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Conserved domains on  [gi|755498566|ref|XP_011237561|]
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attractin isoform X1 [Mus musculus]

Protein Classification

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 ...
 674-806 1.33e-76

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: 249.04  E-value: 1.33e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  674 CGNGWHLVGNSCLKITTAKENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQLRLMQssqsMSKLTLTPWVGLRKINVSYW 753
Cdd:cd03597     1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQ----MTKQKLTPWVGLRKINVSYW 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755498566  754 CWEDMSPFTNSLLQWMPSEPSDAGFCGILSEPSTRGLKAATCINPLNGSVCER 806
Cdd:cd03597    77 CWEDMSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
215-520 5.08e-24

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 103.31  E-value: 5.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  215 WTReeYSDLKLPRASHKAVVNGNIMWVVGGYMFNhSDYSMVLAYDLTSREW-----LPLNHsvnsvvvRYGHSLALHKDK 289
Cdd:COG3055     3 WSS--LPDLPTPRSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATNTWselapLPGPP-------RHHAAAVAQDGK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  290 IYMYGG--KIDSTGNVTNELRVFHIHNESWVLLTPKAkdqyavVGHSAHIVTLASGRVvmLVIFGHCPLyGYISVVQEYD 367
Cdd:COG3055    73 LYVFGGftGANPSSTPLNDVYVYDPATNTWTKLAPMP------TPRGGATALLLDGKI--YVVGGWDDG-GNVAWVEVYD 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  368 LEKNTWSILhtqGALVQGGYGHSSV--YDDRtkaLYVHGGYkafsankyrladdlyRYDVDTQMWTILKDSRFFRYLHTA 445
Cdd:COG3055   144 PATGTWTQL---APLPTPRDHLAAAvlPDGK---ILVIGGR---------------NGSGFSNTWTTLAPLPTARAGHAA 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498566  446 VIVSGTMLVFGGNTHndtsmshgakcFSSDFMAYDIACDRWSVLPrpELhhDVNRFGHSAVLYNSTMYVFGGFNS 520
Cdd:COG3055   203 AVLGGKILVFGGESG-----------FSDEVEAYDPATNTWTALG--EL--PTPRHGHAAVLTDGKVYVIGGETK 262
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 25-133 9.51e-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: 83.23  E-value: 9.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566   25 TGSSGFVT--DGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLIAAFSglivperdG 98
Cdd:cd00041     7 ASTSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFC--------G 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755498566   99 NETAPEVTVTSGYALLHFFSDAAYNLTGFNITYNF 133
Cdd:cd00041    79 STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 948-993 9.41e-06

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: 43.88  E-value: 9.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755498566  948 ACQCNGHSK----CINQS-ICEkCEDLTTGKHCETCISGFYGDPTNGGKCQ 993
Cdd:cd00055     1 PCDCNGHGSlsgqCDPGTgQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 818-869 1.33e-05

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: 43.85  E-value: 1.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 755498566   818 PCALRTACGECTSSSS-ECMWCSNMKQCVDSNAYvaSFPFGQCMEWYTMSS-CP 869
Cdd:pfam01437    1 RCSQYTSCSSCLAARDpYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASSkCP 52
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 994-1039 2.66e-03

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: 36.95  E-value: 2.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755498566  994 PCKCNGHASL---CNTNTGKCFCtTKGVKGDECQLCevENRYQGNPLKG 1039
Cdd:cd00055     1 PCDCNGHGSLsgqCDPGTGQCEC-KPNTTGRRCDRC--APGYYGLPSQG 46
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
533-579 4.54e-03

domain found in Plexins, Semaphorins and Integrins;


:

Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 36.37  E-value: 4.54e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 755498566    533 QCDAHRSEAACVAAGPGiRCLWDTQSSRCTSWELATEEQAEKLKSEC 579
Cdd:smart00423    1 RCSKYTSCSECLLARDP-YCAWCSSQGRCTSGERCDSRRQNWLSGGC 46
 
