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Conserved domains on  [gi|1491416264|ref|XP_026652844|]
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attractin [Zonotrichia albicollis]

Protein Classification

attractin( domain architecture ID 12869866)

attractin is involved in the initial immune cell clustering during inflammatory response and may regulate chemotactic activity of chemokines

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CLECT super family cl02432
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 697-825 2.91e-73

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.


The actual alignment was detected with superfamily member cd03597:

Pssm-ID: 470576  Cd Length: 129  Bit Score: 239.41  E-value: 2.91e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  697 CGTNWHLVGNSCLRITNAKENYDHAKLSCRSNGALLASLTTQKKVEFVLKELQKIQSSPKTLTPWVGLRKINVSYWCWED 776
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1491416264  777 MSPFTNTLVQWLPSEPSDAGFCGYLAEPSQQGLKAATCINEVNGSVCER 825
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
244-543 1.23e-26

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 111.02  E-value: 1.23e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  244 TLPKL--ARASHKAVIHDNKMWIVGGYVFNhSDSQKVLAYDLISEEWLPLNSSvnSVEMRYGHSLALHKDNIYMYGG--K 319
Cdd:COG3055      5 SLPDLptPRSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATNTWSELAPL--PGPPRHHAAAVAQDGKLYVFGGftG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  320 LDATGNVSSQLWVFHIPRQSWAVLAPRAkeqyavVGHSAHVVTLRDNStvmLVLFGHCPLYGYISNVQEYNLLTNTWSIL 399
Cdd:COG3055     82 ANPSSTPLNDVYVYDPATNTWTKLAPMP------TPRGGATALLLDGK---IYVVGGWDDGGNVAWVEVYDPATGTWTQL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  400 qtsGALVQGGYGHSSVYDPNTRsIYIHGGYKAFSANKYrladdlykyevdsrmWTILKDSRFFRYLHTAVIVSGTMLVFG 479
Cdd:COG3055    153 ---APLPTPRDHLAAAVLPDGK-ILVIGGRNGSGFSNT---------------WTTLAPLPTARAGHAAAVLGGKILVFG 213

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491416264  480 GNTHndtsmshgakcFSSDFMAYDIACDRWSVLPRLAlhhdVNRFGHSAVLYNSTMYVFGGFNS 543
Cdd:COG3055    214 GESG-----------FSDEVEAYDPATNTWTALGELP----TPRHGHAAVLTDGKVYVIGGETK 262
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 48-156 4.35e-19

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


:

Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 84.00  E-value: 4.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264   48 TEPSGYVT--DGPGNYKYKTKCTWLIEGRPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSGlivpekds 121
Cdd:cd00041      7 ASTSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFCG-------- 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1491416264  122 NETVPEVVATSGYALLHFFSDAAYNLTGFNITYNF 156
Cdd:cd00041     79 STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 967-1012 2.58e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 48.50  E-value: 2.58e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1491416264  967 ACQCNGHS----RCVNES-VCEkCENLTTGRHCETCISGYYGDPTNGGTCQ 1012
Cdd:cd00055      1 PCDCNGHGslsgQCDPGTgQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 837-888 2.20e-04

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


:

Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 40.38  E-value: 2.20e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1491416264  837 PCALRAACAECT-SGSSECMWCSNMQQCVDSNAYvaSFPYGQCMEWYTMSS-CP 888
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASSkCP 52
 
Name Accession Description Interval E-value
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 697-825 2.91e-73

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: 239.41  E-value: 2.91e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  697 CGTNWHLVGNSCLRITNAKENYDHAKLSCRSNGALLASLTTQKKVEFVLKELQKIQSSPKTLTPWVGLRKINVSYWCWED 776
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1491416264  777 MSPFTNTLVQWLPSEPSDAGFCGYLAEPSQQGLKAATCINEVNGSVCER 825
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
244-543 1.23e-26

