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Conserved domains on  [gi|755563242|ref|XP_011245546|]
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attractin-like protein 1 isoform X3 [Mus musculus]

Protein Classification

attractin-like protein 1( domain architecture ID 18860411)

attractin-like protein 1 (ATRNL1) may play a role in melanocortin signaling pathways that regulate energy homeostasis

Graphical summary

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List of domain hits

 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 ...
 704-830 7.23e-80

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: 258.28  E-value: 7.23e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  704 CGEGWNHVGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQK--FTQQKVSPWVGLRKINISYWGWED 781
Cdd:cd03597     1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKhqMTKQKLTPWVGLRKINVSYWCWED 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 755563242  782 MSPFTNTSLQWLPGEPNDSGFCAYLERAAVAGLKANPCTSMADGLVCEK 830
Cdd:cd03597    81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
259-554 1.19e-22

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.46  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  259 VGRASHKAVLHGKFMWVIGGYTFN--YSSFQMvlnYNLESSIWNVGAvsRGPLQRYGHS-LALYQENIFMYGGRMETSD- 334
Cdd:COG3055    11 TPRSEAAAALLDGKVYVAGGLSGGsaSNSFEV---YDPATNTWSELA--PLPGPPRHHAaAVAQDGKLYVFGGFTGANPs 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  335 GNVTDELWVFNVRSQSWSTKTPtvlghsqqyAVEGHSAHIMELDSRDVvmIVIFGYSAiYGYTSSIQEYHISSNTWlvpE 414
Cdd:COG3055    86 STPLNDVYVYDPATNTWTKLAP---------MPTPRGGATALLLDGKI--YVVGGWDD-GGNVAWVEVYDPATGTW---T 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  415 TKGAIVQGGYGHTSVYDEVTKsIYVHGGYKalpgnkyglvddlykYEVNTRTWTILKESGFARYLHSAVLINGAMLIFGG 494
Cdd:COG3055   151 QLAPLPTPRDHLAAAVLPDGK-ILVIGGRN---------------GSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGG 214

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  495 NTHndtslsngakcFSADFLAYDIACDEWKTLPKPNlhrdVNRFGHSAVVINGSMYIFGG 554
Cdd:COG3055   215 ESG-----------FSDEVEAYDPATNTWTALGELP----TPRHGHAAVLTDGKVYVIGG 259
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 969-1014 8.70e-08

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: 49.66  E-value: 8.70e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755563242  969 ACQCNGHSTciNNNVCEQ------CKNLTTGRQCQECMPGYYGDPTNGGQCT 1014
Cdd:cd00055     1 PCDCNGHGS--LSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 92-162 1.11e-07

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: 51.64  E-value: 1.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755563242   92 CQGRFKLTePSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVAVL 162
Cdd:cd00041     1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRF 76
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 845-894 7.71e-06

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: 44.24  E-value: 7.71e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 755563242   845 PCSLRTSCANCTSSG-MECMWCSSTKRCVDSNAYiiSFPYGQCLEWQTATC 894
Cdd:pfam01437    1 RCSQYTSCSSCLAARdPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASS 49
DSL super family cl19567
Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain ...
 191-237 3.46e-03

Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain defined by structure.


The actual alignment was detected with superfamily member pfam01414:

Pssm-ID: 473190  Cd Length: 46  Bit Score: 36.83  E-value: 3.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 755563242   191 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 237
Cdd:pfam01414    1 CDENYYGSTCSK-FCRPRDDKFGHYTCDANGNK--VCLPGWTGPYCD 44
 
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 ...
 704-830 7.23e-80

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: 258.28  E-value: 7.23e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  704 CGEGWNHVGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQK--FTQQKVSPWVGLRKINISYWGWED 781
Cdd:cd03597     1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKhqMTKQKLTPWVGLRKINVSYWCWED 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 755563242  782 MSPFTNTSLQWLPGEPNDSGFCAYLERAAVAGLKANPCTSMADGLVCEK 830
Cdd:cd03597    81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
259-554 1.19e-22

