAYLQDGAVF----AENC 300
Cdd:cd03594    81 DGSKLDY-RSWDRNPPYA--RGGYCAELSRSTGFlkwnDANC 119
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 208-310 4.73e-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: 67.12  E-value: 4.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 208 SWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSPFWIGLHRKKPGQPWLWENGTPLNFQFFKTRGVSLQlySSGNC 287
Cdd:pfam00059   3 TWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAPEPNNNG--ENEDC 80

                          90       100
                  ....*....|....*....|....*
gi 1039773951 288 AYLQ--DGAVFAENCILIAFSICQK 310
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 ...
 189-268 2.94e-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: 65.40  E-value: 2.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 189 CPQDWLWHKENCYLF-HGPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSpFWIGLHRKKPGQPWLWENGTPL 267
Cdd:cd03590     1 CPTNWKSFQSSCYFFsTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRS-YWIGLSDEETEGEWKWVDGTPL 79


                  .
gi 1039773951 268 N 268
Cdd:cd03590    80 N 80
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 189-317 1.40e-10

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 60.13  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 189 CPQDWLWHKENCYLF-HGPFSWEKNRQTCQSLGGQLLQINGADDLTFILQaiSHTTSPFWIGLHRKKPGQPWLWENGTPL 267
Cdd:PHA02642   88 CPKGWIGFGYKCFYFsEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKR--YKDSSDHWIGLNRESSNHPWKWADNSNY 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039773951 268 NFQFFKTrgvslqlySSGNCAYLQDGAVFAENCILIAFSICQKKTNHLQI 317
Cdd:PHA02642  166 NASFVIT--------GTGECAYLNDIRISSSRVYANRKWICSKTYTNIYI 207
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 189-269 4.76e-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: 53.90  E-value: 4.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 189 CPQDWLWHKENCYLFHGP-FSWEKNRQTCQSLG-----GQLLQINGADDLTFILQ-----AISHTTSPFWIGLHRKKPGQ 257
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDrLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDlfessRGPDTPYGLWIGLHDRTSEG 80

                          90
                  ....*....|..
gi 1039773951 258 PWLWENGTPLNF 269
Cdd:cd03589    81 PFEWTDGSPVDF 92
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 201-272 6.17e-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: 6.17e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039773951 201 YLF-HGPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAIShTTSPFWIGLHRKKPGQPWLWENGTPLNFQFF 272
Cdd:cd03603     3 YKFvDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFG-GYGASWIGASDAATEGTWKWSDGEESTYTNW 74
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 58-184 7.20e-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: 56.99  E-value: 7.20e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   58 QLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKEL---KGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQ 134
Cdd:TIGR02168  247 ELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELyalANEISRLEQQKQILRERLANLERQLEELEAQLE 326

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  135 RAANSSEESQR----------ELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 184
Cdd:TIGR02168  327 ELESKLDELAEelaeleekleELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386
PRK12704 PRK12704
phosphodiesterase; Provisional
 39-186 1.14e-08

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 55.94  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  39 MTLVILCLVLSVTLIV-----QWTQLRQVSDLLKQYQAnltQQDRILEGqmlAQQKAENTSQESKKELKGKIDTLTQKLN 113
Cdd:PRK12704    1 MMLLIIILIALVALVVgavigYFVRKKIAEAKIKEAEE---EAKRILEE---AKKEAEAIKKEALLEAKEEIHKLRNEFE 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039773951 114 EKSKEQEELLQKNQN--LQ--EALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAANFS 186
Cdd:PRK12704   75 KELRERRNELQKLEKrlLQkeENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLT 151
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 58-183 1.56e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 1.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  58 QLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKK---ELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQ 134
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1039773951 135 RAANSSEE---SQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 183
Cdd:COG1196   313 ELEERLEEleeELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 58-183 2.67e-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: 51.98  E-value: 2.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   58 QLRQVSDLLKQYQANLTQQDRilegQMLAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAA 137
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELES----KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1039773951  138 N---SSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 183
Cdd:TIGR02168  386 SkvaQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE 434
PRK12705 PRK12705
hypothetical protein; Provisional
 38-186 1.32e-06

