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Conserved domains on  [gi|1985390783|ref|XP_039403601|]
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attractin-like protein 1 isoform X8 [Mauremys reevesii]

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 ...
 817-943 2.34e-79

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: 256.74  E-value: 2.34e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  817 CGEGWSHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQK--YTVQKISPWVGLRKINISYWGWDD 894
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKhqMTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1985390783  895 MSPFTNTTLQWLPGEPNDSGFCAYLERAEVSGLKANPCTAKADGLVCEK 943
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
372-667 1.84e-22

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.07  E-value: 1.84e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  372 VGRASHKAVLHGKFMWVIGGYTFN--YSSFQMvlnYNLDSNIWNVVPvsKGPLQRYGHS-LALYQEDIYMYGGKIETNN- 447
Cdd:COG3055     11 TPRSEAAAALLDGKVYVAGGLSGGsaSNSFEV---YDPATNTWSELA--PLPGPPRHHAaAVAQDGKLYVFGGFTGANPs 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  448 GNVTDELWIFNINSQTWsTKIPAILVhgqqyAVEGHSAhiVELDSRdvvmIIIFGYSAVYGYTSSVQEYYIRSNSWlvaE 527
Cdd:COG3055     86 STPLNDVYVYDPATNTW-TKLAPMPT-----PRGGATA--LLLDGK----IYVVGGWDDGGNVAWVEVYDPATGTW---T 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  528 TKGAIVQGGYGHTSVYDEMTKsIYVHGGYkalpgnkyglvddlyRYEVNTRTWTILKESGFAKYLHSAVLISGAMLIFGG 607
Cdd:COG3055    151 QLAPLPTPRDHLAAAVLPDGK-ILVIGGR---------------NGSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGG 214

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  608 NTHndtslsngakcFSADFLAYDIACDEWKILPKPNLhrdlNRFGHTAVVSNGSMYIFGG 667
Cdd:COG3055    215 ESG-----------FSDEVEAYDPATNTWTALGELPT----PRHGHAAVLTDGKVYVIGG 259
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 162-277 1.22e-17

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: 79.76  E-value: 1.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  162 CQGRFKLTePSGYLT--DGPINYKYKTKCTWLIEGYPNAILRLRFNHFATE----CSWDHMYVYDGDSVYAPLIAVFSGl 235
Cdd:cd00041      1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFCG- 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1985390783  236 ivpevrgNETVPEVVTTSGYVLLHFFSDAAYNLTGFNIFYSI 277
Cdd:cd00041     79 -------STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1082-1127 7.89e-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: 50.05  E-value: 7.89e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1985390783 1082 ACQCNGHSTciNGNICDQ------CKNLTTGKQCETCMPGYYGDPTNGGQCT 1127
Cdd:cd00055      1 PCDCNGHGS--LSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 958-1007 3.76e-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: 45.39  E-value: 3.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1985390783  958 TCSLRTTCSNCT-SNGMECMWCSSTKRCVDSNAYiiSFPYGQCLEWQTATC 1007
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 ...
 304-350 3.20e-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: 3.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1985390783  304 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 350
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 ...
 817-943 2.34e-79

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: 256.74  E-value: 2.34e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  817 CGEGWSHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQK--YTVQKISPWVGLRKINISYWGWDD 894
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKhqMTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1985390783  895 MSPFTNTTLQWLPGEPNDSGFCAYLERAEVSGLKANPCTAKADGLVCEK 943
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
372-667 1.84e-22

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.07  E-value: 1.84e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  372 VGRASHKAVLHGKFMWVIGGYTFN--YSSFQMvlnYNLDSNIWNVVPvsKGPLQRYGHS-LALYQEDIYMYGGKIETNN- 447
Cdd:COG3055     11 TPRSEAAAALLDGKVYVAGGLSGGsaSNSFEV---YDPATNTWSELA--PLPGPPRHHAaAVAQDGKLYVFGGFTGANPs 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  448 GNVTDELWIFNINSQTWsTKIPAILVhgqqyAVEGHSAhiVELDSRdvvmIIIFGYSAVYGYTSSVQEYYIRSNSWlvaE 527
Cdd:COG3055     86 STPLNDVYVYDPATNTW-TKLAPMPT-----PRGGATA--LLLDGK----IYVVGGWDDGGNVAWVEVYDPATGTW---T 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  528 TKGAIVQGGYGHTSVYDEMTKsIYVHGGYkalpgnkyglvddlyRYEVNTRTWTILKESGFAKYLHSAVLISGAMLIFGG 607
Cdd:COG3055    151 QLAPLPTPRDHLAAAVLPDGK-ILVIGGR---------------NGSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGG 214