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.46  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  259 VGRASHKAVLHGKFMWVIGGYTFN--YSSFQMvlnYNLESSIWNVGAvsRGPLQRYGHS-LALYQENIFMYGGRMETSD- 334
Cdd:COG3055    11 TPRSEAAAALLDGKVYVAGGLSGGsaSNSFEV---YDPATNTWSELA--PLPGPPRHHAaAVAQDGKLYVFGGFTGANPs 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  335 GNVTDELWVFNVRSQSWSTKTPtvlghsqqyAVEGHSAHIMELDSRDVvmIVIFGYSAiYGYTSSIQEYHISSNTWlvpE 414
Cdd:COG3055    86 STPLNDVYVYDPATNTWTKLAP---------MPTPRGGATALLLDGKI--YVVGGWDD-GGNVAWVEVYDPATGTW---T 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  415 TKGAIVQGGYGHTSVYDEVTKsIYVHGGYKalpgnkyglvddlykYEVNTRTWTILKESGFARYLHSAVLINGAMLIFGG 494
Cdd:COG3055   151 QLAPLPTPRDHLAAAVLPDGK-ILVIGGRN---------------GSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGG 214

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  495 NTHndtslsngakcFSADFLAYDIACDEWKTLPKPNlhrdVNRFGHSAVVINGSMYIFGG 554
Cdd:COG3055   215 ESG-----------FSDEVEAYDPATNTWTALGELP----TPRHGHAAVLTDGKVYVIGG 259
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 722-830 3.34e-14

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 69.81  E-value: 3.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242   722 RESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIqkfTQQKVSPWVGLRKINIS-YWGWEDMSPFTNTSLQWLPGEPNDS 800
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTL---KKSNKYFWIGLTDRKNEgTWKWVDGSPVNYTNWAPEPNNNGEN 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 755563242   801 GFCAYLERAAvAGLKANPCTSMAdGLVCEK 830
Cdd:pfam00059   78 EDCVELSSSS-GKWNDENCNSKN-PFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 704-806 6.50e-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: 69.55  E-value: 6.50e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242    704 CGEGWNHVGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKFTQQKvSPWVGLRKINISY-WGWEDM 782
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGsWQWSDG 79

                            90       100
                    ....*....|....*....|....*
gi 755563242    783 SPFTNTSLqWLPGEPNDS-GFCAYL 806
Cdd:smart00034   80 SGPVSYSN-WAPGEPNNSsGDCVVL 103
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 969-1014 8.70e-08

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: 49.66  E-value: 8.70e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755563242  969 ACQCNGHSTciNNNVCEQ------CKNLTTGRQCQECMPGYYGDPTNGGQCT 1014
Cdd:cd00055     1 PCDCNGHGS--LSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 92-162 1.11e-07

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: 51.64  E-value: 1.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755563242   92 CQGRFKLTePSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVAVL 162
Cdd:cd00041     1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRF 76
CUB pfam00431
CUB domain;
92-160 1.56e-06

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 48.06  E-value: 1.56e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755563242    92 CQGRFklTEPSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVA 160
Cdd:pfam00431    1 CGGVL--TDSSGSISspNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLG 73
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 845-894 7.71e-06

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: 44.24  E-value: 7.71e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 755563242   845 PCSLRTSCANCTSSG-MECMWCSSTKRCVDSNAYiiSFPYGQCLEWQTATC 894
Cdd:pfam01437    1 RCSQYTSCSSCLAARdPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASS 49
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 308-348 1.20e-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: 43.32  E-value: 1.20e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 755563242   308 PLQRYGHSLALYQENIFMYGGrMETSDGNVTDELWVFNVRS 348
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGG-YTGGEGQPSDDVYVLSLPT 40
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 970-1013 2.24e-05

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 43.11  E-value: 2.24e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 755563242   970 CQCNGHSTciNNNVCEQ------CKNLTTGRQCQECMPGYYGDP-TNGGQC 1013
Cdd:pfam00053    1 CDCNPHGS--LSDTCDPetgqclCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
PLN02153 PLN02153
epithiospecifier protein
 410-556 6.96e-05