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 49.71  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  38 AMTLVILCLVLSVTLIVQWTQLrqvsdLLKQYQANLTQQDRIL-EGQMLAQQKAENTSQESKKELKGKIDtltQKLNEKS 116
Cdd:PRK12705    2 AMSILLVILLLLIGLLLGVLVV-----LLKKRQRLAKEAERILqEAQKEAEEKLEAALLEAKELLLRERN---QQRQEAR 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 117 KEQEELlqknQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAANFS 186
Cdd:PRK12705   74 REREEL----QREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELELEELEKQLDNELYRVAGLT 139
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 70-184 1.75e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 1.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  70 QANLTQQDRILEGQMLAQQKAENTSQESKKE-LKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELK 148
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039773951 149 GKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 184
Cdd:COG1196   383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 85-181 3.19e-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: 48.22  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  85 LAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAanssEESQRELKGKIDTLTLKLNEKSKE 164
Cdd:COG4942    16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL----ARRIRALEQELAALEAELAELEKE 91

                          90
                  ....*....|....*..
gi 1039773951 165 QEELLQKNQNLQEALQR 181
Cdd:COG4942    92 IAELRAELEAQKEELAE 108
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 58-183 5.33e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 5.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  58 QLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAA 137
Cdd:COG1196   247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039773951 138 nSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 183
Cdd:COG1196   327 -ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 39-154 8.78e-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: 8.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  39 MTLVILCLVLSVTLIVQWTQLRQVSDLLKQYQANLTQQDRILEgqmlAQQKAENTSQESKKELKGKIDTLTQKLNEKSKE 118
Cdd:COG4942     2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAALERRIAALARRIRALEQE 77

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1039773951 119 QEELLQKNQNLQEALQRAANSSEESQRELKGKIDTL 154
Cdd:COG4942    78 LAALEAELAELEKEIAELRAELEAQKEELAELLRAL 113
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-183 9.22e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 9.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  67 KQYQAnLTQQDRILEGQMLAQQKAEntSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQ-- 144
Cdd:COG1196   213 ERYRE-LKEELKELEAELLLLKLRE--LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQae 289

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039773951 145 -RELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 183
Cdd:COG1196   290 eYELLAELARLEQDIARLEERRRELEERLEELEEELAELE 329
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
58-182 1.81e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.30  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  58 QLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKK--------ELKGKIDTLTQKLNEKSKEQEELLQKNQNL 129
Cdd:COG4717    79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlekllqllPLYQELEALEAELAELPERLEELEERLEEL 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039773951 130 QEALQRAANSSEEsQRELKGKIDTLTLKLNEKSKEQ--------EELLQKNQNLQEALQRA 182
Cdd:COG4717   159 RELEEELEELEAE-LAELQEELEELLEQLSLATEEElqdlaeelEELQQRLAELEEELEEA 218
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 59-182 2.11e-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: 46.20  E-value: 2.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   59 LRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEEL---LQKNQNLQEALQR 135
Cdd:TIGR02168  808 LRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELeseLEALLNERASLEE 887

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1039773951  136 AANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRA 182
Cdd:TIGR02168  888 ALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL 934
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 51-177 2.59e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 2.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   51 TLIVQWTQLRQVSDLLKQYQANLTQQ--DRILEGQMLAQQkaENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQN 128
Cdd:TIGR02169  692 SLQSELRRIENRLDELSQELSDASRKigEIEKEIEQLEQE--EEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039773951  129 LQEAL----------------------QRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQE 177
Cdd:TIGR02169  770 LEEDLhkleealndlearlshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE 840
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 65-184 2.94e-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: 45.14  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  65 LLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKElkgKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQ 144
Cdd:COG4942   125 LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA---ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLL 201

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039773951 145 RELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 184
Cdd:COG4942   202 ARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PHA02867 PHA02867
C-type lectin protein; Provisional
 184-315 4.37e-05