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  608 NTHndtslsngakcFSADFLAYDIACDEWKILPKPNLhrdlNRFGHTAVVSNGSMYIFGG 667
Cdd:COG3055    215 ESG-----------FSDEVEAYDPATNTWTALGELPT----PRHGHAAVLTDGKVYVIGG 259
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 162-277 1.22e-17

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: 79.76  E-value: 1.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  162 CQGRFKLTePSGYLT--DGPINYKYKTKCTWLIEGYPNAILRLRFNHFATE----CSWDHMYVYDGDSVYAPLIAVFSGl 235
Cdd:cd00041      1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFCG- 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1985390783  236 ivpevrgNETVPEVVTTSGYVLLHFFSDAAYNLTGFNIFYSI 277
Cdd:cd00041     79 -------STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 817-942 1.77e-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: 71.48  E-value: 1.77e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783   817 CGEGWSHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYTVQKiSPWVGLRKINISY-WGWDDM 895
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGsWQWSDG 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1985390783   896 SPFTNTTLqWLPGEPNDS-GFCAYLERAEVsGLKANPCTAKAdGLVCE 942
Cdd:smart00034   80 SGPVSYSN-WAPGEPNNSsGDCVVLSTSGG-KWNDVSCTSKL-PFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 835-943 2.31e-13

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 67.50  E-value: 2.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  835 RESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYTVqkiSPWVGLRKINIS-YWGWDDMSPFTNTTLQWLPGEPNDS 913
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNK---YFWIGLTDRKNEgTWKWVDGSPVNYTNWAPEPNNNGEN 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 1985390783  914 GFCAYLERAEvSGLKANPCTAKAdGLVCEK 943
Cdd:pfam00059   78 EDCVELSSSS-GKWNDENCNSKN-PFVCEK 105
CUB pfam00431
CUB domain;
162-275 3.52e-13

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 66.93  E-value: 3.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  162 CQGRFklTEPSGYLT--DGPINYKYKTKCTWLIEGYPNAILRLRFNHFATE----CSWDHMYVYDGDSVYAPLIAVFSGL 235
Cdd:pfam00431    1 CGGVL--TDSSGSISspNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1985390783  236 IVPEVrgnetvpeVVTTSGYVLLHFFSDAAYNLTGFNIFY 275
Cdd:pfam00431   79 GIPED--------IVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 179-275 2.41e-12

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: 64.33  E-value: 2.41e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783   179 PINYKYKTKCTWLIEGYPNAILRLRFNHFATE----CSWDHMYVYDGDSVYAPLIAVFSGLIVPEvrgnetvPEVVTTSG 254
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPP-------PVISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 1985390783   255 YVLLHFFSDAAYNLTGFNIFY 275
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1082-1127 7.89e-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: 50.05  E-value: 7.89e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1985390783 1082 ACQCNGHSTciNGNICDQ------CKNLTTGKQCETCMPGYYGDPTNGGQCT 1127
Cdd:cd00055      1 PCDCNGHGS--LSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 421-461 1.81e-06

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: 45.63  E-value: 1.81e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1985390783  421 PLQRYGHSLALYQEDIYMYGGKIeTNNGNVTDELWIFNINS 461
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGGYT-GGEGQPSDDVYVLSLPT 40
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 958-1007 3.76e-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: 45.39  E-value: 3.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1985390783  958 TCSLRTTCSNCT-SNGMECMWCSSTKRCVDSNAYiiSFPYGQCLEWQTATC 1007
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASS 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1083-1126 9.51e-06

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 43.88  E-value: 9.51e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1985390783 1083 CQCNGHSTciNGNICDQ------CKNLTTGKQCETCMPGYYGDP-TNGGQC 1126
Cdd:pfam00053    1 CDCNPHGS--LSDTCDPetgqclCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
PLN02153 PLN02153
epithiospecifier protein
 523-669 1.64e-05

