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Conserved domains on  [gi|1020158887|ref|NP_001310261|]
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attractin isoform 5 precursor [Homo sapiens]

Protein Classification

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 ...
 788-920 2.40e-78

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: 253.66  E-value: 2.40e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  788 CGIGWHLVGNSCLKITTAKENYDNAKLFCRNHNALLASLTTQKKVEFVLKQLRIMQssqsMSKLTLTPWVGLRKINVSYW 867
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQ----MTKQKLTPWVGLRKINVSYW 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1020158887  868 CWEDMSPFTNSLLQWMPSEPSDAGFCGILSEPSTRGLKAATCINPLNGSVCER 920
Cdd:cd03597     77 CWEDMSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
329-634 5.65e-25

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


:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 106.01  E-value: 5.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  329 WTReeYSNLKLPRASHKAVVNGNIMWVVGGYMFNhSDYNMVLAYDLASREW-----LPLNRsvnnvvvRYGHSLALYKDK 403
Cdd:COG3055      3 WSS--LPDLPTPRSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATNTWselapLPGPP-------RHHAAAVAQDGK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  404 IYMYGG--KIDSTGNVTNELRVFHIHNESWVLLTPKAkeqyavVGHSAHIVTLKNGRVvmLVIFGHCPLyGYISNVQEYD 481
Cdd:COG3055     73 LYVFGGftGANPSSTPLNDVYVYDPATNTWTKLAPMP------TPRGGATALLLDGKI--YVVGGWDDG-GNVAWVEVYD 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  482 LDKNTWSILhtqGALVQGGYGHSSVYdHRTRALYVHGGYkafsankyrladdlyRYDVDTQMWTILKDSRFFRYLHTAVI 561
Cdd:COG3055    144 PATGTWTQL---APLPTPRDHLAAAV-LPDGKILVIGGR---------------NGSGFSNTWTTLAPLPTARAGHAAAV 204

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1020158887  562 VSGTMLVFGGNTHndtsmshgakcFSSDFMAYDIACDRWSV---LPRPdlhhdvnRFGHSAVLHNSTMYVFGGFNS 634
Cdd:COG3055    205 LGGKILVFGGESG-----------FSDEVEAYDPATNTWTAlgeLPTP-------RHGHAAVLTDGKVYVIGGETK 262
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 132-247 1.40e-20

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: 88.24  E-value: 1.40e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  132 CGGRFRLTgSSGFVT--DGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLVAAFSgl 205
Cdd:cd00041      1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFC-- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1020158887  206 ivperdGNETVPEVVATSGYALLHFFSDAAYNLTGFNITYSF 247
Cdd:cd00041     78 ------GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1062-1107 7.63e-05

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: 41.57  E-value: 7.63e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1020158887 1062 ACQCNGHSK----CINQS-ICEkCENLTTGKHCETCISGFYGDPTNGGKCQ 1107
Cdd:cd00055      1 PCDCNGHGSlsgqCDPGTgQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 932-983 1.04e-04

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


:

Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 41.15  E-value: 1.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1020158887  932 PCALRTACGDCT-SGSSECMWCSNMKQCVDSNAYvaSFPFGQCMEWYT-MSTCP 983
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQaSSKCP 52
 
Name Accession Description Interval E-value
CLECT_attractin_like cd03597
C-type lectin-like domain (CTLD) of the type found in human and mouse attractin (AtrN) and ...
 788-920 2.40e-78

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: 253.66  E-value: 2.40e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  788 CGIGWHLVGNSCLKITTAKENYDNAKLFCRNHNALLASLTTQKKVEFVLKQLRIMQssqsMSKLTLTPWVGLRKINVSYW 867
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQ----MTKQKLTPWVGLRKINVSYW 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1020158887  868 CWEDMSPFTNSLLQWMPSEPSDAGFCGILSEPSTRGLKAATCINPLNGSVCER 920
Cdd:cd03597     77 CWEDMSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
329-634 5.65e-25

