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Conserved domains on  [gi|1910408511|ref|XP_036078038|]
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attractin-like protein 1 isoform X6 [Rousettus aegyptiacus]

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 ...
 920-1046 1.42e-81

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: 263.67  E-value: 1.42e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  920 CGEGWNHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQK--YTQQKVSPWVGLRKINISYWGWED 997
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKhqMTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1910408511  998 MSPFTNTTLQWLPGEPNDSGFCAYLERAAVAGLKANPCTSMADGLVCEK 1046
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
475-770 4.81e-23

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 101.00  E-value: 4.81e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  475 VGRASHKAVLHGKFMWVIGGYTFN--YSSFQMvlnYNLENSIWNvgTVSRGPLQRYGHS-LALYQENIFMYGGRIETND- 550
Cdd:COG3055     11 TPRSEAAAALLDGKVYVAGGLSGGsaSNSFEV---YDPATNTWS--ELAPLPGPPRHHAaAVAQDGKLYVFGGFTGANPs 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  551 GNVTDELWVFNIRSQSWSTKTPTVIGHGqqyaveghsAHIMELDSRDvvmIIIFGYSAIYGYSSSIQEYHISSNTWlvpE 630
Cdd:COG3055     86 STPLNDVYVYDPATNTWTKLAPMPTPRG---------GATALLLDGK---IYVVGGWDDGGNVAWVEVYDPATGTW---T 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  631 TKGAIVQGGYGHTSVYDEITKsIYVHGGYKalpgnkyglvddlykYEVNTKTWTILKESGFARYLHSAVLINGAMLIFGG 710
Cdd:COG3055    151 QLAPLPTPRDHLAAAVLPDGK-ILVIGGRN---------------GSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGG 214

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  711 NTHndtslsngakcFSADFLAYDIACDEWKTLPKPNlhrdVNRFGHSAVVINGSMYIFGG 770
Cdd:COG3055    215 ESG-----------FSDEVEAYDPATNTWTALGELP----TPRHGHAAVLTDGKVYVIGG 259
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 272-380 1.13e-16

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: 77.45  E-value: 1.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  272 TEPSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLIAVLSGlivpeirg 345
Cdd:cd00041      7 ASTSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFCG-------- 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1910408511  346 NETVPEVVTTSGYALLHFFSDAAYNLTGFNIFYSI 380
Cdd:cd00041     79 STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1185-1230 1.15e-06

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


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 46.96  E-value: 1.15e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1910408511 1185 ACQCNGHSTciNHNVCE------HCKNLTTGKQCQDCMPGYYGDPTNGGQCT 1230
Cdd:cd00055      1 PCDCNGHGS--LSGQCDpgtgqcECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 1061-1110 2.55e-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: 45.78  E-value: 2.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1910408511 1061 PCSLRTSCSNCT-SNGMECMWCSSTRRCVDSNAYiiSFPYGQCLEWQTATC 1110
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQASS 49
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 86-266 2.08e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511   86 PGAPRARGPHLGGHHPSAARPGGAGARGgvpgSCQGGARPRRRACGGSAGRRGAGGPssaprapavapaagsRRRREHGC 165
Cdd:PHA03247  2628 PPSPSPAANEPDPHPPPTVPPPERPRDD----PAPGRVSRPRRARRLGRAAQASSPP---------------QRPRRRAA 2688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  166 WGAAGCVPGGAGLTPAFRLPPPALGAPTSRLPLAPALPGARGWAPRQLARAAGEAGPLAGSPPPPAGSPPR--VPSGAPR 243
Cdd:PHA03247  2689 RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARppTTAGPPA 2768

                          170       180
                   ....*....|....*....|....*
gi 1910408511  244 VAcsagsqPPAGP--GAPRRWARPA 266
Cdd:PHA03247  2769 PA------PPAAPaaGPPRRLTRPA 2787
DSL super family cl19567
Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain ...
 407-453 2.32e-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: 37.22  E-value: 2.32e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1910408511  407 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 453
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 ...
 920-1046 1.42e-81

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: 263.67  E-value: 1.42e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  920 CGEGWNHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQK--YTQQKVSPWVGLRKINISYWGWED 997
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKhqMTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1910408511  998 MSPFTNTTLQWLPGEPNDSGFCAYLERAAVAGLKANPCTSMADGLVCEK 1046
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
475-770 4.81e-23