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 43.13  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 184 NFSGPCPQDWLWHKENCYLFH-GPFSWEKNRQTCQSLGGQLLQINGADDLTFILQaisHTTSPFWIglHRKKpgqpwlWE 262
Cdd:PHA02867   44 YFSKVCPDEWIGYNSKCYYFTiNETNWNDSKKLCDVMDSSLIRFDNIETLNFVSR---YGKGSYWI--DINQ------NR 112

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039773951 263 NgtplnfqffkTRGVSLQLYSSGN----CAYLQDGAVFAENCILIAFSICQKKTNHL 315
Cdd:PHA02867  113 K----------IPGINFSLYYEQGvndiCLLFDTSNIIEMSCIFHERTICVKEDRYT 159
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 58-179 4.92e-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: 45.05  E-value: 4.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   58 QLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKELKgkiDTLTQKLNEKSKEQEELLQKNQNLQEaLQRAA 137
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELE---SELEALLNERASLEEALALLRSELEE-LSEEL 903

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1039773951  138 NSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEAL 179
Cdd:TIGR02168  904 RELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERL 945
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
57-183 1.12e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.35  E-value: 1.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  57 TQLRQVSDLLKQYQANLTQqdriLEGQMLAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRA 136
Cdd:COG4372    66 EELEQARSELEQLEEELEE----LNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAEL 141

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1039773951 137 ANSSEESQRELKgkidTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 183
Cdd:COG4372   142 QSEIAEREEELK----ELEEQLESLQEELAALEQELQALSEAEAEQA 184
PRK09039 PRK09039
peptidoglycan -binding protein;
35-176 1.13e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.42  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  35 FPAAMT--LVILCLVLSVTLIVQW-----------------TQLRQVSDLLK-QYQANLTQQDRI---------LEGQML 85
Cdd:PRK09039   19 FVDALStlLLVIMFLLTVFVVAQFflsreisgkdsaldrlnSQIAELADLLSlERQGNQDLQDSVanlraslsaAEAERS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  86 AQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQK----NQNLQE------ALQRAANSSEESQRELKGKIDTLT 155
Cdd:PRK09039   99 RLQALLAELAGAGAAAEGRAGELAQELDSEKQVSARALAQvellNQQIAAlrrqlaALEAALDASEKRDRESQAKIADLG 178

                         170       180
                  ....*....|....*....|.
gi 1039773951 156 LKLNEKskeqeeLLQKNQNLQ 176
Cdd:PRK09039  179 RRLNVA------LAQRVQELN 193
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-187 1.67e-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: 43.51  E-value: 1.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   54 VQWTQLRQVSDLLKQYQANLTQQDRILEGQM------LAQQKAENTSQESKKELKgKIDTLTQKLNEKSKEQEELLQKNQ 127
Cdd:TIGR02168  379 EQLETLRSKVAQLELQIASLNNEIERLEARLerledrRERLQQEIEELLKKLEEA-ELKELQAELEELEEELEELQEELE 457

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039773951  128 NLQEALQRAANSSEESQREL---KGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAANFSG 187
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALdaaERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 99-177 2.05e-04

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: 41.82  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  99 KELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQREL-------------KGKIDTLTLKLNEKSKEQ 165
Cdd:pfam13851  29 KSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLenyekdkqslknlKARLKVLEKELKDLKWEH 108

                          90
                  ....*....|..
gi 1039773951 166 EELLQKNQNLQE 177
Cdd:pfam13851 109 EVLEQRFEKVER 120
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
57-184 2.30e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  57 TQLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAE-----NTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQE 131
Cdd:COG4717   102 EELEELEAELEELREELEKLEKLLQLLPLYQELEAleaelAELPERLEELEERLEELRELEEELEELEAELAELQEELEE 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1039773951 132 ALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 184
Cdd:COG4717   182 LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 55-150 2.86e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  55 QWTQLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQ 134
Cdd:COG4942   151 QAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230

                          90
                  ....*....|....*.
gi 1039773951 135 RAANSSEESQRELKGK 150
Cdd:COG4942   231 RLEAEAAAAAERTPAA 246
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 57-184 4.12e-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: 4.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   57 TQLRQVSDLLKQYQANLTQQDRI---LEGQMLAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEAL 133
Cdd:TIGR02168  323 AQLEELESKLDELAEELAELEEKleeLKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI 402

