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Conserved domains on  [gi|1552642776|ref|XP_027519982|]
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nicotinamide riboside kinase 2 isoform X4 [Corapipo altera]

Protein Classification

nicotinamide riboside kinase( domain architecture ID 10113996)

nicotinamide riboside kinase catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
4-169 2.99e-101

Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside.


:

Pssm-ID: 238982 [Multi-domain]  Cd Length: 187  Bit Score: 290.38  E-value: 2.99e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   4 IIGIGGVTNGGKTTLTNRLIKALPNCCVVHQDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAWIENP--VKFAR 81
Cdd:cd02024     1 IVGISGVTNSGKTTLAKLLQRILPNCCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRETGhfPKFLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776  82 SHGVNVTPGSKEPTS-------------QDIHILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTRNYTV----- 143
Cdd:cd02024    81 SHGNENDPEKEFIEDaqieetkadllgaEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREARTGYVtlegf 160
                         170       180
                  ....*....|....*....|....*..
gi 1552642776 144 -PDPPGLFDGHVWPMYLKHRKEMEDCG 169
Cdd:cd02024   161 wPDPPGYFDGHVWPMYLKHHAEMFENG 187
 
Name Accession Description Interval E-value
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
4-169 2.99e-101

Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside.


Pssm-ID: 238982 [Multi-domain]  Cd Length: 187  Bit Score: 290.38  E-value: 2.99e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   4 IIGIGGVTNGGKTTLTNRLIKALPNCCVVHQDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAWIENP--VKFAR 81
Cdd:cd02024     1 IVGISGVTNSGKTTLAKLLQRILPNCCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRETGhfPKFLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776  82 SHGVNVTPGSKEPTS-------------QDIHILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTRNYTV----- 143
Cdd:cd02024    81 SHGNENDPEKEFIEDaqieetkadllgaEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREARTGYVtlegf 160
                         170       180
                  ....*....|....*....|....*..
gi 1552642776 144 -PDPPGLFDGHVWPMYLKHRKEMEDCG 169
Cdd:cd02024   161 wPDPPGYFDGHVWPMYLKHHAEMFENG 187
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
3-167 2.66e-27

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 102.61  E-value: 2.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   3 YIIGIGGVTNGGKTTLTNRLIKALP--NCCVVHQDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAWIEN-PVK- 78
Cdd:COG0572     8 RIIGIAGPSGSGKTTFARRLAEQLGadKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGeSVEl 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776  79 ----FARshgvnvtpGSKEPTSQDIH---ILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRR-----STRNYTVPDp 146
Cdd:COG0572    88 pvydFAT--------GTRSGETVKVEpadVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRivrdgEERGRTAES- 158
                         170       180
                  ....*....|....*....|.
gi 1552642776 147 pglfdghVWPMYLKHRKEMED 167
Cdd:COG0572   159 -------VIEQYWATVRPGHE 172
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
4-139 2.55e-09

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 54.78  E-value: 2.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   4 IIGIGGVTNGGKTTLTNRLIKALPNCCVVH--QDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAW-----IENP 76
Cdd:PRK05480    8 IIGIAGGSGSGKTTVASTIYEELGDESIAVipQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALkagkaIEIP 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552642776  77 V----KFARS-HGVNVTPgskeptsqdIHILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTR 139
Cdd:PRK05480   88 VydytEHTRSkETIRVEP---------KDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKR 146
AAA_18 pfam13238
AAA domain;
5-155 1.40e-06

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 45.88  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   5 IGIGGVTNGGKTTLTNRLIKALpNCCVVHQDDFFKPQDQIEVGEDgfkqWDVLDSLDMEAMVSTVRAWIENPVkfarshg 84
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRL-GFGDNVRDLALENGLVLGDDPE----TRESKRLDEDKLDRLLDLLEENAA------- 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1552642776  85 vnvtpgskeptSQDIHILVIEGFLLYNYKP-LIDLFDIryYLAVPYDECKRRRSTRNYTVPDPPGLFDGHVW 155
Cdd:pfam13238  69 -----------LEEGGNLIIDGHLAELEPErAKDLVGI--VLRASPEELLERLEKRGYEEAKIKENEEAEIL 127
 
Name Accession Description Interval E-value
NRK1 cd02024
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ...
4-169 2.99e-101

Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside.


