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Conserved domains on  [gi|569003254|ref|XP_006525703|]
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collectin-12 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 543-668 5.01e-61

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: 199.84  E-value: 5.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 543 CPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTVGRESHWIGLTDSEQESEWKWLDGSPV- 621
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 569003254 622 -DYKNWKAGQPDNWGsghGPGEDCAGLIY-AGQWNDFQCDEINNFICEK 668
Cdd:cd03590   81 sSKTFWHPGEPNNWG---GGGEDCAELVYdSGGWNDVPCNLEYRWICEK 126
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 391-499 1.96e-11

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


:

Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.43  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  391 GSQGPPGPTGNKGqkgekgepgppgpagergtigPVGPPGERGSKGSKGSQGPKGSRGSPGKPgpqgpsgdpgppgppgk 470
Cdd:pfam01391   1 GPPGPPGPPGPPG---------------------PPGPPGPPGPPGPPGPPGEPGPPGPPGPP----------------- 42

                          90       100
                  ....*....|....*....|....*....
gi 569003254  471 dglpgpqgppgfqglqGTVGEPGVPGPRG 499
Cdd:pfam01391  43 ----------------GPPGPPGAPGAPG 55
PRK11281 super family cl46976
mechanosensitive channel MscK;
21-347 3.30e-10

mechanosensitive channel MscK;


The actual alignment was detected with superfamily member PRK11281:

Pssm-ID: 481316 [Multi-domain]  Cd Length: 1113  Bit Score: 63.39  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   21 AVESDLKKLGDQ----AGKKALSTNSE--LSTF------RSDILDLRQQLQEITEKTSKNKDTLEKLQANGD-------- 80
Cdd:PRK11281   40 DVQAQLDALNKQklleAEDKLVQQDLEqtLALLdkidrqKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDeetretls 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   81 --SLVDRQSQLKETLQNnsflITTVNKTLQAYNGYVTNLQQDTSvlqgNLQSQMYSQSVVIMNLNN-----------LNL 147
Cdd:PRK11281  120 tlSLRQLESRLAQTLDQ----LQNAQNDLAEYNSQLVSLQTQPE----RAQAALYANSQRLQQIRNllkggkvggkaLRP 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  148 TQVQQRN----------------------LISNLQQSVDDTSLAIQRIKNDFQNLQQVFLQakkdtdwlKEKVQSLQTL- 204
Cdd:PRK11281  192 SQRVLLQaeqallnaqndlqrkslegntqLQDLLQKQRDYLTARIQRLEHQLQLLQEAINS--------KRLTLSEKTVq 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  205 -AANNSALAKANNDTL----EDMNSQLSSF-TGQMDNITTISQAN-------------EQSLKD----LQ---------- 251
Cdd:PRK11281  264 eAQSQDEAARIQANPLvaqeLEINLQLSQRlLKATEKLNTLTQQNlrvknwldrltqsERNIKEqisvLKgslllsrily 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  252 ---------DLHKDTENRTA-VKFSQLE---ERFQVFETDivniisniSYTAHHLRTLTSNLND-VRTTCTDTLTRHTDD 317
Cdd:PRK11281  344 qqqqalpsaDLIEGLADRIAdLRLEQFEinqQRDALFQPD--------AYIDKLEAGHKSEVTDeVRDALLQLLDERREL 415

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 569003254  318 LTSLNNTLVNIRLDSISLRMQQ-------DMMRSKLD 347
Cdd:PRK11281  416 LDQLNKQLNNQLNLAINLQLNQqqllsvsDSLQSTLT 452
 
Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 543-668 5.01e-61

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: 199.84  E-value: 5.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 543 CPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTVGRESHWIGLTDSEQESEWKWLDGSPV- 621
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 569003254 622 -DYKNWKAGQPDNWGsghGPGEDCAGLIY-AGQWNDFQCDEINNFICEK 668
Cdd:cd03590   81 sSKTFWHPGEPNNWG---GGGEDCAELVYdSGGWNDVPCNLEYRWICEK 126
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 543-667 2.57e-37

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: 135.42  E-value: 2.57e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   543 CPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHT---VGRESHWIGLTDSEQESEWKWLDGS 619
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsGSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 569003254   620 P-VDYKNWKAGQPDNwgsghgPGEDCAGLIYA-GQWNDFQCDEINNFICE 667
Cdd:smart00034  81 GpVSYSNWAPGEPNN------SSGDCVVLSTSgGKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 561-668 7.12e-27

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 105.25  E-value: 7.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  561 KEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTVGR-ESHWIGLTDSEQESEWKWLDGSPVDYKNWKAgqpdnWGSGHG 639
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-----EPNNNG 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 569003254  640 PGEDCAGLIYA-GQWNDFQCDEINNFICEK 668
Cdd:pfam00059  76 ENEDCVELSSSsGKWNDENCNSKNPFVCEK 105
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 391-499 1.96e-11

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.43  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  391 GSQGPPGPTGNKGqkgekgepgppgpagergtigPVGPPGERGSKGSKGSQGPKGSRGSPGKPgpqgpsgdpgppgppgk 470
Cdd:pfam01391   1 GPPGPPGPPGPPG---------------------PPGPPGPPGPPGPPGPPGEPGPPGPPGPP----------------- 42

                          90       100
                  ....*....|....*....|....*....
gi 569003254  471 dglpgpqgppgfqglqGTVGEPGVPGPRG 499
Cdd:pfam01391  43 ----------------GPPGPPGAPGAPG 55
PRK11281 PRK11281
mechanosensitive channel MscK;
21-347 3.30e-10

