NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1838086999|ref|XP_033969893|]
View 

attractin isoform X2 [Trematomus bernacchii]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 729-858 1.59e-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: 254.43  E-value: 1.59e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  729 CGESWHLVGNSCVKIITAKDSYDNAKLACRSHNAVLASLTTQKKVDFVLKELQIMSVvYKASLTPWVGLRKINVSYWCWE 808
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQM-TKQKLTPWVGLRKINVSYWCWE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1838086999  809 DMSPFTNTSLQWLPGEPSDAGFCGYLAEPASSGLKAQTCINPVNGSLCER 858
Cdd:cd03597     80 DMSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 71-186 1.99e-21

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: 90.93  E-value: 1.99e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999   71 CGGRFRLTgPSGHLS--DGPGNYKYKTKCTWLIEGQPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSgl 144
Cdd:cd00041      1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFC-- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1838086999  145 ivperyGNETVPEVVSQSGYALLHFFSDAAYNLTGFNISYRV 186
Cdd:cd00041     78 ------GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
NanM super family cl34543
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
282-572 5.09e-18

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


The actual alignment was detected with superfamily member COG3055:

Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 85.98  E-value: 5.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  282 AVVDQGIMWVIGGYvFNASDYHVVKAYNLSSKSWLTLDPSvnTVTPRYGHSLALHEGRIYMYGG--KIDSTGNVSSQLWV 359
Cdd:COG3055     18 AALLDGKVYVAGGL-SGGSASNSFEVYDPATNTWSELAPL--PGPPRHHAAAVAQDGKLYVFGGftGANPSSTPLNDVYV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  360 FHIQNQTWVLLSPRAKdqyPVVGHSAHIVpplqeeDSPIMLVlfGHCPLYGYINQVQEYNIVRNTWSMVAtdgALVQGGY 439
Cdd:COG3055     95 YDPATNTWTKLAPMPT---PRGGATALLL------DGKIYVV--GGWDDGGNVAWVEVYDPATGTWTQLA---PLPTPRD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  440 GHSSAFDPSSRaIYTHGGYKAFSANKyglagdlykfevdkmKWTILRDSGFFRYLHTAVMVSGTMLVFGGNTHndtsmsh 519
Cdd:COG3055    161 HLAAAVLPDGK-ILVIGGRNGSGFSN---------------TWTTLAPLPTARAGHAAAVLGGKILVFGGESG------- 217

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1838086999  520 gakcFSSEFLSYSLACDEWTV---LPRPdlfqdvnRFGHSAVISDSVMYVFGGFNS 572
Cdd:COG3055    218 ----FSDEVEAYDPATNTWTAlgeLPTP-------RHGHAAVLTDGKVYVIGGETK 262
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1009-1054 2.46e-07

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: 48.50  E-value: 2.46e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1838086999 1009 ACQCNGHS----QCVNES-VCEkCEDLTTGRHCESCISGFYGDPTNGGNCQ 1054
Cdd:cd00055      1 PCDCNGHGslsgQCDPGTgQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
Sema super family cl15693
The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins ...
 921-951 1.32e-03

The Sema domain, a protein interacting module, of semaphorins and plexins; Both semaphorins and plexins have a Sema domain on their N-termini. Plexins function as receptors for the semaphorins. Evolutionarily, plexins may be the ancestor of semaphorins. Semaphorins are regulatory molecules in the development of the nervous system and in axonal guidance. They also play important roles in other biological processes, such as angiogenesis, immune regulation, respiration systems, and cancer. Semaphorins can be divided into 7 classes. Vertebrates have members in classes 3-7, whereas classes 1 and 2 are known only in invertebrates. Class 2 and 3 semaphorins are secreted; classes 1 and 4 through 6 are transmembrane proteins; and class 7 is membrane associated via glycosylphosphatidylinositol (GPI) linkage. Plexins are a large family of transmembrane proteins, which are divided into four types (A-D) according to sequence similarity. In vertebrates, type A plexins serve as co-receptors for neuropilins to mediate the signalling of class 3 semaphorins. Plexins serve as direct receptors for several other members of the semaphorin family: class 6 semaphorins signal through type A plexins and class 4 semaphorins through type B plexins. This family also includes the MET and RON receptor tyrosine kinases. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves to recognize and bind receptors.