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 48.83  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  523 WLVAETKGAIVQG---GYGHTSVYDEMtksiYVHGGykALPGNKYgLVDDLYRYEVNTRTWTILKESGFAKYLHS----A 595
Cdd:PLN02153     9 WIKVEQKGGKGPGprcSHGIAVVGDKL----YSFGG--ELKPNEH-IDKDLYVFDFNTHTWSIAPANGDVPRISClgvrM 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985390783  596 VLISGAMLIFGGNTHNdtslsngaKCFSaDFLAYDIACDEWKILPKPNLHRDLN-RFGHTAVVSNGSMYIFGGFS 669
Cdd:PLN02153    82 VAVGTKLYIFGGRDEK--------REFS-DFYSYDTVKNEWTFLTKLDEEGGPEaRTFHSMASDENHVYVFGGVS 147
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1083-1123 4.08e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.22  E-value: 4.08e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1985390783  1083 CQCNGHSTciNGNICDQ------CKNLTTGKQCETCMPGYYGDPTNG 1123
Cdd:smart00180    1 CDCDPGGS--ASGTCDPdtgqceCKPNVTGRRCDRCAPGYYGDGPPG 45
DSL pfam01414
Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain ...
 304-350 3.20e-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: 3.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1985390783  304 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 350
Cdd:pfam01414    1 CDENYYGSTCSK-FCRPRDDKFGHYTCDANGNK--VCLPGWTGPYCD 44
DSL smart00051
delta serrate ligand;
303-349 3.72e-03

delta serrate ligand;


Pssm-ID: 128366  Cd Length: 63  Bit Score: 37.31  E-value: 3.72e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1985390783   303 ECDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKLCvcNDSWQGPDC 349
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 ...
 817-943 2.34e-79

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: 256.74  E-value: 2.34e-79
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  817 CGEGWSHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQK--YTVQKISPWVGLRKINISYWGWDD 894
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKhqMTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1985390783  895 MSPFTNTTLQWLPGEPNDSGFCAYLERAEVSGLKANPCTAKADGLVCEK 943
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
372-667 1.84e-22

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 99.07  E-value: 1.84e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  372 VGRASHKAVLHGKFMWVIGGYTFN--YSSFQMvlnYNLDSNIWNVVPvsKGPLQRYGHS-LALYQEDIYMYGGKIETNN- 447
Cdd:COG3055     11 TPRSEAAAALLDGKVYVAGGLSGGsaSNSFEV---YDPATNTWSELA--PLPGPPRHHAaAVAQDGKLYVFGGFTGANPs 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  448 GNVTDELWIFNINSQTWsTKIPAILVhgqqyAVEGHSAhiVELDSRdvvmIIIFGYSAVYGYTSSVQEYYIRSNSWlvaE 527
Cdd:COG3055     86 STPLNDVYVYDPATNTW-TKLAPMPT-----PRGGATA--LLLDGK----IYVVGGWDDGGNVAWVEVYDPATGTW---T 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  528 TKGAIVQGGYGHTSVYDEMTKsIYVHGGYkalpgnkyglvddlyRYEVNTRTWTILKESGFAKYLHSAVLISGAMLIFGG 607
Cdd:COG3055    151 QLAPLPTPRDHLAAAVLPDGK-ILVIGGR---------------NGSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGG 214

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  608 NTHndtslsngakcFSADFLAYDIACDEWKILPKPNLhrdlNRFGHTAVVSNGSMYIFGG 667
Cdd:COG3055    215 ESG-----------FSDEVEAYDPATNTWTALGELPT----PRHGHAAVLTDGKVYVIGG 259
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
370-611 1.87e-20

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 92.91  E-value: 1.87e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  370 PSVGRASHKAVLHGKFMWVIGGYTFNYSSFQM---VLNYNLDSNIWNVVPVSkgPLQRYGHSLALYQEDIYMYGGkieTN 446
Cdd:COG3055     57 PGPPRHHAAAVAQDGKLYVFGGFTGANPSSTPlndVYVYDPATNTWTKLAPM--PTPRGGATALLLDGKIYVVGG---WD 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  447 NGNVTDELWIFNINSQTWSTKIPAILvhgqqyAVEGHSAHIVELDsrdvvMIIIFGysavyGYTSSVQeyyirSNSWlva 526
Cdd:COG3055    132 DGGNVAWVEVYDPATGTWTQLAPLPT------PRDHLAAAVLPDG-----KILVIG-----GRNGSGF-----SNTW--- 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  527 ETKGAIVQGGYGHTSVYdeMTKSIYVHGGYkalpgnkYGLVDDLYRYEVNTRTWTILKESGFAKYLHSAVLISGAMLIFG 606
Cdd:COG3055    188 TTLAPLPTARAGHAAAV--LGGKILVFGGE-------SGFSDEVEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYVIG 258


                   ....*
gi 1985390783  607 GNTHN 611
Cdd:COG3055    259 GETKP 263
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 162-277 1.22e-17

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: 79.76  E-value: 1.22e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  162 CQGRFKLTePSGYLT--DGPINYKYKTKCTWLIEGYPNAILRLRFNHFATE----CSWDHMYVYDGDSVYAPLIAVFSGl 235
Cdd:cd00041      1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFCG- 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1985390783  236 ivpevrgNETVPEVVTTSGYVLLHFFSDAAYNLTGFNIFYSI 277
Cdd:cd00041     79 -------STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
421-681 1.18e-15