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039773951  134 QRAANSSEESQREL---------------KGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 184
Cdd:TIGR02168  403 ERLEARLERLEDRRerlqqeieellkkleEAELKELQAELEELEEELEELQEELERLEEALEELRE 468
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 231-308 4.37e-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: 39.28  E-value: 4.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039773951 231 DLTFILQAISHTTSPFWIGLHRKKpgQPWLWENGTPLNFQFFKTrgvsLQLYSSGNCAYL-QDGAVFAENCILIAFSIC 308
Cdd:cd03602    34 DNALLSNLSRVSNSAAWIGLYRDV--DSWRWSDGSESSFRNWNT----FQPFGQGDCATMySSGRWYAALCSALKPFIC 106
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
54-182 4.74e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 4.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   54 VQWTQLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKELK--------GKIDTLTQKLNEKSKEQEELLQK 125
Cdd:COG4913    281 LRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEaqirgnggDRLEQLEREIERLERELEERERR 360

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  126 NQNLQEALQR---AANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRA 182
Cdd:COG4913    361 RARLEALLAAlglPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 80-188 5.17e-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: 41.58  E-value: 5.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  80 LEGQMLAQQKAENTSQESKKELkgkidTLTQKLNEKSKEQeellQKNQNL-QEALQRAANSSEESQRELKGKIDTLTLKL 158
Cdd:pfam05911 711 LESTKSQLQESEQLIAELRSEL-----ASLKESNSLAETQ----LKCMAEsYEDLETRLTELEAELNELRQKFEALEVEL 781

                          90       100       110
                  ....*....|....*....|....*....|
gi 1039773951 159 NEKSKEQEELLQKNQNLQEALQRAANFSGP 188
Cdd:pfam05911 782 EEEKNCHEELEAKCLELQEQLERNEKKESS 811
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 92-172 6.03e-04

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 40.87  E-value: 6.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  92 NTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAanssEESQRELKGKIDTLTLKLNEKSKEQEELLQK 171
Cdd:COG4026   131 NELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKL----REENSILEEEFDNIKSEYSDLKSRFEELLKK 206


                  .
gi 1039773951 172 N 172
Cdd:COG4026   207 R 207
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
55-181 6.09e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 6.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  55 QWTQLRQVSDLLKQYQANLTQQDRIlegQMLAQQKAENTSQESK------------KELKGKIDTLTQKLNEkskEQEEL 122
Cdd:COG3206   241 RLAALRAQLGSGPDALPELLQSPVI---QQLRAQLAELEAELAElsarytpnhpdvIALRAQIAALRAQLQQ---EAQRI 314

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039773951 123 LQKNQNLQEALQRAANSSEESQRELKGKIDTltlkLNEKSKEQEELLQ----KNQNLQEALQR 181
Cdd:COG3206   315 LASLEAELEALQAREASLQAQLAQLEARLAE----LPELEAELRRLERevevARELYESLLQR 373
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
58-181 6.65e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 6.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  58 QLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQ------E 131
Cdd:COG4372    39 ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEelqeelE 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1039773951 132 ALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQR 181
Cdd:COG4372   119 ELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 58-182 6.87e-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: 40.29  E-value: 6.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  58 QLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKELKGKIDTLTQKLnEKSKEQEELLQKN---QNLQ---E 131
Cdd:COG1579    21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-KKYEEQLGNVRNNkeyEALQkeiE 99

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1039773951 132 ALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRA 182
Cdd:COG1579   100 SLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEE 150
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 48-178 7.29e-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: 7.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   48 LSVTLIVQWTQLRQVSDLLKQYQANLTQQDRILEgqmlAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQ 127
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALD----ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039773951  128 NLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEA 178
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEEL 899
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 60-184 7.61e-04

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: 41.21  E-value: 7.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   60 RQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKEL---KGKIDTLTQKLNEKSKE----QEELLQKNQNLQEA 132
Cdd:TIGR02169  290 LRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIdklLAEIEELEREIEEERKRrdklTEEYAELKEELEDL 369