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 ...
 674-806 1.33e-76

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: 249.04  E-value: 1.33e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  674 CGNGWHLVGNSCLKITTAKENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQLRLMQssqsMSKLTLTPWVGLRKINVSYW 753
Cdd:cd03597     1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQ----MTKQKLTPWVGLRKINVSYW 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755498566  754 CWEDMSPFTNSLLQWMPSEPSDAGFCGILSEPSTRGLKAATCINPLNGSVCER 806
Cdd:cd03597    77 CWEDMSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
215-520 5.08e-24

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 103.31  E-value: 5.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  215 WTReeYSDLKLPRASHKAVVNGNIMWVVGGYMFNhSDYSMVLAYDLTSREW-----LPLNHsvnsvvvRYGHSLALHKDK 289
Cdd:COG3055     3 WSS--LPDLPTPRSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATNTWselapLPGPP-------RHHAAAVAQDGK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  290 IYMYGG--KIDSTGNVTNELRVFHIHNESWVLLTPKAkdqyavVGHSAHIVTLASGRVvmLVIFGHCPLyGYISVVQEYD 367
Cdd:COG3055    73 LYVFGGftGANPSSTPLNDVYVYDPATNTWTKLAPMP------TPRGGATALLLDGKI--YVVGGWDDG-GNVAWVEVYD 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  368 LEKNTWSILhtqGALVQGGYGHSSV--YDDRtkaLYVHGGYkafsankyrladdlyRYDVDTQMWTILKDSRFFRYLHTA 445
Cdd:COG3055   144 PATGTWTQL---APLPTPRDHLAAAvlPDGK---ILVIGGR---------------NGSGFSNTWTTLAPLPTARAGHAA 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498566  446 VIVSGTMLVFGGNTHndtsmshgakcFSSDFMAYDIACDRWSVLPrpELhhDVNRFGHSAVLYNSTMYVFGGFNS 520
Cdd:COG3055   203 AVLGGKILVFGGESG-----------FSDEVEAYDPATNTWTALG--EL--PTPRHGHAAVLTDGKVYVIGGETK 262
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 25-133 9.51e-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: 83.23  E-value: 9.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566   25 TGSSGFVT--DGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLIAAFSglivperdG 98
Cdd:cd00041     7 ASTSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFC--------G 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755498566   99 NETAPEVTVTSGYALLHFFSDAAYNLTGFNITYNF 133
Cdd:cd00041    79 STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 35-131 8.05e-16

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: 74.35  E-value: 8.05e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566     35 PGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLIAAFSGLIVPErdgnetaPEVTVTSG 110
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPP-------PVISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 755498566    111 YALLHFFSDAAYNLTGFNITY 131
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 692-806 5.38e-15

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 72.13  E-value: 5.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566   692 KENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQLRlmQSSQSmskltltPWVGL-RKINVSYWCWEDMSPFTNSLLQWMP 770
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLK--KSNKY-------FWIGLtDRKNEGTWKWVDGSPVNYTNWAPEP 71

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 755498566   771 SEPSDAGFCGILSePSTRGLKAATCINPlNGSVCER 806
Cdd:pfam00059   72 NNNGENEDCVELS-SSSGKWNDENCNSK-NPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 674-805 1.90e-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: 71.09  E-value: 1.90e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566    674 CGNGWHLVGNSCLKITTAKENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQLRLMQSSQSMskltltpWVGLRKINVSYW 753
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYY-------WIGLSDPDSNGS 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 755498566    754 C-WEDMSPFTNSLLqWMPSEPSDA-GFCGILSePSTRGLKAATCiNPLNGSVCE 805
Cdd:smart00034   74 WqWSDGSGPVSYSN-WAPGEPNNSsGDCVVLS-TSGGKWNDVSC-TSKLPFVCE 124
CUB pfam00431
CUB domain;
21-131 9.88e-14

