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Conserved domains on  [gi|1802853274|ref|XP_032059761|]
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nicotinamide riboside kinase 2 [Aythya fuligula]

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 7.27e-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: 289.22  E-value: 7.27e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   4 IIGIGGVTNGGKTTLTNRLVKALPNCCVVHQDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAWIENP--VKFAR 81
Cdd:cd02024     1 IVGISGVTNSGKTTLAKLLQRILPNCCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRETGhfPKFLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274  82 SHGVNVTPGSKEPAS-------------KDIHILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTRNYTV----- 143
Cdd:cd02024    81 SHGNENDPEKEFIEDaqieetkadllgaEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREARTGYVtlegf 160

                         170       180
                  ....*....|....*....|....*..
gi 1802853274 144 -PDPPGLFDGHVWPMYLKHRKEMEDNG 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 7.27e-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: 289.22  E-value: 7.27e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   4 IIGIGGVTNGGKTTLTNRLVKALPNCCVVHQDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAWIENP--VKFAR 81
Cdd:cd02024     1 IVGISGVTNSGKTTLAKLLQRILPNCCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRETGhfPKFLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274  82 SHGVNVTPGSKEPAS-------------KDIHILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTRNYTV----- 143
Cdd:cd02024    81 SHGNENDPEKEFIEDaqieetkadllgaEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREARTGYVtlegf 160

                         170       180
                  ....*....|....*....|....*..
gi 1802853274 144 -PDPPGLFDGHVWPMYLKHRKEMEDNG 169
Cdd:cd02024   161 wPDPPGYFDGHVWPMYLKHHAEMFENG 187
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 3-194 2.08e-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: 2.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   3 YIIGIGGVTNGGKTTLTNRLVKALP--NCCVVHQDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAWIEN-PVK- 78
Cdd:COG0572     8 RIIGIAGPSGSGKTTFARRLAEQLGadKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGeSVEl 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274  79 ----FARshgvnvtpGSKEPASKDIH---ILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRR-----STRNYTVPDp 146
Cdd:COG0572    88 pvydFAT--------GTRSGETVKVEpadVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRivrdgEERGRTAES- 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1802853274 147 pglfdghVWPMYLKHRKEMEDNGV-------DVVYLDGLKSRDELYNQVFEDIQN 194
Cdd:COG0572   159 -------VIEQYWATVRPGHEQYIeptkeyaDIVIPNGGPLNPVALDLLVARLLS 206
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 4-139 1.42e-09

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 55.16  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   4 IIGIGGVTNGGKTTLTNRLVKALPNCCVVH--QDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAW-----IENP 76
Cdd:PRK05480    8 IIGIAGGSGSGKTTVASTIYEELGDESIAVipQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALkagkaIEIP 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802853274  77 V----KFARS-HGVNVTPgskepasKDIHILviEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTR 139
Cdd:PRK05480   88 VydytEHTRSkETIRVEP-------KDVIIL--EGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKR 146
AAA_18 pfam13238
AAA domain;
5-155 3.64e-07

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 47.42  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   5 IGIGGVTNGGKTTLTNRLVKALpNCCVVHQDDFFKPQDQIEVGEDgfkqWDVLDSLDMEAMVSTVRAWIENpvkfarshg 84
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRL-GFGDNVRDLALENGLVLGDDPE----TRESKRLDEDKLDRLLDLLEEN--------- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802853274  85 vnvtpgskePASKDIHILVIEGFLLYNYKP-LIDLFDIryYLAVPYDECKRRRSTRNYTVPDPPGLFDGHVW 155
Cdd:pfam13238  67 ---------AALEEGGNLIIDGHLAELEPErAKDLVGI--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 7.27e-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: 289.22  E-value: 7.27e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   4 IIGIGGVTNGGKTTLTNRLVKALPNCCVVHQDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAWIENP--VKFAR 81
Cdd:cd02024     1 IVGISGVTNSGKTTLAKLLQRILPNCCVIHQDDFFKPEDEIPVDENGFKQWDVLEALDMEAMMSTLDYWRETGhfPKFLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274  82 SHGVNVTPGSKEPAS-------------KDIHILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTRNYTV----- 143
Cdd:cd02024    81 SHGNENDPEKEFIEDaqieetkadllgaEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRREARTGYVtlegf 160