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 63.39  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   21 AVESDLKKLGDQ----AGKKALSTNSE--LSTF------RSDILDLRQQLQEITEKTSKNKDTLEKLQANGD-------- 80
Cdd:PRK11281   40 DVQAQLDALNKQklleAEDKLVQQDLEqtLALLdkidrqKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDeetretls 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   81 --SLVDRQSQLKETLQNnsflITTVNKTLQAYNGYVTNLQQDTSvlqgNLQSQMYSQSVVIMNLNN-----------LNL 147
Cdd:PRK11281  120 tlSLRQLESRLAQTLDQ----LQNAQNDLAEYNSQLVSLQTQPE----RAQAALYANSQRLQQIRNllkggkvggkaLRP 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  148 TQVQQRN----------------------LISNLQQSVDDTSLAIQRIKNDFQNLQQVFLQakkdtdwlKEKVQSLQTL- 204
Cdd:PRK11281  192 SQRVLLQaeqallnaqndlqrkslegntqLQDLLQKQRDYLTARIQRLEHQLQLLQEAINS--------KRLTLSEKTVq 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  205 -AANNSALAKANNDTL----EDMNSQLSSF-TGQMDNITTISQAN-------------EQSLKD----LQ---------- 251
Cdd:PRK11281  264 eAQSQDEAARIQANPLvaqeLEINLQLSQRlLKATEKLNTLTQQNlrvknwldrltqsERNIKEqisvLKgslllsrily 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  252 ---------DLHKDTENRTA-VKFSQLE---ERFQVFETDivniisniSYTAHHLRTLTSNLND-VRTTCTDTLTRHTDD 317
Cdd:PRK11281  344 qqqqalpsaDLIEGLADRIAdLRLEQFEinqQRDALFQPD--------AYIDKLEAGHKSEVTDeVRDALLQLLDERREL 415

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 569003254  318 LTSLNNTLVNIRLDSISLRMQQ-------DMMRSKLD 347
Cdd:PRK11281  416 LDQLNKQLNNQLNLAINLQLNQqqllsvsDSLQSTLT 452
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 536-619 5.07e-09

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 57.05  E-value: 5.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 536 PASEVNGCPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTvGRESHWIGLTDSEQESEWKW 615
Cdd:PHA02642  81 PTIKYVTCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYK-DSSDHWIGLNRESSNHPWKW 159


                 ....
gi 569003254 616 LDGS 619
Cdd:PHA02642 160 ADNS 163
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 390-499 2.09e-07

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 53.76  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 390 RGSQGPPGPTGNKGQKGEKGEPGPPGPAGERGTIGPVGPPGERGSKGSKGSQGPKGSRGSPGKPGPQGPSGDPGPPGPP- 468
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQg 207

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 569003254 469 -------GKDGLPGPQGPPGFQGLQGTVGEPGVPGPRG 499
Cdd:NF038329 208 pagpagpDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTG 245
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 389-452 2.12e-06

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 50.67  E-value: 2.12e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569003254 389 DRGSQGPPGPTGNKGQKgekgepgppgpagergtiGPVGPPGERGSKGSKGSQGPKGSRGSPGK 452
Cdd:NF038329 234 QQGPDGDPGPTGEDGPQ------------------GPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 49-262 3.23e-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: 49.76  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  49 SDILDLRQQLQEITEKTSKNKDTLEKLQANGDSLVDRQSQLKETLQNNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNL 128
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 129 QSQ-------------MYSQSVVIMNLNNLNLTQVQQRnlISNLQQSVDDTSLAIQRIKNDFQNLQQVFLQAKKDTDWLK 195
Cdd:COG4942  100 EAQkeelaellralyrLGRQPPLALLLSPEDFLDAVRR--LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569003254 196 EKVQSLQTLAANNSALAKANNDTLEDMNSQLSSFTGQMDNITTISQANEQSLKDLQDLHKDTENRTA 262
Cdd:COG4942  178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 391-499 1.19e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 48.36  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 391 GSQGPPGPTGNKGQKgekgepgppgpagergtiGPVGPPGERGSKGSKGSQGPKGSRGSPGKPGPQGPSGDPGPPGPPGK 470
Cdd:NF038329 117 GEKGEPGPAGPAGPA------------------GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK 178

                         90       100
                 ....*....|....*....|....*....
gi 569003254 471 DGLPGPQGPPGFQGLQGTVGEPGVPGPRG 499
Cdd:NF038329 179 DGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 17-323 1.96e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.09  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   17 NKLTAVESDLKKLGDQAGKKALSTNSELSTFRSDILDLRQQLQEITEKTSKNKDTLEklqangdslvDRQSQlketLQNN 96
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS----------EKQKE----LEQN 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   97 SFLITTVNKTLQAYNGYVTNL-QQDTSVLQGNLQSQMYSQSVVIMNLNnlnltqvqqrNLISNLQQSVDDTSLAIQRIKN 175
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLnNQKEQDWNKELKSELKNQEKKLEEIQ----------NQISQNNKIISQLNEQISQLKK 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  176 DFQNLQQVFLQAKKDtdwLKEKVQSLQTLAANNSalakANNDTLEDMNSQLSSFTGQMDNITTISQANEQSLKDLQ---- 251
Cdd:TIGR04523 350 ELTNSESENSEKQRE---LEEKQNEIEKLKKENQ----SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQqeke 422

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  252 ------DLHKDTENRTAVKFSQLEERFQVFETDIVNIISNISYTAHHLRTLTSNLNDVRTTCTDT---LTRHTDDLTSLN 322
Cdd:TIGR04523 423 llekeiERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKqkeLKSKEKELKKLN 502


                  .
gi 569003254  323 N 323
Cdd:TIGR04523 503 E 503
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 391-499 3.99e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.44  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 391 GSQGPPGPTGNKGQKGEKGEPGPPGPAGERGTIGPVGPP-----GERGSKGSKGSQGPKGSRGSPGKPGPQGPSGDPGPP 465
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                         90       100       110
                 ....*....|....*....|....*....|....
gi 569003254 466 GPPGKDGLPGPQGPPGFQGLQGTVGEPGVPGPRG 499
Cdd:NF038329 272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 53-252 6.72e-04

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 42.01  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   53 DLRQQLQEITEKTSKNKDTLEKLQANGDSLVDRQSQLKETLQNNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQSQM 132
Cdd:pfam06008  23 NLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEIN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  133 YSQSVVIMNLNNLNLTQvqqrnlISNLQQSVDDTsLAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALA 212
Cdd:pfam06008 103 EKVATLGENDFALPSSD------LSRMLAEAQRM-LGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALA 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 569003254  213 KANNDTLEDMNSQLSSF-------TGQMDNITTISQANEQSLKDLQD 252
Cdd:pfam06008 176 NALRDSLAEYEAKLSDLrellreaAAKTRDANRLNLANQANLREFQR 222
 
Name Accession Description Interval E-value
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 543-668 5.01e-61

