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Conserved domains on  [gi|1916443857|emb|VDI76635|]
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Hypothetical predicted protein [Mytilus galloprovincialis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 109-321 2.16e-39

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.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 147.36  E-value: 2.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 109 GNFPKGEKGSRGERGPIGHKGINGDRGQqgiKGETGHKGSTGSKGQLGDVGPIGGKGQNGTKGSKGEKGMSGEKGLRGEg 188
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGE---TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 189 sqgaKGSAGDKGIIGDKGQSGQKGEVGEKGALGAKGYNGNKGMDGtmgmPGEMGKTGLVGPTGRKGSIGERGPTGDKGPK 268
Cdd:NF038329  191 ----KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1916443857 269 GEIGLAGLKGGNGEKGIRGDKGLSG---NKGPVGDKGRIGARGQNGEKGNPGESGR 321
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGkdgQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 335-452 9.77e-39

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: 136.21  E-value: 9.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 335 SCYYFqFKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIIiDKNPGHVWIGAHDSVQESRFIWESDNAVLTYTDWN 414
Cdd:cd00037     1 SCYKF-STEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLK-KSSSSDVWIGLNDLSSEGTWKWSDGSPLVDYTNWA 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1916443857 415 PGEPNNAGQEDCAHMSSGAKYRWNDVQCSHKFSFICEK 452
Cdd:cd00037    79 PGEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 109-321 2.16e-39

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: 147.36  E-value: 2.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 109 GNFPKGEKGSRGERGPIGHKGINGDRGQqgiKGETGHKGSTGSKGQLGDVGPIGGKGQNGTKGSKGEKGMSGEKGLRGEg 188
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGE---TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 189 sqgaKGSAGDKGIIGDKGQSGQKGEVGEKGALGAKGYNGNKGMDGtmgmPGEMGKTGLVGPTGRKGSIGERGPTGDKGPK 268
Cdd:NF038329  191 ----KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1916443857 269 GEIGLAGLKGGNGEKGIRGDKGLSG---NKGPVGDKGRIGARGQNGEKGNPGESGR 321
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGkdgQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 335-452 9.77e-39

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: 136.21  E-value: 9.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 335 SCYYFqFKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIIiDKNPGHVWIGAHDSVQESRFIWESDNAVLTYTDWN 414
Cdd:cd00037     1 SCYKF-STEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLK-KSSSSDVWIGLNDLSSEGTWKWSDGSPLVDYTNWA 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1916443857 415 PGEPNNAGQEDCAHMSSGAKYRWNDVQCSHKFSFICEK 452
Cdd:cd00037    79 PGEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 325-451 1.65e-35

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: 127.72  E-value: 1.65e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857  325 CGSGWVQFMRSCYYFqFKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIIIDKNPGHVWIGAHDSVQESRFIWESD 404
Cdd:smart00034   1 CPSGWISYGGKCYKF-STEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWIGLSDPDSNGSWQWSDG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1916443857  405 NAVLTYTDWNPGEPNNAGqEDCAHMSSGaKYRWNDVQCSHKFSFICE 451
Cdd:smart00034  80 SGPVSYSNWAPGEPNNSS-GDCVVLSTS-GGKWNDVSCTSKLPFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 344-452 4.95e-23

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 93.31  E-value: 4.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 344 KMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIiidKNPG-HVWIGAHDSVQESRFIWEsDNAVLTYTDWNPGEPNNAG 422
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTL---KKSNkYFWIGLTDRKNEGTWKWV-DGSPVNYTNWAPEPNNNGE 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1916443857 423 QEDCAHMSSGAkYRWNDVQCSHKFSFICEK 452
Cdd:pfam00059  77 NEDCVELSSSS-GKWNDENCNSKNPFVCEK 105
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 239-293 2.40e-08

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: 50.18  E-value: 2.40e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1916443857 239 GEMGKTGLVGPTGRKGSIGERGPTGDKGPKGEIGLAGLKGGNGEKGIRGDKGLSG 293
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 321-406 6.10e-07