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 79.04  E-value: 1.18e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  421 PLQRYGHSLALYQEDIYMYGGKietNNGNVTDELWIFNINSQTWSTK--IPAILVHgqqyavegHSAHIVeLDSRdvvmI 498
Cdd:COG3055     10 PTPRSEAAAALLDGKVYVAGGL---SGGSASNSFEVYDPATNTWSELapLPGPPRH--------HAAAVA-QDGK----L 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  499 IIF-GYSAVYG---YTSSVQEYYIRSNSWlvaETKGAIVQGGYGHTSVYDEmtKSIYVHGGYkalpgNKYGLVDDLYRYE 574
Cdd:COG3055     74 YVFgGFTGANPsstPLNDVYVYDPATNTW---TKLAPMPTPRGGATALLLD--GKIYVVGGW-----DDGGNVAWVEVYD 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  575 VNTRTWTILKESGFAKYLHSA-VLISGAMLIFGGNthNDTSLSNgakcfsadflaydiacdEWKILPkpnlHRDLNRFGH 653
Cdd:COG3055    144 PATGTWTQLAPLPTPRDHLAAaVLPDGKILVIGGR--NGSGFSN-----------------TWTTLA----PLPTARAGH 200

                          250       260
                   ....*....|....*....|....*...
gi 1985390783  654 TAVVSNGSMYIFGGFSSVlLNDILVYKP 681
Cdd:COG3055    201 AAAVLGGKILVFGGESGF-SDEVEAYDP 227
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 828-943 2.65e-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: 73.42  E-value: 2.65e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  828 CLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYTVQKIspWVGLRKINI-SYWGWDDMSPFTNTTlQWL 906
Cdd:cd00037      2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDV--WIGLNDLSSeGTWKWSDGSPLVDYT-NWA 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1985390783  907 PGEPN--DSGFCAYLERAEVSGLKANPCTAKAdGLVCEK 943
Cdd:cd00037     79 PGEPNpgGSEDCVVLSSSSDGKWNDVSCSSKL-PFICEK 116
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 817-942 1.77e-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: 71.48  E-value: 1.77e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783   817 CGEGWSHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYTVQKiSPWVGLRKINISY-WGWDDM 895
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGsWQWSDG 79

                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....*...
gi 1985390783   896 SPFTNTTLqWLPGEPNDS-GFCAYLERAEVsGLKANPCTAKAdGLVCE 942
Cdd:smart00034   80 SGPVSYSN-WAPGEPNNSsGDCVVLSTSGG-KWNDVSCTSKL-PFVCE 124
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 835-943 2.31e-13

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 67.50  E-value: 2.31e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  835 RESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYTVqkiSPWVGLRKINIS-YWGWDDMSPFTNTTLQWLPGEPNDS 913
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKSNK---YFWIGLTDRKNEgTWKWVDGSPVNYTNWAPEPNNNGEN 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 1985390783  914 GFCAYLERAEvSGLKANPCTAKAdGLVCEK 943
Cdd:pfam00059   78 EDCVELSSSS-GKWNDENCNSKN-PFVCEK 105
CUB pfam00431
CUB domain;
162-275 3.52e-13

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 66.93  E-value: 3.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  162 CQGRFklTEPSGYLT--DGPINYKYKTKCTWLIEGYPNAILRLRFNHFATE----CSWDHMYVYDGDSVYAPLIAVFSGL 235
Cdd:pfam00431    1 CGGVL--TDSSGSISspNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1985390783  236 IVPEVrgnetvpeVVTTSGYVLLHFFSDAAYNLTGFNIFY 275
Cdd:pfam00431   79 GIPED--------IVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 179-275 2.41e-12

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: 64.33  E-value: 2.41e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783   179 PINYKYKTKCTWLIEGYPNAILRLRFNHFATE----CSWDHMYVYDGDSVYAPLIAVFSGLIVPEvrgnetvPEVVTTSG 254
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPP-------PVISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 1985390783   255 YVLLHFFSDAAYNLTGFNIFY 275
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
579-681 4.93e-09

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 59.01  E-value: 4.93e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  579 TWTILKESGFAKYLHSAVLISGAMLIFGGNTHNDTSlsngakcfsADFLAYDIACDEWKILPKPNLHRdlnRFGHTAVVS 658
Cdd:COG3055      2 TWSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSAS---------NSFEVYDPATNTWSELAPLPGPP---RHHAAAVAQ 69