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: 199.84  E-value: 5.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 543 CPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTVGRESHWIGLTDSEQESEWKWLDGSPV- 621
Cdd:cd03590    1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSYWIGLSDEETEGEWKWVDGTPLn 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 569003254 622 -DYKNWKAGQPDNWGsghGPGEDCAGLIY-AGQWNDFQCDEINNFICEK 668
Cdd:cd03590   81 sSKTFWHPGEPNNWG---GGGEDCAELVYdSGGWNDVPCNLEYRWICEK 126
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 543-667 2.57e-37

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: 135.42  E-value: 2.57e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   543 CPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHT---VGRESHWIGLTDSEQESEWKWLDGS 619
Cdd:smart00034   1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLknsGSSDYYWIGLSDPDSNGSWQWSDGS 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 569003254   620 P-VDYKNWKAGQPDNwgsghgPGEDCAGLIYA-GQWNDFQCDEINNFICE 667
Cdd:smart00034  81 GpVSYSNWAPGEPNN------SSGDCVVLSTSgGKWNDVSCTSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 553-668 4.41e-36

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: 131.59  E-value: 4.41e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 553 KCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTV--GRESHWIGLTDSEQESEWKWLDGSP-VDYKNWKAG 629
Cdd:cd00037    1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKksSSSDVWIGLNDLSSEGTWKWSDGSPlVDYTNWAPG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 569003254 630 QPDNwgsghGPGEDCAGLIY--AGQWNDFQCDEINNFICEK 668
Cdd:cd00037   81 EPNP-----GGSEDCVVLSSssDGKWNDVSCSSKLPFICEK 116
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 543-666 9.37e-32

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: 120.16  E-value: 9.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 543 CPPHWKNFTDKCY-YFSLEKEiFEDAKLFCED-----KSSHLVFINSREEQQWI--------KKHTVGResHWIGLTDSE 608
Cdd:cd03589    1 CPTFWTAFGGYCYrFFGDRLT-WEEAELRCRSfsipgLIAHLVSIHSQEENDFVydlfessrGPDTPYG--LWIGLHDRT 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569003254 609 QESEWKWLDGSPVDYKNWKAGQPDNWGSghgpGEDCAGLIY----AGQWNDFQCDEINNFIC 666
Cdd:cd03589   78 SEGPFEWTDGSPVDFTKWAGGQPDNYGG----NEDCVQMWRrgdaGQSWNDMPCDAVFPYIC 135
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 561-668 7.12e-27

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 105.25  E-value: 7.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  561 KEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTVGR-ESHWIGLTDSEQESEWKWLDGSPVDYKNWKAgqpdnWGSGHG 639
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSnKYFWIGLTDRKNEGTWKWVDGSPVNYTNWAP-----EPNNNG 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 569003254  640 PGEDCAGLIYA-GQWNDFQCDEINNFICEK 668
Cdd:pfam00059  76 ENEDCVELSSSsGKWNDENCNSKNPFVCEK 105
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 543-668 1.47e-26

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: 104.72  E-value: 1.47e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 543 CPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHtVGRESHWIGLTDSEQESEWKWLDGSPvd 622
Cdd:cd03593    1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQ-IGSSSYWIGLSREKSEKPWKWIDGSP-- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 569003254 623 yknwkagqPDNWG--SGHGPGEDCAgLIYAGQWNDFQCDEINNFICEK 668
Cdd:cd03593   78 --------LNNLFniRGSTKSGNCA-YLSSTGIYSEDCSTKKRWICEK 116
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 543-668 1.15e-24

C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins; CLECT_CSPGs: C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core proteins (CSPGs) in human and chicken aggrecan, frog brevican, and zebra fish dermacan. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In cartilage, aggrecan forms cartilage link protein stabilized aggregates with hyaluronan (HA). These aggregates contribute to the tissue's load bearing properties. Aggregates having other CSPGs substituting for aggrecan may contribute to the structural integrity of many different tissues. Xenopus brevican is expressed in the notochord and the brain during early embryogenesis. Zebra fish dermacan is expressed in dermal bones and may play a role in dermal bone development. CSPGs do contain LINK domain(s) which bind HA. These LINK domains are considered by one classification system to be a variety of CTLD, but are omitted from this hierarchical classification based on insignificant sequence similarity.


Pssm-ID: 153058  Cd Length: 124  Bit Score: 99.57  E-value: 1.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 543 CPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHtvGRESHWIGLTDSEQESEWKWLDGSPVD 622
Cdd:cd03588    1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNN--AQDYQWIGLNDRTIEGDFRWSDGHPLQ 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 569003254 623 YKNWKAGQPDNWGSGhgpGEDCAGLIY--AGQWNDFQCDEINNFICEK 668
Cdd:cd03588   79 FENWRPNQPDNFFAT---GEDCVVMIWheEGEWNDVPCNYHLPFTCKK 123
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 552-667 1.35e-22

C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1); CLECT_collectin_like: C-type lectin-like domain (CTLD) of the type found in human collectins including lung surfactant proteins A and D, mannose- or mannan binding lectin (MBL), and CL-L1 (collectin liver 1). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. The CTLDs of these collectins bind carbohydrates on surfaces (e.g. pathogens, allergens, necrotic, or apoptotic cells) and mediate functions associated with killing and phagocytosis. MBPs recognize high mannose oligosaccharides in a calcium dependent manner, bind to a broad range of pathogens, and trigger cell killing by activating the complement pathway. MBP also acts directly as an opsonin. SP-A and SP-D in addition to functioning as host defense components, are components of pulmonary surfactant which play a role in surfactant homeostasis. Pulmonary surfactant is a phospholipid-protein complex which reduces the surface tension within the lungs. SP-A binds the major surfactant lipid: dipalmitoylphosphatidylcholine (DPPC). SP-D binds two minor components of surfactant that contain sugar moieties: glucosylceramide and phosphatidylinositol (PI). MBP and SP-A, -D monomers are homotrimers with an N-terminal collagen region and three CTLDs. Multiple homotrimeric units associate to form supramolecular complexes. MBL deficiency results in an increased susceptibility to a large number of different infections and to inflammatory disease, such as rheumatoid arthritis.