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039773951  133 LQRAANSSEESQR------ELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 184
Cdd:TIGR02169  370 RAELEEVDKEFAEtrdelkDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 57-179 8.04e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 41.31  E-value: 8.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   57 TQLRQVSDLLK---QYQANLTQQDRILEGQMLAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQknqnlqeal 133
Cdd:pfam01576  468 SQLQDTQELLQeetRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAG--------- 538

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1039773951  134 qrAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEAL 179
Cdd:pfam01576  539 --TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQEL 582
Seryl_tRNA_N pfam02403
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ...
 96-170 9.26e-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: 9.26e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773951  96 ESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAansseesqRELKGKIDTLTLKLNEKSKEQEELLQ 170
Cdd:pfam02403  36 EKRRELQVELEELQAERNELSKEIGQAKKKKEDADALIAEV--------KELKDELKALEAELKELEAELDKLLL 102
PRK05431 PRK05431
seryl-tRNA synthetase; Provisional
 96-169 9.44e-04

seryl-tRNA synthetase; Provisional


Pssm-ID: 235461 [Multi-domain]  Cd Length: 425  Bit Score: 40.44  E-value: 9.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039773951  96 ESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAansseesqRELKGKIDTLTLKLNEKSKEQEELL 169
Cdd:PRK05431   35 EERRELQTELEELQAERNALSKEIGQAKRKGEDAEALIAEV--------KELKEEIKALEAELDELEAELEELL 100
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
61-184 1.05e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  61 QVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKELKGK-----IDTLTQKLnEKSKEQEELLQKNQNLQEALQR 135
Cdd:COG4717   335 SPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEagvedEEELRAAL-EQAEEYQELKEELEELEEQLEE 413

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039773951 136 AANSSEESQR-----ELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 184
Cdd:COG4717   414 LLGELEELLEaldeeELEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 83-177 1.21e-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: 40.44  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   83 QMLAQQKAENTSQESKK------ELKGKIDTLTQKLNEKSKEQEELLQKNQNLQE---ALQRAANSSEESQRELKGKIDT 153
Cdd:TIGR02169  786 ARLSHSRIPEIQAELSKleeevsRIEARLREIEQKLNRLTLEKEYLEKEIQELQEqriDLKEQIKSIEKEIENLNGKKEE 865

                           90       100
                   ....*....|....*....|....
gi 1039773951  154 LTLKLNEKSKEQEELLQKNQNLQE 177
Cdd:TIGR02169  866 LEEELEELEAALRDLESRLGDLKK 889
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 81-186 1.30e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  81 EGQMLAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELKGKIDTL-----T 155
Cdd:COG3883    15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerarA 94

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1039773951 156 LKLNEKSKEQEELLQKNQNLQEALQRAANFS 186
Cdd:COG3883    95 LYRSGGSVSYLDVLLGSESFSDFLDRLSALS 125
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
25-182 1.36e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.14  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  25 GLHLLSSPWWFPAamtlvILCLVLSVTLIVQWTQLRQVSDLLKQ-YQANLTQQDRILEGQMLAQQKAE-----NTSQESK 98
Cdd:COG4717   265 GGSLLSLILTIAG-----VLFLVLGLLALLFLLLAREKASLGKEaEELQALPALEELEEEELEELLAAlglppDLSPEEL 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  99 KELKGKIDTLTQKLNEKSKEQEEL-LQKNQNLQEALQRAANSSEESQ-----------RELKGKIDTLTLKLNEKSKEQE 166
Cdd:COG4717   340 LELLDRIEELQELLREAEELEEELqLEELEQEIAALLAEAGVEDEEElraaleqaeeyQELKEELEELEEQLEELLGELE 419

                         170
                  ....*....|....*...
gi 1039773951 167 ELLQKNQ--NLQEALQRA 182
Cdd:COG4717   420 ELLEALDeeELEEELEEL 437
GvpT NF041669
GvpT/GvpP family gas vesicle accessory protein;
97-181 1.48e-03

GvpT/GvpP family gas vesicle accessory protein;