The actual alignment was detected with superfamily member cd11272:

Pssm-ID: 472829 [Multi-domain]  Cd Length: 515  Bit Score: 43.00  E-value: 1.32e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1838086999  921 PPENCSGYRTCGQCLDQ--PGCGWCTDHNNTGR 951
Cdd:cd11272    470 PVESCEQYTTCGECLSSgdPHCGWCALHNMCSR 502
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1055-1100 3.26e-03

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


:

Pssm-ID: 238012  Cd Length: 50  Bit Score: 36.95  E-value: 3.26e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1838086999 1055 PCKCNGHASM---CNPNNGKCFCtTKGIKGDRCHLCevENRYQGNPLKG 1100
Cdd:cd00055      1 PCDCNGHGSLsgqCDPGTGQCEC-KPNTTGRRCDRC--APGYYGLPSQG 46
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 870-921 6.27e-03

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: 36.15  E-value: 6.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1838086999  870 PCAMRAMCSECT-SGSSECMWCSNMKQCVDSNAYvaSFPFGQCMEWFT-MNTCP 921
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 ...
 729-858 1.59e-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: 254.43  E-value: 1.59e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  729 CGESWHLVGNSCVKIITAKDSYDNAKLACRSHNAVLASLTTQKKVDFVLKELQIMSVvYKASLTPWVGLRKINVSYWCWE 808
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQM-TKQKLTPWVGLRKINVSYWCWE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1838086999  809 DMSPFTNTSLQWLPGEPSDAGFCGYLAEPASSGLKAQTCINPVNGSLCER 858
Cdd:cd03597     80 DMSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 71-186 1.99e-21

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: 90.93  E-value: 1.99e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999   71 CGGRFRLTgPSGHLS--DGPGNYKYKTKCTWLIEGQPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSgl 144
Cdd:cd00041      1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFC-- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1838086999  145 ivperyGNETVPEVVSQSGYALLHFFSDAAYNLTGFNISYRV 186
Cdd:cd00041     78 ------GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
282-572 5.09e-18

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 85.98  E-value: 5.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  282 AVVDQGIMWVIGGYvFNASDYHVVKAYNLSSKSWLTLDPSvnTVTPRYGHSLALHEGRIYMYGG--KIDSTGNVSSQLWV 359
Cdd:COG3055     18 AALLDGKVYVAGGL-SGGSASNSFEVYDPATNTWSELAPL--PGPPRHHAAAVAQDGKLYVFGGftGANPSSTPLNDVYV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  360 FHIQNQTWVLLSPRAKdqyPVVGHSAHIVpplqeeDSPIMLVlfGHCPLYGYINQVQEYNIVRNTWSMVAtdgALVQGGY 439
Cdd:COG3055     95 YDPATNTWTKLAPMPT---PRGGATALLL------DGKIYVV--GGWDDGGNVAWVEVYDPATGTWTQLA---PLPTPRD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  440 GHSSAFDPSSRaIYTHGGYKAFSANKyglagdlykfevdkmKWTILRDSGFFRYLHTAVMVSGTMLVFGGNTHndtsmsh 519
Cdd:COG3055    161 HLAAAVLPDGK-ILVIGGRNGSGFSN---------------TWTTLAPLPTARAGHAAAVLGGKILVFGGESG------- 217

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1838086999  520 gakcFSSEFLSYSLACDEWTV---LPRPdlfqdvnRFGHSAVISDSVMYVFGGFNS 572
Cdd:COG3055    218 ----FSDEVEAYDPATNTWTAlgeLPTP-------RHGHAAVLTDGKVYVIGGETK 262
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 88-184 5.37e-17

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: 77.82  E-value: 5.37e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999    88 PGNYKYKTKCTWLIEGQPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSGLIVPERYgnetvpeVVSQSG 163
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPPPV-------ISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 1838086999   164 YALLHFFSDAAYNLTGFNISY 184
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
71-184 6.42e-16

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 75.02  E-value: 6.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999   71 CGGRFrlTGPSGHLS--DGPGNYKYKTKCTWLIEGQPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSGL 144
Cdd:pfam00431    1 CGGVL--TDSSGSISspNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1838086999  145 IVPerygnetvPEVVSQSGYALLHFFSDAAYNLTGFNISY 184
Cdd:pfam00431   79 GIP--------EDIVSSSNQMTIKFVSDASVQKRGFKATY 110
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 747-858 5.86e-15