Pssm-ID: 153061 [Multi-domain]  Cd Length: 114  Bit Score: 93.13  E-value: 1.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 552 DKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREE----QQWIKKhtvGRESHWIGLTDSEQESEWKWLDGSPVDYKNWK 627
Cdd:cd03591    1 EKIFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAEnaaiASYVKK---GNTYAFIGITDLETEGQFVYLDGGPLTYTNWK 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 569003254 628 AGQPDNwgsgHGPGEDCAGLIYAGQWNDFQCDEINNFICE 667
Cdd:cd03591   78 PGEPNN----AGGGEDCVEMYTSGKWNDVACNLTRLFVCE 113
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 555-664 1.57e-22

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: 93.26  E-value: 1.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 555 YYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTVGRESHWIGLTDSEQESEWKWLDGSPVDYKNWKAGQPDNW 634
Cdd:cd03603    3 YKFVDGGMTWEAAQTLAESLGGHLVTINSAEENDWLLSNFGGYGASWIGASDAATEGTWKWSDGEESTYTNWGSGEPHNN 82

                         90       100       110
                 ....*....|....*....|....*....|....
gi 569003254 635 GSGhgpGEDCAGLIYA----GQWNDFQCDEINNF 664
Cdd:cd03603   83 GGG---NEDYAAINHFpgisGKWNDLANSYNTLG 113
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 543-667 9.29e-21

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: 88.58  E-value: 9.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 543 CPPHWKNFTDKCY-YFSLEKEiFEDAKLFCED--KSSHLVFINSREEQQ----WIKKHTVGRESHWIGLTDSEQESEWKW 615
Cdd:cd03594    1 CPKGWLPYKGNCYgYFRQPLS-WSDAELFCQKygPGAHLASIHSPAEAAaiasLISSYQKAYQPVWIGLHDPQQSRGWEW 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 569003254 616 LDGSPVDYKNWKAGQPdnwgsgHGPGEDCAGLI----YAgQWNDFQCDEINNFICE 667
Cdd:cd03594   80 SDGSKLDYRSWDRNPP------YARGGYCAELSrstgFL-KWNDANCEERNPFICK 128
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 555-668 9.94e-17

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: 76.65  E-value: 9.94e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 555 YYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWI----KKHTVGResHWIGLTDSEQEseWKWLD--GSPVDYKNWKA 628
Cdd:cd03592    3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLngfaLKYNLGY--YWIDGNDINNE--GTWVDtdKKELEYKNWAP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 569003254 629 GQPDNWGsghgpGEDCA-GLIYA-GQWNDFQCDEINNFICEK 668
Cdd:cd03592   79 GEPNNGR-----NENCLeIYIKDnGKWNDEPCSKKKSAICYT 115
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 555-666 8.89e-16

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: 73.56  E-value: 8.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 555 YYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTVGRESH-WIGLtdSEQESEWKWLDGSPVDYKNWKAGQPDN 633
Cdd:cd03602    3 FYLVNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLSRVSNSAaWIGL--YRDVDSWRWSDGSESSFRNWNTFQPFG 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 569003254 634 wgsghgpGEDCAGLIYAGQWNDFQCDEINNFIC 666
Cdd:cd03602   81 -------QGDCATMYSSGRWYAALCSALKPFIC 106
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 554-667 2.16e-13

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: 67.99  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 554 CY---YF--SLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKK--HTVGRES--HWIGLTDSEQ--------ESEWKWL 616
Cdd:cd03595   12 CYkiaYFqdSRRRLNFEEARQACREDGGELLSIESENEQKLIERfiQTLRASDgdFWIGLRRSSQynvtssacSSLYYWL 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569003254 617 DGSPVDYKNWKAGQPdNWGSghgpgEDCAGLIY-----AG-------QWNDFQCDEINNFICE 667
Cdd:cd03595   92 DGSISTFRNWYVDEP-SCGS-----EVCVVMYHqpsapAGqggpylfQWNDDNCNMKNNFICK 148
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 553-667 6.78e-13

C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF); CLECT_tetranectin_like: C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived C-type lectin (CLECSF1), and stem cell growth factor (SCGF). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TN binds to plasminogen and stimulates activation of plasminogen, playing a key role in the regulation of proteolytic processes. The TN CTLD binds two calcium ions. Its calcium free form binds to various kringle-like protein ligands. Two residues involved in the coordination of calcium are critical for the binding of TN to the fourth kringle (K4) domain of plasminogen (Plg K4). TN binds the kringle 1-4 form of angiostatin (AST K1-4). AST K1-4 is a fragment of Plg, commonly found in cancer tissues. TN inhibits the binding of Plg and AST K1-4 to the extracellular matrix (EMC) of endothelial cells and counteracts the antiproliferative effects of AST K1-4 on these cells. TN also binds the tenth kringle domain of apolipoprotein (a). In addition, TN binds fibrin and complex polysaccharides in a Ca2+ dependent manner. The binding site for complex sulfated polysaccharides is N-terminal to the CTLD. TN is homotrimeric; N-terminal to the CTLD is an alpha helical domain responsible for trimerization of monomeric units. TN may modulate angiogenesis through interactions with angiostatin and coagulation through interaction with fibrin. TN may play a role in myogenesis and in bone development. Mice having a deletion in the TN gene exhibit a kyphotic spine abnormality. TN is a useful prognostic marker of certain cancer types. CLECSF1 is expressed in cartilage tissue, which is primarily intracellular matrix (ECM), and is a candidate for organizing ECM. SCGF is strongly expressed in bone marrow and is a cytokine for primitive hematopoietic progenitor cells.


Pssm-ID: 153066  Cd Length: 129  Bit Score: 65.87  E-value: 6.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 553 KCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIK---KHTVGRESH-WIGLTDSEQESEWKWLDGSPVDYKNWK- 627
Cdd:cd03596   10 KCYLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRdyvKASVPGNWEvWLGINDMVAEGKWVDVNGSPISYFNWEr 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 569003254 628 --AGQPDNwgsghGPGEDCAGLIYA--GQWNDFQCDEINNFICE 667
Cdd:cd03596   90 eiTAQPDG-----GKRENCVALSSSaqGKWFDEDCRREKPYVCE 128
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 556-668 9.94e-13

C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm; CLECT_TC14_like: C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 from the budding tunicate Polyandrocarpa misakiensis and PfG6 from the Acorn worm. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. TC14 is homodimeric. The CTLD of TC14 binds D-galactose and D-fucose. TC14 is expressed constitutively by multipotent epithelial and mesenchymal cells and plays in role during budding, in inducing the aggregation of undifferentiated mesenchymal cells to give rise to epithelial forming tissue. TC14-2 and TC14-3 shows calcium-dependent galactose binding activity. TC14-3 is a cytostatic factor which blocks cell growth and dedifferentiation of the atrial epithelium during asexual reproduction. It may also act as a differentiation inducing factor. Galactose inhibits the cytostatic activity of TC14-3. The gene for Acorn worm PfG6 is gill-specific; PfG6 may be a secreted protein.