Pssm-ID: 469551  Cd Length: 122  Bit Score: 37.94  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  97 SKKELKGKIDTLTQKLNEKSKE-QEELLQKNQNLqeaLQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNL 175
Cdd:NF041669   32 DQEELKSKGKDLGKAAKEKSKQaAGSLKSSTANL---FKKDKDSEEEEDEENETEDEEEEETEEEDSEDYEELKEENKQL 108


                  ....*.
gi 1039773951 176 QEALQR 181
Cdd:NF041669  109 QDRLQK 114
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-183 1.88e-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: 40.04  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   50 VTLIVQWTQLRQVSDLLKQYQANLTQQDRILEgQMLAQQKAENTS-QESKKELKGKIDTLTQKLNEKSKEQEELLQKNQN 128
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLARLEAEVEQLE-ERIAQLSKELTElEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773951  129 LQEALQ---RAANSSEESQRELKGKIDTLTLKLN-------EKSKEQEELLQKNQNLQEALQRAA 183
Cdd:TIGR02168  794 LKEELKalrEALDELRAELTLLNEEAANLRERLEslerriaATERRLEDLEEQIEELSEDIESLA 858
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 208-270 2.85e-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: 37.56  E-value: 2.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039773951 208 SWEKNRQTCQSLGGQLLQINGADDLTFI---LQAISHTTSPFWIGLHRKKPGQP--------WLWENGTPLNFQ 270
Cdd:cd03595    26 NFEEARQACREDGGELLSIESENEQKLIerfIQTLRASDGDFWIGLRRSSQYNVtssacsslYYWLDGSISTFR 99
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
71-181 3.04e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 3.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  71 ANLTQQDRILEGQMLAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSEESQRELK-- 148
Cdd:COG4372    27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELEsl 106

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1039773951 149 -GKIDTLTLKLNEKSKEQEELLQKNQNLQEALQR 181
Cdd:COG4372   107 qEEAEELQEELEELQKERQDLEQQRKQLEAQIAE 140
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 55-183 3.25e-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: 39.27  E-value: 3.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   55 QWTQLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALq 134
Cdd:TIGR02168  846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL- 924

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1039773951  135 raaNSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAA 183
Cdd:TIGR02168  925 ---AQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEA 970
PhaF COG3937
Polyhydroxyalkanoate synthesis regulator phasin [Secondary metabolites biosynthesis, transport ...
 85-164 3.54e-03

Polyhydroxyalkanoate synthesis regulator phasin [Secondary metabolites biosynthesis, transport and catabolism, Signal transduction mechanisms];


Pssm-ID: 443138 [Multi-domain]  Cd Length: 103  Bit Score: 36.32  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  85 LAQQKAENTSQE-------SKKELKGKIDTLTQKLNEKSKEQEELLQKNqnLQEALQRAANSSEESQRELKGKIDTLTLK 157
Cdd:COG3937    18 LTKEKAEELVDElvekgelTEEEAKKFVDELVEKGEEEKEELEEKIEEQ--VEEALEKLGLATKEEVDELEERIDRLEKQ 95


                  ....*..
gi 1039773951 158 LNEKSKE 164
Cdd:COG3937    96 LRELENK 102
TFB3 COG5220
Cdk activating kinase (CAK)/RNA polymerase II transcription initiation/nucleotide excision ...
 61-187 3.58e-03

Cdk activating kinase (CAK)/RNA polymerase II transcription initiation/nucleotide excision repair factor TFIIH, subunit TFB3 [Cell division and chromosome partitioning / Transcription / DNA replication, recombination, and repair];


Pssm-ID: 227545 [Multi-domain]  Cd Length: 314  Bit Score: 38.46  E-value: 3.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  61 QVSDLLKQYQAnlTQQDRILEGQMLAQQKAENTSQESKKELKGKidtLTQKLNEKSKEQEELLQKNQNLQEALQRAANSS 140
Cdd:COG5220   128 LTEEKVKKYEE--MNQDSILNNLERPTPEVMPGKQKNVLQKRMK---LKKRQLERQIEEEERMNKEWTKKEIGNRLGTAS 202