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 50.11  E-value: 6.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 321 RIITCGSGWVQFMRSCYYFQFKSKmTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFiiidKNPGHVWIGAHDSVQESRFI 400
Cdd:PHA02642   84 KYVTCPKGWIGFGYKCFYFSEDSK-NWTFGNTFCTSLGATLVKVETEEELNFLKRY----KDSSDHWIGLNRESSNHPWK 158


                  ....*.
gi 1916443857 401 WeSDNA 406
Cdd:PHA02642  159 W-ADNS 163
PHA03169 PHA03169
hypothetical protein; Provisional
 162-320 4.84e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.81  E-value: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 162 GGKGQNGTKGSKGEKGMSGEKGLRGEGSQGAKGSAGDKGIIGDKGQSGQKGEVGEKGALGAKGYNGNKGMDGTMGMPGEM 241
Cdd:PHA03169   70 ESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 242 GKTGLVGPTGRKGSIGERGPTGDKGP---KGEIGLAGLKGGNGEKGIRGDKGLSGNKGPVGDKGRIGARGQNGEKGNPGE 318
Cdd:PHA03169  150 APPESHNPSPNQQPSSFLQPSHEDSPeepEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQ 229


                  ..
gi 1916443857 319 SG 320
Cdd:PHA03169  230 AV 231
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 45-320 1.49e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 44.22  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857   45 RDKAFLALTIMLLICFSLAVIVI----VVYLEEY------IEKSSELEKQI-QQLNtsglKRQSHLSNQLGSSDHGNFPK 113
Cdd:TIGR00927  562 RDVSFYILDLMMLILFFLDSLIAwwesLLLLLAYalyvftMKWNKQIELWVkEQLS----RRPVAKVMALGDLSKGDVAE 637

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857  114 GE-----KGSRGERgPIGHKGINGDR--GQQGIKGETGHKGSTGSKGQLgdvgPIGGKGQNGTKGSKGEKGmSGEKGLRG 186
Cdd:TIGR00927  638 AEhtgerTGEEGER-PTEAEGENGEEsgGEAEQEGETETKGENESEGEI----PAERKGEQEGEGEIEAKE-ADHKGETE 711

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857  187 EGSQGAKGSAGDKGIIGD-KGQSGQKGEVGE---KGALGAKGYNGNKGMDGTMGMPGEMGKTGLVGPTGRKGSIGERGP- 261
Cdd:TIGR00927  712 AEEVEHEGETEAEGTEDEgEIETGEEGEEVEdegEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEm 791

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1916443857  262 TGDKGPKGEIGLAGLKGGNGEKGIRGDKGLSGNKGPVGDK-------GRIGARGQNGEKGNPGESG 320
Cdd:TIGR00927  792 KGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDEtgeqelnAENQGEAKQDEKGVDGGGG 857
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 109-321 2.16e-39

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: 147.36  E-value: 2.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 109 GNFPKGEKGSRGERGPIGHKGINGDRGQqgiKGETGHKGSTGSKGQLGDVGPIGGKGQNGTKGSKGEKGMSGEKGLRGEg 188
Cdd:NF038329  115 GDGEKGEPGPAGPAGPAGEQGPRGDRGE---TGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGE- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 189 sqgaKGSAGDKGIIGDKGQSGQKGEVGEKGALGAKGYNGNKGMDGtmgmPGEMGKTGLVGPTGRKGSIGERGPTGDKGPK 268
Cdd:NF038329  191 ----KGPQGPRGETGPAGEQGPAGPAGPDGEAGPAGEDGPAGPAG----DGQQGPDGDPGPTGEDGPQGPDGPAGKDGPR 262

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1916443857 269 GEIGLAGLKGGNGEKGIRGDKGLSG---NKGPVGDKGRIGARGQNGEKGNPGESGR 321
Cdd:NF038329  263 GDRGEAGPDGPDGKDGERGPVGPAGkdgQNGKDGLPGKDGKDGQNGKDGLPGKDGK 318
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 335-452 9.77e-39