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 72.13  E-value: 5.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  747 KDSYDNAKLACRSHNAVLASLTTQKKVDFvlkelqIMSVVYKASLTPWVGL-RKINVSYWCWEDMSPFTNTSLQWLPGEP 825
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDF------LSSTLKKSNKYFWIGLtDRKNEGTWKWVDGSPVNYTNWAPEPNNN 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1838086999  826 SDAGFCGYLaEPASSGLKAQTCINpVNGSLCER 858
Cdd:pfam00059   75 GENEDCVEL-SSSSGKWNDENCNS-KNPFVCEK 105
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 729-857 2.98e-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: 68.01  E-value: 2.98e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999   729 CGESWHLVGNSCVKIITAKDSYDNAKLACRSHNAVLASLTTQKKVDFVLKELQIMSvvykASLTPWVGLRKINVSYWC-W 807
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSG----SSDYYWIGLSDPDSNGSWqW 76

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1838086999   808 EDMSPFTNTSLqWLPGEPSDA-GFCGYLaEPASSGLKAQTCINPvNGSLCE 857
Cdd:smart00034   77 SDGSGPVSYSN-WAPGEPNNSsGDCVVL-STSGGKWNDVSCTSK-LPFVCE 124
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1009-1054 2.46e-07

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: 48.50  E-value: 2.46e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1838086999 1009 ACQCNGHS----QCVNES-VCEkCEDLTTGRHCESCISGFYGDPTNGGNCQ 1054
Cdd:cd00055      1 PCDCNGHGslsgQCDPGTgQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PHA03098 PHA03098
kelch-like protein; Provisional
 282-428 1.81e-06

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 52.46  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  282 AVVDQGIMWVIGGYVFNASDYHVVKAYNLSSKSWLTLDPsvnTVTPRYGHSLALHEGRIYMYGGKIDSTG-NVSSQLWVF 360
Cdd:PHA03098   385 VVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSP---LPISHYGGCAIYHDGKIYVIGGISYIDNiKVYNIVESY 461

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838086999  361 HIQNQTWVLLSPRakdQYPVVGHSAHIVpplqeEDSpiMLVLFGHCPLYgYINQVQEYNIVRNTWSMV 428
Cdd:PHA03098   462 NPVTNKWTELSSL---NFPRINASLCIF-----NNK--IYVVGGDKYEY-YINEIEVYDDKTNTWTLF 518
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 326-362 7.80e-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: 44.09  E-value: 7.80e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1838086999  326 TPRYGHSLALHEGRIYMYGGKIDSTGNVSSQLWVFHI 362
Cdd:pfam13854    2 VPRYGHCAVTVGDYIYLYGGYTGGEGQPSDDVYVLSL 38
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1010-1053 2.23e-04

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 40.03  E-value: 2.23e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1838086999 1010 CQCNGH----SQCVNES-VCEkCEDLTTGRHCESCISGFYGDP-TNGGNC 1053
Cdd:pfam00053    1 CDCNPHgslsDTCDPETgQCL-CKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1010-1050 9.81e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.06  E-value: 9.81e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1838086999  1010 CQCNG----HSQCVNES-VCEkCEDLTTGRHCESCISGFYGDPTNG 1050
Cdd:smart00180    1 CDCDPggsaSGTCDPDTgQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
 921-951 1.32e-03

The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor for class 6 semaphorins. Interactions between Plexin A2, A4 and semaphorins 6A and 6B control the lamina-restricted projection of hippocampal mossy fibers. Sema6B also repels the growth of mossy fibers in a Plexin A4 dependent manner. Plexin A2 does not suppress Sema6B function. In addition, studies have shown that Plexin A2 may be related to anxiety and other psychiatric disorders. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200533 [Multi-domain]  Cd Length: 515  Bit Score: 43.00  E-value: 1.32e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1838086999  921 PPENCSGYRTCGQCLDQ--PGCGWCTDHNNTGR 951
Cdd:cd11272    470 PVESCEQYTTCGECLSSgdPHCGWCALHNMCSR 502
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1055-1100 3.26e-03

