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Conserved domains on  [gi|1774959470|ref|NP_001363255|]
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tRNA-queuosine alpha-mannosyltransferase isoform h [Homo sapiens]

Protein Classification

DUF3524 and Glycosyltransferase_GTB_type domain-containing protein( domain architecture ID 10572306)

DUF3524 and Glycosyltransferase_GTB_type domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 2-164 1.52e-92

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


:

Pssm-ID: 432280  Cd Length: 165  Bit Score: 272.90  E-value: 1.52e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470   2 SILIIEAFYGGSHKQLVDLLQEEL-GDCVVYTLPAKKWHWRARTSALYFSQTIPISEHY-RTLFASSVLNLTELAALRPD 79
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSpHEVDLLTLPARKWKWRMRGSALYFAQEIPDLSAYgDLLFATSMLDLAELRALRPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470  80 LGKLKKILYFHENQLIYPVKKCQERDFQYGYNQILSCLVADVVVFNSVFNMESFLTSMGKFMKLIPDHRPKDLESIIRPK 159
Cdd:pfam12038  81 LANCPKLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRAK 160


                  ....*
gi 1774959470 160 CQVIY 164
Cdd:pfam12038 161 SRVLY 165
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 173-281 4.58e-09

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


:

Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 56.26  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 173 SREHDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHWGYLPSKDDYFQVLCMADVVISTAKH 252
Cdd:cd01635   118 RLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRS 197

                          90       100
                  ....*....|....*....|....*....
gi 1774959470 253 EFFGVAMLEAVYCGCYPLCPKDLVYPEIF 281
Cdd:cd01635   198 EGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 240-332 8.49e-04

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 38.82  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 240 LCMADVVISTAKHEFFGVAMLEAVYCGCYPLC-----PKDLVYPE----IFPAEylysTPEQLSKRLQNFCKRPDIIRKH 310
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIAtdvggLPEVIEDGetglLVPPG----DPEALAEAILRLLEDPELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 1774959470 311 LYKG-EIA--PFSWAALHGKFRSLL 332
Cdd:COG0438    94 GEAArERAeeRFSWEAIAERLLALY 118
 
Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 2-164 1.52e-92

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


Pssm-ID: 432280  Cd Length: 165  Bit Score: 272.90  E-value: 1.52e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470   2 SILIIEAFYGGSHKQLVDLLQEEL-GDCVVYTLPAKKWHWRARTSALYFSQTIPISEHY-RTLFASSVLNLTELAALRPD 79
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSpHEVDLLTLPARKWKWRMRGSALYFAQEIPDLSAYgDLLFATSMLDLAELRALRPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470  80 LGKLKKILYFHENQLIYPVKKCQERDFQYGYNQILSCLVADVVVFNSVFNMESFLTSMGKFMKLIPDHRPKDLESIIRPK 159
Cdd:pfam12038  81 LANCPKLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRAK 160


                  ....*
gi 1774959470 160 CQVIY 164
Cdd:pfam12038 161 SRVLY 165
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 173-281 4.58e-09

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 56.26  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 173 SREHDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHWGYLPSKDDYFQVLCMADVVISTAKH 252
Cdd:cd01635   118 RLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRS 197

                          90       100
                  ....*....|....*....|....*....
gi 1774959470 253 EFFGVAMLEAVYCGCYPLCPKDLVYPEIF 281
Cdd:cd01635   198 EGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 172-340 8.43e-04

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 39.56  E-value: 8.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 172 VSR-EHDKDPESFFKVLMHLKDLGLNFHVSVLGETfTDVPDIFSEAKKALGSSVLHW-GYLPSKD--DYFQvlcMADVVI 247
Cdd:pfam00534   8 VGRlEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG-EEEKRLKKLAEKLGLGDNVIFlGFVSDEDlpELLK---IADVFV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 248 STAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIFpaeylystpeqlskrlqnfckrpdiirKHLYKGE-IAPFSWAALHG 326
Cdd:pfam00534  84 LPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV---------------------------KDGETGFlVKPNNAEALAE 136