                           90       100
                   ....*....|....*....|....*...
gi 1985390783  659 NGSMYIFGGF-----SSVLLNDILVYKP 681
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 ...
 817-919 4.61e-08

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: 53.08  E-value: 4.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  817 CGEGWSHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFvldeIQKYTVQKISPWVGLRKINI-SYWGWDDM 895
Cdd:cd03590      1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEF----ISKILSGNRSYWIGLSDEETeGEWKWVDG 76

                           90       100
                   ....*....|....*....|....*...
gi 1985390783  896 SPFTNTTLQWLPGEPNDSGF----CAYL 919
Cdd:cd03590     77 TPLNSSKTFWHPGEPNNWGGggedCAEL 104
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1082-1127 7.89e-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: 50.05  E-value: 7.89e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1985390783 1082 ACQCNGHSTciNGNICDQ------CKNLTTGKQCETCMPGYYGDPTNGGQCT 1127
Cdd:cd00055      1 PCDCNGHGS--LSGQCDPgtgqceCKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 817-943 1.56e-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: 48.48  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  817 CGEGWSHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFvldeIQKYtVQKISPWVGLRKINISY-WGWDDM 895
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEF----LQSQ-IGSSSYWIGLSREKSEKpWKWIDG 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1985390783  896 SPFTNttlqWL-PGEPNDSGFCAYLERaevSGLKANPCTAKAdGLVCEK 943
Cdd:cd03593     76 SPLNN----LFnIRGSTKSGNCAYLSS---TGIYSEDCSTKK-RWICEK 116
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 421-461 1.81e-06

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: 45.63  E-value: 1.81e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1985390783  421 PLQRYGHSLALYQEDIYMYGGKIeTNNGNVTDELWIFNINS 461
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGGYT-GGEGQPSDDVYVLSLPT 40
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 958-1007 3.76e-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: 45.39  E-value: 3.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1985390783  958 TCSLRTTCSNCT-SNGMECMWCSSTKRCVDSNAYiiSFPYGQCLEWQTATC 1007
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASS 49
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1083-1126 9.51e-06

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 43.88  E-value: 9.51e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1985390783 1083 CQCNGHSTciNGNICDQ------CKNLTTGKQCETCMPGYYGDP-TNGGQC 1126
Cdd:pfam00053    1 CDCNPHGS--LSDTCDPetgqclCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
PLN02153 PLN02153
epithiospecifier protein
 523-669 1.64e-05

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 48.83  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  523 WLVAETKGAIVQG---GYGHTSVYDEMtksiYVHGGykALPGNKYgLVDDLYRYEVNTRTWTILKESGFAKYLHS----A 595
Cdd:PLN02153     9 WIKVEQKGGKGPGprcSHGIAVVGDKL----YSFGG--ELKPNEH-IDKDLYVFDFNTHTWSIAPANGDVPRISClgvrM 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985390783  596 VLISGAMLIFGGNTHNdtslsngaKCFSaDFLAYDIACDEWKILPKPNLHRDLN-RFGHTAVVSNGSMYIFGGFS 669
Cdd:PLN02153    82 VAVGTKLYIFGGRDEK--------REFS-DFYSYDTVKNEWTFLTKLDEEGGPEaRTFHSMASDENHVYVFGGVS 147
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 817-923 2.58e-05

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: 45.06  E-value: 2.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  817 CGEGWSHIGDACLRINSSRESYDNAKLYC--YNLSGNLASLTTSKEVEFVLDEIQKYTVQKISPWVGLRKINISY-WGWD 893
Cdd:cd03594      1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCqkYGPGAHLASIHSPAEAAAIASLISSYQKAYQPVWIGLHDPQQSRgWEWS 80

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1985390783  894 DMSPFTNTTlqWLPGEP-NDSGFCAYLERAE 923
Cdd:cd03594     81 DGSKLDYRS--WDRNPPyARGGYCAELSRST 109
PHA03098 PHA03098
kelch-like protein; Provisional
 379-645 4.52e-05

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 47.84  E-value: 4.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  379 AVLHGKFMWVIGGYTFNYSSFQMVLNYNLDSNIWNVVPVSKGPlqRYGHSLALYQEDIYMYGGkIETNNGNVTDELWIFn 458
Cdd:PHA03098   290 SVVLNNVIYFIGGMNKNNLSVNSVVSYDTKTKSWNKVPELIYP--RKNPGVTVFNNRIYVIGG-IYNSISLNTVESWKP- 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  459 iNSQTWSTKIPAILVHgqqyavegHSAHIVELDSRDVVMiiiFGYSAVYGYTSSVQEYYIRSNSW-LVAETKGAIVqggY 537
Cdd:PHA03098   366 -GESKWREEPPLIFPR--------YNPCVVNVNNLIYVI---GGISKNDELLKTVECFSLNTNKWsKGSPLPISHY---G 430