Pssm-ID: 153071  Cd Length: 119  Bit Score: 65.25  E-value: 9.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 556 YFSLEKEIFEDAKLFCEDKSSHLVFINSR--EEQQWIKKHT-VGRESHWIGLTDSEQ-ESEWKWLDGS--PVDYKNWKAG 629
Cdd:cd03601    4 LCSDETMNYAKAGAFCRSRGMRLASLAMRdsEMRDAILAFTlVKGHGYWVGADNLQDgEYDFLWNDGVslPTDSDLWAPN 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 569003254 630 QPDNWGSghgpGEDCAGLIYA-GQWNDFQCDEINNFICEK 668
Cdd:cd03601   84 EPSNPQS----RQLCVQLWSKyNLLDDEYCGRAKRVICEK 119
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 391-499 1.96e-11

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 59.43  E-value: 1.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  391 GSQGPPGPTGNKGqkgekgepgppgpagergtigPVGPPGERGSKGSKGSQGPKGSRGSPGKPgpqgpsgdpgppgppgk 470
Cdd:pfam01391   1 GPPGPPGPPGPPG---------------------PPGPPGPPGPPGPPGPPGEPGPPGPPGPP----------------- 42

                          90       100
                  ....*....|....*....|....*....
gi 569003254  471 dglpgpqgppgfqglqGTVGEPGVPGPRG 499
Cdd:pfam01391  43 ----------------GPPGPPGAPGAPG 55
PRK11281 PRK11281
mechanosensitive channel MscK;
21-347 3.30e-10

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 63.39  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   21 AVESDLKKLGDQ----AGKKALSTNSE--LSTF------RSDILDLRQQLQEITEKTSKNKDTLEKLQANGD-------- 80
Cdd:PRK11281   40 DVQAQLDALNKQklleAEDKLVQQDLEqtLALLdkidrqKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDeetretls 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   81 --SLVDRQSQLKETLQNnsflITTVNKTLQAYNGYVTNLQQDTSvlqgNLQSQMYSQSVVIMNLNN-----------LNL 147
Cdd:PRK11281  120 tlSLRQLESRLAQTLDQ----LQNAQNDLAEYNSQLVSLQTQPE----RAQAALYANSQRLQQIRNllkggkvggkaLRP 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  148 TQVQQRN----------------------LISNLQQSVDDTSLAIQRIKNDFQNLQQVFLQakkdtdwlKEKVQSLQTL- 204
Cdd:PRK11281  192 SQRVLLQaeqallnaqndlqrkslegntqLQDLLQKQRDYLTARIQRLEHQLQLLQEAINS--------KRLTLSEKTVq 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  205 -AANNSALAKANNDTL----EDMNSQLSSF-TGQMDNITTISQAN-------------EQSLKD----LQ---------- 251
Cdd:PRK11281  264 eAQSQDEAARIQANPLvaqeLEINLQLSQRlLKATEKLNTLTQQNlrvknwldrltqsERNIKEqisvLKgslllsrily 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  252 ---------DLHKDTENRTA-VKFSQLE---ERFQVFETDivniisniSYTAHHLRTLTSNLND-VRTTCTDTLTRHTDD 317
Cdd:PRK11281  344 qqqqalpsaDLIEGLADRIAdLRLEQFEinqQRDALFQPD--------AYIDKLEAGHKSEVTDeVRDALLQLLDERREL 415

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 569003254  318 LTSLNNTLVNIRLDSISLRMQQ-------DMMRSKLD 347
Cdd:PRK11281  416 LDQLNKQLNNQLNLAINLQLNQqqllsvsDSLQSTLT 452
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 390-451 3.50e-10

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 55.96  E-value: 3.50e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569003254  390 RGSQGPPGPTGNKGQKgekgepgppgpagergtiGPVGPPGERGSKGSKGSQGPKGSRGSPG 451
Cdd:pfam01391   9 PGPPGPPGPPGPPGPP------------------GPPGPPGEPGPPGPPGPPGPPGPPGAPG 52
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 553-666 1.81e-09

C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH); CLECT_EMBP_like: C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major basic protein (EMBP) and prepro major basic protein homolog (MBPH). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Eosinophils and basophils carry out various functions in allergic, parasitic, and inflammatory diseases. EMBP is stored in eosinophil crystalloid granules and is released upon degranulation. EMBP is also expressed in basophils. The proform of EMBP is expressed in placental X cells and breast tissue and increases significantly during human pregnancy. EMBP has cytotoxic properties and damages bacteria and mammalian cells, in vitro, as well as, helminth parasites. EMBP deposition has been observed in the inflamed tissue of allergy patients in a variety of diseases including asthma, atopic dermatitis, and rhinitis. In addition to its cytotoxic functions, EMBP activates cells and stimulates cytokine production. EMBP has been shown to bind the proteoglycan heparin. The binding site is similar to the carbohydrate binding site of other classical CTLD, such as mannose-binding protein (MBP1), however, heparin binding to EMBP is calcium ion independent. MBPH has reduced potency in cytotoxic and cytostimulatory assays compared with EMBP.