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 106.01  E-value: 5.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  329 WTReeYSNLKLPRASHKAVVNGNIMWVVGGYMFNhSDYNMVLAYDLASREW-----LPLNRsvnnvvvRYGHSLALYKDK 403
Cdd:COG3055      3 WSS--LPDLPTPRSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATNTWselapLPGPP-------RHHAAAVAQDGK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  404 IYMYGG--KIDSTGNVTNELRVFHIHNESWVLLTPKAkeqyavVGHSAHIVTLKNGRVvmLVIFGHCPLyGYISNVQEYD 481
Cdd:COG3055     73 LYVFGGftGANPSSTPLNDVYVYDPATNTWTKLAPMP------TPRGGATALLLDGKI--YVVGGWDDG-GNVAWVEVYD 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  482 LDKNTWSILhtqGALVQGGYGHSSVYdHRTRALYVHGGYkafsankyrladdlyRYDVDTQMWTILKDSRFFRYLHTAVI 561
Cdd:COG3055    144 PATGTWTQL---APLPTPRDHLAAAV-LPDGKILVIGGR---------------NGSGFSNTWTTLAPLPTARAGHAAAV 204

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1020158887  562 VSGTMLVFGGNTHndtsmshgakcFSSDFMAYDIACDRWSV---LPRPdlhhdvnRFGHSAVLHNSTMYVFGGFNS 634
Cdd:COG3055    205 LGGKILVFGGESG-----------FSDEVEAYDPATNTWTAlgeLPTP-------RHGHAAVLTDGKVYVIGGETK 262
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 132-247 1.40e-20

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: 88.24  E-value: 1.40e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  132 CGGRFRLTgSSGFVT--DGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLVAAFSgl 205
Cdd:cd00041      1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFC-- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1020158887  206 ivperdGNETVPEVVATSGYALLHFFSDAAYNLTGFNITYSF 247
Cdd:cd00041     78 ------GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 149-245 2.26e-14

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: 70.11  E-value: 2.26e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887   149 PGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLVAAFSGLIVPErdgnetvPEVVATSG 224
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPP-------PVISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 1020158887   225 YALLHFFSDAAYNLTGFNITY 245
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
132-245 5.40e-14

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 69.25  E-value: 5.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  132 CGGRFrlTGSSG--FVTDGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLVAAFSGL 205
Cdd:pfam00431    1 CGGVL--TDSSGsiSSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1020158887  206 IVPerdgnetvPEVVATSGYALLHFFSDAAYNLTGFNITY 245
Cdd:pfam00431   79 GIP--------EDIVSSSNQMTIKFVSDASVQKRGFKATY 110
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 806-920 2.36e-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: 2.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  806 KENYDNAKLFCRNHNALLASLTTQKKVEFVLKQLRimQSSQSmskltltPWVGL-RKINVSYWCWEDMSPFTNSLLQWMP 884
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLK--KSNKY-------FWIGLtDRKNEGTWKWVDGSPVNYTNWAPEP 71

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1020158887  885 SEPSDAGFCGILSePSTRGLKAATCINPlNGSVCER 920
Cdd:pfam00059   72 NNNGENEDCVELS-SSSGKWNDENCNSK-NPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 788-919 9.93e-13

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: 66.08  E-value: 9.93e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887   788 CGIGWHLVGNSCLKITTAKENYDNAKLFCRNHNALLASLTTQKKVEFVLKQLRIMQSSQSMskltltpWVGLRKINVSYW 867
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYY-------WIGLSDPDSNGS 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1020158887   868 C-WEDMSPFTNSLLqWMPSEPSDA-GFCGILSePSTRGLKAATCiNPLNGSVCE 919
Cdd:smart00034   74 WqWSDGSGPVSYSN-WAPGEPNNSsGDCVVLS-TSGGKWNDVSC-TSKLPFVCE 124
PHA03098 PHA03098
kelch-like protein; Provisional
 327-491 4.48e-09

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 60.55  E-value: 4.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  327 SFWTREeySNLKLPRASHKAVVNGNIMWVVGGYMFNHSDYNMVLAYDLASREWLPLNRSvnnVVVRYGHSLALYKDKIYM 406
Cdd:PHA03098   368 SKWREE--PPLIFPRYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSPL---PISHYGGCAIYHDGKIYV 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  407 YGGKIDSTG-NVTNELRVFHIHNESWVLLTPKakeQYAVVGHSAHIVTLKngrvvMLVIFGHCPLYgYISNVQEYDLDKN 485
Cdd:PHA03098   443 IGGISYIDNiKVYNIVESYNPVTNKWTELSSL---NFPRINASLCIFNNK-----IYVVGGDKYEY-YINEIEVYDDKTN 513


                   ....*.
gi 1020158887  486 TWSILH 491
Cdd:PHA03098   514 TWTLFC 519
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1062-1107 7.63e-05

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: 41.57  E-value: 7.63e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1020158887 1062 ACQCNGHSK----CINQS-ICEkCENLTTGKHCETCISGFYGDPTNGGKCQ 1107
Cdd:cd00055      1 PCDCNGHGSlsgqCDPGTgQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 932-983 1.04e-04