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  538 GHTSVYDEMtksIYVHGGYKALpgNKYGLVDDLYRYEVNTRTWTILKESGFAKYLHSAVLISGAMLIFGGNTHNDtslsn 617
Cdd:PHA03098   431 GCAIYHDGK---IYVIGGISYI--DNIKVYNIVESYNPVTNKWTELSSLNFPRINASLCIFNNKIYVVGGDKYEY----- 500

                          250       260
                   ....*....|....*....|....*...
gi 1985390783  618 gakcFSADFLAYDIACDEWKILPKPNLH 645
Cdd:PHA03098   501 ----YINEIEVYDDKTNTWTLFCKFPKV 524
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 817-936 4.85e-05

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: 44.66  E-value: 4.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  817 CGEGWSHIGDACLRINSSRESYDNAKLYCYN-----LSGNLASLTTSKEVEFVLDEIQKYTVQKISP--WVGL-RKINIS 888
Cdd:cd03589      1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDLFESSRGPDTPYglWIGLhDRTSEG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1985390783  889 YWGWDDMSPFTNTtlQWLPGEPNDSGF---CAYLERAEVSGLKAN--PCTAKA 936
Cdd:cd03589     81 PFEWTDGSPVDFT--KWAGGQPDNYGGnedCVQMWRRGDAGQSWNdmPCDAVF 131
PLN02153 PLN02153
epithiospecifier protein
 419-673 6.56e-05

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 46.90  E-value: 6.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  419 KGPLQRYGHSLALYQEDIYMYGGKIeTNNGNVTDELWIFNINSQTWSTKIPailvhgqqyaveghsahiveldSRDVVMI 498
Cdd:PLN02153    18 KGPGPRCSHGIAVVGDKLYSFGGEL-KPNEHIDKDLYVFDFNTHTWSIAPA----------------------NGDVPRI 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  499 IIFGYSAVygytssvqeyyirsnswlvaetkgaivqggyghtsvydEMTKSIYVHGGYkalpgNKYGLVDDLYRYEVNTR 578
Cdd:PLN02153    75 SCLGVRMV--------------------------------------AVGTKLYIFGGR-----DEKREFSDFYSYDTVKN 111

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  579 TWTIL----KESG-FAKYLHSAVLISGAMLIFGGNTHNdtSLSNGAKCFSAdFLAYDIACDEWKILPKPNLHRDlNRFGH 653
Cdd:PLN02153   112 EWTFLtkldEEGGpEARTFHSMASDENHVYVFGGVSKG--GLMKTPERFRT-IEAYNIADGKWVQLPDPGENFE-KRGGA 187

                          250       260
                   ....*....|....*....|
gi 1985390783  654 TAVVSNGSMYIFGGFSSVLL 673
Cdd:PLN02153   188 GFAVVQGKIWVVYGFATSIL 207
PLN02193 PLN02193
nitrile-specifier protein
 369-464 7.83e-05

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 46.87  E-value: 7.83e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  369 SPSVGRASHKAVLH------GKFMWVIGGYTFN--YSSFqmvlnYNLDS--NIWNVV-PVSKGPLQRYGHSLALYQEDIY 437
Cdd:PLN02193   208 SPATGDVPHLSCLGvrmvsiGSTLYVFGGRDASrqYNGF-----YSFDTttNEWKLLtPVEEGPTPRSFHSMAADEENVY 282

                           90       100
                   ....*....|....*....|....*..
gi 1985390783  438 MYGGKIETNNGNVTDElwiFNINSQTW 464
Cdd:PLN02193   283 VFGGVSATARLKTLDS---YNIVDKKW 306
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 817-917 3.24e-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: 41.79  E-value: 3.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  817 CGEGWSHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYTvqkispWVGLRKINISY-WGWDDM 895
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ------WIGLNDRTIEGdFRWSDG 74

                           90       100
                   ....*....|....*....|....
gi 1985390783  896 SP--FTNttlqWLPGEPnDSGFCA 917
Cdd:cd03588     75 HPlqFEN----WRPNQP-DNFFAT 93
PLN02193 PLN02193
nitrile-specifier protein
 441-670 3.35e-04

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 44.95  E-value: 3.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  441 GKIETNNGNVTDELWIFNINSQTWSTKIPAILVHGQQYAVEGhsAHIVELDSRDVVMIIIFGysavyGYTSSVQEYYIRS 520
Cdd:PLN02193    79 GYREKVNDMTSEMITFLSFKTYKGKTSHPIEKRPGVKFVLQG--GKIVGFHGRSTDVLHSLG-----AYISLPSTPKLLG 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  521 NsWLVAETKGAivqgGYGHTSVYD--EMTKSIYVHGG--YKALPGNKYglvddLYRYEVNTRTWTILKESGFAKYLH--- 593
Cdd:PLN02193   152 K-WIKVEQKGE----GPGLRCSHGiaQVGNKIYSFGGefTPNQPIDKH-----LYVFDLETRTWSISPATGDVPHLSclg 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  594 -SAVLISGAMLIFGGnthNDTSLS-NGakcfsadFLAYDIACDEWKIL------PKPnlhrdlnRFGHTAVVSNGSMYIF 665
Cdd:PLN02193   222 vRMVSIGSTLYVFGG---RDASRQyNG-------FYSFDTTTNEWKLLtpveegPTP-------RSFHSMAADEENVYVF 284


                   ....*
gi 1985390783  666 GGFSS 670
Cdd:PLN02193   285 GGVSA 289
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1083-1123 4.08e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.22  E-value: 4.08e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1985390783  1083 CQCNGHSTciNGNICDQ------CKNLTTGKQCETCMPGYYGDPTNG 1123
Cdd:smart00180    1 CDCDPGGS--ASGTCDPdtgqceCKPNVTGRRCDRCAPGYYGDGPPG 45
Kelch_6 pfam13964
Kelch motif;
424-466 4.30e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 39.24  E-value: 4.30e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1985390783  424 RYGHSLALYQEDIYMYGGkiETNNGNVTDELWIFNINSQTWST 466
Cdd:pfam13964    2 RTFHSVVSVGGYIYVFGG--YTNASPALNKLEVYNPLTKSWEE 42
Kelch_4 pfam13418
Galactose oxidase, central domain;
538-583 4.35e-04

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 39.13  E-value: 4.35e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1985390783  538 GHTSVYDEmTKSIYVHGGYkalpGNKYGLVDDLYRYEVNTRTWTIL 583
Cdd:pfam13418    4 YHTSTSIP-DDTIYLFGGE----GEDGTLLSDLWVFDLSTNEWTRL 44
CLECT_DGCR2_like cd03599
C-type lectin-like domain (CTLD) of the type found in DGCR2, an integral membrane protein ...
 817-928 9.55e-04

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: 41.06  E-value: 9.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  817 CGEGWSHI-GDA-CLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVL----DEIQKYTVQK--ISPWVGLRKI--- 885
Cdd:cd03599      1 CPSGWHHYeGTAsCYKVYLSGENYWDAVQTCQKVNGSLATFTTDQELQFILaqewDFDERVFGRKdqCKFWVGYQYVitn 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1985390783  886 -NISYWG-WDdmSPFTNTTLQWLPGEP--------NDSGFCAYLERAEVSGLK 928
Cdd:cd03599     81 rNHSLEGrWE--VAYKGSMEVFLPPEPifatgmstNDNVFCAQLQCFQIPSLR 131
PHA03098 PHA03098
kelch-like protein; Provisional
 430-679 2.23e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 42.45  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  430 ALYQEDIYMYGGKIetNNGNVTDELWIFNINSQTWsTKIPAILVHGQQYAVeghsahiVELDSRdvvmIIIFGYSAVYGY 509
Cdd:PHA03098   291 VVLNNVIYFIGGMN--KNNLSVNSVVSYDTKTKSW-NKVPELIYPRKNPGV-------TVFNNR----IYVIGGIYNSIS 356

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  510 TSSVQEYYIRSNSWlvaETKGAIVQGGYGHTSVYDEMTksIYVHGGYkalpgNKYG-LVDDLYRYEVNTRTWTILKESGF 588
Cdd:PHA03098   357 LNTVESWKPGESKW---REEPPLIFPRYNPCVVNVNNL--IYVIGGI-----SKNDeLLKTVECFSLNTNKWSKGSPLPI 426

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  589 AKYLHSAVLISGAMLIFGGNTHndtslSNGAKCFSADFLaYDIACDEWKILPKPNLHrdlnRFGHTAVVSNGSMYIFGGF 668
Cdd:PHA03098   427 SHYGGCAIYHDGKIYVIGGISY-----IDNIKVYNIVES-YNPVTNKWTELSSLNFP----RINASLCIFNNKIYVVGGD 496