                         170
                  ....*....|....*
gi 1774959470 327 KFRSLLT-TEPREDL 340
Cdd:pfam00534 137 AIDKLLEdEELRERL 151
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 240-332 8.49e-04

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 38.82  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 240 LCMADVVISTAKHEFFGVAMLEAVYCGCYPLC-----PKDLVYPE----IFPAEylysTPEQLSKRLQNFCKRPDIIRKH 310
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIAtdvggLPEVIEDGetglLVPPG----DPEALAEAILRLLEDPELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 1774959470 311 LYKG-EIA--PFSWAALHGKFRSLL 332
Cdd:COG0438    94 GEAArERAeeRFSWEAIAERLLALY 118
 
Name Accession Description Interval E-value
DUF3524 pfam12038
Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. ...
 2-164 1.52e-92

Domain of unknown function (DUF3524); This presumed domain is functionally uncharacterized. This domain is found in bacteria and eukaryotes. This domain is about 170 amino acids in length. This domain is found associated with pfam00534. This domain has two conserved sequence motifs: HENQ and FNS. This domain has a single completely conserved residue S that may be functionally important.


Pssm-ID: 432280  Cd Length: 165  Bit Score: 272.90  E-value: 1.52e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470   2 SILIIEAFYGGSHKQLVDLLQEEL-GDCVVYTLPAKKWHWRARTSALYFSQTIPISEHY-RTLFASSVLNLTELAALRPD 79
Cdd:pfam12038   1 KILLLEPFYGGSHKQLADGLAEHSpHEVDLLTLPARKWKWRMRGSALYFAQEIPDLSAYgDLLFATSMLDLAELRALRPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470  80 LGKLKKILYFHENQLIYPVKKCQERDFQYGYNQILSCLVADVVVFNSVFNMESFLTSMGKFMKLIPDHRPKDLESIIRPK 159
Cdd:pfam12038  81 LANCPKLLYFHENQLTYPVRPGQERDFQYGFNNILSALAADRVLFNSRFNRDSFLEAIPALLKKMPDARPKGLVEKIRAK 160


                  ....*
gi 1774959470 160 CQVIY 164
Cdd:pfam12038 161 SRVLY 165
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 173-281 4.58e-09

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 56.26  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 173 SREHDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHWGYLPSKDDYFQVLCMADVVISTAKH 252
Cdd:cd01635   118 RLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRS 197

                          90       100
                  ....*....|....*....|....*....
gi 1774959470 253 EFFGVAMLEAVYCGCYPLCPKDLVYPEIF 281
Cdd:cd01635   198 EGFGLVLLEAMAAGKPVIATDVGGIPEFV 226
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 20-323 7.41e-08

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 53.52  E-value: 7.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470  20 LLQEELGDCVVYTLPAKKWHWRARTSALYFSQTIPISEHYRTLFASSVLNLTELAALRPDL------------GKLKKIL 87
Cdd:cd03809    27 LAKNDPDESVLAVPPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKPDLlhsphntaplllKGCPQVV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470  88 YFHE-NQLIYPvkKCQERDFQYGYNQILSCLV--ADVVVFNSVFNMESFLtsmgKFMKLIPDHRpkdleSIIRPKCQVIY 164
Cdd:cd03809   107 TIHDlIPLRYP--EFFPKRFRLYYRLLLPISLrrADAIITVSEATRDDII----KFYGVPPEKI-----VVIPLGVDPSF 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 165 FPIRFPDVSREHDKDPESFF----------------KVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHW- 227
Cdd:cd03809   176 FPPESAAVLIAKYLLPEPYFlyvgtleprknherllKAFALLKKQGGDLKLVIVGGKGWEDEELLDLVKKLGLGGRVRFl 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 228 GYLPsKDDYFQVLCMADVVISTAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIFPAEYLY---STPEQLSKRLQNFCKRP 304
Cdd:cd03809   256 GYVS-DEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDAALYfdpLDPESIADAILRLLEDP 334