Pssm-ID: 153068  Cd Length: 117  Bit Score: 55.92  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 553 KCYYFSLEKEIFEDAKLFCED-KSSHLVFINS----REEQQWIKKHTVGREshWIG--LTDSEQESEWKWLDGSPVDYKN 625
Cdd:cd03598    2 RCYRFVKSPRTFRDAQVICRRcYRGNLASIHSfafnYRVQRLVSTLNQAQV--WIGgiITGKGRCRRFSWVDGSVWNYAY 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 569003254 626 WKAGQPDNwGSGHgpgedCAGL-IYAGQWNDFQCDEINNFIC 666
Cdd:cd03598   80 WAPGQPGN-RRGH-----CVELcTRGGHWRRAHCKLRRPFIC 115
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 536-619 5.07e-09

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 57.05  E-value: 5.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 536 PASEVNGCPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTvGRESHWIGLTDSEQESEWKW 615
Cdd:PHA02642  81 PTIKYVTCPKGWIGFGYKCFYFSEDSKNWTFGNTFCTSLGATLVKVETEEELNFLKRYK-DSSDHWIGLNRESSNHPWKW 159


                 ....
gi 569003254 616 LDGS 619
Cdd:PHA02642 160 ADNS 163
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 390-499 2.09e-07

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 53.76  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 390 RGSQGPPGPTGNKGQKGEKGEPGPPGPAGERGTIGPVGPPGERGSKGSKGSQGPKGSRGSPGKPGPQGPSGDPGPPGPP- 468
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQg 207

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 569003254 469 -------GKDGLPGPQGPPGFQGLQGTVGEPGVPGPRG 499
Cdd:NF038329 208 pagpagpDGEAGPAGEDGPAGPAGDGQQGPDGDPGPTG 245
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 389-452 2.12e-06

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 50.67  E-value: 2.12e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569003254 389 DRGSQGPPGPTGNKGQKgekgepgppgpagergtiGPVGPPGERGSKGSKGSQGPKGSRGSPGK 452
Cdd:NF038329 234 QQGPDGDPGPTGEDGPQ------------------GPDGPAGKDGPRGDRGEAGPDGPDGKDGE 279
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 49-262 3.23e-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: 49.76  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  49 SDILDLRQQLQEITEKTSKNKDTLEKLQANGDSLVDRQSQLKETLQNNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNL 128
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 129 QSQ-------------MYSQSVVIMNLNNLNLTQVQQRnlISNLQQSVDDTSLAIQRIKNDFQNLQQVFLQAKKDTDWLK 195
Cdd:COG4942  100 EAQkeelaellralyrLGRQPPLALLLSPEDFLDAVRR--LQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569003254 196 EKVQSLQTLAANNSALAKANNDTLEDMNSQLSSFTGQMDNITTISQANEQSLKDLQDLHKDTENRTA 262
Cdd:COG4942  178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 552-667 5.48e-06

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: 46.66  E-value: 5.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 552 DKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWI--------KKHTVGRESHWIGL--------TDSEQESEWKW 615
Cdd:cd03600    4 DACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVslllaagpGRHGRGSLRLWIGLqreprqcsDPSLPLRGFSW 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 616 LDG-SPVDYKNWKAGQPdnwgsGHGPGEDCAGLIYAGQ------WNDFQCD-EINNFICE 667
Cdd:cd03600   84 VTGdQDTDFSNWLQEPA-----GTCTSPRCVALSAAGStpdnlkWKDGPCSaRADGYLCK 138
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 391-499 1.19e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 48.36  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 391 GSQGPPGPTGNKGQKgekgepgppgpagergtiGPVGPPGERGSKGSKGSQGPKGSRGSPGKPGPQGPSGDPGPPGPPGK 470
Cdd:NF038329 117 GEKGEPGPAGPAGPA------------------GEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGK 178

                         90       100
                 ....*....|....*....|....*....
gi 569003254 471 DGLPGPQGPPGFQGLQGTVGEPGVPGPRG 499
Cdd:NF038329 179 DGEAGAKGPAGEKGPQGPRGETGPAGEQG 207
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 17-323 1.96e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.09  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   17 NKLTAVESDLKKLGDQAGKKALSTNSELSTFRSDILDLRQQLQEITEKTSKNKDTLEklqangdslvDRQSQlketLQNN 96
Cdd:TIGR04523 214 KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS----------EKQKE----LEQN 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   97 SFLITTVNKTLQAYNGYVTNL-QQDTSVLQGNLQSQMYSQSVVIMNLNnlnltqvqqrNLISNLQQSVDDTSLAIQRIKN 175
Cdd:TIGR04523 280 NKKIKELEKQLNQLKSEISDLnNQKEQDWNKELKSELKNQEKKLEEIQ----------NQISQNNKIISQLNEQISQLKK 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  176 DFQNLQQVFLQAKKDtdwLKEKVQSLQTLAANNSalakANNDTLEDMNSQLSSFTGQMDNITTISQANEQSLKDLQ---- 251
Cdd:TIGR04523 350 ELTNSESENSEKQRE---LEEKQNEIEKLKKENQ----SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQqeke 422

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  252 ------DLHKDTENRTAVKFSQLEERFQVFETDIVNIISNISYTAHHLRTLTSNLNDVRTTCTDT---LTRHTDDLTSLN 322
Cdd:TIGR04523 423 llekeiERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKqkeLKSKEKELKKLN 502


                  .
gi 569003254  323 N 323
Cdd:TIGR04523 503 E 503
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
13-290 1.99e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  13 QTYDNKLTAVESDLKKLG---DQAGKKALSTNSELSTFRSDILDLRQQLQEITEKTSKNKDTLEKLQANGDSLVDRQSQL 89
Cdd:COG4372   55 EQAREELEQLEEELEQARselEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  90 KETLQNNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQ--SQMYSQSVVIMNLNNLNLTQVQQRNLISNLQQSVDD-T 166
Cdd:COG4372  135 EAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLpR 214

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 167 SLAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLEDMNSQLSSFTGQM-DNITTISQANEQ 245
Cdd:COG4372  215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAaLELEALEEAALE 294

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 569003254 246 SLKDLQDLHKDTENRTAVKFSQLEERFQVFETDIVNIISNISYTA 290
Cdd:COG4372  295 LKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAEL 339
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 391-499 3.99e-05

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.44  E-value: 3.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 391 GSQGPPGPTGNKGQKGEKGEPGPPGPAGERGTIGPVGPP-----GERGSKGSKGSQGPKGSRGSPGKPGPQGPSGDPGPP 465
Cdd:NF038329 192 GPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAgdgqqGPDGDPGPTGEDGPQGPDGPAGKDGPRGDRGEAGPD 271