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 68.48  E-value: 9.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566    21 SSRLTGSSG--FVTDGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLIAAFSGLIVP 94
Cdd:pfam00431    2 GGVLTDSSGsiSSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGSGIP 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 755498566    95 erdgnetaPEVTVTSGYALLHFFSDAAYNLTGFNITY 131
Cdd:pfam00431   82 --------EDIVSSSNQMTIKFVSDASVQKRGFKATY 110
PHA03098 PHA03098
kelch-like protein; Provisional
 213-377 2.67e-09

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 61.32  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  213 SFWTREeySDLKLPRASHKAVVNGNIMWVVGGYMFNHSDYSMVLAYDLTSREWLPLNHSVNSvvvRYGHSLALHKDKIYM 292
Cdd:PHA03098  368 SKWREE--PPLIFPRYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSPLPIS---HYGGCAIYHDGKIYV 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  293 YGGKIDSTG-NVTNELRVFHIHNESWVLLTPkakdqyavVGHSAHIVTLASGRVVMLVIFGHCPLYgYISVVQEYDLEKN 371
Cdd:PHA03098  443 IGGISYIDNiKVYNIVESYNPVTNKWTELSS--------LNFPRINASLCIFNNKIYVVGGDKYEY-YINEIEVYDDKTN 513


                  ....*.
gi 755498566  372 TWSILH 377
Cdd:PHA03098  514 TWTLFC 519
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 948-993 9.41e-06

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: 43.88  E-value: 9.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755498566  948 ACQCNGHSK----CINQS-ICEkCEDLTTGKHCETCISGFYGDPTNGGKCQ 993
Cdd:cd00055     1 PCDCNGHGSlsgqCDPGTgQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 818-869 1.33e-05

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: 43.85  E-value: 1.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 755498566   818 PCALRTACGECTSSSS-ECMWCSNMKQCVDSNAYvaSFPFGQCMEWYTMSS-CP 869
Cdd:pfam01437    1 RCSQYTSCSSCLAARDpYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASSkCP 52
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 276-314 1.71e-04

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: 40.24  E-value: 1.71e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 755498566   276 VVRYGHSLALHKDKIYMYGGKIDSTGNVTNELRVFHIHN 314
Cdd:pfam13854    2 VPRYGHCAVTVGDYIYLYGGYTGGEGQPSDDVYVLSLPT 40
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 949-992 1.72e-03

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 37.72  E-value: 1.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 755498566   949 CQCNGHSkcINQSICEK------CEDLTTGKHCETCISGFYGDP-TNGGKC 992
Cdd:pfam00053    1 CDCNPHG--SLSDTCDPetgqclCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 994-1039 2.66e-03

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: 36.95  E-value: 2.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755498566  994 PCKCNGHASL---CNTNTGKCFCtTKGVKGDECQLCevENRYQGNPLKG 1039
Cdd:cd00055     1 PCDCNGHGSLsgqCDPGTGQCEC-KPNTTGRRCDRC--APGYYGLPSQG 46
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
533-579 4.54e-03

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 36.37  E-value: 4.54e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 755498566    533 QCDAHRSEAACVAAGPGiRCLWDTQSSRCTSWELATEEQAEKLKSEC 579
Cdd:smart00423    1 RCSKYTSCSECLLARDP-YCAWCSSQGRCTSGERCDSRRQNWLSGGC 46
 
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 ...
 674-806 1.33e-76

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: 249.04  E-value: 1.33e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  674 CGNGWHLVGNSCLKITTAKENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQLRLMQssqsMSKLTLTPWVGLRKINVSYW 753
Cdd:cd03597     1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQ----MTKQKLTPWVGLRKINVSYW 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755498566  754 CWEDMSPFTNSLLQWMPSEPSDAGFCGILSEPSTRGLKAATCINPLNGSVCER 806
Cdd:cd03597    77 CWEDMSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
215-520 5.08e-24

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 103.31  E-value: 5.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  215 WTReeYSDLKLPRASHKAVVNGNIMWVVGGYMFNhSDYSMVLAYDLTSREW-----LPLNHsvnsvvvRYGHSLALHKDK 289
Cdd:COG3055     3 WSS--LPDLPTPRSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATNTWselapLPGPP-------RHHAAAVAQDGK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  290 IYMYGG--KIDSTGNVTNELRVFHIHNESWVLLTPKAkdqyavVGHSAHIVTLASGRVvmLVIFGHCPLyGYISVVQEYD 367
Cdd:COG3055    73 LYVFGGftGANPSSTPLNDVYVYDPATNTWTKLAPMP------TPRGGATALLLDGKI--YVVGGWDDG-GNVAWVEVYD 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  368 LEKNTWSILhtqGALVQGGYGHSSV--YDDRtkaLYVHGGYkafsankyrladdlyRYDVDTQMWTILKDSRFFRYLHTA 445
Cdd:COG3055   144 PATGTWTQL---APLPTPRDHLAAAvlPDGK---ILVIGGR---------------NGSGFSNTWTTLAPLPTARAGHAA 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755498566  446 VIVSGTMLVFGGNTHndtsmshgakcFSSDFMAYDIACDRWSVLPrpELhhDVNRFGHSAVLYNSTMYVFGGFNS 520
Cdd:COG3055   203 AVLGGKILVFGGESG-----------FSDEVEAYDPATNTWTALG--EL--PTPRHGHAAVLTDGKVYVIGGETK 262
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
276-529 6.02e-20

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 91.37  E-value: 6.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  276 VVRYGHSLALHKDKIYMYGGKidSTGNVTNELRVFHIHNESWVLLTPkakdqYAVVGHSAHIVTLASGRVvmLVI---FG 352
Cdd:COG3055    11 TPRSEAAAALLDGKVYVAGGL--SGGSASNSFEVYDPATNTWSELAP-----LPGPPRHHAAAVAQDGKL--YVFggfTG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  353 HCPLYGYISVVQEYDLEKNTWSilhTQGALVQGGYGHSS-VYDDRtkaLYVHGGYKAFSANKyrladDLYRYDVDTQMWT 431
Cdd:COG3055    82 ANPSSTPLNDVYVYDPATNTWT---KLAPMPTPRGGATAlLLDGK---IYVVGGWDDGGNVA-----WVEVYDPATGTWT 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  432 ILKDSRFFRYLHTAVIV-SGTMLVFGGNThndtsmshgakcfssdfmaYDIACDRWSVLPrpelHHDVNRFGHSAVLYNS 510
Cdd:COG3055   151 QLAPLPTPRDHLAAAVLpDGKILVIGGRN-------------------GSGFSNTWTTLA----PLPTARAGHAAAVLGG 207

                         250
                  ....*....|....*....
gi 755498566  511 TMYVFGGFNSlLLSDVLVF 529
Cdd:COG3055   208 KILVFGGESG-FSDEVEAY 225
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 25-133 9.51e-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: 83.23  E-value: 9.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566   25 TGSSGFVT--DGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLIAAFSglivperdG 98
Cdd:cd00041     7 ASTSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFC--------G 78

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 755498566   99 NETAPEVTVTSGYALLHFFSDAAYNLTGFNITYNF 133
Cdd:cd00041    79 STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 35-131 8.05e-16

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: 74.35  E-value: 8.05e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566     35 PGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLIAAFSGLIVPErdgnetaPEVTVTSG 110
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPP-------PVISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 755498566    111 YALLHFFSDAAYNLTGFNITY 131
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 692-806 5.38e-15

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 72.13  E-value: 5.38e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566   692 KENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQLRlmQSSQSmskltltPWVGL-RKINVSYWCWEDMSPFTNSLLQWMP 770
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLK--KSNKY-------FWIGLtDRKNEGTWKWVDGSPVNYTNWAPEP 71

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 755498566   771 SEPSDAGFCGILSePSTRGLKAATCINPlNGSVCER 806
Cdd:pfam00059   72 NNNGENEDCVELS-SSSGKWNDENCNSK-NPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 674-805 1.90e-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: 71.09  E-value: 1.90e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566    674 CGNGWHLVGNSCLKITTAKENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQLRLMQSSQSMskltltpWVGLRKINVSYW 753
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYY-------WIGLSDPDSNGS 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 755498566    754 C-WEDMSPFTNSLLqWMPSEPSDA-GFCGILSePSTRGLKAATCiNPLNGSVCE 805
Cdd:smart00034   74 WqWSDGSGPVSYSN-WAPGEPNNSsGDCVVLS-TSGGKWNDVSC-TSKLPFVCE 124
CUB pfam00431
CUB domain;
21-131 9.88e-14

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 68.48  E-value: 9.88e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566    21 SSRLTGSSG--FVTDGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLIAAFSGLIVP 94
Cdd:pfam00431    2 GGVLTDSSGsiSSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGSGIP 81

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 755498566    95 erdgnetaPEVTVTSGYALLHFFSDAAYNLTGFNITY 131
Cdd:pfam00431   82 --------EDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 684-806 2.00e-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: 68.03  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  684 SCLKITTAKENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQLRLMQSSQSmskltltpWVGLRKINV-SYWCWEDMSPFT 762
Cdd:cd00037     1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDV--------WIGLNDLSSeGTWKWSDGSPLV 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 755498566  763 NsLLQWMPSEPSDAG--FCGILSEPSTRGLKAATCiNPLNGSVCER 806
Cdd:cd00037    73 D-YTNWAPGEPNPGGseDCVVLSSSSDGKWNDVSC-SSKLPFICEK 116
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 674-806 1.41e-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: 56.96  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  674 CGNGWHLVGNSCLKITTAKENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQLRLMqssqsmskltlTPWVGLRKINVSY- 752
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSS-----------SYWIGLSREKSEKp 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 755498566  753 WCWEDMSPFTNSLlqwMPSEPSDAGFCGILSEPstrGLKAATCINPlNGSVCER 806
Cdd:cd03593    70 WKWIDGSPLNNLF---NIRGSTKSGNCAYLSST---GIYSEDCSTK-KRWICEK 116
PHA03098 PHA03098
kelch-like protein; Provisional
 213-377 2.67e-09

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 61.32  E-value: 2.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  213 SFWTREeySDLKLPRASHKAVVNGNIMWVVGGYMFNHSDYSMVLAYDLTSREWLPLNHSVNSvvvRYGHSLALHKDKIYM 292
Cdd:PHA03098  368 SKWREE--PPLIFPRYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSPLPIS---HYGGCAIYHDGKIYV 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  293 YGGKIDSTG-NVTNELRVFHIHNESWVLLTPkakdqyavVGHSAHIVTLASGRVVMLVIFGHCPLYgYISVVQEYDLEKN 371
Cdd:PHA03098  443 IGGISYIDNiKVYNIVESYNPVTNKWTELSS--------LNFPRINASLCIFNNKIYVVGGDKYEY-YINEIEVYDDKTN 513


                  ....*.
gi 755498566  372 TWSILH 377
Cdd:PHA03098  514 TWTLFC 519
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 674-780 4.75e-09

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: 55.77  E-value: 4.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  674 CGNGWHLVGNSCLKITTAKENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQLRLMQSSqsmskltltpWVGLRKINV-SY 752
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSY----------WIGLSDEETeGE 70

                          90       100
                  ....*....|....*....|....*...
gi 755498566  753 WCWEDMSPFTNSLLQWMPSEPSDAGFCG 780
Cdd:cd03590    71 WKWVDGTPLNSSKTFWHPGEPNNWGGGG 98
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
430-529 1.31e-08

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 57.86  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  430 WTILKDSRFFRYLHTAVIVSGTMLVFGGNTHNDTsmshgakcfSSDFMAYDIACDRWSVL---PRPELHHdvnrfgHSAV 506
Cdd:COG3055     3 WSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSA---------SNSFEVYDPATNTWSELaplPGPPRHH------AAAV 67

                          90       100
                  ....*....|....*....|....*...
gi 755498566  507 LYNSTMYVFGGFN-----SLLLSDVLVF 529
Cdd:COG3055    68 AQDGKLYVFGGFTganpsSTPLNDVYVY 95
PHA03098 PHA03098
kelch-like protein; Provisional
 232-495 4.49e-06

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 50.92  E-value: 4.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  232 AVVNGNIMWVVGGYMFNHSDYSMVLAYDLTSREWlplNHSVNSVVVRYGHSLALHKDKIYMYGGKIDStgNVTNELRVFH 311
Cdd:PHA03098  290 SVVLNNVIYFIGGMNKNNLSVNSVVSYDTKTKSW---NKVPELIYPRKNPGVTVFNNRIYVIGGIYNS--ISLNTVESWK 364

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  312 IHNESWVLLTPKAKDQYavvghSAHIVTLASgrvVMLVIFGHCPLYGYISVVQEYDLEKNTWSILHtqgALVQGGYGHSS 391
Cdd:PHA03098  365 PGESKWREEPPLIFPRY-----NPCVVNVNN---LIYVIGGISKNDELLKTVECFSLNTNKWSKGS---PLPISHYGGCA 433

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  392 VYDDrtKALYVHGGYKafSANKYRLADDLYRYDVDTQMWTILKDSRFFRYLHTAVIVSGTMLVFGGNTHNDtsmshgakc 471
Cdd:PHA03098  434 IYHD--GKIYVIGGIS--YIDNIKVYNIVESYNPVTNKWTELSSLNFPRINASLCIFNNKIYVVGGDKYEY--------- 500

                         250       260
                  ....*....|....*....|....
gi 755498566  472 FSSDFMAYDIACDRWSVLPRPELH 495
Cdd:PHA03098  501 YINEIEVYDDKTNTWTLFCKFPKV 524
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 948-993 9.41e-06

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: 43.88  E-value: 9.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 755498566  948 ACQCNGHSK----CINQS-ICEkCEDLTTGKHCETCISGFYGDPTNGGKCQ 993
Cdd:cd00055     1 PCDCNGHGSlsgqCDPGTgQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 818-869 1.33e-05

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: 43.85  E-value: 1.33e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 755498566   818 PCALRTACGECTSSSS-ECMWCSNMKQCVDSNAYvaSFPFGQCMEWYTMSS-CP 869
Cdd:pfam01437    1 RCSQYTSCSSCLAARDpYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASSkCP 52
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 276-314 1.71e-04

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: 40.24  E-value: 1.71e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 755498566   276 VVRYGHSLALHKDKIYMYGGKIDSTGNVTNELRVFHIHN 314
Cdd:pfam13854    2 VPRYGHCAVTVGDYIYLYGGYTGGEGQPSDDVYVLSLPT 40
PHA03098 PHA03098
kelch-like protein; Provisional
 358-518 7.59e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 43.60  E-value: 7.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  358 GYISVVQEYDLEKNTWSILHTqgaLVQGGYGHSSVYDDRTkaLYVHGGYKAFsankYRLADDLYRYDVDTQMWTILKDSR 437
Cdd:PHA03098  355 ISLNTVESWKPGESKWREEPP---LIFPRYNPCVVNVNNL--IYVIGGISKN----DELLKTVECFSLNTNKWSKGSPLP 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  438 FFRYLHTAVIVSGTMLVFGGNTHNDtsmshGAKCFSSDFMaYDIACDRWSVLPrpELHHdvNRFGHSAVLYNSTMYVFGG 517
Cdd:PHA03098  426 ISHYGGCAIYHDGKIYVIGGISYID-----NIKVYNIVES-YNPVTNKWTELS--SLNF--PRINASLCIFNNKIYVVGG 495


                  .
gi 755498566  518 F 518
Cdd:PHA03098  496 D 496
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 226-265 1.55e-03

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: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 37.59  E-value: 1.55e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 755498566   226 PRASHKAVVNGNIMWVVGGYMFNHSDYSmVLAYDLTSREW 265
Cdd:pfam01344    1 RRSGAGVVVVGGKIYVIGGFDGNQSLNS-VEVYDPETNTW 39
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 949-992 1.72e-03