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: 136.21  E-value: 9.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 335 SCYYFqFKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIIiDKNPGHVWIGAHDSVQESRFIWESDNAVLTYTDWN 414
Cdd:cd00037     1 SCYKF-STEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLK-KSSSSDVWIGLNDLSSEGTWKWSDGSPLVDYTNWA 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1916443857 415 PGEPNNAGQEDCAHMSSGAKYRWNDVQCSHKFSFICEK 452
Cdd:cd00037    79 PGEPNPGGSEDCVVLSSSSDGKWNDVSCSSKLPFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 325-451 1.65e-35

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: 127.72  E-value: 1.65e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857  325 CGSGWVQFMRSCYYFqFKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIIIDKNPGHVWIGAHDSVQESRFIWESD 404
Cdd:smart00034   1 CPSGWISYGGKCYKF-STEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYYWIGLSDPDSNGSWQWSDG 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1916443857  405 NAVLTYTDWNPGEPNNAGqEDCAHMSSGaKYRWNDVQCSHKFSFICE 451
Cdd:smart00034  80 SGPVSYSNWAPGEPNNSS-GDCVVLSTS-GGKWNDVSCTSKLPFVCE 124
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 325-452 2.92e-30

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: 113.55  E-value: 2.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 325 CGSGWVQFMRSCYYFQfKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIiidKNPGHVWIGAHDSVQESRFIWeSD 404
Cdd:cd03590     1 CPTNWKSFQSSCYFFS-TEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKIL---SGNRSYWIGLSDEETEGEWKW-VD 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1916443857 405 NAVL--TYTDWNPGEPNNAGQ--EDCAHMSSgAKYRWNDVQCSHKFSFICEK 452
Cdd:cd03590    76 GTPLnsSKTFWHPGEPNNWGGggEDCAELVY-DSGGWNDVPCNLEYRWICEK 126
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 325-450 2.20e-26

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: 103.59  E-value: 2.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 325 CGSGWVQFMRSCYYFqFKSKMTWNAAKTDCH-----RKGGFLVKIDNTVESWFLKSF---IIIDKNPGHVWIGAHDSVQE 396
Cdd:cd03589     1 CPTFWTAFGGYCYRF-FGDRLTWEEAELRCRsfsipGLIAHLVSIHSQEENDFVYDLfesSRGPDTPYGLWIGLHDRTSE 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1916443857 397 SRFIWeSDNAVLTYTDWNPGEPNNAGQ-EDCAHMSSGAK--YRWNDVQCSHKFSFIC 450
Cdd:cd03589    80 GPFEW-TDGSPVDFTKWAGGQPDNYGGnEDCVQMWRRGDagQSWNDMPCDAVFPYIC 135
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 344-452 4.95e-23

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 93.31  E-value: 4.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 344 KMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIiidKNPG-HVWIGAHDSVQESRFIWEsDNAVLTYTDWNPGEPNNAG 422
Cdd:pfam00059   1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTL---KKSNkYFWIGLTDRKNEGTWKWV-DGSPVNYTNWAPEPNNNGE 76

                          90       100       110
                  ....*....|....*....|....*....|
gi 1916443857 423 QEDCAHMSSGAkYRWNDVQCSHKFSFICEK 452
Cdd:pfam00059  77 NEDCVELSSSS-GKWNDENCNSKNPFVCEK 105
CLECT_collectin_like cd03591
C-type lectin-like domain (CTLD) of the type found in human collectins including lung ...
 337-451 1.33e-21

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: 89.66  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 337 YYFQFKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIiiDKNPGHVWIGAHDSVQESRFIWeSDNAVLTYTDWNPG 416
Cdd:cd03591     3 IFVTNGEEKNFDDAQKLCSEAGGTLAMPRNAAENAAIASYV--KKGNTYAFIGITDLETEGQFVY-LDGGPLTYTNWKPG 79