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 101.00  E-value: 4.81e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  475 VGRASHKAVLHGKFMWVIGGYTFN--YSSFQMvlnYNLENSIWNvgTVSRGPLQRYGHS-LALYQENIFMYGGRIETND- 550
Cdd:COG3055     11 TPRSEAAAALLDGKVYVAGGLSGGsaSNSFEV---YDPATNTWS--ELAPLPGPPRHHAaAVAQDGKLYVFGGFTGANPs 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  551 GNVTDELWVFNIRSQSWSTKTPTVIGHGqqyaveghsAHIMELDSRDvvmIIIFGYSAIYGYSSSIQEYHISSNTWlvpE 630
Cdd:COG3055     86 STPLNDVYVYDPATNTWTKLAPMPTPRG---------GATALLLDGK---IYVVGGWDDGGNVAWVEVYDPATGTW---T 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  631 TKGAIVQGGYGHTSVYDEITKsIYVHGGYKalpgnkyglvddlykYEVNTKTWTILKESGFARYLHSAVLINGAMLIFGG 710
Cdd:COG3055    151 QLAPLPTPRDHLAAAVLPDGK-ILVIGGRN---------------GSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGG 214

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  711 NTHndtslsngakcFSADFLAYDIACDEWKTLPKPNlhrdVNRFGHSAVVINGSMYIFGG 770
Cdd:COG3055    215 ESG-----------FSDEVEAYDPATNTWTALGELP----TPRHGHAAVLTDGKVYVIGG 259
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 272-380 1.13e-16

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: 77.45  E-value: 1.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  272 TEPSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLIAVLSGlivpeirg 345
Cdd:cd00041      7 ASTSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFCG-------- 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1910408511  346 NETVPEVVTTSGYALLHFFSDAAYNLTGFNIFYSI 380
Cdd:cd00041     79 STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 938-1046 4.87e-15

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 72.51  E-value: 4.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  938 RESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYtqqKVSPWVGLRKINIS-YWGWEDMSPFTNTTLQWLPGEPNDS 1016
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKS---NKYFWIGLTDRKNEgTWKWVDGSPVNYTNWAPEPNNNGEN 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 1910408511 1017 GFCAYLERAAvAGLKANPCTSMAdGLVCEK 1046
Cdd:pfam00059   78 EDCVELSSSS-GKWNDENCNSKN-PFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 920-1022 7.64e-15

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: 72.63  E-value: 7.64e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511   920 CGEGWNHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYTQQKvSPWVGLRKINISY-WGWEDM 998
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGsWQWSDG 79

                            90       100
                    ....*....|....*....|....*
gi 1910408511   999 SPFTNTTLqWLPGEPNDS-GFCAYL 1022
Cdd:smart00034   80 SGPVSYSN-WAPGEPNNSsGDCVVL 103
CUB pfam00431
CUB domain;
270-378 6.56e-12

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 63.47  E-value: 6.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  270 RLTEPSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLIAVLSGLIVPei 343
Cdd:pfam00431    4 VLTDSSGSISspNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGSGIP-- 81

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1910408511  344 rgnetvPEVVTTSGYALLHFFSDAAYNLTGFNIFY 378
Cdd:pfam00431   82 ------EDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 282-378 6.63e-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: 63.56  E-value: 6.63e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511   282 PINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLIAVLSGLIVPEirgnetvPEVVTTSG 357
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPP-------PVISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 1910408511   358 YALLHFFSDAAYNLTGFNIFY 378
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1185-1230 1.15e-06

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 46.96  E-value: 1.15e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1910408511 1185 ACQCNGHSTciNHNVCE------HCKNLTTGKQCQDCMPGYYGDPTNGGQCT 1230
Cdd:cd00055      1 PCDCNGHGS--LSGQCDpgtgqcECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 1061-1110 2.55e-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: 45.78  E-value: 2.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1910408511 1061 PCSLRTSCSNCT-SNGMECMWCSSTRRCVDSNAYiiSFPYGQCLEWQTATC 1110
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 ...
 524-564 5.44e-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: 44.48  E-value: 5.44e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1910408511  524 PLQRYGHSLALYQENIFMYGGRIeTNDGNVTDELWVFNIRS 564
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGGYT-GGEGQPSDDVYVLSLPT 40
PHA03098 PHA03098
kelch-like protein; Provisional
 485-782 6.92e-06

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 50.54  E-value: 6.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  485 HGKFMWVIGGYTFNYSSfqMVLNYNLENSIWNVgtVSRGPLQRYGHslALYQENIFMYGGRIETNDgnVTDELWVFNIRS 564
Cdd:PHA03098   249 FGSIIYIHITMSIFTYN--YITNYSPLSEINTI--IDIHYVYCFGS--VVLNNVIYFIGGMNKNNL--SVNSVVSYDTKT 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  565 QSWsTKTPTVIghgqqYAVEGHSAHImeLDSRdvvmiiIFGYSAIY--GYSSSIQEYHISSNTW------LVPETKGAIV 636
Cdd:PHA03098   321 KSW-NKVPELI-----YPRKNPGVTV--FNNR------IYVIGGIYnsISLNTVESWKPGESKWreepplIFPRYNPCVV 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  637 qggyghtsVYDEItksIYVHGGYkalpgNKYG-LVDDLYKYEVNTKTWTILKESGFARYLHSAVLINGAMLIFGGNTHnd 715
Cdd:PHA03098   387 --------NVNNL---IYVIGGI-----SKNDeLLKTVECFSLNTNKWSKGSPLPISHYGGCAIYHDGKIYVIGGISY-- 448