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1039773951 141 EESQRELKGKIDTLTLK-------LNEKSKEQEELLQKNQNLQEALQRAANFSG 187
Cdd:COG5220   203 EDGNKTIKIGIISDKFDpeelpriVVEPTRNNKIYLSNVQGFLKDLQPFAPGGG 256
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 60-177 3.78e-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: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  60 RQVSDL---LKQYQANLTQQDRiLEGQMLAQQKaenTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRA 136
Cdd:pfam05483 506 QEASDMtleLKKHQEDIINCKK-QEERMLKQIE---NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYE 581

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1039773951 137 ANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQE 177
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKK 622
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 58-185 3.93e-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: 38.59  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  58 QLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENT-------SQES--------------KKELKGKIDTLTQKLNEKS 116
Cdd:COG4942    84 ELAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplalllSPEDfldavrrlqylkylAPARREQAEELRADLAELA 163

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039773951 117 KEQEELLQKNQNLQEALQRAanssEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAANF 185
Cdd:COG4942   164 ALRAELEAERAELEALLAEL----EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 200-256 4.13e-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: 37.03  E-value: 4.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773951 200 CY-LFHGPFSWEKNRQTCQSLGGQLLQINGADDLTFILQAISHTTSP-------FWIGLHRKKPG 256
Cdd:cd03600     6 CYtLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSLLLAAGPGRhgrgslrLWIGLQREPRQ 70
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 204-310 4.19e-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: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 204 HGPFSWEKNRQTCQSLGGQLLQINGADDLTFIL-QAISHTTSPFWIGLHRKKPGQPWLWENGTPLNFQFFktrgvslqly 282
Cdd:cd03592     7 TEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNgFALKYNLGYYWIDGNDINNEGTWVDTDKKELEYKNW---------- 76

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1039773951 283 SSG--------NC---AYLQDGAVFAENCILIAFSICQK 310
Cdd:cd03592    77 APGepnngrneNCleiYIKDNGKWNDEPCSKKKSAICYT 115
mukB PRK04863
chromosome partition protein MukB;
55-192 4.26e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.78  E-value: 4.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   55 QWTQLRQVSDLLKQYQANLTQQDRIL-----EGQMLAQQKAE-NTSQESKKELKGKIDTLT---QKLNEKSKEQ-EELLQ 124
Cdd:PRK04863   902 QLDEAEEAKRFVQQHGNALAQLEPIVsvlqsDPEQFEQLKQDyQQAQQTQRDAKQQAFALTevvQRRAHFSYEDaAEMLA 981

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039773951  125 KNQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQ----KNQNLQEALQRAANFSGPCPQD 192
Cdd:PRK04863   982 KNSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSsydaKRQMLQELKQELQDLGVPADSG 1053
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
62-181 4.40e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 4.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  62 VSDLLKQYQANLTQqdriLEGQMlaQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAANSSE 141
Cdd:PRK02224  178 VERVLSDQRGSLDQ----LKAQI--EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE 251

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1039773951 142 ESQrELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQR 181
Cdd:PRK02224  252 ELE-TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE 290
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 58-179 4.57e-03

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: 37.98  E-value: 4.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  58 QLRQVSDLLKQYQANLTQQDRILEGQMLAQQKAENTSQESK----------------KELKG---KIDTLTQKLNEKSKE 118
Cdd:COG1579    32 ELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEarikkyeeqlgnvrnnKEYEAlqkEIESLKRRISDLEDE 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039773951 119 QEELLQKNQNLQEALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEAL 179
Cdd:COG1579   112 ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 94-181 4.99e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 38.65  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  94 SQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQE----ALQRAANSSEESQRELKGKIDTLTLKLNEKSKEQEElL 169
Cdd:PRK00409  525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEeedkLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYA-S 603

                          90
                  ....*....|..
gi 1039773951 170 QKNQNLQEALQR 181
Cdd:PRK00409  604 VKAHELIEARKR 615
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
59-184 5.15e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  59 LRQVSDLLKQYQANLTQQDRILEgqMLAQQKAENTSQE-SKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEAlqraa 137
Cdd:PRK03918  216 LPELREELEKLEKEVKELEELKE--EIEELEKELESLEgSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL----- 288