                          250
                   ....*....|..
gi 1985390783  669 S-SVLLNDILVY 679
Cdd:PHA03098   497 KyEYYINEIEVY 508
Kelch_3 pfam13415
Galactose oxidase, central domain;
547-598 2.33e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 37.27  E-value: 2.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1985390783  547 TKSIYVHGGYKALPGNKYglvDDLYRYEVNTRTWTILKESGFAKYLHSAVLI 598
Cdd:pfam13415    1 GDKLYIFGGLGFDGQTRL---NDLYVYDLDTNTWTQIGDLPPPRSGHSATYI 49
Kelch_4 pfam13418
Galactose oxidase, central domain;
424-466 2.88e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.82  E-value: 2.88e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1985390783  424 RYGHSL-ALYQEDIYMYGGkiETNNGNVTDELWIFNINSQTWST 466
Cdd:pfam13418    2 RAYHTStSIPDDTIYLFGG--EGEDGTLLSDLWVFDLSTNEWTR 43
DSL pfam01414
Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain ...
 304-350 3.20e-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: 3.20e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1985390783  304 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 350
Cdd:pfam01414    1 CDENYYGSTCSK-FCRPRDDKFGHYTCDANGNK--VCLPGWTGPYCD 44
DSL smart00051
delta serrate ligand;
303-349 3.72e-03

delta serrate ligand;


Pssm-ID: 128366  Cd Length: 63  Bit Score: 37.31  E-value: 3.72e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1985390783   303 ECDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKLCvcNDSWQGPDC 349
Cdd:smart00051   20 TCDENYYGEGCNK-FCRPRDDFFGHYTCDENGNKGC--LEGWMGPYC 63
Kelch_3 pfam13415
Galactose oxidase, central domain;
383-432 4.65e-03

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 36.50  E-value: 4.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1985390783  383 GKFMWVIGGYTF-NYSSFQMVLNYNLDSNIWnvVPVSKGPLQRYGHSLALY 432
Cdd:pfam13415    1 GDKLYIFGGLGFdGQTRLNDLYVYDLDTNTW--TQIGDLPPPRSGHSATYI 49
CLECT_thrombomodulin_like cd03600
C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, ...
 824-942 6.49e-03

C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR; CLECT_thrombomodulin_like: C-type lectin-like domain (CTLD) of the type found in human thrombomodulin(TM), Endosialin, C14orf27, and C1qR. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. In these thrombomodulin-like proteins the residues involved in coordinating Ca2+ in the classical MBP-A CTLD are not conserved. TM exerts anti-fibrinolytic and anti-inflammatory activity. TM also regulates blood coagulation in the anticoagulant protein C pathway. In this pathway, the procoagulant properties of thrombin (T) are lost when it binds TM. TM also plays a key role in tumor biology. It is expressed on endothelial cells and on several type of tumor cell including squamous cell carcinoma. Loss of TM expression correlates with advanced stage and poor prognosis. Loss of function of TM function may be associated with arterial or venous thrombosis and with late fetal loss. Soluble molecules of TM retaining the CTLD are detected in human plasma and urine where higher levels indicate injury and/or enhanced turnover of the endothelium. C1qR is expressed on endothelial cells and stem cells. It is also expressed on monocots and neutrophils, where it is subject to ectodomain shedding. Soluble forms of C1qR retaining the CTLD is detected in human plasma. C1qR modulates the phagocytosis of apoptotic cells in vivo. C1qR-deficient mice are defective in clearance of apoptotic cells in vivo. The cytoplasmic tail of C1qR, C-terminal to the CTLD of CD93, contains a PDZ binding domain which interacts with the PDZ domain-containing adaptor protein, GIPC. The juxtamembrane region of this tail interacts with the ezrin/radixin/moesin family. Endosialin functions in the growth and progression of abdominal tumors and is expressed in the stroma of several tumors.


Pssm-ID: 153070  Cd Length: 141  Bit Score: 38.57  E-value: 6.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985390783  824 IGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVL----DEIQKYTVQKISPWVGLRKI------------NI 887
Cdd:cd03600      2 VSDACYTLHPQKLTFLEAQRSCIELGGNLATVRSGEEADVVSlllaAGPGRHGRGSLRLWIGLQREprqcsdpslplrGF 81

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985390783  888 SYWGWDDMSPFTNttlqWL--PGEPNDSGFCAYLERAEVS----GLKANPCTAKADGLVCE 942
Cdd:cd03600     82 SWVTGDQDTDFSN----WLqePAGTCTSPRCVALSAAGSTpdnlKWKDGPCSARADGYLCK 138
 
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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