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1910408511  716 tslSNGAKCFSADFLaYDIACDEWKTLPKPNLHRdvnrFGHSAVVINGSMYIFGGFS-SVLLNDILVY 782
Cdd:PHA03098   449 ---IDNIKVYNIVES-YNPVTNKWTELSSLNFPR----INASLCIFNNKIYVVGGDKyEYYINEIEVY 508
PHA03247 PHA03247
large tegument protein UL36; Provisional
 86-266 2.08e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511   86 PGAPRARGPHLGGHHPSAARPGGAGARGgvpgSCQGGARPRRRACGGSAGRRGAGGPssaprapavapaagsRRRREHGC 165
Cdd:PHA03247  2628 PPSPSPAANEPDPHPPPTVPPPERPRDD----PAPGRVSRPRRARRLGRAAQASSPP---------------QRPRRRAA 2688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  166 WGAAGCVPGGAGLTPAFRLPPPALGAPTSRLPLAPALPGARGWAPRQLARAAGEAGPLAGSPPPPAGSPPR--VPSGAPR 243
Cdd:PHA03247  2689 RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARppTTAGPPA 2768

                          170       180
                   ....*....|....*....|....*
gi 1910408511  244 VAcsagsqPPAGP--GAPRRWARPA 266
Cdd:PHA03247  2769 PA------PPAAPaaGPPRRLTRPA 2787
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1186-1229 3.53e-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: 42.73  E-value: 3.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1910408511 1186 CQCNGH----STCINHN-VCeHCKNLTTGKQCQDCMPGYYGDP-TNGGQC 1229
Cdd:pfam00053    1 CDCNPHgslsDTCDPETgQC-LCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1186-1226 4.26e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.60  E-value: 4.26e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1910408511  1186 CQCNG----HSTCINHN-VCeHCKNLTTGKQCQDCMPGYYGDPTNG 1226
Cdd:smart00180    1 CDCDPggsaSGTCDPDTgQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
DSL pfam01414
Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain ...
 407-453 2.32e-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: 37.22  E-value: 2.32e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1910408511  407 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 453
Cdd:pfam01414    1 CDENYYGSTCSK-FCRPRDDKFGHYTCDANGNK--VCLPGWTGPYCD 44
DSL smart00051
delta serrate ligand;
406-452 2.57e-03

delta serrate ligand;


Pssm-ID: 128366  Cd Length: 63  Bit Score: 37.69  E-value: 2.57e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1910408511   406 ECDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKLCvcNDSWQGPDC 452
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 ...
 920-1046 1.42e-81

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: 263.67  E-value: 1.42e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  920 CGEGWNHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQK--YTQQKVSPWVGLRKINISYWGWED 997
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKhqMTKQKLTPWVGLRKINVSYWCWED 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1910408511  998 MSPFTNTTLQWLPGEPNDSGFCAYLERAAVAGLKANPCTSMADGLVCEK 1046
Cdd:cd03597     81 MSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
475-770 4.81e-23

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 101.00  E-value: 4.81e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  475 VGRASHKAVLHGKFMWVIGGYTFN--YSSFQMvlnYNLENSIWNvgTVSRGPLQRYGHS-LALYQENIFMYGGRIETND- 550
Cdd:COG3055     11 TPRSEAAAALLDGKVYVAGGLSGGsaSNSFEV---YDPATNTWS--ELAPLPGPPRHHAaAVAQDGKLYVFGGFTGANPs 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  551 GNVTDELWVFNIRSQSWSTKTPTVIGHGqqyaveghsAHIMELDSRDvvmIIIFGYSAIYGYSSSIQEYHISSNTWlvpE 630
Cdd:COG3055     86 STPLNDVYVYDPATNTWTKLAPMPTPRG---------GATALLLDGK---IYVVGGWDDGGNVAWVEVYDPATGTW---T 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  631 TKGAIVQGGYGHTSVYDEITKsIYVHGGYKalpgnkyglvddlykYEVNTKTWTILKESGFARYLHSAVLINGAMLIFGG 710
Cdd:COG3055    151 QLAPLPTPRDHLAAAVLPDGK-ILVIGGRN---------------GSGFSNTWTTLAPLPTARAGHAAAVLGGKILVFGG 214