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 111.02  E-value: 1.23e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  244 TLPKL--ARASHKAVIHDNKMWIVGGYVFNhSDSQKVLAYDLISEEWLPLNSSvnSVEMRYGHSLALHKDNIYMYGG--K 319
Cdd:COG3055      5 SLPDLptPRSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATNTWSELAPL--PGPPRHHAAAVAQDGKLYVFGGftG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  320 LDATGNVSSQLWVFHIPRQSWAVLAPRAkeqyavVGHSAHVVTLRDNStvmLVLFGHCPLYGYISNVQEYNLLTNTWSIL 399
Cdd:COG3055     82 ANPSSTPLNDVYVYDPATNTWTKLAPMP------TPRGGATALLLDGK---IYVVGGWDDGGNVAWVEVYDPATGTWTQL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  400 qtsGALVQGGYGHSSVYDPNTRsIYIHGGYKAFSANKYrladdlykyevdsrmWTILKDSRFFRYLHTAVIVSGTMLVFG 479
Cdd:COG3055    153 ---APLPTPRDHLAAAVLPDGK-ILVIGGRNGSGFSNT---------------WTTLAPLPTARAGHAAAVLGGKILVFG 213

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491416264  480 GNTHndtsmshgakcFSSDFMAYDIACDRWSVLPRLAlhhdVNRFGHSAVLYNSTMYVFGGFNS 543
Cdd:COG3055    214 GESG-----------FSDEVEAYDPATNTWTALGELP----TPRHGHAAVLTDGKVYVIGGETK 262
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 48-156 4.35e-19

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 84.00  E-value: 4.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264   48 TEPSGYVT--DGPGNYKYKTKCTWLIEGRPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSGlivpekds 121
Cdd:cd00041      7 ASTSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFCG-------- 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1491416264  122 NETVPEVVATSGYALLHFFSDAAYNLTGFNITYNF 156
Cdd:cd00041     79 STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 715-825 5.19e-16

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 74.82  E-value: 5.19e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  715 KENYDHAKLSCRSNGALLASLTTQKKVEFVLKELQKIQSSPktltpWVGL-RKINVSYWCWEDMSPFTNTLVQWLPSEPS 793
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYF-----WIGLtDRKNEGTWKWVDGSPVNYTNWAPEPNNNG 75

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1491416264  794 DAGFCGYLaEPSQQGLKAATCiNEVNGSVCER 825
Cdd:pfam00059   76 ENEDCVEL-SSSSGKWNDENC-NSKNPFVCEK 105
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 58-154 1.41e-15

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 73.58  E-value: 1.41e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264    58 PGNYKYKTKCTWLIEGRPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSGLIVPEkdsnetvPEVVATSG 133
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPP-------PVISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 1491416264   134 YALLHFFSDAAYNLTGFNITY 154
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
46-154 1.73e-14

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 70.79  E-value: 1.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264   46 RLTEPSGYVT--DGPGNYKYKTKCTWLIEGRPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSGLIVPek 119
Cdd:pfam00431    4 VLTDSSGSISspNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGSGIP-- 81

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1491416264  120 dsnetvPEVVATSGYALLHFFSDAAYNLTGFNITY 154
Cdd:pfam00431   82 ------EDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 697-824 8.68e-14

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: 69.17  E-value: 8.68e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264   697 CGTNWHLVGNSCLRITNAKENYDHAKLSCRSNGALLASLTTQKKVEFVlkeLQKIQSSPKTLTPWVGLRKINVSYWC-WE 775
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFV---ASLLKNSGSSDYYWIGLSDPDSNGSWqWS 77

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 1491416264   776 DMSPFTNTLVqWLPSEPSDA-GFCGYLaEPSQQGLKAATCiNEVNGSVCE 824
Cdd:smart00034   78 DGSGPVSYSN-WAPGEPNNSsGDCVVL-STSGGKWNDVSC-TSKLPFVCE 124
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 967-1012 2.58e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 48.50  E-value: 2.58e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1491416264  967 ACQCNGHS----RCVNES-VCEkCENLTTGRHCETCISGYYGDPTNGGTCQ 1012
Cdd:cd00055      1 PCDCNGHGslsgQCDPGTgQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PHA03098 PHA03098
kelch-like protein; Provisional
 255-518 8.69e-06