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 41.15  E-value: 1.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1020158887  932 PCALRTACGDCT-SGSSECMWCSNMKQCVDSNAYvaSFPFGQCMEWYT-MSTCP 983
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQaSSKCP 52
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 390-428 4.19e-04

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


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 39.09  E-value: 4.19e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1020158887  390 VVRYGHSLALYKDKIYMYGGKIDSTGNVTNELRVFHIHN 428
Cdd:pfam13854    2 VPRYGHCAVTVGDYIYLYGGYTGGEGQPSDDVYVLSLPT 40
 
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 ...
 788-920 2.40e-78

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: 253.66  E-value: 2.40e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  788 CGIGWHLVGNSCLKITTAKENYDNAKLFCRNHNALLASLTTQKKVEFVLKQLRIMQssqsMSKLTLTPWVGLRKINVSYW 867
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQ----MTKQKLTPWVGLRKINVSYW 76

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1020158887  868 CWEDMSPFTNSLLQWMPSEPSDAGFCGILSEPSTRGLKAATCINPLNGSVCER 920
Cdd:cd03597     77 CWEDMSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
329-634 5.65e-25

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 106.01  E-value: 5.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  329 WTReeYSNLKLPRASHKAVVNGNIMWVVGGYMFNhSDYNMVLAYDLASREW-----LPLNRsvnnvvvRYGHSLALYKDK 403
Cdd:COG3055      3 WSS--LPDLPTPRSEAAAALLDGKVYVAGGLSGG-SASNSFEVYDPATNTWselapLPGPP-------RHHAAAVAQDGK 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  404 IYMYGG--KIDSTGNVTNELRVFHIHNESWVLLTPKAkeqyavVGHSAHIVTLKNGRVvmLVIFGHCPLyGYISNVQEYD 481
Cdd:COG3055     73 LYVFGGftGANPSSTPLNDVYVYDPATNTWTKLAPMP------TPRGGATALLLDGKI--YVVGGWDDG-GNVAWVEVYD 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  482 LDKNTWSILhtqGALVQGGYGHSSVYdHRTRALYVHGGYkafsankyrladdlyRYDVDTQMWTILKDSRFFRYLHTAVI 561
Cdd:COG3055    144 PATGTWTQL---APLPTPRDHLAAAV-LPDGKILVIGGR---------------NGSGFSNTWTTLAPLPTARAGHAAAV 204

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1020158887  562 VSGTMLVFGGNTHndtsmshgakcFSSDFMAYDIACDRWSV---LPRPdlhhdvnRFGHSAVLHNSTMYVFGGFNS 634
Cdd:COG3055    205 LGGKILVFGGESG-----------FSDEVEAYDPATNTWTAlgeLPTP-------RHGHAAVLTDGKVYVIGGETK 262
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 132-247 1.40e-20

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: 88.24  E-value: 1.40e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  132 CGGRFRLTgSSGFVT--DGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLVAAFSgl 205
Cdd:cd00041      1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFC-- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1020158887  206 ivperdGNETVPEVVATSGYALLHFFSDAAYNLTGFNITYSF 247
Cdd:cd00041     78 ------GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
390-643 1.12e-19

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 90.60  E-value: 1.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  390 VVRYGHSLALYKDKIYMYGGKidSTGNVTNELRVFHIHNESWVLLTPkakeqYAVVGHSAHIVTLKNGRVvmLVI---FG 466
Cdd:COG3055     11 TPRSEAAAALLDGKVYVAGGL--SGGSASNSFEVYDPATNTWSELAP-----LPGPPRHHAAAVAQDGKL--YVFggfTG 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  467 HCPLYGYISNVQEYDLDKNTWSilhTQGALVQGGYGHSS-VYDHRtraLYVHGGYKAFSANKyrladDLYRYDVDTQMWT 545
Cdd:COG3055     82 ANPSSTPLNDVYVYDPATNTWT---KLAPMPTPRGGATAlLLDGK---IYVVGGWDDGGNVA-----WVEVYDPATGTWT 150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  546 ILKDSRFFRYLHTAVIV-SGTMLVFGGNThndtsmshgakcfssdfmaYDIACDRWSVLPrpdlHHDVNRFGHSAVLHNS 624
Cdd:COG3055    151 QLAPLPTPRDHLAAAVLpDGKILVIGGRN-------------------GSGFSNTWTTLA----PLPTARAGHAAAVLGG 207

                          250
                   ....*....|....*....
gi 1020158887  625 TMYVFGGFNSlLLSDILVF 643
Cdd:COG3055    208 KILVFGGESG-FSDEVEAY 225
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 149-245 2.26e-14

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: 70.11  E-value: 2.26e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887   149 PGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLVAAFSGLIVPErdgnetvPEVVATSG 224
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPP-------PVISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 1020158887   225 YALLHFFSDAAYNLTGFNITY 245
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
132-245 5.40e-14

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 69.25  E-value: 5.40e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  132 CGGRFrlTGSSG--FVTDGPGNYKYKTKCTWLIEGQPNRIMRLRFNHFATE----CSWDHLYVYDGDSIYAPLVAAFSGL 205
Cdd:pfam00431    1 CGGVL--TDSSGsiSSPNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1020158887  206 IVPerdgnetvPEVVATSGYALLHFFSDAAYNLTGFNITY 245
Cdd:pfam00431   79 GIP--------EDIVSSSNQMTIKFVSDASVQKRGFKATY 110
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 806-920 2.36e-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: 2.36e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  806 KENYDNAKLFCRNHNALLASLTTQKKVEFVLKQLRimQSSQSmskltltPWVGL-RKINVSYWCWEDMSPFTNSLLQWMP 884
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDFLSSTLK--KSNKY-------FWIGLtDRKNEGTWKWVDGSPVNYTNWAPEP 71

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1020158887  885 SEPSDAGFCGILSePSTRGLKAATCINPlNGSVCER 920
Cdd:pfam00059   72 NNNGENEDCVELS-SSSGKWNDENCNSK-NPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 788-919 9.93e-13

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: 66.08  E-value: 9.93e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887   788 CGIGWHLVGNSCLKITTAKENYDNAKLFCRNHNALLASLTTQKKVEFVLKQLRIMQSSQSMskltltpWVGLRKINVSYW 867
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSGSSDYY-------WIGLSDPDSNGS 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 1020158887   868 C-WEDMSPFTNSLLqWMPSEPSDA-GFCGILSePSTRGLKAATCiNPLNGSVCE 919
Cdd:smart00034   74 WqWSDGSGPVSYSN-WAPGEPNNSsGDCVVLS-TSGGKWNDVSC-TSKLPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 798-920 4.64e-12

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: 64.18  E-value: 4.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  798 SCLKITTAKENYDNAKLFCRNHNALLASLTTQKKVEFVLKQLRIMQSSQSmskltltpWVGLRKINV-SYWCWEDMSPFT 876
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSSSSDV--------WIGLNDLSSeGTWKWSDGSPLV 72

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1020158887  877 NsLLQWMPSEPSDAG--FCGILSEPSTRGLKAATCiNPLNGSVCER 920
Cdd:cd00037     73 D-YTNWAPGEPNPGGseDCVVLSSSSDGKWNDVSC-SSKLPFICEK 116
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 788-894 1.89e-09

C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR); CLECT_DC-SIGN_like: C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN) and the related receptor, DC-SIGN receptor (DC-SIGNR). This group also contains proteins similar to hepatic asialoglycoprotein receptor (ASGP-R) and langerin in human. These proteins are type II membrane proteins with a CTLD ectodomain. CTLD refers to a domain homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. DC-SIGN is thought to mediate the initial contact between dendritic cells and resting T cells, and may also mediate the rolling of DCs on epithelium. DC-SIGN and DC-SIGNR bind to oligosaccharides present on human tissues, as well as, on pathogens including parasites, bacteria, and viruses. DC-SIGN and DC-SIGNR bind to HIV enhancing viral infection of T cells. DC-SIGN and DC-SIGNR are homotetrameric, and contain four CTLDs stabilized by a coiled coil of alpha helices. The hepatic ASGP-R is an endocytic recycling receptor which binds and internalizes desialylated glycoproteins having a terminal galactose or N-acetylgalactosamine residues on their N-linked carbohydrate chains, via the clathrin-coated pit mediated endocytic pathway, and delivers them to lysosomes for degradation. It has been proposed that glycoproteins bearing terminal Sia (sialic acid) alpha2, 6GalNAc and Sia alpha2, 6Gal are endogenous ligands for ASGP-R and that ASGP-R participates in regulating the relative concentration of serum glycoproteins bearing alpha 2,6-linked Sia. The human ASGP-R is a hetero-oligomer composed of two subunits, both of which are found within this group. Langerin is expressed in a subset of dendritic leukocytes, the Langerhans cells (LC). Langerin induces the formation of Birbeck Granules (BGs) and associates with these BGs following internalization. Langerin binds, in a calcium-dependent manner, to glyco-conjugates containing mannose and related sugars mediating their uptake and degradation. Langerin molecules oligomerize as trimers with three CTLDs held together by a coiled-coil of alpha helices.