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1916443857 417 EPNNAG-QEDCAHM-SSGakyRWNDVQCSHKFSFICE 451
Cdd:cd03591    80 EPNNAGgGEDCVEMyTSG---KWNDVACNLTRLFVCE 113
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 338-452 1.67e-20

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: 86.66  E-value: 1.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 338 YFQFKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIIiDKNPGHVWIGAHDSVQESRfiWE-SDNAVLTYTDWNPG 416
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFAL-KYNLGYYWIDGNDINNEGT--WVdTDKKELEYKNWAPG 79

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1916443857 417 EPNNAGQEDCAHMSSGAKYRWNDVQCSHKFSFICEK 452
Cdd:cd03592    80 EPNNGRNENCLEIYIKDNGKWNDEPCSKKKSAICYT 115
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 325-451 1.08e-18

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: 82.03  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 325 CGSGWVQFMRSCYYFqFKSKMTWNAAKTDC--HRKGGFLVKIDNTVESWFLKSFII-IDKNPGHVWIGAHDSVQESRFIW 401
Cdd:cd03594     1 CPKGWLPYKGNCYGY-FRQPLSWSDAELFCqkYGPGAHLASIHSPAEAAAIASLISsYQKAYQPVWIGLHDPQQSRGWEW 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1916443857 402 eSDNAVLTYTDWNPGEPNNAGqEDCAHMSSGAKY-RWNDVQCSHKFSFICE 451
Cdd:cd03594    80 -SDGSKLDYRSWDRNPPYARG-GYCAELSRSTGFlKWNDANCEERNPFICK 128
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 325-452 7.13e-17

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: 76.46  E-value: 7.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 325 CGSGWVQFMRSCYYFqFKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSfiiidKNPGHVWIGAHDSVQESRFIWeSD 404
Cdd:cd03588     1 CEEGWDKFQGHCYRH-FPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNN-----NAQDYQWIGLNDRTIEGDFRW-SD 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1916443857 405 NAVLTYTDWNPGEPNN--AGQEDCAHMSSGAKYRWNDVQCSHKFSFICEK 452
Cdd:cd03588    74 GHPLQFENWRPNQPDNffATGEDCVVMIWHEEGEWNDVPCNYHLPFTCKK 123
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 325-452 3.80e-15

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: 71.59  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 325 CGSGWVQFMRSCYYFqFKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIIIDKnpghVWIGAHDSVQESRFIWEsD 404
Cdd:cd03593     1 CPKDWICYGNKCYYF-SMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSSS----YWIGLSREKSEKPWKWI-D 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1916443857 405 NAvlTYTDWNpGEPNNAGQEDCAHMSSGAKYrwnDVQCSHKFSFICEK 452
Cdd:cd03593    75 GS--PLNNLF-NIRGSTKSGNCAYLSSTGIY---SEDCSTKKRWICEK 116
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 337-450 4.65e-14

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: 68.17  E-value: 4.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 337 YYFqFKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIiiDKNPGHVWIGAHDSVQEsrFIWeSDNAVLTYTDWNPG 416
Cdd:cd03602     3 FYL-VNESKTWSEAQQYCRENYTDLATVQNQEDNALLSNLS--RVSNSAAWIGLYRDVDS--WRW-SDGSESSFRNWNTF 76

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1916443857 417 EPnnAGQEDCAHM-SSGakyRWNDVQCSHKFSFIC 450
Cdd:cd03602    77 QP--FGQGDCATMySSG---RWYAALCSALKPFIC 106
CLECT_VCBS cd03603
A bacterial subgroup of the C-type lectin-like (CTLD) domain; a subgroup of bacterial protein ...
 337-444 6.15e-14