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 50.15  E-value: 8.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  255 AVIHDNKMWIVGGYVFNHSDSQKVLAYDLISEEWLPLNssvNSVEMRYGHSLALHKDNIYMYGGkLDATGNVSSQLWVFH 334
Cdd:PHA03098   290 SVVLNNVIYFIGGMNKNNLSVNSVVSYDTKTKSWNKVP---ELIYPRKNPGVTVFNNRIYVIGG-IYNSISLNTVESWKP 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  335 iPRQSWAVLAPRAKEQYavvghSAHVVTLRDnstVMLVLFGHCPLYGYISNVQEYNLLTNTWSILQtsgALVQGGYGHSS 414
Cdd:PHA03098   366 -GESKWREEPPLIFPRY-----NPCVVNVNN---LIYVIGGISKNDELLKTVECFSLNTNKWSKGS---PLPISHYGGCA 433

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  415 VYDPNTrsIYIHGGYKafSANKYRLADDLYKYEVDSRMWTILKDSRFFRYLHTAVIVSGTMLVFGGNTHNDtsmshgakc 494
Cdd:PHA03098   434 IYHDGK--IYVIGGIS--YIDNIKVYNIVESYNPVTNKWTELSSLNFPRINASLCIFNNKIYVVGGDKYEY--------- 500

                          250       260
                   ....*....|....*....|....
gi 1491416264  495 FSSDFMAYDIACDRWSVLPRLALH 518
Cdd:PHA03098   501 YINEIEVYDDKTNTWTLFCKFPKV 524
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 301-336 3.08e-05

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 42.17  E-value: 3.08e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1491416264  301 RYGHSLALHKDNIYMYGGKLDATGNVSSQLWVFHIP 336
Cdd:pfam13854    4 RYGHCAVTVGDYIYLYGGYTGGEGQPSDDVYVLSLP 39
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 837-888 2.20e-04

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 40.38  E-value: 2.20e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1491416264  837 PCALRAACAECT-SGSSECMWCSNMQQCVDSNAYvaSFPYGQCMEWYTMSS-CP 888
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASSkCP 52
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 968-1011 7.40e-04

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 38.49  E-value: 7.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1491416264  968 CQCNGH----SRCVNES-VCEkCENLTTGRHCETCISGYYGDP-TNGGTC 1011
Cdd:pfam00053    1 CDCNPHgslsDTCDPETgQCL-CKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
968-1008 1.06e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.06  E-value: 1.06e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1491416264   968 CQCNG----HSRCVNES-VCEkCENLTTGRHCETCISGYYGDPTNG 1008
Cdd:smart00180    1 CDCDPggsaSGTCDPDTgQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
 
Name Accession Description Interval E-value
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 697-825 2.91e-73

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: 239.41  E-value: 2.91e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  697 CGTNWHLVGNSCLRITNAKENYDHAKLSCRSNGALLASLTTQKKVEFVLKELQKIQSSPKTLTPWVGLRKINVSYWCWED 776
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQMTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1491416264  777 MSPFTNTLVQWLPSEPSDAGFCGYLAEPSQQGLKAATCINEVNGSVCER 825
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
244-543 1.23e-26

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 111.02  E-value: 1.23e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  244 TLPKL--ARASHKAVIHDNKMWIVGGYVFNhSDSQKVLAYDLISEEWLPLNSSvnSVEMRYGHSLALHKDNIYMYGG--K 319
Cdd:COG3055      5 SLPDLptPRSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATNTWSELAPL--PGPPRHHAAAVAQDGKLYVFGGftG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  320 LDATGNVSSQLWVFHIPRQSWAVLAPRAkeqyavVGHSAHVVTLRDNStvmLVLFGHCPLYGYISNVQEYNLLTNTWSIL 399
Cdd:COG3055     82 ANPSSTPLNDVYVYDPATNTWTKLAPMP------TPRGGATALLLDGK---IYVVGGWDDGGNVAWVEVYDPATGTWTQL 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  400 qtsGALVQGGYGHSSVYDPNTRsIYIHGGYKAFSANKYrladdlykyevdsrmWTILKDSRFFRYLHTAVIVSGTMLVFG 479
Cdd:COG3055    153 ---APLPTPRDHLAAAVLPDGK-ILVIGGRNGSGFSNT---------------WTTLAPLPTARAGHAAAVLGGKILVFG 213