                         330       340
                  ....*....|....*....|.
gi 1774959470 305 DIIRKHLYKG--EIAPFSWAA 323
Cdd:cd03809   335 SLREELIRKGleRAKKFSWEK 355
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 114-267 8.97e-06

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 46.82  E-value: 8.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 114 LSCLVADVVVFNSVFNMESFLTSMGKFMK---LIP------DHRPKDLESIIRPKCQVIYfpirfpdVSR-EHDKDPESF 183
Cdd:cd03808   135 LALLFTDKVIFVNEDDRDLAIKKGIIKKKktvLIPgsgvdlDRFQYSPESLPSEKVVFLF-------VARlLKDKGIDEL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 184 FKVLMHLKDLGLNFHVSVLGETFTDVPDIFSEAKKALGSSVLHWGYlpsKDDYFQVLCMADVVISTAKHEFFGVAMLEAV 263
Cdd:cd03808   208 IEAAKILKKKGPNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGF---RSDVPELLAESDVFVLPSYREGLPRSLLEAM 284


                  ....
gi 1774959470 264 YCGC 267
Cdd:cd03808   285 AAGR 288
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 172-340 8.43e-04

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 39.56  E-value: 8.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 172 VSR-EHDKDPESFFKVLMHLKDLGLNFHVSVLGETfTDVPDIFSEAKKALGSSVLHW-GYLPSKD--DYFQvlcMADVVI 247
Cdd:pfam00534   8 VGRlEPEKGLDLLIKAFALLKEKNPNLKLVIAGDG-EEEKRLKKLAEKLGLGDNVIFlGFVSDEDlpELLK---IADVFV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 248 STAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIFpaeylystpeqlskrlqnfckrpdiirKHLYKGE-IAPFSWAALHG 326
Cdd:pfam00534  84 LPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVV---------------------------KDGETGFlVKPNNAEALAE 136

                         170
                  ....*....|....*
gi 1774959470 327 KFRSLLT-TEPREDL 340
Cdd:pfam00534 137 AIDKLLEdEELRERL 151
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 240-332 8.49e-04

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 38.82  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 240 LCMADVVISTAKHEFFGVAMLEAVYCGCYPLC-----PKDLVYPE----IFPAEylysTPEQLSKRLQNFCKRPDIIRKH 310
Cdd:COG0438    18 LAAADVFVLPSRSEGFGLVLLEAMAAGLPVIAtdvggLPEVIEDGetglLVPPG----DPEALAEAILRLLEDPELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 1774959470 311 LYKG-EIA--PFSWAALHGKFRSLL 332
Cdd:COG0438    94 GEAArERAeeRFSWEAIAERLLALY 118
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 73-332 3.93e-03

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 38.67  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470  73 LAALRPDLGKLKKILYFH--ENQLIYPVKKCQERDFQYGYNQILSclvADVVVFNSVFnMESFLTSMGKfmklipdhrpk 150
Cdd:cd03801    96 LAALLALLLGAPLVVTLHgaEPGRLLLLLAAERRLLARAEALLRR---ADAVIAVSEA-LRDELRALGG----------- 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 151 dlesIIRPKCQVIYFPI---RFPDVSRE------------------HDKDPESFFKVLMHLKDLGLNFHVSVLGETFTDV 209
Cdd:cd03801   161 ----IPPEKIVVIPNGVdleRFSPPLRRklgippdrpvllfvgrlsPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLR 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774959470 210 PDIfSEAKKALGSSVLHWGYLPsKDDYFQVLCMADVVISTAKHEFFGVAMLEAVYCGCYPLCPKDLVYPEIFPAEYLY-- 287
Cdd:cd03801   237 AEL-EELELGLGDRVRFLGFVP-DEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGlv 314

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1774959470 288 ---STPEQLSKRLQNFCKRPDI---IRKHLYKGEIAPFSWAALHGKFRSLL 332
Cdd:cd03801   315 vppDDVEALADALLRLLADPELrarLGRAARERVAERFSWERVAERLLDLY 365
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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