                         170       180
                  ....*....|....*....|....*..
gi 1802853274 144 -PDPPGLFDGHVWPMYLKHRKEMEDNG 169
Cdd:cd02024   161 wPDPPGYFDGHVWPMYLKHHAEMFENG 187
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
 3-194 2.08e-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: 2.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   3 YIIGIGGVTNGGKTTLTNRLVKALP--NCCVVHQDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAWIEN-PVK- 78
Cdd:COG0572     8 RIIGIAGPSGSGKTTFARRLAEQLGadKVVVISLDDYYKDREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLKAGeSVEl 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274  79 ----FARshgvnvtpGSKEPASKDIH---ILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRR-----STRNYTVPDp 146
Cdd:COG0572    88 pvydFAT--------GTRSGETVKVEpadVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRivrdgEERGRTAES- 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1802853274 147 pglfdghVWPMYLKHRKEMEDNGV-------DVVYLDGLKSRDELYNQVFEDIQN 194
Cdd:COG0572   159 -------VIEQYWATVRPGHEQYIeptkeyaDIVIPNGGPLNPVALDLLVARLLS 206
UMPK cd02023
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ...
 4-139 9.73e-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: 61.03  E-value: 9.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   4 IIGIGGVTNGGKTTLTNRLVKALPNCCVVH--QDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAW-----IENP 76
Cdd:cd02023     1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIisQDSYYKDLSHEELEERKNNNYDHPDAFDFDLLISHLQDLkngksVEIP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802853274  77 VKFARSHGVNVTPGSKEPASkdihILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTR 139
Cdd:cd02023    81 VYDFKTHSRLKETVTVYPAD----VIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIER 139
PRK05480 PRK05480
uridine/cytidine kinase; Provisional
 4-139 1.42e-09

uridine/cytidine kinase; Provisional


Pssm-ID: 235492 [Multi-domain]  Cd Length: 209  Bit Score: 55.16  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   4 IIGIGGVTNGGKTTLTNRLVKALPNCCVVH--QDDFFKPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAW-----IENP 76
Cdd:PRK05480    8 IIGIAGGSGSGKTTVASTIYEELGDESIAVipQDSYYKDQSHLSFEERVKTNYDHPDAFDHDLLIEHLKALkagkaIEIP 87

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1802853274  77 V----KFARS-HGVNVTPgskepasKDIHILviEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTR 139
Cdd:PRK05480   88 VydytEHTRSkETIRVEP-------KDVIIL--EGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKR 146
PRK08233 PRK08233
hypothetical protein; Provisional
 4-192 1.43e-08

hypothetical protein; Provisional


Pssm-ID: 181310 [Multi-domain]  Cd Length: 182  Bit Score: 52.05  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   4 IIGIGGVTNGGKTTLTNRLVKALPNCCVVHQDDF-FK--PQDQIEVGEDG--FKQWdvldslDMEAMVSTVRAWIENpvk 78
Cdd:PRK08233    5 IITIAAVSGGGKTTLTERLTHKLKNSKALYFDRYdFDncPEDICKWIDKGanYSEW------VLTPLIKDIQELIAK--- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274  79 farshgvnvtpgskepaSKDIHILVIEGFlLYNYKPLIDLFDIRYYLAVPYDECKRRRSTRNYTVPDPPGLFD------G 152
Cdd:PRK08233   76 -----------------SNVDYIIVDYPF-AYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDTGNEIHNdlkhylN 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1802853274 153 HVWPMYLKHRKEMEDNGvDVVyLDGLKSRDELYNQVFEDI 192
Cdd:PRK08233  138 YARPLYLEALHTVKPNA-DIV-LDGALSVEEIINQIEEEL 175
AAA_18 pfam13238
AAA domain;
5-155 3.64e-07