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 36.95  E-value: 3.26e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1838086999 1055 PCKCNGHASM---CNPNNGKCFCtTKGIKGDRCHLCevENRYQGNPLKG 1100
Cdd:cd00055      1 PCDCNGHGSLsgqCDPGTGQCEC-KPNTTGRRCDRC--APGYYGLPSQG 46
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 924-947 4.71e-03

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: 36.53  E-value: 4.71e-03
                           10        20
                   ....*....|....*....|....*.
gi 1838086999  924 NCSGYRTCGQCL--DQPGCGWCTDHN 947
Cdd:pfam01437    1 RCSQYTSCSSCLaaRDPYCGWCSSEG 26
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 870-921 6.27e-03

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: 36.15  E-value: 6.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1838086999  870 PCAMRAMCSECT-SGSSECMWCSNMKQCVDSNAYvaSFPFGQCMEWFT-MNTCP 921
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 ...
 729-858 1.59e-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: 254.43  E-value: 1.59e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  729 CGESWHLVGNSCVKIITAKDSYDNAKLACRSHNAVLASLTTQKKVDFVLKELQIMSVvYKASLTPWVGLRKINVSYWCWE 808
Cdd:cd03597      1 CGEGWHLVGNSCLKINTARESYDNAKLYCRNLNAVLASLTTQKKVEFVLKELQKHQM-TKQKLTPWVGLRKINVSYWCWE 79

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1838086999  809 DMSPFTNTSLQWLPGEPSDAGFCGYLAEPASSGLKAQTCINPVNGSLCER 858
Cdd:cd03597     80 DMSPFTNTTLQWLPGEPSDAGFCGYLEEPAVSGLKANPCTNPVNGSVCER 129
CUB cd00041
CUB domain; extracellular domain; present in proteins mostly known to be involved in ...
 71-186 1.99e-21

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: 90.93  E-value: 1.99e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999   71 CGGRFRLTgPSGHLS--DGPGNYKYKTKCTWLIEGQPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSgl 144
Cdd:cd00041      1 CGGTLTAS-TSGTISspNYPNNYPNNLNCVWTIEAPPGYRIRLTFEDFDLEsspnCSYDYLEIYDGPSTSSPLLGRFC-- 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1838086999  145 ivperyGNETVPEVVSQSGYALLHFFSDAAYNLTGFNISYRV 186
Cdd:cd00041     78 ------GSTLPPPIISSGNSLTVRFRSDSSVTGRGFKATYSA 113
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
282-572 5.09e-18

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 85.98  E-value: 5.09e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  282 AVVDQGIMWVIGGYvFNASDYHVVKAYNLSSKSWLTLDPSvnTVTPRYGHSLALHEGRIYMYGG--KIDSTGNVSSQLWV 359
Cdd:COG3055     18 AALLDGKVYVAGGL-SGGSASNSFEVYDPATNTWSELAPL--PGPPRHHAAAVAQDGKLYVFGGftGANPSSTPLNDVYV 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  360 FHIQNQTWVLLSPRAKdqyPVVGHSAHIVpplqeeDSPIMLVlfGHCPLYGYINQVQEYNIVRNTWSMVAtdgALVQGGY 439
Cdd:COG3055     95 YDPATNTWTKLAPMPT---PRGGATALLL------DGKIYVV--GGWDDGGNVAWVEVYDPATGTWTQLA---PLPTPRD 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  440 GHSSAFDPSSRaIYTHGGYKAFSANKyglagdlykfevdkmKWTILRDSGFFRYLHTAVMVSGTMLVFGGNTHndtsmsh 519
Cdd:COG3055    161 HLAAAVLPDGK-ILVIGGRNGSGFSN---------------TWTTLAPLPTARAGHAAAVLGGKILVFGGESG------- 217

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1838086999  520 gakcFSSEFLSYSLACDEWTV---LPRPdlfqdvnRFGHSAVISDSVMYVFGGFNS 572
Cdd:COG3055    218 ----FSDEVEAYDPATNTWTAlgeLPTP-------RHGHAAVLTDGKVYVIGGETK 262
CUB smart00042
Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein; This domain is found ...
 88-184 5.37e-17

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: 77.82  E-value: 5.37e-17
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999    88 PGNYKYKTKCTWLIEGQPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSGLIVPERYgnetvpeVVSQSG 163
Cdd:smart00042    9 PQSYPNNLDCVWTIRAPPGYRIELQFTDFDLEssdnCEYDYVEIYDGPSASSPLLGRFCGSEAPPPV-------ISSSSN 81