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1491416264  480 GNTHndtsmshgakcFSSDFMAYDIACDRWSVLPRLAlhhdVNRFGHSAVLYNSTMYVFGGFNS 543
Cdd:COG3055    214 GESG-----------FSDEVEAYDPATNTWTALGELP----TPRHGHAAVLTDGKVYVIGGETK 262
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 48-156 4.35e-19

CUB domain; extracellular domain; present in proteins mostly known to be involved in development; not found in prokaryotes, plants and yeast.


Pssm-ID: 238001 [Multi-domain]  Cd Length: 113  Bit Score: 84.00  E-value: 4.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264   48 TEPSGYVT--DGPGNYKYKTKCTWLIEGRPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSGlivpekds 121
Cdd:cd00041      7 ASTSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFCG-------- 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1491416264  122 NETVPEVVATSGYALLHFFSDAAYNLTGFNITYNF 156
Cdd:cd00041     79 STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
301-554 4.58e-16

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 80.20  E-value: 4.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  301 RYGHSLALHKDNIYMYGGKldATGNVSSQLWVFHIPRQSWAVLAPrakeqyAVVGHSAHVVTLRDNSTVMLV--LFGHCP 378
Cdd:COG3055     13 RSEAAAALLDGKVYVAGGL--SGGSASNSFEVYDPATNTWSELAP------LPGPPRHHAAAVAQDGKLYVFggFTGANP 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  379 LYGYISNVQEYNLLTNTWSilqTSGALVQGGYGHSSVYDPNTrsIYIHGGYKAFSANKyrladDLYKYEVDSRMWTILKD 458
Cdd:COG3055     85 SSTPLNDVYVYDPATNTWT---KLAPMPTPRGGATALLLDGK--IYVVGGWDDGGNVA-----WVEVYDPATGTWTQLAP 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  459 SRFFRYLHTAVIV-SGTMLVFGGNThndtsmshgakcfssdfmaYDIACDRWSVLPrlalHHDVNRFGHSAVLYNSTMYV 537
Cdd:COG3055    155 LPTPRDHLAAAVLpDGKILVIGGRN-------------------GSGFSNTWTTLA----PLPTARAGHAAAVLGGKILV 211

                          250
                   ....*....|....*..
gi 1491416264  538 FGGFNSlLLSDILKFTP 554
Cdd:COG3055    212 FGGESG-FSDEVEAYDP 227
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 715-825 5.19e-16

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 74.82  E-value: 5.19e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  715 KENYDHAKLSCRSNGALLASLTTQKKVEFVLKELQKIQSSPktltpWVGL-RKINVSYWCWEDMSPFTNTLVQWLPSEPS 793
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNKYF-----WIGLtDRKNEGTWKWVDGSPVNYTNWAPEPNNNG 75

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1491416264  794 DAGFCGYLaEPSQQGLKAATCiNEVNGSVCER 825
Cdd:pfam00059   76 ENEDCVEL-SSSSGKWNDENC-NSKNPFVCEK 105
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 58-154 1.41e-15

Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found mostly among developmentally-regulated proteins. Spermadhesins contain only this domain.


Pssm-ID: 214483 [Multi-domain]  Cd Length: 102  Bit Score: 73.58  E-value: 1.41e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264    58 PGNYKYKTKCTWLIEGRPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSGLIVPEkdsnetvPEVVATSG 133
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPP-------PVISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 1491416264   134 YALLHFFSDAAYNLTGFNITY 154
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
46-154 1.73e-14

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 70.79  E-value: 1.73e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264   46 RLTEPSGYVT--DGPGNYKYKTKCTWLIEGRPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSGLIVPek 119
Cdd:pfam00431    4 VLTDSSGSISspNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGSGIP-- 81