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 47.42  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   5 IGIGGVTNGGKTTLTNRLVKALpNCCVVHQDDFFKPQDQIEVGEDgfkqWDVLDSLDMEAMVSTVRAWIENpvkfarshg 84
Cdd:pfam13238   1 ILITGTPGVGKTTLAKELSKRL-GFGDNVRDLALENGLVLGDDPE----TRESKRLDEDKLDRLLDLLEEN--------- 66

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1802853274  85 vnvtpgskePASKDIHILVIEGFLLYNYKP-LIDLFDIryYLAVPYDECKRRRSTRNYTVPDPPGLFDGHVW 155
Cdd:pfam13238  67 ---------AALEEGGNLIIDGHLAELEPErAKDLVGI--VLRASPEELLERLEKRGYEEAKIKENEEAEIL 127
PRK cd02026
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ...
 4-135 6.48e-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: 6.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   4 IIGIGGVTNGGKTTLTNRLVKAL--PNCCVVHQDDFFKpQDQIEVGEDGFKQWDVL-DSLD-MEAMVSTVRAW--IENPV 77
Cdd:cd02026     1 IIGVAGDSGCGKSTFLRRLTSLFgsDLVTVICLDDYHS-LDRKGRKETGITALDPRaNNFDlMYEQLKALKEGqaIEKPI 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274  78 kfarshgVNVTPGSKEPAS--KDIHILVIEGFLLYNYKPLIDLFDIRYYLAVPyDECKRR 135
Cdd:cd02026    80 -------YNHVTGLIDPPEliKPTKIVVIEGLHPLYDERVRELLDFSVYLDIS-DEVKFA 131
PTZ00301 PTZ00301
uridine kinase; Provisional
 4-140 1.39e-04

uridine kinase; Provisional


Pssm-ID: 140322 [Multi-domain]  Cd Length: 210  Bit Score: 41.14  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   4 IIGIGGVTNGGKTTLTNRLVKAL-----PNCCVVHQDDFF-KPQDQIEVGEDGFKQWDVLDSLDMEAMVSTVRAW----- 72
Cdd:PTZ00301    5 VIGISGASGSGKSSLSTNIVSELmahcgPVSIGVICEDFYyRDQSNIPESERAYTNYDHPKSLEHDLLTTHLRELksgkt 84

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1802853274  73 IENP----VKFARS-HGVNVTPGSkepaskdihILVIEGFLLYNYKPLIDLFDIRYYLAVPYDECKRRRSTRN 140
Cdd:PTZ00301   85 VQIPqydyVHHTRSdTAVTMTPKS---------VLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRD 148
UMPK_like cd02028
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ...
 4-128 5.85e-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: 39.21  E-value: 5.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   4 IIGIGGVTNGGKTTLTNRLVKAL----PNCCVVHQDDFFKPQDQIEVgEDGFkqWDVLDSLDMEAMVSTVRAWIEN-PVK 78
Cdd:cd02028     1 VVGIAGPSGSGKTTFAKKLSNQLrvngIGPVVISLDDYYVPRKTPRD-EDGN--YDFESILDLDLLNKNLHDLLNGkEVE 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1802853274  79 FARshgVNVTPGSKEPASKDI----HILVIEGFLLYNYKpLIDLFDIRYYLAVP 128
Cdd:cd02028    78 LPI---YDFRTGKRRGYRKLKlppsGVVILEGIYALNER-LRSLLDIRVAVSGG 127
PanK cd02025
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ...
 4-124 5.96e-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: 36.52  E-value: 5.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1802853274   4 IIGIGGVTNGGKTTlTNRLVKAL-------PNCCVVHQDDFFKP-QDQIEVG---EDGFKqwdvlDSLDMEAM---VSTV 69
Cdd:cd02025     1 IIGIAGSVAVGKST-TARVLQALlsrwpdhPNVELITTDGFLYPnKELIERGlmdRKGFP-----ESYDMEALlkfLKDI 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1802853274  70 RAWIEN---PVkfaRSHGV-NVTPGSKEPASKDiHILVIEG--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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