Pssm-ID: 238982 [Multi-domain]  Cd Length: 187  Bit Score: 290.38  E-value: 2.99e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   4 IIGIGGVTNGGKTTLTNRLIKALPNCCVVHQDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAWIENP--VKFAR 81
Cdd:cd02024     1 IVGISGVTNSGKTTLAKLLQRILPNCCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRETGhfPKFLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776  82 SHGVNVTPGSKEPTS-------------QDIHILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTRNYTV----- 143
Cdd:cd02024    81 SHGNENDPEKEFIEDaqieetkadllgaEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREARTGYVtlegf 160
                         170       180
                  ....*....|....*....|....*..
gi 1552642776 144 -PDPPGLFDGHVWPMYLKHRKEMEDCG 169
Cdd:cd02024   161 wPDPPGYFDGHVWPMYLKHHAEMFENG 187
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
3-167 2.66e-27

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 102.61  E-value: 2.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   3 YIIGIGGVTNGGKTTLTNRLIKALP--NCCVVHQDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAWIEN-PVK- 78
Cdd:COG0572     8 RIIGIAGPSGSGKTTFARRLAEQLGadKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGeSVEl 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776  79 ----FARshgvnvtpGSKEPTSQDIH---ILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRR-----STRNYTVPDp 146
Cdd:COG0572    88 pvydFAT--------GTRSGETVKVEpadVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRivrdgEERGRTAES- 158
                         170       180
                  ....*....|....*....|.
gi 1552642776 147 pglfdghVWPMYLKHRKEMED 167
Cdd:COG0572   159 -------VIEQYWATVRPGHE 172
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
4-139 2.20e-12

Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK), catalyzes the reversible phosphoryl transfer from ATP to uridine or cytidine to yield UMP or CMP. In the primidine nucleotide-salvage pathway, this enzyme combined with nucleoside diphosphate kinases further phosphorylates UMP and CMP to form UTP and CTP. This kinase also catalyzes the phosphorylation of several cytotoxic ribonucleoside analogs such as 5-flurrouridine and cyclopentenyl-cytidine.


Pssm-ID: 238981 [Multi-domain]  Cd Length: 198  Bit Score: 62.96  E-value: 2.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   4 IIGIGGVTNGGKTTLTNRLIKALPNCCVVH--QDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAW-----IENP 76
Cdd:cd02023     1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIisQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLkngksVEIP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552642776  77 V-KFarshgVNVTPGSKEPTSQDIHILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTR 139
Cdd:cd02023    81 VyDF-----KTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIER 139
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
4-139 2.55e-09

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 54.78  E-value: 2.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   4 IIGIGGVTNGGKTTLTNRLIKALPNCCVVH--QDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAW-----IENP 76
Cdd:PRK05480    8 IIGIAGGSGSGKTTVASTIYEELGDESIAVipQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALkagkaIEIP 87
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1552642776  77 V----KFARS-HGVNVTPgskeptsqdIHILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTR 139
Cdd:PRK05480   88 VydytEHTRSkETIRVEP---------KDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKR 146
PRK08233 PRK08233
hypothetical protein; Provisional
4-192 1.02e-07

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 49.74  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   4 IIGIGGVTNGGKTTLTNRLIKALPNCCVVHQDDF-FK--PQDQIEVGEDG--FKQWdvldslDMEAMVSTVRAWIENpvk 78
Cdd:PRK08233    5 IITIAAVSGGGKTTLTERLTHKLKNSKALYFDRYdFDncPEDICKWIDKGanYSEW------VLTPLIKDIQELIAK--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776  79 farshgvnvtpgskeptSQDIHILVIEGFlLYNYKPLIDLFDIRYYLAVPYDECKRRRSTRNYTVPDPPGLFD------G 152
Cdd:PRK08233   76 -----------------SNVDYIIVDYPF-AYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDTGNEIHNdlkhylN 137
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1552642776 153 HVWPMYLKHRKEMEDcGVDVVyLDGLKSREELYNQVFEDI 192
Cdd:PRK08233  138 YARPLYLEALHTVKP-NADIV-LDGALSVEEIINQIEEEL 175
AAA_18 pfam13238
AAA domain;
5-155 1.40e-06