Pssm-ID: 153060 [Multi-domain]  Cd Length: 126  Bit Score: 56.93  E-value: 1.89e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  788 CGIGWHLVGNSCLKITTAKENYDNAKLFCRNHNALLASLTTQKKVEFVLKQLRIMQSSqsmskltltpWVGLRKINV-SY 866
Cdd:cd03590      1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSY----------WIGLSDEETeGE 70

                           90       100
                   ....*....|....*....|....*...
gi 1020158887  867 WCWEDMSPFTNSLLQWMPSEPSDAGFCG 894
Cdd:cd03590     71 WKWVDGTPLNSSKTFWHPGEPNNWGGGG 98
PHA03098 PHA03098
kelch-like protein; Provisional
 327-491 4.48e-09

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 60.55  E-value: 4.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  327 SFWTREeySNLKLPRASHKAVVNGNIMWVVGGYMFNHSDYNMVLAYDLASREWLPLNRSvnnVVVRYGHSLALYKDKIYM 406
Cdd:PHA03098   368 SKWREE--PPLIFPRYNPCVVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSPL---PISHYGGCAIYHDGKIYV 442

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  407 YGGKIDSTG-NVTNELRVFHIHNESWVLLTPKakeQYAVVGHSAHIVTLKngrvvMLVIFGHCPLYgYISNVQEYDLDKN 485
Cdd:PHA03098   443 IGGISYIDNiKVYNIVESYNPVTNKWTELSSL---NFPRINASLCIFNNK-----IYVVGGDKYEY-YINEIEVYDDKTN 513


                   ....*.
gi 1020158887  486 TWSILH 491
Cdd:PHA03098   514 TWTLFC 519
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 788-920 2.56e-08

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: 53.49  E-value: 2.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  788 CGIGWHLVGNSCLKITTAKENYDNAKLFCRNHNALLASLTTQKKVEFVLKQLRIMqssqsmskltlTPWVGLRKINVSY- 866
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQSQIGSS-----------SYWIGLSREKSEKp 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1020158887  867 WCWEDMSPFTNSLlqwMPSEPSDAGFCGILSEPstrGLKAATCINPlNGSVCER 920
Cdd:cd03593     70 WKWIDGSPLNNLF---NIRGSTKSGNCAYLSST---GIYSEDCSTK-KRWICEK 116
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
544-643 2.68e-07

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 53.62  E-value: 2.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  544 WTILKDSRFFRYLHTAVIVSGTMLVFGGNTHNDTsmshgakcfSSDFMAYDIACDRWSVL---PRPDLHHdvnrfgHSAV 620
Cdd:COG3055      3 WSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSA---------SNSFEVYDPATNTWSELaplPGPPRHH------AAAV 67

                           90       100
                   ....*....|....*....|....*...
gi 1020158887  621 LHNSTMYVFGGFN-----SLLLSDILVF 643
Cdd:COG3055     68 AQDGKLYVFGGFTganpsSTPLNDVYVY 95
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1062-1107 7.63e-05

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: 41.57  E-value: 7.63e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1020158887 1062 ACQCNGHSK----CINQS-ICEkCENLTTGKHCETCISGFYGDPTNGGKCQ 1107
Cdd:cd00055      1 PCDCNGHGSlsgqCDPGTgQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 932-983 1.04e-04

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


Pssm-ID: 396154 [Multi-domain]  Cd Length: 52  Bit Score: 41.15  E-value: 1.04e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1020158887  932 PCALRTACGDCT-SGSSECMWCSNMKQCVDSNAYvaSFPFGQCMEWYT-MSTCP 983
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQaSSKCP 52
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 390-428 4.19e-04

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


Pssm-ID: 433528 [Multi-domain]  Cd Length: 41  Bit Score: 39.09  E-value: 4.19e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1020158887  390 VVRYGHSLALYKDKIYMYGGKIDSTGNVTNELRVFHIHN 428
Cdd:pfam13854    2 VPRYGHCAVTVGDYIYLYGGYTGGEGQPSDDVYVLSLPT 40
PRK14131 PRK14131
N-acetylneuraminate epimerase;
532-633 5.55e-04