                         90       100       110
                 ....*....|....*....|....*....|....
gi 569003254 466 GPPGKDGLPGPQGPPGFQGLQGTVGEPGVPGPRG 499
Cdd:NF038329 272 GPDGKDGERGPVGPAGKDGQNGKDGLPGKDGKDG 305
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 9-304 6.22e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 46.17  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254    9 ETSHQTYDNKLTAVESDLKKLGDQAGKKalstNSELSTFRSDILDLRQQLQEItEKTSKNKDT-LEKLQANGDSLVDRQS 87
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSY----KQEIKNLESQINDLESKIQNQ-EKLNQQKDEqIKKLQQEKELLEKEIE 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   88 QLKETLQNNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQSQMYSqsvviMNLNNLNLTQVQQrnlisNLQQSVDDts 167
Cdd:TIGR04523 430 RLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS-----INKIKQNLEQKQK-----ELKSKEKE-- 497

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  168 laIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLEDMNSQLSSftgqmDNITTISQANEQSL 247
Cdd:TIGR04523 498 --LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK-----ENLEKEIDEKNKEI 570

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 569003254  248 KDLqdlhKDTENRTAVKFSQLEERFQVFETDIVNIISNISYTAHHLRTLTSNLNDVR 304
Cdd:TIGR04523 571 EEL----KQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 15-287 9.65e-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: 45.82  E-value: 9.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254    15 YDNKLTAVESDLKKLGDQA--GKKALST--------NSELSTFRSDILDLRQQLQEITEKTSKNKDTLEKLQANGDSLVD 84
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIaeLEKALAElrkeleelEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254    85 RQSQLKETLQNNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQSQMYSQSVVIMNLNNLNLTQVQQRNLISNLQQSVD 164
Cdd:TIGR02168  755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   165 DTSLAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLEDMNSQLSSFTGQMDNITTISQANE 244
Cdd:TIGR02168  835 ATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 569003254   245 QSLKDLQDlhkdtenrtavKFSQLEERFQVFETDIVNIISNIS 287
Cdd:TIGR02168  915 RELEELRE-----------KLAQLELRLEGLEVRIDNLQERLS 946
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 22-271 2.24e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  22 VESDLKKLGDQAGK--KALSTNSELSTFRSDIL-----DLRQQLQEITEKTSKNKDTLEKLQANGDSLVDRQSQLKETLQ 94
Cdd:COG1196  198 LERQLEPLERQAEKaeRYRELKEELKELEAELLllklrELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  95 NNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQSQmysqsvvIMNLNNLNLTQVQQRNLISNLQQSVDDTSLAIQRIK 174
Cdd:COG1196  278 ELELELEEAQAEEYELLAELARLEQDIARLEERRREL-------EERLEELEEELAELEEELEELEEELEELEEELEEAE 350

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 175 NDFQNLQQVFLQAKkdtdwlKEKVQSLQTLAANNSALAKANNDTLEDMNSQLSsftgQMDNITTISQANEQSLKDLQDLH 254
Cdd:COG1196  351 EELEEAEAELAEAE------EALLEAEAELAEAEEELEELAEELLEALRAAAE----LAAQLEELEEAEEALLERLERLE 420

                        250
                 ....*....|....*..
gi 569003254 255 KDTENRTAVKFSQLEER 271
Cdd:COG1196  421 EELEELEEALAELEEEE 437
PHA02867 PHA02867
C-type lectin protein; Provisional
 543-602 2.74e-04

C-type lectin protein; Provisional


Pssm-ID: 165201  Cd Length: 167  Bit Score: 41.98  E-value: 2.74e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 543 CPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHtvGRESHWI 602
Cdd:PHA02867  49 CPDEWIGYNSKCYYFTINETNWNDSKKLCDVMDSSLIRFDNIETLNFVSRY--GKGSYWI 106
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
39-283 2.96e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  39 STNSELSTFRSDILDLRQQLQEITEKTSKNKDTLEKLQANGDSLVDRQSQLKETLQNNSFLITTVNKTLQAYNGYVTNLQ 118
Cdd:COG4372   35 KALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQ 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 119 QDTSVLQGNLQSQMYSQSVVIMNLNNLNLTQVQQRNLISNLQQSVDDTSLAIQRIKNDFQNLQQVFLQAKKDTdwlkekv 198
Cdd:COG4372  115 EELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDE------- 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 199 qslQTLAANNSALAKANNDTLEDMNSQLSSFTGQMDNITTISQANEQSLKDLQDLHKDTENRTAVKFSQLEERFQVFETD 278
Cdd:COG4372  188 ---LLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264


                 ....*
gi 569003254 279 IVNII 283
Cdd:COG4372  265 LAILV 269
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 530-666 3.55e-04

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 41.77  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 530 LQNEPTPAS-EVNGCPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTvGRESHWIGLTDSE 608
Cdd:PHA03097  32 LSCKLSPGDrSGLNCRSGWVGYNNKCYTFSENITNKHLAIERCADMDGILTLIDDQKEVLFVSRYK-GGQDLWIGIEKKK 110

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 569003254 609 QESEWKWLDGSPVdyknwkagqpdnwgsgHGPG-EDCAgLIYAGQWNDFQCDEINNFIC 666
Cdd:PHA03097 111 GDDDDREVLDKVV----------------KPPKsGKCA-YLKDKTIISSNCNATKGWIC 152
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 24-232 4.65e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.89  E-value: 4.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  24 SDLKKLGDQAGKKALSTNSELSTFRSDILDLRQQLQEITEKTSKNKDTLEKLQANgdsLVDRQSQLKETLQnnsflittv 103
Cdd:COG3883   26 SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAE---IEERREELGERAR--------- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 104 nktlQAY-NGYVTNLqqdTSVLqgnLQSQMYSQsvVIMNLNNLNLTQVQQRNLISNLQQsvddtslAIQRIKNDFQNLQQ 182
Cdd:COG3883   94 ----ALYrSGGSVSY---LDVL---LGSESFSD--FLDRLSALSKIADADADLLEELKA-------DKAELEAKKAELEA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 569003254 183 VFLQAKKDTDWLKEKVQSLQTLAANNSALAKANNDTLEDMNSQLSSFTGQ 232
Cdd:COG3883  155 KLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 543-635 6.10e-04

C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP); CLECT_attractin_like: C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and attractin-like protein (ALP). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. Mouse AtrN (the product of the mahogany gene) has been shown to bind Agouti protein and to function in agouti-induced pigmentation and obesity. Mutations in AtrN have also been shown to cause spongiform encephalopathy and hypomyelination in rats and hamsters. The cytoplasmic region of mouse ALP has been shown to binds to melanocortin receptor (MCR4). Signaling through MCR4 plays a role in appetite suppression. Attractin may have therapeutic potential in the treatment of obesity. Human attractin (hAtrN) has been shown to be expressed on activated T cells and released extracellularly. The circulating serum attractin induces the spreading of monocytes that become the focus of the clustering of non-proliferating T cells.