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 45.88  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   5 IGIGGVTNGGKTTLTNRLIKALpNCCVVHQDDFFKPQDQIEVGEDgfkqWDVLDSLDMEAMVSTVRAWIENPVkfarshg 84
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRL-GFGDNVRDLALENGLVLGDDPE----TRESKRLDEDKLDRLLDLLEENAA------- 68
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1552642776  85 vnvtpgskeptSQDIHILVIEGFLLYNYKP-LIDLFDIryYLAVPYDECKRRRSTRNYTVPDPPGLFDGHVW 155
Cdd:pfam13238  69 -----------LEEGGNLIIDGHLAELEPErAKDLVGI--VLRASPEELLERLEKRGYEEAKIKENEEAEIL 127
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
4-135 6.54e-05

Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. This enzyme catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis.


Pssm-ID: 238984 [Multi-domain]  Cd Length: 273  Bit Score: 42.32  E-value: 6.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   4 IIGIGGVTNGGKTTLTNRLIKAL--PNCCVVHQDDFFKpQDQIEVGEDGFKQWDVL-DSLD-MEAMVSTVRAW--IENPV 77
Cdd:cd02026     1 IIGVAGDSGCGKSTFLRRLTSLFgsDLVTVICLDDYHS-LDRKGRKETGITALDPRaNNFDlMYEQLKALKEGqaIEKPI 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776  78 kfaRSH--GVNVTPGSKEPTsqdiHILVIEGFLLYNYKPLIDLFDIRYYLAVPyDECKRR 135
Cdd:cd02026    80 ---YNHvtGLIDPPELIKPT----KIVVIEGLHPLYDERVRELLDFSVYLDIS-DEVKFA 131
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
4-128 2.12e-04

Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or uridine-cytidine kinase (UCK).


Pssm-ID: 238986 [Multi-domain]  Cd Length: 179  Bit Score: 40.37  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   4 IIGIGGVTNGGKTTLTNRLIKAL----PNCCVVHQDDFFKPQDQIEVgEDGFkqWDVLDSLDMEAMVSTVRAWIEN---- 75
Cdd:cd02028     1 VVGIAGPSGSGKTTFAKKLSNQLrvngIGPVVISLDDYYVPRKTPRD-EDGN--YDFESILDLDLLNKNLHDLLNGkeve 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1552642776  76 -PVKFARSHGVNVTPGSKEPTSqdiHILVIEGFLLYNYKpLIDLFDIRYYLAVP 128
Cdd:cd02028    78 lPIYDFRTGKRRGYRKLKLPPS---GVVILEGIYALNER-LRSLLDIRVAVSGG 127
PTZ00301 PTZ00301
uridine kinase; Provisional
4-140 2.19e-04

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 40.76  E-value: 2.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   4 IIGIGGVTNGGKTTLTNRLIKAL-----PNCCVVHQDDFF-KPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAW----- 72
Cdd:PTZ00301    5 VIGISGASGSGKSSLSTNIVSELmahcgPVSIGVICEDFYyRDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELksgkt 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1552642776  73 IENP----VKFARS-HGVNVTPGSkeptsqdihILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTRN 140
Cdd:PTZ00301   85 VQIPqydyVHHTRSdTAVTMTPKS---------VLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRD 148
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
4-124 1.89e-03

Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4'-phosphopantothenic, which is the first of five steps in coenzyme A (CoA) biosynthetic pathway. The reaction carried out by this enzyme is a key regulatory point in CoA biosynthesis.


Pssm-ID: 238983  Cd Length: 220  Bit Score: 37.68  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1552642776   4 IIGIGGVTNGGKTTlTNRLIKAL-------PNCCVVHQDDFFKP-QDQIEVG---EDGFKqwdvlDSLDMEAM---VSTV 69
Cdd:cd02025     1 IIGIAGSVAVGKST-TARVLQALlsrwpdhPNVELITTDGFLYPnKELIERGlmdRKGFP-----ESYDMEALlkfLKDI 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1552642776  70 RAWIEN---PVkfaRSHGV-NVTPGSKEPTSQDiHILVIEG--FLLYNYKPLI---DLFDIRYY 124
Cdd:cd02025    75 KSGKKNvkiPV---YSHLTyDVIPGEKQTVDQP-DILIIEGlnVLQTGQNPRLfvsDFFDFSIY 134
 
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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