                            90       100
                    ....*....|....*....|.
gi 1838086999   164 YALLHFFSDAAYNLTGFNISY 184
Cdd:smart00042   82 SLTLTFVSDSSVQKRGFSARY 102
CUB pfam00431
CUB domain;
71-184 6.42e-16

CUB domain;


Pssm-ID: 395345 [Multi-domain]  Cd Length: 110  Bit Score: 75.02  E-value: 6.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999   71 CGGRFrlTGPSGHLS--DGPGNYKYKTKCTWLIEGQPNTILRLRFNHFATE----CSWDHLYVYDGDSIYAPLLAAFSGL 144
Cdd:pfam00431    1 CGGVL--TDSSGSISspNYPNPYPPNKDCVWLIRAPPGFRVKLTFQDFELEdhdeCGYDYVEIRDGPSASSPLLGRFCGS 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1838086999  145 IVPerygnetvPEVVSQSGYALLHFFSDAAYNLTGFNISY 184
Cdd:pfam00431   79 GIP--------EDIVSSSNQMTIKFVSDASVQKRGFKATY 110
Lectin_C pfam00059
Lectin C-type domain; This family includes both long and short form C-type
 747-858 5.86e-15

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


Pssm-ID: 459655 [Multi-domain]  Cd Length: 105  Bit Score: 72.13  E-value: 5.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  747 KDSYDNAKLACRSHNAVLASLTTQKKVDFvlkelqIMSVVYKASLTPWVGL-RKINVSYWCWEDMSPFTNTSLQWLPGEP 825
Cdd:pfam00059    1 SKTWDEAREACRKLGGHLVSINSAEELDF------LSSTLKKSNKYFWIGLtDRKNEGTWKWVDGSPVNYTNWAPEPNNN 74

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1838086999  826 SDAGFCGYLaEPASSGLKAQTCINpVNGSLCER 858
Cdd:pfam00059   75 GENEDCVEL-SSSSGKWNDENCNS-KNPFVCEK 105
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
273-513 2.50e-14

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 74.81  E-value: 2.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  273 PGLAKASHKAVVDQGIMWVIGGYVFNASDYHVVK---AYNLSSKSWLTLDPSVntvTPRYGHSLALHEGRIYMYGGkIDS 349
Cdd:COG3055     57 PGPPRHHAAAVAQDGKLYVFGGFTGANPSSTPLNdvyVYDPATNTWTKLAPMP---TPRGGATALLLDGKIYVVGG-WDD 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  350 TGNVSSqLWVFHIQNQTWVLLS--PRAKDqypvvGHSAHIVPplqeeDSpiMLVLFGhcplyGYINQVQEynivrNTWSm 427
Cdd:COG3055    133 GGNVAW-VEVYDPATGTWTQLAplPTPRD-----HLAAAVLP-----DG--KILVIG-----GRNGSGFS-----NTWT- 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  428 vaTDGALVQGGYGHSSAFDpsSRAIYTHGGYKAFSANkyglagdLYKFEVDKMKWTILRDSGFFRYLHTAVMVSGTMLVF 507
Cdd:COG3055    189 --TLAPLPTARAGHAAAVL--GGKILVFGGESGFSDE-------VEAYDPATNTWTALGELPTPRHGHAAVLTDGKVYVI 257


                   ....*.
gi 1838086999  508 GGNTHN 513
Cdd:COG3055    258 GGETKP 263
CLECT smart00034
C-type lectin (CTL) or carbohydrate-recognition domain (CRD); Many of these domains function ...
 729-857 2.98e-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: 68.01  E-value: 2.98e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999   729 CGESWHLVGNSCVKIITAKDSYDNAKLACRSHNAVLASLTTQKKVDFVLKELQIMSvvykASLTPWVGLRKINVSYWC-W 807
Cdd:smart00034    1 CPSGWISYGGKCYKFSTEKKTWEDAQAFCQSLGGHLASIHSEAENDFVASLLKNSG----SSDYYWIGLSDPDSNGSWqW 76