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  711 NTHndtslsngakcFSADFLAYDIACDEWKTLPKPNlhrdVNRFGHSAVVINGSMYIFGG 770
Cdd:COG3055    215 ESG-----------FSDEVEAYDPATNTWTALGELP----TPRHGHAAVLTDGKVYVIGG 259
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
473-714 6.76e-20

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 91.76  E-value: 6.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  473 PSVGRASHKAVLHGKFMWVIGGYTFNYSSFQM---VLNYNLENSIWNVGTVSrgPLQRYGHSLALYQENIFMYGGRietN 549
Cdd:COG3055     57 PGPPRHHAAAVAQDGKLYVFGGFTGANPSSTPlndVYVYDPATNTWTKLAPM--PTPRGGATALLLDGKIYVVGGW---D 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  550 DGNVTDELWVFNIRSQSWSTKTPTVIghgqqyAVEGHSAHIMELDsrdvvMIIIFGysaiyGYSSSIqeyhiSSNTWlvp 629
Cdd:COG3055    132 DGGNVAWVEVYDPATGTWTQLAPLPT------PRDHLAAAVLPDG-----KILVIG-----GRNGSG-----FSNTW--- 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  630 ETKGAIVQGGYGHTSVYdeITKSIYVHGGYkalpgnkYGLVDDLYKYEVNTKTWTILKESGFARYLHSAVLINGAMLIFG 709
Cdd:COG3055    188 TTLAPLPTARAGHAAAV--LGGKILVFGGE-------SGFSDEVEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYVIG 258


                   ....*
gi 1910408511  710 GNTHN 714
Cdd:COG3055    259 GETKP 263
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
524-784 2.70e-17

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 84.05  E-value: 2.70e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  524 PLQRYGHSLALYQENIFMYGGRietNDGNVTDELWVFNIRSQSWSTKTP---TVIGHGQQYAVEGHsahimeldsrdvvm 600
Cdd:COG3055     10 PTPRSEAAAALLDGKVYVAGGL---SGGSASNSFEVYDPATNTWSELAPlpgPPRHHAAAVAQDGK-------------- 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  601 IIIF-GYSAIYG---YSSSIQEYHISSNTWlvpETKGAIVQGGYGHTSVYdeITKSIYVHGGYkalpgNKYGLVDDLYKY 676
Cdd:COG3055     73 LYVFgGFTGANPsstPLNDVYVYDPATNTW---TKLAPMPTPRGGATALL--LDGKIYVVGGW-----DDGGNVAWVEVY 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  677 EVNTKTWTILKESGFARYLHSA-VLINGAMLIFGGNthNDTSLSNgakcfsadflaydiacdEWKTLPkpnlHRDVNRFG 755
Cdd:COG3055    143 DPATGTWTQLAPLPTPRDHLAAaVLPDGKILVIGGR--NGSGFSN-----------------TWTTLA----PLPTARAG 199

                          250       260
                   ....*....|....*....|....*....
gi 1910408511  756 HSAVVINGSMYIFGGFSSVlLNDILVYKP 784
Cdd:COG3055    200 HAAAVLGGKILVFGGESGF-SDEVEAYDP 227
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 272-380 1.13e-16

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: 77.45  E-value: 1.13e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  272 TEPSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLIAVLSGlivpeirg 345
Cdd:cd00041      7 ASTSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFCG-------- 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1910408511  346 NETVPEVVTTSGYALLHFFSDAAYNLTGFNIFYSI 380
Cdd:cd00041     79 STLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 931-1046 1.43e-16

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: 77.27  E-value: 1.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  931 CLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYTQQKVspWVGLRKINI-SYWGWEDMSPFTNTTlQWL 1009
Cdd:cd00037      2 CYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDV--WIGLNDLSSeGTWKWSDGSPLVDYT-NWA 78

                           90       100       110
                   ....*....|....*....|....*....|....*....
gi 1910408511 1010 PGEPN--DSGFCAYLERAAVAGLKANPCTSMAdGLVCEK 1046
Cdd:cd00037     79 PGEPNpgGSEDCVVLSSSSDGKWNDVSCSSKL-PFICEK 116
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 938-1046 4.87e-15

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 72.51  E-value: 4.87e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  938 RESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYtqqKVSPWVGLRKINIS-YWGWEDMSPFTNTTLQWLPGEPNDS 1016
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLKKS---NKYFWIGLTDRKNEgTWKWVDGSPVNYTNWAPEPNNNGEN 77

                           90       100       110
                   ....*....|....*....|....*....|
gi 1910408511 1017 GFCAYLERAAvAGLKANPCTSMAdGLVCEK 1046
Cdd:pfam00059   78 EDCVELSSSS-GKWNDENCNSKN-PFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 920-1022 7.64e-15