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: 68.22  E-value: 6.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 337 YYFQFKSKMTWNAAKTDCHRKGGFLVKIDNTVE-SWFLKSFiiidKNPGHVWIGAHDSVQESRFIWeSDNAVLTYTDWNP 415
Cdd:cd03603     2 FYKFVDGGMTWEAAQTLAESLGGHLVTINSAEEnDWLLSNF----GGYGASWIGASDAATEGTWKW-SDGEESTYTNWGS 76

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1916443857 416 GEP--NNAGQEDCAHMSS--GAKYRWNDVQCSH 444
Cdd:cd03603    77 GEPhnNGGGNEDYAAINHfpGISGKWNDLANSY 109
CLECT_EMBP_like cd03598
C-type lectin-like domain (CTLD) of the type found in the human proteins, eosinophil major ...
 335-450 1.91e-10

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: 58.23  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 335 SCYYFqFKSKMTWNAAKTDCHR-KGGFLVKIDNT-----VESWFLKSfiiidkNPGHVWIGA--HDSVQESRFIWeSDNA 406
Cdd:cd03598     2 RCYRF-VKSPRTFRDAQVICRRcYRGNLASIHSFafnyrVQRLVSTL------NQAQVWIGGiiTGKGRCRRFSW-VDGS 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1916443857 407 VLTYTDWNPGEPNNAGqEDCAHMSSGAKYrWNDVQCSHKFSFIC 450
Cdd:cd03598    74 VWNYAYWAPGQPGNRR-GHCVELCTRGGH-WRRAHCKLRRPFIC 115
CLECT_chondrolectin_like cd03595
C-type lectin-like domain (CTLD) of the type found in the human type-1A transmembrane proteins ...
 332-451 5.79e-10

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: 57.59  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 332 FMRSCY---YFQ-FKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFI-IIDKNPGHVWIGAHDSVQ--------ESR 398
Cdd:cd03595     8 TEKPCYkiaYFQdSRRRLNFEEARQACREDGGELLSIESENEQKLIERFIqTLRASDGDFWIGLRRSSQynvtssacSSL 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1916443857 399 FIWeSDNAVLTYTDWNPGEPNnAGQEDCAHM------SSGAK----YRWNDVQCSHKFSFICE 451
Cdd:cd03595    88 YYW-LDGSISTFRNWYVDEPS-CGSEVCVVMyhqpsaPAGQGgpylFQWNDDNCNMKNNFICK 148
CLECT_tetranectin_like cd03596
C-type lectin-like domain (CTLD) of the type found in the tetranectin (TN), cartilage derived ...
 338-451 3.47e-09

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: 54.70  E-value: 3.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 338 YFQFKSKMTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFIIIDKNPG-HVWIGAHDSVQESRFIWESDNAVlTYTDWN-- 414
Cdd:cd03596    12 YLVSEETKHYHEASEDCIARGGTLATPRDSDENDALRDYVKASVPGNwEVWLGINDMVAEGKWVDVNGSPI-SYFNWEre 90

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1916443857 415 -PGEPNNAGQEDCAHMSSGAKYRWNDVQCSHKFSFICE 451
Cdd:cd03596    91 iTAQPDGGKRENCVALSSSAQGKWFDEDCRREKPYVCE 128
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 239-293 2.40e-08

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: 50.18  E-value: 2.40e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1916443857 239 GEMGKTGLVGPTGRKGSIGERGPTGDKGPKGEIGLAGLKGGNGEKGIRGDKGLSG 293
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 251-307 4.91e-08

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: 49.41  E-value: 4.91e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1916443857 251 GRKGSIGERGPTGDKGPKGEIGLAGLKGGNGEKGIRGDKGLSGNKGPVGDKGRIGAR 307
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 263-318 5.69e-08

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: 49.03  E-value: 5.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1916443857 263 GDKGPKGEIGLAGLKGGNGEKGIRGDKGLSGNKGPVGDKGRIGARGQNGEKGNPGE 318
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 236-290 8.84e-08

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: 48.64  E-value: 8.84e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1916443857 236 GMPGEMGKTGLVGPTGRKGSIGERGPTGDKGPKGEIGLAGLKGGNGEKGIRGDKG 290
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 233-287 2.60e-07

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: 47.10  E-value: 2.60e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1916443857 233 GTMGMPGEMGKTGLVGPTGRKGSIGERGPTGDKGPKGEIGLAGLKGGNGEKGIRG 287
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 266-320 3.26e-07

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: 47.10  E-value: 3.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1916443857 266 GPKGEIGLAGLKGGNGEKGIRGDKGLSGNKGPVGDKGRIGARGQNGEKGNPGESG 320
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 245-299 3.29e-07

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: 47.10  E-value: 3.29e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1916443857 245 GLVGPTGRKGSIGERGPTGDKGPKGEIGLAGLKGGNGEKGIRGDKGLSGNKGPVG 299
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 221-275 3.66e-07

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: 46.72  E-value: 3.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1916443857 221 GAKGYNGNKGMDGTMGMPGEMGKTGLVGPTGRKGSIGERGPTGDKGPKGEIGLAG 275
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA02642 PHA02642
C-type lectin-like protein; Provisional
 321-406 6.10e-07

C-type lectin-like protein; Provisional


Pssm-ID: 165024 [Multi-domain]  Cd Length: 216  Bit Score: 50.11  E-value: 6.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 321 RIITCGSGWVQFMRSCYYFQFKSKmTWNAAKTDCHRKGGFLVKIDNTVESWFLKSFiiidKNPGHVWIGAHDSVQESRFI 400
Cdd:PHA02642   84 KYVTCPKGWIGFGYKCFYFSEDSK-NWTFGNTFCTSLGATLVKVETEEELNFLKRY----KDSSDHWIGLNRESSNHPWK 158


                  ....*.
gi 1916443857 401 WeSDNA 406
Cdd:PHA02642  159 W-ADNS 163
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 112-162 8.10e-07

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: 45.95  E-value: 8.10e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1916443857 112 PKGEKGSRGERGPIGHKGINGDRGQQGIKGETGHKGSTGSKGQLGDVGPIG 162
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
CLECT_TC14_like cd03601
C-type lectin-like domain (CTLD) of the type found in lectins TC14, TC14-2, TC14-3, and TC14-4 ...
 387-452 2.01e-06

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: 46.76  E-value: 2.01e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 387 WIGAHDSVQ-ESRFIWESDNAVLT-YTDWNPGEPNN-AGQEDCAHMSSgaKY-RWNDVQCSHKFSFICEK 452
Cdd:cd03601    52 WVGADNLQDgEYDFLWNDGVSLPTdSDLWAPNEPSNpQSRQLCVQLWS--KYnLLDDEYCGRAKRVICEK 119
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 230-284 2.10e-06

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: 44.79  E-value: 2.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1916443857 230 GMDGTMGMPGEMGKTGLVGPTGRKGSIGERGPTGDKGPKGEIGLAGLKGGNGEKG 284
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
PHA03169 PHA03169
hypothetical protein; Provisional
 162-320 4.84e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.81  E-value: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 162 GGKGQNGTKGSKGEKGMSGEKGLRGEGSQGAKGSAGDKGIIGDKGQSGQKGEVGEKGALGAKGYNGNKGMDGTMGMPGEM 241
Cdd:PHA03169   70 ESDTETAEESRHGEKEERGQGGPSGSGSESVGSPTPSPSGSAEELASGLSPENTSGSSPESPASHSPPPSPPSHPGPHEP 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 242 GKTGLVGPTGRKGSIGERGPTGDKGP---KGEIGLAGLKGGNGEKGIRGDKGLSGNKGPVGDKGRIGARGQNGEKGNPGE 318
Cdd:PHA03169  150 APPESHNPSPNQQPSSFLQPSHEDSPeepEPPTSEPEPDSPGPPQSETPTSSPPPQSPPDEPGEPQSPTPQQAPSPNTQQ 229