Pssm-ID: 153067  Cd Length: 129  Bit Score: 40.26  E-value: 6.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 543 CPPHWKNFTDKCYYFSLEKEIFEDAKLFCEDKSSHLVFINSREEQQWIKKHTVGRE------SHWIGLTDSEQeSEWKWL 616
Cdd:cd03597    1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQmtkqklTPWVGLRKINV-SYWCWE 79

                         90       100
                 ....*....|....*....|...
gi 569003254 617 DGSPvdYKN----WKAGQPDNWG 635
Cdd:cd03597   80 DMSP--FTNttlqWLPGEPSDAG 100
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 53-252 6.72e-04

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 42.01  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   53 DLRQQLQEITEKTSKNKDTLEKLQANGDSLVDRQSQLKETLQNNSFLITTVNKTLQAYNGYVTNLQQDTSVLQGNLQSQM 132
Cdd:pfam06008  23 NLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEIN 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  133 YSQSVVIMNLNNLNLTQvqqrnlISNLQQSVDDTsLAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALA 212
Cdd:pfam06008 103 EKVATLGENDFALPSSD------LSRMLAEAQRM-LGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALA 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 569003254  213 KANNDTLEDMNSQLSSF-------TGQMDNITTISQANEQSLKDLQD 252
Cdd:pfam06008 176 NALRDSLAEYEAKLSDLrellreaAAKTRDANRLNLANQANLREFQR 222
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
31-242 8.63e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.70  E-value: 8.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  31 DQAGKKALSTNSELSTFR--SDILDLRQQLQEITEKTSKNKDTLEKLQANGDSLVDRQSQLKETLQNNSFLITTVNKtlq 108
Cdd:COG3206  185 PELRKELEEAEAALEEFRqkNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--- 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254 109 ayNGYVTNLQQDTSVLQGNLQ--SQMYS-QSVVIMNLNNlnltqvQQRNLISNLQQSVDDtslAIQRIKNDFQNLQQ--V 183
Cdd:COG3206  262 --SPVIQQLRAQLAELEAELAelSARYTpNHPDVIALRA------QIAALRAQLQQEAQR---ILASLEAELEALQAreA 330

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569003254 184 FLQAKKDTdwLKEKVQSLQTLAANNSAL---AKANNDTLEDMNSQL----SSFTGQMDNITTISQA 242
Cdd:COG3206  331 SLQAQLAQ--LEARLAELPELEAELRRLereVEVARELYESLLQRLeearLAEALTVGNVRVIDPA 394
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 1-349 1.21e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 42.34  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254     1 MDNVTDGMETSHQTYDNKLTAVESDLKKL---GDQAGKKALSTNSELSTFRSDILDLRQQLQEITEKTSKNKDTLEKlqa 77
Cdd:TIGR00606  693 LQEFISDLQSKLRLAPDKLKSTESELKKKekrRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEE--- 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254    78 ngdslvdrqsqlketlqnNSFLITTVNKTLQAyngyVTNLQQDTSVLQgNLQSQM------YSQSVVIMNLNNLNLTQVQ 151
Cdd:TIGR00606  770 ------------------QETLLGTIMPEEES----AKVCLTDVTIME-RFQMELkdverkIAQQAAKLQGSDLDRTVQQ 826

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   152 QRNLISNLQQSVDDTSLAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAkannDTLEDMNSQLSSFtg 231
Cdd:TIGR00606  827 VNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFE----EQLVELSTEVQSL-- 900

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254   232 qmdnITTISQANEQSLKDLQDLHKD-TENRTAVkfSQLEERFQVFETDIVNIISNISYTAHHLRTLtsnLNDVRTTCTDT 310
Cdd:TIGR00606  901 ----IREIKDAKEQDSPLETFLEKDqQEKEELI--SSKETSNKKAQDKVNDIKEKVKNIHGYMKDI---ENKIQDGKDDY 971

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 569003254   311 LTRHTDDLTSLNNTLVniRLDSISLRMQQDM--MRSKLDTE 349
Cdd:TIGR00606  972 LKQKETELNTVNAQLE--ECEKHQEKINEDMrlMRQDIDTQ 1010
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 17-216 1.66e-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: 41.29  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  17 NKLTAVESDLKKLGDQAGK--KAL-STNSELSTFRSDILDLRQQLQEITEKTSKNKDTLEKLQAngdSLVDRQSQLKETL 93
Cdd:COG4942   34 QEIAELEKELAALKKEEKAllKQLaALERRIAALARRIRALEQELAALEAELAELEKEIAELRA---ELEAQKEELAELL 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569003254  94 Q------NNSFL--------ITTVNKTLQAYNGYVTNLQQDTSVLQGNLQSQMYSQSVVIMNLNNLNLTQVQQRNLISNL 159
Cdd:COG4942  111 RalyrlgRQPPLalllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 569003254 160 QQSVDDTSLAIQRIKNDFQNLQQVFLQAKKDTDWLKEKVQSLQTLAANNSALAKANN 216
Cdd:COG4942  191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
PRK15239 PRK15239
putative fimbrial protein StaA; Provisional
 222-295 1.77e-03

putative fimbrial protein StaA; Provisional


Pssm-ID: 185152  Cd Length: 197  Bit Score: 40.10  E-value: 1.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569003254 222 MNSQLSSFTGQMDNITTISQANEQSLKDLQDLHKDTENRTAVKFSQLEERFQVFETDIVNIISNISYTAHHLRT 295
Cdd:PRK15239 101 MSSSFSNTKGTLDNDETLTRSGIEAAKAVDIAVHHVDDANALSLVKINDPSNTMEESFTNGIATYNFKASYVKS 174
 
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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