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1491416264  120 dsnetvPEVVATSGYALLHFFSDAAYNLTGFNITY 154
Cdd:pfam00431   82 ------EDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 697-824 8.68e-14

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: 69.17  E-value: 8.68e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264   697 CGTNWHLVGNSCLRITNAKENYDHAKLSCRSNGALLASLTTQKKVEFVlkeLQKIQSSPKTLTPWVGLRKINVSYWC-WE 775
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFV---ASLLKNSGSSDYYWIGLSDPDSNGSWqWS 77

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|
gi 1491416264   776 DMSPFTNTLVqWLPSEPSDA-GFCGYLaEPSQQGLKAATCiNEVNGSVCE 824
Cdd:smart00034   78 DGSGPVSYSN-WAPGEPNNSsGDCVVL-STSGGKWNDVSC-TSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 707-825 7.46e-13

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: 66.49  E-value: 7.46e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  707 SCLRITNAKENYDHAKLSCRSNGALLASLTTQKKVEFVLKELQKIQSSPktltPWVGLRKINV-SYWCWEDMSPFTNTLv 785
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSD----VWIGLNDLSSeGTWKWSDGSPLVDYT- 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1491416264  786 QWLPSEPSDAG--FCGYLAEPSQQGLKAATCiNEVNGSVCER 825
Cdd:cd00037     76 NWAPGEPNPGGseDCVVLSSSSDGKWNDVSC-SSKLPFICEK 116
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 697-825 2.48e-11

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: 62.32  E-value: 2.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  697 CGTNWHLVGNSCLRITNAKENYDHAKLSCRSNGALLASLTTQKKVEFVLKELQKIQSSpktltpWVGLRKINV-SYWCWE 775
Cdd:cd03590      1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSY------WIGLSDEETeGEWKWV 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1491416264  776 DMSPFTNTLVQWLPSEPSDAGF----CGYLaEPSQQGLKAATCiNEVNGSVCER 825
Cdd:cd03590     75 DGTPLNSSKTFWHPGEPNNWGGggedCAEL-VYDSGGWNDVPC-NLEYRWICEK 126
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 697-825 5.84e-09

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: 55.42  E-value: 5.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  697 CGTNWHLVGNSCLRITNAKENYDHAKLSCRSNGALLASLTTQKKVEFvlkelqkIQSSPKTLTPWVGLRKINVSY-WCWE 775
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEF-------LQSQIGSSSYWIGLSREKSEKpWKWI 73

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1491416264  776 DMSPFTNTLvqwLPSEPSDAGFCGYLaepSQQGLKAATCiNEVNGSVCER 825
Cdd:cd03593     74 DGSPLNNLF---NIRGSTKSGNCAYL---SSTGIYSEDC-STKKRWICEK 116
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
453-555 2.51e-08

N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 56.70  E-value: 2.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  453 WTILKDSRFFRYLHTAVIVSGTMLVFGGNTHNDTsmshgakcfSSDFMAYDIACDRWSVLPRLALHHdvnRFGHSAVLYN 532
Cdd:COG3055      3 WSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSA---------SNSFEVYDPATNTWSELAPLPGPP---RHHAAAVAQD 70

                           90       100
                   ....*....|....*....|....*...
gi 1491416264  533 STMYVFGGFN-----SLLLSDILKFTPE 555
Cdd:COG3055     71 GKLYVFGGFTganpsSTPLNDVYVYDPA 98
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 967-1012 2.58e-07

Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies


Pssm-ID: 238012  Cd Length: 50  Bit Score: 48.50  E-value: 2.58e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1491416264  967 ACQCNGHS----RCVNES-VCEkCENLTTGRHCETCISGYYGDPTNGGTCQ 1012
Cdd:cd00055      1 PCDCNGHGslsgQCDPGTgQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PHA03098 PHA03098
kelch-like protein; Provisional
 255-518 8.69e-06