                  ..
gi 1916443857 319 SG 320
Cdd:PHA03169  230 AV 231
PHA03169 PHA03169
hypothetical protein; Provisional
 136-319 7.99e-06

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 48.04  E-value: 7.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 136 QQGIKGETGHKGSTGSKGQLGDVGPiGGKGQNGTKGSKGEKGMSGEKGlrgeGSQGAKGSAGDKGIIGDKGQSGQKGEVG 215
Cdd:PHA03169   68 QTESDTETAEESRHGEKEERGQGGP-SGSGSESVGSPTPSPSGSAEEL----ASGLSPENTSGSSPESPASHSPPPSPPS 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 216 EKGalgakgyngnkgmDGTMGMPGEMGKTGLVGPTGRKGSIGERGPTGDKGPKGEIGLAGLKGGNGEKGIRGDKGLSGNK 295
Cdd:PHA03169  143 HPG-------------PHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPD 209

                         170       180
                  ....*....|....*....|....
gi 1916443857 296 GPVGDKGRIGARGQNGEKGNPGES 319
Cdd:PHA03169  210 EPGEPQSPTPQQAPSPNTQQAVEH 233
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 120-175 1.36e-05

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: 42.48  E-value: 1.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1916443857 120 GERGPIGHKGINGDRGQQGIKGETGHKGSTGSKGQLGDVGPIGGKGQNGTKGSKGE 175
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 212-267 1.62e-05

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: 42.10  E-value: 1.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1916443857 212 GEVGEKGALGAKGYNGNKGMDGTMGMPGEMGKTGLVGPTGRKGSIGERGPTGDKGP 267
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 272-322 1.95e-05

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: 42.10  E-value: 1.95e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1916443857 272 GLAGLKGGNGEKGIRGDKGLSGNKGPVGDKGRIGARGQNGEKGNPGESGRI 322
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAP 51
PHA03169 PHA03169
hypothetical protein; Provisional
 106-270 5.55e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 45.35  E-value: 5.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 106 SDHGNFPKGEKGSRGERGPIGHKGINGDRGQQGiKGETGHKGSTGSKGQLGDVGPIGGKGQNGTKGskGEKGMSGEKGLR 185
Cdd:PHA03169   62 AEQGHRQTESDTETAEESRHGEKEERGQGGPSG-SGSESVGSPTPSPSGSAEELASGLSPENTSGS--SPESPASHSPPP 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 186 GEGSQGAKGSAGDKGIIGDKGQSGQKGEVGEKGALGAKGYNGNKGMDGTMGMPGEMGKTGLVGPTGRKGS---------I 256
Cdd:PHA03169  139 SPPSHPGPHEPAPPESHNPSPNQQPSSFLQPSHEDSPEEPEPPTSEPEPDSPGPPQSETPTSSPPPQSPPdepgepqspT 218

                         170
                  ....*....|....
gi 1916443857 257 GERGPTGDKGPKGE 270
Cdd:PHA03169  219 PQQAPSPNTQQAVE 232
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 188-240 6.53e-05

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: 40.55  E-value: 6.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1916443857 188 GSQGAKGSAGDKGIIGDKGQSGQKGEVGEKGALGAKGYNGNKGMDGTMGMPGE 240
Cdd:pfam01391   4 GPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 45-320 1.49e-04

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 44.22  E-value: 1.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857   45 RDKAFLALTIMLLICFSLAVIVI----VVYLEEY------IEKSSELEKQI-QQLNtsglKRQSHLSNQLGSSDHGNFPK 113
Cdd:TIGR00927  562 RDVSFYILDLMMLILFFLDSLIAwwesLLLLLAYalyvftMKWNKQIELWVkEQLS----RRPVAKVMALGDLSKGDVAE 637

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857  114 GE-----KGSRGERgPIGHKGINGDR--GQQGIKGETGHKGSTGSKGQLgdvgPIGGKGQNGTKGSKGEKGmSGEKGLRG 186
Cdd:TIGR00927  638 AEhtgerTGEEGER-PTEAEGENGEEsgGEAEQEGETETKGENESEGEI----PAERKGEQEGEGEIEAKE-ADHKGETE 711