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 37.72  E-value: 1.72e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 755498566   949 CQCNGHSkcINQSICEK------CEDLTTGKHCETCISGFYGDP-TNGGKC 992
Cdd:pfam00053    1 CDCNPHG--SLSDTCDPetgqclCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 994-1039 2.66e-03

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: 36.95  E-value: 2.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 755498566  994 PCKCNGHASL---CNTNTGKCFCtTKGVKGDECQLCevENRYQGNPLKG 1039
Cdd:cd00055     1 PCDCNGHGSLsgqCDPGTGQCEC-KPNTTGRRCDRC--APGYYGLPSQG 46
PRK14131 PRK14131
N-acetylneuraminate epimerase;
418-519 4.13e-03

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 41.15  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755498566  418 DDLYRYDVDTQM--WTILKDsrfF----RYLHTAVIVSGTMLVFGGNTHNDTSmshGAKCFSSDFMAYDIACDRWSVLPR 491
Cdd:PRK14131   50 TSWYKLDLNAPSkgWTKIAA---FpggpREQAVAAFIDGKLYVFGGIGKTNSE---GSPQVFDDVYKYDPKTNSWQKLDT 123

                          90       100
                  ....*....|....*....|....*....
gi 755498566  492 pelHHDVNRFGHSAVLYNSTM-YVFGGFN 519
Cdd:PRK14131  124 ---RSPVGLAGHVAVSLHNGKaYITGGVN 149
PSI smart00423
domain found in Plexins, Semaphorins and Integrins;
533-579 4.54e-03

domain found in Plexins, Semaphorins and Integrins;


Pssm-ID: 214655 [Multi-domain]  Cd Length: 47  Bit Score: 36.37  E-value: 4.54e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 755498566    533 QCDAHRSEAACVAAGPGiRCLWDTQSSRCTSWELATEEQAEKLKSEC 579
Cdd:smart00423    1 RCSKYTSCSECLLARDP-YCAWCSSQGRCTSGERCDSRRQNWLSGGC 46
Kelch_6 pfam13964
Kelch motif;
278-322 7.45e-03

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 35.77  E-value: 7.45e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 755498566   278 RYGHSLALHKDKIYMYGGKIDStGNVTNELRVFHIHNESWVLLTP 322
Cdd:pfam13964    2 RTFHSVVSVGGYIYVFGGYTNA-SPALNKLEVYNPLTKSWEELPP 45
CLECT_DGCR2_like cd03599
C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein ...
 674-724 7.96e-03

C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS); CLECT_DGCR2_like: C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein deleted in DiGeorge Syndrome (DGS). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DGS is also known velo-cardio-facial syndrome (VCFS). DGS is a genetic abnormality that results in malformations of the heart, face, and limbs and is associated with schizophrenia and depressive disorders. DGCR2 is a candidate for involvement in the pathogenesis of DGS since the DGCR2 gene lies within the minimal DGS critical region (MDGRC) of 22q11, which when deleted gives rise to DGS, and the DGCR2 gene is in close proximity to the balanced translocation breakpoint in a DGS patient having a balanced translocation.


Pssm-ID: 153069  Cd Length: 153  Bit Score: 38.36  E-value: 7.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755498566  674 CGNGWHLVGN--SCLKITTAKENYDNAKLSCRNHNAFLASLTSQKKVEFVLKQ 724
Cdd:cd03599     1 CPSGWHHYEGtaSCYKVYLSGENYWDAVQTCQKVNGSLATFTTDQELQFILAQ 53
Kelch_4 pfam13418
Galactose oxidase, central domain;
388-436 8.91e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 35.67  E-value: 8.91e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 755498566   388 GHSSVYDDRTKaLYVHGGYKafsaNKYRLADDLYRYDVDTQMWTILKDS 436
Cdd:pfam13418    4 YHTSTSIPDDT-IYLFGGEG----EDGTLLSDLWVFDLSTNEWTRLGSL 47
 
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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