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|.
gi 1838086999   808 EDMSPFTNTSLqWLPGEPSDA-GFCGYLaEPASSGLKAQTCINPvNGSLCE 857
Cdd:smart00034   77 SDGSGPVSYSN-WAPGEPNNSsGDCVVL-STSGGKWNDVSCTSK-LPFVCE 124
CLECT cd00037
C-type lectin (CTL)/C-type lectin-like (CTLD) domain; CLECT: C-type lectin (CTL)/C-type ...
 739-858 1.10e-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: 66.10  E-value: 1.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  739 SCVKIITAKDSYDNAKLACRSHNAVLASLTTQKKVDFVLKELQIMSvvykaSLTPWVGLRKINV-SYWCWEDMSPFTNTS 817
Cdd:cd00037      1 SCYKFSTEKLTWEEAQEYCRSLGGHLASIHSEEENDFLASLLKKSS-----SSDVWIGLNDLSSeGTWKWSDGSPLVDYT 75

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1838086999  818 lQWLPGEPSDAG--FCGYLAEPASSGLKAQTCiNPVNGSLCER 858
Cdd:cd00037     76 -NWAPGEPNPGGseDCVVLSSSSDGKWNDVSC-SSKLPFICEK 116
CLECT_NK_receptors_like cd03593
C-type lectin-like domain (CTLD) of the type found in natural killer cell receptors (NKRs); ...
 729-858 1.17e-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: 51.56  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  729 CGESWHLVGNSCVKIITAKDSYDNAKLACRSHNAVLASLTTQKKVDFVLKelqimsvvYKASLTPWVGLRKINVSY-WCW 807
Cdd:cd03593      1 CPKDWICYGNKCYYFSMEKKTWNESKEACSSKNSSLLKIDDEEELEFLQS--------QIGSSSYWIGLSREKSEKpWKW 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1838086999  808 EDMSPFTNtslqWL-PGEPSDAGFCGYLaepASSGLKAQTCINPvNGSLCER 858
Cdd:cd03593     73 IDGSPLNN----LFnIRGSTKSGNCAYL---SSTGIYSEDCSTK-KRWICEK 116
CLECT_DC-SIGN_like cd03590
C-type lectin-like domain (CTLD) of the type found in human dendritic cell (DC)-specific ...
 729-832 1.46e-07

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: 51.54  E-value: 1.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  729 CGESWHLVGNSCVKIITAKDSYDNAKLACRSHNAVLASLTTQKKVDFVLKELQIMSVVykasltpWVGLRKINV-SYWCW 807
Cdd:cd03590      1 CPTNWKSFQSSCYFFSTEKKSWEESRQFCEDMGAHLVIINSQEEQEFISKILSGNRSY-------WIGLSDEETeGEWKW 73

                           90       100
                   ....*....|....*....|....*
gi 1838086999  808 EDMSPFTNTSLQWLPGEPSDAGFCG 832
Cdd:cd03590     74 VDGTPLNSSKTFWHPGEPNNWGGGG 98
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1009-1054 2.46e-07

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: 48.50  E-value: 2.46e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1838086999 1009 ACQCNGHS----QCVNES-VCEkCEDLTTGRHCESCISGFYGDPTNGGNCQ 1054
Cdd:cd00055      1 PCDCNGHGslsgQCDPGTgQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
PHA03098 PHA03098
kelch-like protein; Provisional
 282-428 1.81e-06

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 52.46  E-value: 1.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  282 AVVDQGIMWVIGGYVFNASDYHVVKAYNLSSKSWLTLDPsvnTVTPRYGHSLALHEGRIYMYGGKIDSTG-NVSSQLWVF 360
Cdd:PHA03098   385 VVNVNNLIYVIGGISKNDELLKTVECFSLNTNKWSKGSP---LPISHYGGCAIYHDGKIYVIGGISYIDNiKVYNIVESY 461

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838086999  361 HIQNQTWVLLSPRakdQYPVVGHSAHIVpplqeEDSpiMLVLFGHCPLYgYINQVQEYNIVRNTWSMV 428
Cdd:PHA03098   462 NPVTNKWTELSSL---NFPRINASLCIF-----NNK--IYVVGGDKYEY-YINEIEVYDDKTNTWTLF 518
Kelch_5 pfam13854
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 326-362 7.80e-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: 44.09  E-value: 7.80e-06
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1838086999  326 TPRYGHSLALHEGRIYMYGGKIDSTGNVSSQLWVFHI 362
Cdd:pfam13854    2 VPRYGHCAVTVGDYIYLYGGYTGGEGQPSDDVYVLSL 38
Kelch_6 pfam13964
Kelch motif;
327-372 1.24e-05