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857  187 EGSQGAKGSAGDKGIIGD-KGQSGQKGEVGE---KGALGAKGYNGNKGMDGTMGMPGEMGKTGLVGPTGRKGSIGERGP- 261
Cdd:TIGR00927  712 AEEVEHEGETEAEGTEDEgEIETGEEGEEVEdegEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGEIQAGEDGEm 791

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1916443857  262 TGDKGPKGEIGLAGLKGGNGEKGIRGDKGLSGNKGPVGDK-------GRIGARGQNGEKGNPGESG 320
Cdd:TIGR00927  792 KGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDEtgeqelnAENQGEAKQDEKGVDGGGG 857
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 112-154 6.99e-04

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: 37.47  E-value: 6.99e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1916443857 112 PKGEKGSRGERGPIGHKGINGDRGQQGIKGETGHKGSTGSKGQ 154
Cdd:pfam01391  14 PPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGP 56
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 113-282 2.20e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 40.75  E-value: 2.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857  113 KGEKGSRGERGPIGHKGINGDRGQQGiKGETGHKGSTGSKGQLGDvGPIGGKGQNGTKGSKGEKGMSGEKGLRGEGSQga 192
Cdd:TIGR00927  703 EADHKGETEAEEVEHEGETEAEGTED-EGEIETGEEGEEVEDEGE-GEAEGKHEVETEGDRKETEHEGETEAEGKEDE-- 778

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857  193 kgsagDKGIIGDKGQSGQKGEVGEKGALGAKGYNGNKGMDGTMGMPGEMGK-TGLVGPTGRKGSIGERGPTGDKGPKGEI 271
Cdd:TIGR00927  779 -----DEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADdTEVKDETGEQELNAENQGEAKQDEKGVD 853

                          170
                   ....*....|.
gi 1916443857  272 GLAGLKGGNGE 282
Cdd:TIGR00927  854 GGGGSDGGDSE 864
PHA03097 PHA03097
C-type lectin-like protein; Provisional
 315-450 3.00e-03

C-type lectin-like protein; Provisional


Pssm-ID: 222982 [Multi-domain]  Cd Length: 157  Bit Score: 38.31  E-value: 3.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857 315 NPGESGRIITCGSGWVQFMRSCYYFQFKSKMTWNAAKTdCHRKGGFLVKIDNTVESWFLKSFiiidKNPGHVWIGAhdsv 394
Cdd:PHA03097   36 LSPGDRSGLNCRSGWVGYNNKCYTFSENITNKHLAIER-CADMDGILTLIDDQKEVLFVSRY----KGGQDLWIGI---- 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1916443857 395 qESRFIWESDNAVLTYTDWNPgepnnaGQEDCAHMSSGAKYRWNdvqCSHKFSFIC 450
Cdd:PHA03097  107 -EKKKGDDDDREVLDKVVKPP------KSGKCAYLKDKTIISSN---CNATKGWIC 152
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 76-233 4.65e-03

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 39.59  E-value: 4.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857   76 EKSSELEKQIQQLNTSGLKRQSHLSNQLGSSDHGNFPKGEKGSRGERGPIGHKGINGDRGQ-----QGIKGETGHKGSTG 150
Cdd:TIGR00927  692 EQEGEGEIEAKEADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKhevetEGDRKETEHEGETE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1916443857  151 SKGQLG-DVGPIGGKGQNGTKGSKGEKGMSGEKGLRGEGSQGAKGS-----AGDKGIIGDKGQSGQKGEVGEKGALGAKG 224
Cdd:TIGR00927  772 AEGKEDeDEGEIQAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGqsetqADDTEVKDETGEQELNAENQGEAKQDEKG 851


                   ....*....
gi 1916443857  225 YNGNKGMDG 233
Cdd:TIGR00927  852 VDGGGGSDG 860
 
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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