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 46.52  E-value: 6.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  410 WLVPETKGAIVQG---GYGHTSVYDEvtksIYVHGGykALPGNKYgLVDDLYKYEVNTRTWTILKESGFARYLHS----A 482
Cdd:PLN02153    9 WIKVEQKGGKGPGprcSHGIAVVGDK----LYSFGG--ELKPNEH-IDKDLYVFDFNTHTWSIAPANGDVPRISClgvrM 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755563242  483 VLINGAMLIFGGNTHNdtslsngaKCFSaDFLAYDIACDEWKTLPKPNLHRDVN-RFGHSAVVINGSMYIFGGFS 556
Cdd:PLN02153   82 VAVGTKLYIFGGRDEK--------REFS-DFYSYDTVKNEWTFLTKLDEEGGPEaRTFHSMASDENHVYVFGGVS 147
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 109-160 1.35e-04

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: 42.38  E-value: 1.35e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 755563242    109 PINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVA 160
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLG 64
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
970-1010 1.45e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 40.37  E-value: 1.45e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 755563242    970 CQCNG----HSTCINNN-VCEqCKNLTTGRQCQECMPGYYGDPTNG 1010
Cdd:smart00180    1 CDCDPggsaSGTCDPDTgQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
DSL pfam01414
Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain ...
 191-237 3.46e-03

Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain defined by structure.


Pssm-ID: 460202  Cd Length: 46  Bit Score: 36.83  E-value: 3.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 755563242   191 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 237
Cdd:pfam01414    1 CDENYYGSTCSK-FCRPRDDKFGHYTCDANGNK--VCLPGWTGPYCD 44
DSL smart00051
delta serrate ligand;
190-236 3.68e-03

delta serrate ligand;


Pssm-ID: 128366  Cd Length: 63  Bit Score: 37.31  E-value: 3.68e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 755563242    190 ECDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKLCvcNDSWQGPDC 236
Cdd:smart00051   20 TCDENYYGEGCNK-FCRPRDDFFGHYTCDENGNKGC--LEGWMGPYC 63
 
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 ...
 704-830 7.23e-80

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: 258.28  E-value: 7.23e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  704 CGEGWNHVGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQK--FTQQKVSPWVGLRKINISYWGWED 781
Cdd:cd03597     1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKhqMTKQKLTPWVGLRKINVSYWCWED 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 755563242  782 MSPFTNTSLQWLPGEPNDSGFCAYLERAAVAGLKANPCTSMADGLVCEK 830
Cdd:cd03597    81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
259-554 1.19e-22

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.46  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  259 VGRASHKAVLHGKFMWVIGGYTFN--YSSFQMvlnYNLESSIWNVGAvsRGPLQRYGHS-LALYQENIFMYGGRMETSD- 334
Cdd:COG3055    11 TPRSEAAAALLDGKVYVAGGLSGGsaSNSFEV---YDPATNTWSELA--PLPGPPRHHAaAVAQDGKLYVFGGFTGANPs 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  335 GNVTDELWVFNVRSQSWSTKTPtvlghsqqyAVEGHSAHIMELDSRDVvmIVIFGYSAiYGYTSSIQEYHISSNTWlvpE 414
Cdd:COG3055    86 STPLNDVYVYDPATNTWTKLAP---------MPTPRGGATALLLDGKI--YVVGGWDD-GGNVAWVEVYDPATGTW---T 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  415 TKGAIVQGGYGHTSVYDEVTKsIYVHGGYKalpgnkyglvddlykYEVNTRTWTILKESGFARYLHSAVLINGAMLIFGG 494
Cdd:COG3055   151 QLAPLPTPRDHLAAAVLPDGK-ILVIGGRN---------------GSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGG 214

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  495 NTHndtslsngakcFSADFLAYDIACDEWKTLPKPNlhrdVNRFGHSAVVINGSMYIFGG 554
Cdd:COG3055   215 ESG-----------FSDEVEAYDPATNTWTALGELP----TPRHGHAAVLTDGKVYVIGG 259
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
257-498 8.20e-20

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 90.99  E-value: 8.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  257 PSVGRASHKAVLHGKFMWVIGGYTFNYSSFQM---VLNYNLESSIWNVGAVSrgPLQRYGHSLALYQENIFMYGGRmetS 333
Cdd:COG3055    57 PGPPRHHAAAVAQDGKLYVFGGFTGANPSSTPlndVYVYDPATNTWTKLAPM--PTPRGGATALLLDGKIYVVGGW---D 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  334 DGNVTDELWVFNVRSQSWSTKTPTVLghsqqyAVEGHSAHIMELDsrdvvMIVIFGysaiyGYTSSIqeyhiSSNTWlvp 413
Cdd:COG3055   132 DGGNVAWVEVYDPATGTWTQLAPLPT------PRDHLAAAVLPDG-----KILVIG-----GRNGSG-----FSNTW--- 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  414 ETKGAIVQGGYGHTSVYdeVTKSIYVHGGYkalpgnkYGLVDDLYKYEVNTRTWTILKESGFARYLHSAVLINGAMLIFG 493
Cdd:COG3055   188 TTLAPLPTARAGHAAAV--LGGKILVFGGE-------SGFSDEVEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYVIG 258


                  ....*
gi 755563242  494 GNTHN 498
Cdd:COG3055   259 GETKP 263
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
308-568 4.07e-18

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 85.98  E-value: 4.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  308 PLQRYGHSLALYQENIFMYGGRmetSDGNVTDELWVFNVRSQSWSTKTP---TVLGHSQQYAVEGHsahimeldsrdvvm 384
Cdd:COG3055    10 PTPRSEAAAALLDGKVYVAGGL---SGGSASNSFEVYDPATNTWSELAPlpgPPRHHAAAVAQDGK-------------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  385 IVIF-GYSAIYG---YTSSIQEYHISSNTWlvpETKGAIVQGGYGHTSVYDEvtKSIYVHGGYkalpgNKYGLVDDLYKY 460
Cdd:COG3055    73 LYVFgGFTGANPsstPLNDVYVYDPATNTW---TKLAPMPTPRGGATALLLD--GKIYVVGGW-----DDGGNVAWVEVY 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  461 EVNTRTWTILKESGFARYLHSA-VLINGAMLIFGGNthNDTSLSNgakcfsadflaydiacdEWKTLPkpnlHRDVNRFG 539
Cdd:COG3055   143 DPATGTWTQLAPLPTPRDHLAAaVLPDGKILVIGGR--NGSGFSN-----------------TWTTLA----PLPTARAG 199

                         250       260
                  ....*....|....*....|....*....
gi 755563242  540 HSAVVINGSMYIFGGFSSVlLNDILVYKP 568
Cdd:COG3055   200 HAAAVLGGKILVFGGESGF-SDEVEAYDP 227
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 715-830 1.85e-15

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: 73.81  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  715 CLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKFTQQKVspWVGLRKINI-SYWGWEDMSPFTNTSlQWL 793
Cdd:cd00037     2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDV--WIGLNDLSSeGTWKWSDGSPLVDYT-NWA 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 755563242  794 PGEPN--DSGFCAYLERAAVAGLKANPCTSMAdGLVCEK 830
Cdd:cd00037    79 PGEPNpgGSEDCVVLSSSSDGKWNDVSCSSKL-PFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 722-830 3.34e-14

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 69.81  E-value: 3.34e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242   722 RESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIqkfTQQKVSPWVGLRKINIS-YWGWEDMSPFTNTSLQWLPGEPNDS 800
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTL---KKSNKYFWIGLTDRKNEgTWKWVDGSPVNYTNWAPEPNNNGEN 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 755563242   801 GFCAYLERAAvAGLKANPCTSMAdGLVCEK 830
Cdd:pfam00059   78 EDCVELSSSS-GKWNDENCNSKN-PFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 704-806 6.50e-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: 69.55  E-value: 6.50e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242    704 CGEGWNHVGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKFTQQKvSPWVGLRKINISY-WGWEDM 782
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGsWQWSDG 79

                            90       100
                    ....*....|....*....|....*
gi 755563242    783 SPFTNTSLqWLPGEPNDS-GFCAYL 806
Cdd:smart00034   80 SGPVSYSN-WAPGEPNNSsGDCVVL 103
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
466-568 9.57e-12

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 67.10  E-value: 9.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  466 TWTILKESGFARYLHSAVLINGAMLIFGGNTHNDTslsngakcfSADFLAYDIACDEWKTLPKPNLHRdvnRFGHSAVVI 545
Cdd:COG3055     2 TWSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSA---------SNSFEVYDPATNTWSELAPLPGPP---RHHAAAVAQ 69

                          90       100
                  ....*....|....*....|....*...
gi 755563242  546 NGSMYIFGGF-----SSVLLNDILVYKP 568
Cdd:COG3055    70 DGKLYVFGGFtganpSSTPLNDVYVYDP 97
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 704-806 4.78e-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: 4.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  704 CGEGWNHVGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFvldeIQKFTQQKVSPWVGLRKINI-SYWGWEDM 782
Cdd:cd03590     1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEF----ISKILSGNRSYWIGLSDEETeGEWKWVDG 76

                          90       100
                  ....*....|....*....|....*...
gi 755563242  783 SPFTNTSLQWLPGEPNDSGF----CAYL 806
Cdd:cd03590    77 TPLNSSKTFWHPGEPNNWGGggedCAEL 104
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 969-1014 8.70e-08

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: 49.66  E-value: 8.70e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755563242  969 ACQCNGHSTciNNNVCEQ------CKNLTTGRQCQECMPGYYGDPTNGGQCT 1014
Cdd:cd00055     1 PCDCNGHGS--LSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 92-162 1.11e-07

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: 51.64  E-value: 1.11e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755563242   92 CQGRFKLTePSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVAVL 162
Cdd:cd00041     1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRF 76
CUB pfam00431
CUB domain;
92-160 1.56e-06

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 48.06  E-value: 1.56e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755563242    92 CQGRFklTEPSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVA 160
Cdd:pfam00431    1 CGGVL--TDSSGSISspNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLG 73
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 704-811 1.66e-06

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: 48.10  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  704 CGEGWNHVGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFvldeIQKFTQQKvSPWVGLRKINISY-WGWEDM 782
Cdd:cd03593     1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEF----LQSQIGSS-SYWIGLSREKSEKpWKWIDG 75

                          90       100       110
                  ....*....|....*....|....*....|
gi 755563242  783 SPFTNtslqWL-PGEPNDSGFCAYLERAAV 811
Cdd:cd03593    76 SPLNN----LFnIRGSTKSGNCAYLSSTGI 101
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 845-894 7.71e-06

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: 44.24  E-value: 7.71e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 755563242   845 PCSLRTSCANCTSSG-MECMWCSSTKRCVDSNAYiiSFPYGQCLEWQTATC 894
Cdd:pfam01437    1 RCSQYTSCSSCLAARdPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASS 49
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 308-348 1.20e-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: 43.32  E-value: 1.20e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 755563242   308 PLQRYGHSLALYQENIFMYGGrMETSDGNVTDELWVFNVRS 348
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGG-YTGGEGQPSDDVYVLSLPT 40
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 970-1013 2.24e-05

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 43.11  E-value: 2.24e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 755563242   970 CQCNGHSTciNNNVCEQ------CKNLTTGRQCQECMPGYYGDP-TNGGQC 1013
Cdd:pfam00053    1 CDCNPHGS--LSDTCDPetgqclCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
PLN02153 PLN02153
epithiospecifier protein
 410-556 6.96e-05

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 46.52  E-value: 6.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  410 WLVPETKGAIVQG---GYGHTSVYDEvtksIYVHGGykALPGNKYgLVDDLYKYEVNTRTWTILKESGFARYLHS----A 482
Cdd:PLN02153    9 WIKVEQKGGKGPGprcSHGIAVVGDK----LYSFGG--ELKPNEH-IDKDLYVFDFNTHTWSIAPANGDVPRISClgvrM 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755563242  483 VLINGAMLIFGGNTHNdtslsngaKCFSaDFLAYDIACDEWKTLPKPNLHRDVN-RFGHSAVVINGSMYIFGGFS 556
Cdd:PLN02153   82 VAVGTKLYIFGGRDEK--------REFS-DFYSYDTVKNEWTFLTKLDEEGGPEaRTFHSMASDENHVYVFGGVS 147
CLECT_DGCR2_like cd03599
C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein ...
 704-808 9.40e-05

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: 44.14  E-value: 9.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  704 CGEGWNHV-GDA-CLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKFTQQ------KVSPWVGLRKI--- 772
Cdd:cd03599     1 CPSGWHHYeGTAsCYKVYLSGENYWDAVQTCQKVNGSLATFTTDQELQFILAQEWDFDERvfgrkdQCKFWVGYQYVitn 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 755563242  773 -NISYWG-WEdmSPFTNTSLQWLPGEP--------NDSGFCAYLER 808
Cdd:cd03599    81 rNHSLEGrWE--VAYKGSMEVFLPPEPifatgmstNDNVFCAQLQC 124
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 109-160 1.35e-04

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: 42.38  E-value: 1.35e-04
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*.
gi 755563242    109 PINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLVA 160
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLG 64
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 704-820 1.39e-04

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: 43.12  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  704 CGEGWNHVGDACLRINSSRESYDNAKLYCYN-----LSGNLASLTTSKEVEFVLD--EIQKFTQQKVSPWVGL-RKINIS 775
Cdd:cd03589     1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDlfESSRGPDTPYGLWIGLhDRTSEG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 755563242  776 YWGWEDMSPFTNTslQWLPGEPNDSGF---CAYLERAAVAGLKAN--PCT 820
Cdd:cd03589    81 PFEWTDGSPVDFT--KWAGGQPDNYGGnedCVQMWRRGDAGQSWNdmPCD 128
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
970-1010 1.45e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 40.37  E-value: 1.45e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 755563242    970 CQCNG----HSTCINNN-VCEqCKNLTTGRQCQECMPGYYGDPTNG 1010
Cdd:smart00180    1 CDCDPggsaSGTCDPDTgQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
PHA03098 PHA03098
kelch-like protein; Provisional
 437-566 1.60e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 45.91  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  437 IYVHGGYkalpgNKYG-LVDDLYKYEVNTRTWTILKESGFARYLHSAVLINGAMLIFGGNTHndtslSNGAKCFSADFLa 515
Cdd:PHA03098  392 IYVIGGI-----SKNDeLLKTVECFSLNTNKWSKGSPLPISHYGGCAIYHDGKIYVIGGISY-----IDNIKVYNIVES- 460

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 755563242  516 YDIACDEWKTLPKPNLHRdvnrFGHSAVVINGSMYIFGGFS-SVLLNDILVY 566
Cdd:PHA03098  461 YNPVTNKWTELSSLNFPR----INASLCIFNNKIYVVGGDKyEYYINEIEVY 508
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 704-808 1.85e-04

C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2); CLECT_REG-1_like: C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and avian eggshell-specific proteins: ansocalcin, structhiocalcin-1(SCA-1), and -2(SCA-2). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. REG-1 is a proliferating factor which participates in various kinds of tissue regeneration including pancreatic beta-cell regeneration, regeneration of intestinal mucosa, regeneration of motor neurons, and perhaps in tissue regeneration of damaged heart. REG-1 may play a role on the pathophysiology of Alzheimer's disease and in the development of gastric cancers. Its expression is correlated with reduced survival from early-stage colorectal cancer. REG-1 also binds and aggregates several bacterial strains from the intestinal flora and it has been suggested that it is involved in the control of the intestinal bacterial ecosystem. Rat lithostathine has calcium carbonate crystal inhibitor activity in vitro. REG-IV is unregulated in pancreatic, gastric, hepatocellular, and prostrate adenocarcinomas. REG-IV activates the EGF receptor/Akt/AP-1 signaling pathway in colorectal carcinoma. Ansocalcin, SCA-1 and -2 are found at high concentration in the calcified egg shell layer of goose and ostrich, respectively and tend to form aggregates. Ansocalcin nucleates calcite crystal aggregates in vitro.