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 50.15  E-value: 8.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  255 AVIHDNKMWIVGGYVFNHSDSQKVLAYDLISEEWLPLNssvNSVEMRYGHSLALHKDNIYMYGGkLDATGNVSSQLWVFH 334
Cdd:PHA03098   290 SVVLNNVIYFIGGMNKNNLSVNSVVSYDTKTKSWNKVP---ELIYPRKNPGVTVFNNRIYVIGG-IYNSISLNTVESWKP 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  335 iPRQSWAVLAPRAKEQYavvghSAHVVTLRDnstVMLVLFGHCPLYGYISNVQEYNLLTNTWSILQtsgALVQGGYGHSS 414
Cdd:PHA03098   366 -GESKWREEPPLIFPRY-----NPCVVNVNN---LIYVIGGISKNDELLKTVECFSLNTNKWSKGS---PLPISHYGGCA 433

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  415 VYDPNTrsIYIHGGYKafSANKYRLADDLYKYEVDSRMWTILKDSRFFRYLHTAVIVSGTMLVFGGNTHNDtsmshgakc 494
Cdd:PHA03098   434 IYHDGK--IYVIGGIS--YIDNIKVYNIVESYNPVTNKWTELSSLNFPRINASLCIFNNKIYVVGGDKYEY--------- 500

                          250       260
                   ....*....|....*....|....
gi 1491416264  495 FSSDFMAYDIACDRWSVLPRLALH 518
Cdd:PHA03098   501 YINEIEVYDDKTNTWTLFCKFPKV 524
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 301-336 3.08e-05

Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six copies of the motif. It has been shown that Swiss:Q04652 is related to Galactose Oxidase for which a structure has been solved. The kelch motif forms a beta sheet. Several of these sheets associate to form a beta propeller structure as found in pfam00064, pfam00400 and pfam00415.


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 42.17  E-value: 3.08e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1491416264  301 RYGHSLALHKDNIYMYGGKLDATGNVSSQLWVFHIP 336
Cdd:pfam13854    4 RYGHCAVTVGDYIYLYGGYTGGEGQPSDDVYVLSLP 39
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 837-888 2.20e-04

Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The function of the repeat is unknown. Three copies of the repeat are found Plexin. Two copies of the repeat are found in mahogany protein. A related C. elegans protein contains four copies of the repeat. The Met receptor contains a single copy of the repeat. The Pfam alignment shows 6 conserved cysteine residues that may form three conserved disulphide bridges, whereas some members show 8 conserved cysteines. The pattern of conservation suggests that cysteines 5 and 7 (that are not absolutely conserved) form a disulphide bridge (Personal observation. A Bateman).


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 40.38  E-value: 2.20e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1491416264  837 PCALRAACAECT-SGSSECMWCSNMQQCVDSNAYvaSFPYGQCMEWYTMSS-CP 888
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASSkCP 52
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 968-1011 7.40e-04

Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.


Pssm-ID: 395007  Cd Length: 49  Bit Score: 38.49  E-value: 7.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1491416264  968 CQCNGH----SRCVNES-VCEkCENLTTGRHCETCISGYYGDP-TNGGTC 1011
Cdd:pfam00053    1 CDCNPHgslsDTCDPETgQCL-CKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
PHA03098 PHA03098
kelch-like protein; Provisional
 236-398 9.55e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 43.60  E-value: 9.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  236 SFWEREeytlPKL--ARASHKAVIHDNKMWIVGGYVFNHSDSQKVLAYDLISEEWLPLNSSVNSvemRYGHSLALHKDNI 313
Cdd:PHA03098   368 SKWREE----PPLifPRYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSPLPIS---HYGGCAIYHDGKI 440

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  314 YMYGGKLDATG-NVSSQLWVFHIPRQSWAVLAPRakeQYAVVGHSahvVTLRDNStvMLVLFGHCPLYgYISNVQEYNLL 392
Cdd:PHA03098   441 YVIGGISYIDNiKVYNIVESYNPVTNKWTELSSL---NFPRINAS---LCIFNNK--IYVVGGDKYEY-YINEIEVYDDK 511


                   ....*.
gi 1491416264  393 TNTWSI 398
Cdd:PHA03098   512 TNTWTL 517
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
968-1008 1.06e-03

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.06  E-value: 1.06e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1491416264   968 CQCNG----HSRCVNES-VCEkCENLTTGRHCETCISGYYGDPTNG 1008
Cdd:smart00180    1 CDCDPggsaSGTCDPDTgQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
Kelch_6 pfam13964
Kelch motif;
300-345 1.64e-03

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 37.70  E-value: 1.64e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1491416264  300 MRYGHSLALHKDNIYMYGGkLDATGNVSSQLWVFHIPRQSWAVLAP 345
Cdd:pfam13964    1 PRTFHSVVSVGGYIYVFGG-YTNASPALNKLEVYNPLTKSWEELPP 45
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 697-796 2.89e-03

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: 39.26  E-value: 2.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  697 CGTNWHLVGNSCLRITNAKENYDHAKLSCRSNG-----ALLASLTTQKKVEFVLKELQKIQSSPKTLTPWVGL-RKINVS 770
Cdd:cd03589      1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSFSipgliAHLVSIHSQEENDFVYDLFESSRGPDTPYGLWIGLhDRTSEG 80

                           90       100
                   ....*....|....*....|....*.
gi 1491416264  771 YWCWEDMSPFTNTlvQWLPSEPSDAG 796
Cdd:cd03589     81 PFEWTDGSPVDFT--KWAGGQPDNYG 104
PRK14131 PRK14131
N-acetylneuraminate epimerase;
467-542 3.05e-03

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 41.54  E-value: 3.05e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1491416264  467 TAVIVSGTMLVFGGNTHNDTSmshGAKCFSSDFMAYDIACDRWSvlpRLALHHDVNRFGHSAVLYNSTM-YVFGGFN 542
Cdd:PRK14131    79 VAAFIDGKLYVFGGIGKTNSE---GSPQVFDDVYKYDPKTNSWQ---KLDTRSPVGLAGHVAVSLHNGKaYITGGVN 149
Kelch_4 pfam13418
Galactose oxidase, central domain;
411-459 3.12e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.82  E-value: 3.12e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1491416264  411 GHSSVYDPNTRsIYIHGGYKafsaNKYRLADDLYKYEVDSRMWTILKDS 459
Cdd:pfam13418    4 YHTSTSIPDDT-IYLFGGEG----EDGTLLSDLWVFDLSTNEWTRLGSL 47
PHA03098 PHA03098
kelch-like protein; Provisional
 450-558 3.95e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 41.29  E-value: 3.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  450 SRMWTILKDSRFFRYLHTAVIVSGTMLVFGGNTHNDTSMShgakcfssDFMAYDIACDRWSVLPRLALHHdvnrFGHSAV 529
Cdd:PHA03098   367 ESKWREEPPLIFPRYNPCVVNVNNLIYVIGGISKNDELLK--------TVECFSLNTNKWSKGSPLPISH----YGGCAI 434

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1491416264  530 LYNSTMYVFGGF----NSLLLSDILKFTPERCE 558
Cdd:PHA03098   435 YHDGKIYVIGGIsyidNIKVYNIVESYNPVTNK 467
PHA03098 PHA03098
kelch-like protein; Provisional
 381-541 7.63e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 40.52  E-value: 7.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  381 GYISNVQEYNLLTNTWsilQTSGALVQGGYGHSSVYDPNTrsIYIHGGYKAFsankYRLADDLYKYEVDSRMWTILKDSR 460
Cdd:PHA03098   355 ISLNTVESWKPGESKW---REEPPLIFPRYNPCVVNVNNL--IYVIGGISKN----DELLKTVECFSLNTNKWSKGSPLP 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491416264  461 FFRYLHTAVIVSGTMLVFGGNTHNDtsmshGAKCFSSDFMaYDIACDRWSVLPRLALHhdvnRFGHSAVLYNSTMYVFGG 540
Cdd:PHA03098   426 ISHYGGCAIYHDGKIYVIGGISYID-----NIKVYNIVES-YNPVTNKWTELSSLNFP----RINASLCIFNNKIYVVGG 495


                   .
gi 1491416264  541 F 541
Cdd:PHA03098   496 D 496
 
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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