N-acetylneuraminate epimerase;


Pssm-ID: 237617 [Multi-domain]  Cd Length: 376  Bit Score: 43.85  E-value: 5.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  532 DDLYRYDVDTQM--WTILKDsrfF----RYLHTAVIVSGTMLVFGGNTHNDTSmshGAKCFSSDFMAYDIACDRWSVLpr 605
Cdd:PRK14131    50 TSWYKLDLNAPSkgWTKIAA---FpggpREQAVAAFIDGKLYVFGGIGKTNSE---GSPQVFDDVYKYDPKTNSWQKL-- 121

                           90       100
                   ....*....|....*....|....*....
gi 1020158887  606 pDLHHDVNRFGHSAV-LHNSTMYVFGGFN 633
Cdd:PRK14131   122 -DTRSPVGLAGHVAVsLHNGKAYITGGVN 149
PLN02153 PLN02153
epithiospecifier protein
 514-631 1.35e-03

epithiospecifier protein


Pssm-ID: 177814 [Multi-domain]  Cd Length: 341  Bit Score: 42.67  E-value: 1.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  514 LYVHGGykAFSANKYrLADDLYRYDVDTQMWTILK---DSRFFRYLHTAVIVSGTML-VFGGNTHNdtsmshgaKCFsSD 589
Cdd:PLN02153    35 LYSFGG--ELKPNEH-IDKDLYVFDFNTHTWSIAPangDVPRISCLGVRMVAVGTKLyIFGGRDEK--------REF-SD 102

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1020158887  590 FMAYDIACDRWSVLPRPDLHHDVN-RFGHSAVLHNSTMYVFGG 631
Cdd:PLN02153   103 FYSYDTVKNEWTFLTKLDEEGGPEaRTFHSMASDENHVYVFGG 145
PHA03098 PHA03098
kelch-like protein; Provisional
 330-643 3.67e-03

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 41.68  E-value: 3.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  330 TREEYSNLKLPRASHKAVVNGNIMWVVGGYMFNHSDYNMvlaydlasreWLPLNRSVNNVVVRYGHSlALYKDKIYMYGG 409
Cdd:PHA03098   234 SKKYNLNKILPRSSTFGSIIYIHITMSIFTYNYITNYSP----------LSEINTIIDIHYVYCFGS-VVLNNVIYFIGG 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  410 KIDSTGNVTNELRVfHIHNESWVLLTP--KAKEQYAVvghsahivTLKNGRvvMLVIFGhcpLY--GYISNVQEYDLDKN 485
Cdd:PHA03098   303 MNKNNLSVNSVVSY-DTKTKSWNKVPEliYPRKNPGV--------TVFNNR--IYVIGG---IYnsISLNTVESWKPGES 368

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020158887  486 TWSILHTqgaLVQGGYGHSSVYDHRTraLYVHGGYKAFsankYRLADDLYRYDVDTQMWTILKDSRFFRYLHTAVIVSGT 565
Cdd:PHA03098   369 KWREEPP---LIFPRYNPCVVNVNNL--IYVIGGISKN----DELLKTVECFSLNTNKWSKGSPLPISHYGGCAIYHDGK 439

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1020158887  566 MLVFGGNTHNDtsmshGAKCFSSDFMaYDIACDRWSVLPRPDLHhdvnRFGHSAVLHNSTMYVFGGF-NSLLLSDILVF 643
Cdd:PHA03098   440 IYVIGGISYID-----NIKVYNIVES-YNPVTNKWTELSSLNFP----RINASLCIFNNKIYVVGGDkYEYYINEIEVY 508
Kelch_1 pfam01344
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 340-379 6.92e-03

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


Pssm-ID: 396078 [Multi-domain]  Cd Length: 46  Bit Score: 35.67  E-value: 6.92e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1020158887  340 PRASHKAVVNGNIMWVVGGYMFNHSDyNMVLAYDLASREW 379
Cdd:pfam01344    1 RRSGAGVVVVGGKIYVIGGFDGNQSL-NSVEVYDPETNTW 39
Kelch_6 pfam13964
Kelch motif;
392-436 9.82e-03

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 35.39  E-value: 9.82e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1020158887  392 RYGHSLALYKDKIYMYGGKIDStGNVTNELRVFHIHNESWVLLTP 436
Cdd:pfam13964    2 RTFHSVVSVGGYIYVFGGYTNA-SPALNKLEVYNPLTKSWEELPP 45
 
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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