Pssm-ID: 153064 [Multi-domain]  Cd Length: 129  Bit Score: 42.74  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  704 CGEGWNHVGDACLRINSSRESYDNAKLYC--YNLSGNLASLTTSKEVEFVLDEIQKFTQQKVSPWVGLRKINISY-WGWE 780
Cdd:cd03594     1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCqkYGPGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSRgWEWS 80

                          90       100
                  ....*....|....*....|....*....
gi 755563242  781 DMSPFTNTSlqWLPGEP-NDSGFCAYLER 808
Cdd:cd03594    81 DGSKLDYRS--WDRNPPyARGGYCAELSR 107
Kelch_3 pfam13415
Galactose oxidase, central domain;
434-485 3.70e-04

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 39.58  E-value: 3.70e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 755563242   434 TKSIYVHGGYKALPGNKYglvDDLYKYEVNTRTWTILKESGFARYLHSAVLI 485
Cdd:pfam13415    1 GDKLYIFGGLGFDGQTRL---NDLYVYDLDTNTWTQIGDLPPPRSGHSATYI 49
Kelch_4 pfam13418
Galactose oxidase, central domain;
425-470 3.79e-04

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 39.52  E-value: 3.79e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 755563242   425 GHTSVYDEVTKsIYVHGGYkalpGNKYGLVDDLYKYEVNTRTWTIL 470
Cdd:pfam13418    4 YHTSTSIPDDT-IYLFGGE----GEDGTLLSDLWVFDLSTNEWTRL 44
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 704-804 6.79e-04

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


Pssm-ID: 153058  Cd Length: 124  Bit Score: 41.02  E-value: 6.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  704 CGEGWNHVGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKFTqqkvspWVGLRKINISY-WGWEDM 782
Cdd:cd03588     1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ------WIGLNDRTIEGdFRWSDG 74

                          90       100
                  ....*....|....*....|....
gi 755563242  783 SP--FTNtslqWLPGEPnDSGFCA 804
Cdd:cd03588    75 HPlqFEN----WRPNQP-DNFFAT 93
PLN02193 PLN02193
nitrile-specifier protein
 432-597 1.24e-03

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 43.02  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  432 EVTKSIYVHGG--YKALPGNKYglvddLYKYEVNTRTWTILKESGFARYLH----SAVLINGAMLIFGGnthNDTSLS-N 504
Cdd:PLN02193  173 QVGNKIYSFGGefTPNQPIDKH-----LYVFDLETRTWSISPATGDVPHLSclgvRMVSIGSTLYVFGG---RDASRQyN 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  505 GakcfsadFLAYDIACDEWKTL------PKPnlhrdvnRFGHSAVVINGSMYIFGGFSS-VLLNDILVYKPPNCKAFR-- 575
Cdd:PLN02193  245 G-------FYSFDTTTNEWKLLtpveegPTP-------RSFHSMAADEENVYVFGGVSAtARLKTLDSYNIVDKKWFHcs 310

                         170       180       190
                  ....*....|....*....|....*....|.
gi 755563242  576 --DEELCRNAGPGIKCVWNK-------NHCE 597
Cdd:PLN02193  311 tpGDSFSIRGGAGLEVVQGKvwvvygfNGCE 341
PHA03098 PHA03098
kelch-like protein; Provisional
 272-410 2.45e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 42.06  E-value: 2.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  272 FMWVIGGYTFNYSSFQMVLNYNLESSIWNVGavSRGPLQRYGHSLALYQENIFMYGGRMETSDGNVTDELWVFNVRSQSW 351
Cdd:PHA03098  391 LIYVIGGISKNDELLKTVECFSLNTNKWSKG--SPLPISHYGGCAIYHDGKIYVIGGISYIDNIKVYNIVESYNPVTNKW 468

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755563242  352 STKTPTVLGHSqqyaveghsahIMELDSRDVVMIVIFGYSAIYgYTSSIQEYHISSNTW 410
Cdd:PHA03098  469 TELSSLNFPRI-----------NASLCIFNNKIYVVGGDKYEY-YINEIEVYDDKTNTW 515
DSL pfam01414
Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain ...
 191-237 3.46e-03

Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain defined by structure.