Kelch motif;


Pssm-ID: 404790 [Multi-domain]  Cd Length: 50  Bit Score: 43.86  E-value: 1.24e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1838086999  327 PRYGHSLALHEGRIYMYGGKIDStGNVSSQLWVFHIQNQTWVLLSP 372
Cdd:pfam13964    1 PRTFHSVVSVGGYIYVFGGYTNA-SPALNKLEVYNPLTKSWEELPP 45
NanM COG3055
N-acetylneuraminic acid mutarotase [Cell wall/membrane/envelope biogenesis];
482-581 4.10e-05

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


Pssm-ID: 442289 [Multi-domain]  Cd Length: 277  Bit Score: 47.07  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  482 WTILRDSGFFRYLHTAVMVSGTMLVFGGNTHNDTsmshgakcfSSEFLSYSLACDEWTVLPRpdlFQDVNRFGHSAVISD 561
Cdd:COG3055      3 WSSLPDLPTPRSEAAAALLDGKVYVAGGLSGGSA---------SNSFEVYDPATNTWSELAP---LPGPPRHHAAAVAQD 70

                           90       100
                   ....*....|....*....|....*
gi 1838086999  562 SVMYVFGGFN-----SLLLSDVLMY 581
Cdd:COG3055     71 GKLYVFGGFTganpsSTPLNDVYVY 95
Laminin_EGF pfam00053
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
 1010-1053 2.23e-04

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


Pssm-ID: 395007  Cd Length: 49  Bit Score: 40.03  E-value: 2.23e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1838086999 1010 CQCNGH----SQCVNES-VCEkCEDLTTGRHCESCISGFYGDP-TNGGNC 1053
Cdd:pfam00053    1 CDCNPHgslsDTCDPETgQCL-CKPGVTGRHCDRCKPGYYGLPsDPPQGC 49
CLECT_1 cd03602
C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains ...
 757-834 5.89e-04

C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins; CLECT_1: C-type lectin (CTL)/C-type lectin-like (CTLD) domain subgroup 1; a subgroup of protein domains homologous to the carbohydrate-recognition domains (CRDs) of the C-type lectins. 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. CTLDs may bind a variety of carbohydrate ligands including mannose, N-acetylglucosamine, galactose, N-acetylgalactosamine, and fucose. CTLDs associate with each other through several different surfaces to form dimers, trimers, or tetramers from which ligand-binding sites project in different orientations. In some CTLDs a loop extends to the adjoining domain to form a loop-swapped dimer.


Pssm-ID: 153072  Cd Length: 108  Bit Score: 40.82  E-value: 5.89e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1838086999  757 CRSHNAVLASLTTQKkvdfvlkELQIMSVVYKASLTP-WVGLRKiNVSYWCWEDMSPFTntSLQWLPGEPSDAGFCGYL 834
Cdd:cd03602     19 CRENYTDLATVQNQE-------DNALLSNLSRVSNSAaWIGLYR-DVDSWRWSDGSESS--FRNWNTFQPFGQGDCATM 87
PHA03098 PHA03098
kelch-like protein; Provisional
 282-509 9.15e-04

kelch-like protein; Provisional


Pssm-ID: 222983 [Multi-domain]  Cd Length: 534  Bit Score: 43.60  E-value: 9.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  282 AVVDQGIMWVIGGYVFNASDYHVVKAYNLSSKSWLTLdPSVNtvTPRYGHSLALHEGRIYMYGGkIDSTGNVSSQLWVFH 361
Cdd:PHA03098   290 SVVLNNVIYFIGGMNKNNLSVNSVVSYDTKTKSWNKV-PELI--YPRKNPGVTVFNNRIYVIGG-IYNSISLNTVESWKP 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1838086999  362 IQNQtWVLLSPRakdQYPVVGHSAHIVPPLqeedspiMLVLFGHCPLYGYINQVQEYNIVRNTWSMVAtdgALVQGGYGH 441
Cdd:PHA03098   366 GESK-WREEPPL---IFPRYNPCVVNVNNL-------IYVIGGISKNDELLKTVECFSLNTNKWSKGS---PLPISHYGG 431