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: 72.63  E-value: 7.64e-15
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511   920 CGEGWNHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYTQQKvSPWVGLRKINISY-WGWEDM 998
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSD-YYWIGLSDPDSNGsWQWSDG 79

                            90       100
                    ....*....|....*....|....*
gi 1910408511   999 SPFTNTTLqWLPGEPNDS-GFCAYL 1022
Cdd:smart00034   80 SGPVSYSN-WAPGEPNNSsGDCVVL 103
CUB pfam00431
CUB domain;
270-378 6.56e-12

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 63.47  E-value: 6.56e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  270 RLTEPSGYLT--DGPINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLIAVLSGLIVPei 343
Cdd:pfam00431    4 VLTDSSGSISspNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGSGIP-- 81

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1910408511  344 rgnetvPEVVTTSGYALLHFFSDAAYNLTGFNIFY 378
Cdd:pfam00431   82 ------EDIVSSSNQMTIKFVSDASVQKRGFKATY 110
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 282-378 6.63e-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: 63.56  E-value: 6.63e-12
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511   282 PINYKYKTKCTWLIEGYPNAVLRLRFNHFATE----CSWDHMYVYDGDSIYAPLIAVLSGLIVPEirgnetvPEVVTTSG 357
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPP-------PVISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 1910408511   358 YALLHFFSDAAYNLTGFNIFY 378
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
682-784 1.14e-11

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 67.10  E-value: 1.14e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  682 TWTILKESGFARYLHSAVLINGAMLIFGGNTHNDTslsngakcfSADFLAYDIACDEWKTLPKPNLHRdvnRFGHSAVVI 761
Cdd:COG3055      2 TWSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSA---------SNSFEVYDPATNTWSELAPLPGPP---RHHAAAVAQ 69

                           90       100
                   ....*....|....*....|....*...
gi 1910408511  762 NGSMYIFGGF-----SSVLLNDILVYKP 784
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 ...
 920-1022 1.52e-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: 54.62  E-value: 1.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  920 CGEGWNHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFvldeIQKYTQQKVSPWVGLRKINI-SYWGWEDM 998
Cdd:cd03590      1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEF----ISKILSGNRSYWIGLSDEETeGEWKWVDG 76

                           90       100
                   ....*....|....*....|....*...
gi 1910408511  999 SPFTNTTLQWLPGEPNDSGF----CAYL 1022
Cdd:cd03590     77 TPLNSSKTFWHPGEPNNWGGggedCAEL 104
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 920-1046 2.00e-07

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: 51.18  E-value: 2.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  920 CGEGWNHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFvldeIQKYTQQKvSPWVGLRKINISY-WGWEDM 998
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEF----LQSQIGSS-SYWIGLSREKSEKpWKWIDG 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1910408511  999 SPFTNttlqWL-PGEPNDSGFCAYLERaavAGLKANPCtSMADGLVCEK 1046
Cdd:cd03593     76 SPLNN----LFnIRGSTKSGNCAYLSS---TGIYSEDC-STKKRWICEK 116
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1185-1230 1.15e-06

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 46.96  E-value: 1.15e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1910408511 1185 ACQCNGHSTciNHNVCE------HCKNLTTGKQCQDCMPGYYGDPTNGGQCT 1230
Cdd:cd00055      1 PCDCNGHGS--LSGQCDpgtgqcECKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 1061-1110 2.55e-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: 45.78  E-value: 2.55e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1910408511 1061 PCSLRTSCSNCT-SNGMECMWCSSTRRCVDSNAYiiSFPYGQCLEWQTATC 1110
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 ...
 524-564 5.44e-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: 44.48  E-value: 5.44e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1910408511  524 PLQRYGHSLALYQENIFMYGGRIeTNDGNVTDELWVFNIRS 564
Cdd:pfam13854    1 PVPRYGHCAVTVGDYIYLYGGYT-GGEGQPSDDVYVLSLPT 40
PHA03098 PHA03098
kelch-like protein; Provisional
 485-782 6.92e-06

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 50.54  E-value: 6.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  485 HGKFMWVIGGYTFNYSSfqMVLNYNLENSIWNVgtVSRGPLQRYGHslALYQENIFMYGGRIETNDgnVTDELWVFNIRS 564
Cdd:PHA03098   249 FGSIIYIHITMSIFTYN--YITNYSPLSEINTI--IDIHYVYCFGS--VVLNNVIYFIGGMNKNNL--SVNSVVSYDTKT 320

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  565 QSWsTKTPTVIghgqqYAVEGHSAHImeLDSRdvvmiiIFGYSAIY--GYSSSIQEYHISSNTW------LVPETKGAIV 636
Cdd:PHA03098   321 KSW-NKVPELI-----YPRKNPGVTV--FNNR------IYVIGGIYnsISLNTVESWKPGESKWreepplIFPRYNPCVV 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  637 qggyghtsVYDEItksIYVHGGYkalpgNKYG-LVDDLYKYEVNTKTWTILKESGFARYLHSAVLINGAMLIFGGNTHnd 715
Cdd:PHA03098   387 --------NVNNL---IYVIGGI-----SKNDeLLKTVECFSLNTNKWSKGSPLPISHYGGCAIYHDGKIYVIGGISY-- 448

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1910408511  716 tslSNGAKCFSADFLaYDIACDEWKTLPKPNLHRdvnrFGHSAVVINGSMYIFGGFS-SVLLNDILVY 782
Cdd:PHA03098   449 ---IDNIKVYNIVES-YNPVTNKWTELSSLNFPR----INASLCIFNNKIYVVGGDKyEYYINEIEVY 508
PHA03247 PHA03247
large tegument protein UL36; Provisional
 86-266 2.08e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 2.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511   86 PGAPRARGPHLGGHHPSAARPGGAGARGgvpgSCQGGARPRRRACGGSAGRRGAGGPssaprapavapaagsRRRREHGC 165
Cdd:PHA03247  2628 PPSPSPAANEPDPHPPPTVPPPERPRDD----PAPGRVSRPRRARRLGRAAQASSPP---------------QRPRRRAA 2688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  166 WGAAGCVPGGAGLTPAFRLPPPALGAPTSRLPLAPALPGARGWAPRQLARAAGEAGPLAGSPPPPAGSPPR--VPSGAPR 243
Cdd:PHA03247  2689 RPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARppTTAGPPA 2768

                          170       180
                   ....*....|....*....|....*
gi 1910408511  244 VAcsagsqPPAGP--GAPRRWARPA 266
Cdd:PHA03247  2769 PA------PPAAPaaGPPRRLTRPA 2787
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1186-1229 3.53e-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: 42.73  E-value: 3.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1910408511 1186 CQCNGH----STCINHN-VCeHCKNLTTGKQCQDCMPGYYGDP-TNGGQC 1229
Cdd:pfam00053    1 CDCNPHgslsDTCDPETgQC-LCKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
Kelch_3 pfam13415
Galactose oxidase, central domain;
650-701 4.27e-05

Galactose oxidase, central domain;


Pssm-ID: 433188 [Multi-domain]  Cd Length: 49  Bit Score: 42.28  E-value: 4.27e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1910408511  650 TKSIYVHGGYKALPGNKYglvDDLYKYEVNTKTWTILKESGFARYLHSAVLI 701
Cdd:pfam13415    1 GDKLYIFGGLGFDGQTRL---NDLYVYDLDTNTWTQIGDLPPPRSGHSATYI 49
CLECT_REG-1_like cd03594
C-type lectin-like domain (CTLD) of the type found in Human REG-1 (lithostathine), REG-4, and ...
 920-1037 4.88e-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: 44.67  E-value: 4.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  920 CGEGWNHIGDACLRINSSRESYDNAKLYC--YNLSGNLASLTTSKEVEFVLDEIQKYtQQKVSP-WVGLRKINISY-WGW 995
Cdd:cd03594      1 CPKGWLPYKGNCYGYFRQPLSWSDAELFCqkYGPGAHLASIHSPAEAAAIASLISSY-QKAYQPvWIGLHDPQQSRgWEW 79

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1910408511  996 EDMSPFTNTTlqWLPGEP-NDSGFCAYLER-AAVAGLKANPCTS 1037
Cdd:cd03594     80 SDGSKLDYRS--WDRNPPyARGGYCAELSRsTGFLKWNDANCEE 121
CLECT_CEL-1_like cd03589
C-type lectin-like domain (CTLD) of the type found in CEL-1 from Cucumaria echinata and ...
 920-1036 6.37e-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: 44.27  E-value: 6.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  920 CGEGWNHIGDACLRINSSRESYDNAKLYCYN-----LSGNLASLTTSKEVEFVLD--EIQKYTQQKVSPWVGL-RKINIS 991
Cdd:cd03589      1 CPTFWTAFGGYCYRFFGDRLTWEEAELRCRSfsipgLIAHLVSIHSQEENDFVYDlfESSRGPDTPYGLWIGLhDRTSEG 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1910408511  992 YWGWEDMSPFTNTtlQWLPGEPNDSGF---CAYLERAAVAGLKAN--PCT 1036
Cdd:cd03589     81 PFEWTDGSPVDFT--KWAGGQPDNYGGnedCVQMWRRGDAGQSWNdmPCD 128
CLECT_CSPGs cd03588
C-type lectin-like domain (CTLD) of the type found in chondroitin sulfate proteoglycan core ...
 920-1020 7.78e-05

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: 43.72  E-value: 7.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  920 CGEGWNHIGDACLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYTqqkvspWVGLRKINISY-WGWEDM 998
Cdd:cd03588      1 CEEGWDKFQGHCYRHFPDRETWEDAERRCREQQGHLSSIVTPEEQEFVNNNAQDYQ------WIGLNDRTIEGdFRWSDG 74

                           90       100
                   ....*....|....*....|....
gi 1910408511  999 SP--FTNttlqWLPGEPnDSGFCA 1020
Cdd:cd03588     75 HPlqFEN----WRPNQP-DNFFAT 93
PLN02153 PLN02153
epithiospecifier protein
 626-772 8.54e-05

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 46.52  E-value: 8.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  626 WLVPETKGAIVQG---GYGHTSVYDEItksiYVHGGykALPGNKYgLVDDLYKYEVNTKTWTILKESGFARYLHS----A 698
Cdd:PLN02153     9 WIKVEQKGGKGPGprcSHGIAVVGDKL----YSFGG--ELKPNEH-IDKDLYVFDFNTHTWSIAPANGDVPRISClgvrM 81

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1910408511  699 VLINGAMLIFGGNTHNdtslsngaKCFSaDFLAYDIACDEWKTLPKPNLHRDVN-RFGHSAVVINGSMYIFGGFS 772
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 ...
 920-1024 1.25e-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: 44.14  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  920 CGEGWNHI-GDA-CLRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVL------DEIQKYTQQKVSPWVGLRKI--- 988
Cdd:cd03599      1 CPSGWHHYeGTAsCYKVYLSGENYWDAVQTCQKVNGSLATFTTDQELQFILaqewdfDERVFGRKDQCKFWVGYQYVitn 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1910408511  989 -NISYWG-WEdmSPFTNTTLQWLPGEP--------NDSGFCAYLER 1024
Cdd:cd03599     81 rNHSLEGrWE--VAYKGSMEVFLPPEPifatgmstNDNVFCAQLQC 124
PHA03098 PHA03098
kelch-like protein; Provisional
 463-576 3.09e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 45.14  E-value: 3.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  463 WILPNVKPFSpsvgRASHKAVLHGKFMWVIGGYTF--NYSSFQMVLNYNLENSIWNVGTVSRGPlqRYGHSLALYQENIF 540
Cdd:PHA03098   418 WSKGSPLPIS----HYGGCAIYHDGKIYVIGGISYidNIKVYNIVESYNPVTNKWTELSSLNFP--RINASLCIFNNKIY 491

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1910408511  541 MYGGRIetnDGNVTDELWVFNIRSQSWS--TKTPTVIG 576
Cdd:PHA03098   492 VVGGDK---YEYYINEIEVYDDKTNTWTlfCKFPKVIG 526
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1186-1226 4.26e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 39.60  E-value: 4.26e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1910408511  1186 CQCNG----HSTCINHN-VCeHCKNLTTGKQCQDCMPGYYGDPTNG 1226
Cdd:smart00180    1 CDCDPggsaSGTCDPDTgQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
Kelch_6 pfam13964
Kelch motif;
527-569 6.34e-04

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 39.24  E-value: 6.34e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1910408511  527 RYGHSLALYQENIFMYGGRieTNDGNVTDELWVFNIRSQSWST 569
Cdd:pfam13964    2 RTFHSVVSVGGYIYVFGGY--TNASPALNKLEVYNPLTKSWEE 42
Kelch_4 pfam13418
Galactose oxidase, central domain;
641-686 1.11e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 38.36  E-value: 1.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1910408511  641 GHTSVYDEiTKSIYVHGGYkalpGNKYGLVDDLYKYEVNTKTWTIL 686
Cdd:pfam13418    4 YHTSTSIP-DDTIYLFGGE----GEDGTLLSDLWVFDLSTNEWTRL 44
PLN02193 PLN02193
nitrile-specifier protein
 472-559 1.14e-03

nitrile-specifier protein


Pssm-ID: 177844 [Multi-domain]  Cd Length: 470  Bit Score: 43.41  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  472 SPSVGRASHKAVLH------GKFMWVIGGYTFN--YSSFqmvLNYNLENSIWNVGT-VSRGPLQRYGHSLALYQENIFMY 542
Cdd:PLN02193   208 SPATGDVPHLSCLGvrmvsiGSTLYVFGGRDASrqYNGF---YSFDTTTNEWKLLTpVEEGPTPRSFHSMAADEENVYVF 284

                           90       100
                   ....*....|....*....|...
gi 1910408511  543 GG-----RIETNDG-NVTDELWV 559
Cdd:PLN02193   285 GGvsataRLKTLDSyNIVDKKWF 307
CLECT_selectins_like cd03592
C-type lectin-like domain (CTLD) of the type found in the type 1 transmembrane proteins: P ...
 932-1017 1.56e-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: 40.05  E-value: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  932 LRINSSRESYDNAKLYCYNLSGNLASLTTSKEVEFVLDEIQKYTQQKVspWVGLRKINISyWGWEDMSPFTNTTLQWLPG 1011
Cdd:cd03592      3 YHYSTEKMTFNEAVKYCKSRGTDLVAIQNAEENALLNGFALKYNLGYY--WIDGNDINNE-GTWVDTDKKELEYKNWAPG 79


                   ....*.
gi 1910408511 1012 EPNDSG 1017
Cdd:cd03592     80 EPNNGR 85
PRK14131 PRK14131
N-acetylneuraminate epimerase;
671-777 1.95e-03

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 42.31  E-value: 1.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  671 DDLYKYEVNT--KTWTILKE-SGFARYLHSAVLINGAMLIFGGNTHNDTSLSNGAkcFSaDFLAYDIACDEWKTLPKpnl 747
Cdd:PRK14131    50 TSWYKLDLNApsKGWTKIAAfPGGPREQAVAAFIDGKLYVFGGIGKTNSEGSPQV--FD-DVYKYDPKTNSWQKLDT--- 123

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1910408511  748 HRDVNRFGHSAVVINGSM-YIFGGFSSVLLN 777
Cdd:PRK14131   124 RSPVGLAGHVAVSLHNGKaYITGGVNKNIFD 154
DSL pfam01414
Delta serrate ligand; This family has been redefined to correspond to the EGF-like domain ...
 407-453 2.32e-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: 37.22  E-value: 2.32e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1910408511  407 CDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKlcVCNDSWQGPDCS 453
Cdd:pfam01414    1 CDENYYGSTCSK-FCRPRDDKFGHYTCDANGNK--VCLPGWTGPYCD 44
DSL smart00051
delta serrate ligand;
406-452 2.57e-03

delta serrate ligand;


Pssm-ID: 128366  Cd Length: 63  Bit Score: 37.69  E-value: 2.57e-03
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*..
gi 1910408511   406 ECDKYWKGEACDIpYCKANCGSPDHGYCDLTGEKLCvcNDSWQGPDC 452
Cdd:smart00051   20 TCDENYYGEGCNK-FCRPRDDFFGHYTCDENGNKGC--LEGWMGPYC 63
Kelch_4 pfam13418
Galactose oxidase, central domain;
527-569 4.60e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.44  E-value: 4.60e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1910408511  527 RYGHSL-ALYQENIFMYGGRIEtnDGNVTDELWVFNIRSQSWST 569
Cdd:pfam13418    2 RAYHTStSIPDDTIYLFGGEGE--DGTLLSDLWVFDLSTNEWTR 43
PHA03247 PHA03247
large tegument protein UL36; Provisional
 185-280 7.61e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.08  E-value: 7.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  185 PPPALGAPTSrLPLAPALPGARGWAPRQLARAAGEAGPLAGSPPPPAGSPPRVPSGAPRVACSAGSQPPAGPGAPRRWAR 264
Cdd:PHA03247  2607 DPRGPAPPSP-LPPDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRR 2685

                           90
                   ....*....|....*.
gi 1910408511  265 PAedtrLTEPSGYLTD 280
Cdd:PHA03247  2686 RA----ARPTVGSLTS 2697
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 753-784 7.63e-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: 36.05  E-value: 7.63e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1910408511  753 RFGHSAVVINGSMYIFGGF-SSVLLNDILVYKP 784
Cdd:pfam01344    2 RSGAGVVVVGGKIYVIGGFdGNQSLNSVEVYDP 34
PHA03098 PHA03098
kelch-like protein; Provisional
 674-784 8.57e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 40.52  E-value: 8.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1910408511  674 YKYEVNTKTWTILKESGFARYLHSAVLINGAMLIFGGNTHNDtslsngakcFSADFLAYDIACDEWKTLPKPNlhrdVNR 753
Cdd:PHA03098   267 ITNYSPLSEINTIIDIHYVYCFGSVVLNNVIYFIGGMNKNNL---------SVNSVVSYDTKTKSWNKVPELI----YPR 333

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1910408511  754 FGHSAVVINGSMYIFGG-FSSVLLNDILVYKP 784
Cdd:PHA03098   334 KNPGVTVFNNRIYVIGGiYNSISLNTVESWKP 365
 
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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