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1039773951 138 NSSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 184
Cdd:PRK03918  289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
58-164 5.22e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  58 QLRQVSDLLKQYQANLTQQDRiLEGQMLAQQKA--ENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQR 135
Cdd:COG4717   386 ELRAALEQAEEYQELKEELEE-LEEQLEELLGEleELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQ 464

                          90       100
                  ....*....|....*....|....*....
gi 1039773951 136 AANSSEESqrELKGKIDTLTLKLNEKSKE 164
Cdd:COG4717   465 LEEDGELA--ELLQELEELKAELRELAEE 491
PRK12704 PRK12704
phosphodiesterase; Provisional
 66-165 5.64e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 5.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  66 LKQYQANLTQQDRILegqmlaQQKAENTSQES------KKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAAN- 138
Cdd:PRK12704   77 LRERRNELQKLEKRL------LQKEENLDRKLellekrEEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGl 150

                          90       100
                  ....*....|....*....|....*..
gi 1039773951 139 SSEESQRELkgkIDtltlKLNEKSKEQ 165
Cdd:PRK12704  151 TAEEAKEIL---LE----KVEEEARHE 170
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 59-164 5.76e-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: 38.21  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  59 LRQVSDLLKQYQANLTQQDRILEgqmlAQQKAENTSQESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAAN 138
Cdd:COG4942   141 LKYLAPARREQAEELRADLAELA----ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELA 216

                          90       100
                  ....*....|....*....|....*.
gi 1039773951 139 SSEESQRELKGKIDTLTLKLNEKSKE 164
Cdd:COG4942   217 ELQQEAEELEALIARLEAEAAAAAER 242
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 58-178 5.94e-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: 38.51  E-value: 5.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951   58 QLRQVSDLLKQYQANLTQQDRILEG--QMLAQQKAENTS-QESKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQ 134
Cdd:TIGR02169  316 ELEDAEERLAKLEAEIDKLLAEIEEleREIEEERKRRDKlTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039773951  135 RAANSSEESQRELKGKIDTLT--------------------LKLNEKSKE-QEELLQKNQNLQEA 178
Cdd:TIGR02169  396 KLKREINELKRELDRLQEELQrlseeladlnaaiagieakiNELEEEKEDkALEIKKQEWKLEQL 460
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 62-184 6.57e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 37.89  E-value: 6.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  62 VSDLLKQYQA--NLTQQDR-ILEGQMLAQQKAENTsqesKKELKGKIDTLTQKLNEKSKEQEELLQKNQNLQEALQRAAN 138
Cdd:COG3883   114 FSDFLDRLSAlsKIADADAdLLEELKADKAELEAK----KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1039773951 139 SSEESQRELKGKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAAN 184
Cdd:COG3883   190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAA 235
PRK08475 PRK08475
F0F1 ATP synthase subunit B; Validated
 98-176 9.34e-03

F0F1 ATP synthase subunit B; Validated


Pssm-ID: 236272 [Multi-domain]  Cd Length: 167  Bit Score: 36.53  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  98 KKELKGKIDTLTQKLNE------KSKEQEELLQKNqnLQEALQRAANSSEESQRElkgkIDTLTLKLNEKSKEQEELLQK 171
Cdd:PRK08475   48 KNFYKSRINKISKRLEEiqeklkESKEKKEDALKK--LEEAKEKAELIVETAKKE----AYILTQKIEKQTKDDIENLIK 121


                  ....*
gi 1039773951 172 NQNLQ 176
Cdd:PRK08475  122 SFEEL 126
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
58-190 9.58e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 9.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951  58 QLRQVSDLLKQYQANLTQQDRILEGQMlaqQKAENTSQEsKKELKGKIDTLTQKLNE---KSKEQEELLQKNQNLQEALQ 134
Cdd:PRK03918  304 EYLDELREIEKRLSRLEEEINGIEERI---KELEEKEER-LEELKKKLKELEKRLEEleeRHELYEEAKAKKEELERLKK 379

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039773951 135 RAANSS-EESQRELK---GKIDTLTLKLNEKSKEQEELLQKNQNLQEALQRAANFSGPCP 190
Cdd:PRK03918  380 RLTGLTpEKLEKELEeleKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCP 439
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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