Pssm-ID: 460202  Cd Length: 46  Bit Score: 36.83  E-value: 3.46e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 755563242   191 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 237
Cdd:pfam01414    1 CDENYYGSTCSK-FCRPRDDKFGHYTCDANGNK--VCLPGWTGPYCD 44
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 716-801 3.60e-03

C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels); CLECT_selectins_like: C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P(platlet)-, E(endothelial)-, and L(leukocyte)- selectins (sels). CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. P- E- and L-sels are cell adhesion receptors that mediate the initial attachment, tethering, and rolling of lymphocytes on inflamed vascular walls enabling subsequent lymphocyte adhesion and transmigration. L- sel is expressed constitutively on most leukocytes. P-sel is stored in the Weibel-Palade bodies of endothelial cells and in the alpha granules of platlets. E- sels are present on endothelial cells. Following platelet and/or endothelial cell activation P- sel is rapidly translocated to the cell surface and E-sel expression is induced. The initial step in leukocyte migration involves interactions of selectins with fucosylated, sialylated, and sulfated carbohydrate moieties on target ligands displayed on glycoprotein scaffolds on endothelial cells and leucocytes. A major ligand of P- E- and L-sels is PSGL-1 (P-sel glycoprotein ligand). Interactions of E- and P- sels with tumor cells may promote extravasation of cancer cells. Regulation of L-sel and P-sel function includes proteolytic shedding of the most extracellular portion (containing the CTLD) from the cell surface. Increased levels of the soluble form of P-sel in the plasma have been found in a number of diseases including coronary disease and diabetes. E- and P- sel also play roles in the development of synovial inflammation in inflammatory arthritis. Platelet P-sel, but not endothelial P-sel, plays a role in the inflammatory response and neointimal formation after arterial injury. Selectins may also function as signal-transducing receptors.


Pssm-ID: 153062  Cd Length: 115  Bit Score: 38.51  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563242  716 LRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKFTQQKVspWVGLRKINISyWGWEDMSPFTNTSLQWLPG 795
Cdd:cd03592     3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYY--WIDGNDINNE-GTWVDTDKKELEYKNWAPG 79


                  ....*.
gi 755563242  796 EPNDSG 801
Cdd:cd03592    80 EPNNGR 85
DSL smart00051
delta serrate ligand;
190-236 3.68e-03

delta serrate ligand;


Pssm-ID: 128366  Cd Length: 63  Bit Score: 37.31  E-value: 3.68e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 755563242    190 ECDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKLCvcNDSWQGPDC 236
Cdd:smart00051   20 TCDENYYGEGCNK-FCRPRDDFFGHYTCDENGNKGC--LEGWMGPYC 63
Kelch_6 pfam13964
Kelch motif;
311-353 4.40e-03

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 36.54  E-value: 4.40e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 755563242   311 RYGHSLALYQENIFMYGGRmeTSDGNVTDELWVFNVRSQSWST 353
Cdd:pfam13964    2 RTFHSVVSVGGYIYVFGGY--TNASPALNKLEVYNPLTKSWEE 42
Kelch_4 pfam13418
Galactose oxidase, central domain;
311-353 6.16e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.05  E-value: 6.16e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 755563242   311 RYGHSL-ALYQENIFMYGGRMEtsDGNVTDELWVFNVRSQSWST 353
Cdd:pfam13418    2 RAYHTStSIPDDTIYLFGGEGE--DGTLLSDLWVFDLSTNEWTR 43
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 537-568 9.83e-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: 35.28  E-value: 9.83e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 755563242   537 RFGHSAVVINGSMYIFGGF-SSVLLNDILVYKP 568
Cdd:pfam01344    2 RSGAGVVVVGGKIYVIGGFdGNQSLNSVEVYDP 34
 
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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