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1838086999  442 SSAFdpSSRAIYTHGGYKafSANKYGLAGDLYKFEVDKMKWTILRDSGFFRYLHTAVMVSGTMLVFGG 509
Cdd:PHA03098   432 CAIY--HDGKIYVIGGIS--YIDNIKVYNIVESYNPVTNKWTELSSLNFPRINASLCIFNNKIYVVGG 495
EGF_Lam smart00180
Laminin-type epidermal growth factor-like domai;
1010-1050 9.81e-04

Laminin-type epidermal growth factor-like domai;


Pssm-ID: 214543  Cd Length: 46  Bit Score: 38.06  E-value: 9.81e-04
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....*.
gi 1838086999  1010 CQCNG----HSQCVNES-VCEkCEDLTTGRHCESCISGFYGDPTNG 1050
Cdd:smart00180    1 CDCDPggsaSGTCDPDTgQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
Sema_plexin_A2 cd11272
The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor ...
 921-951 1.32e-03

The Sema domain, a protein interacting module, of Plexin A2; Plexin A2 serves as a receptor for class 6 semaphorins. Interactions between Plexin A2, A4 and semaphorins 6A and 6B control the lamina-restricted projection of hippocampal mossy fibers. Sema6B also repels the growth of mossy fibers in a Plexin A4 dependent manner. Plexin A2 does not suppress Sema6B function. In addition, studies have shown that Plexin A2 may be related to anxiety and other psychiatric disorders. The Sema domain is located at the N-terminus and contains four disulfide bonds formed by eight conserved cysteine residues. It serves as a ligand-recognition and -binding module.


Pssm-ID: 200533 [Multi-domain]  Cd Length: 515  Bit Score: 43.00  E-value: 1.32e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1838086999  921 PPENCSGYRTCGQCLDQ--PGCGWCTDHNNTGR 951
Cdd:cd11272    470 PVESCEQYTTCGECLSSgdPHCGWCALHNMCSR 502
Kelch_2 pfam07646
Kelch motif; The kelch motif was initially discovered in Kelch. In this protein there are six ...
 327-372 1.45e-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: 462220 [Multi-domain]  Cd Length: 47  Bit Score: 37.70  E-value: 1.45e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1838086999  327 PRYGHSLALHEGRIYMYGGKIDSTGNVSSQLWVFHIQNQTWVLLSP 372
Cdd:pfam07646    1 PRYPHASSVPGGKLYVVGGSDGLGDLSSSDVLVYDPETNVWTEVPR 46
EGF_Lam cd00055
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ...
 1055-1100 3.26e-03

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


Pssm-ID: 238012  Cd Length: 50  Bit Score: 36.95  E-value: 3.26e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1838086999 1055 PCKCNGHASM---CNPNNGKCFCtTKGIKGDRCHLCevENRYQGNPLKG 1100
Cdd:cd00055      1 PCDCNGHGSLsgqCDPGTGQCEC-KPNTTGRRCDRC--APGYYGLPSQG 46
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 924-947 4.71e-03

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: 36.53  E-value: 4.71e-03
                           10        20
                   ....*....|....*....|....*.
gi 1838086999  924 NCSGYRTCGQCL--DQPGCGWCTDHN 947
Cdd:pfam01437    1 RCSQYTSCSSCLaaRDPYCGWCSSEG 26
PSI pfam01437
Plexin repeat; A cysteine rich repeat found in several different extracellular receptors. The ...
 870-921 6.27e-03

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: 36.15  E-value: 6.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1838086999  870 PCAMRAMCSECT-SGSSECMWCSNMKQCVDSNAYvaSFPFGQCMEWFT-MNTCP 921
Cdd:pfam01437    1 RCSQYTSCSSCLaARDPYCGWCSSEGRCVRRSAC--GAPEGNCEEWEQaSSKCP 52
Kelch_4 pfam13418
Galactose oxidase, central domain;
327-372 6.80e-03

Galactose oxidase, central domain;


Pssm-ID: 433191 [Multi-domain]  Cd Length: 49  Bit Score: 36.05  E-value: 6.80e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1838086999  327 PRYGHSL-ALHEGRIYMYGGkIDSTGNVSSQLWVFHIQNQTWVLLSP 372
Cdd:pfam13418    1 PRAYHTStSIPDDTIYLFGG-EGEDGTLLSDLWVFDLSTNEWTRLGS 46
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH