|
Name |
Accession |
Description |
Interval |
E-value |
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
95-294 |
4.14e-123 |
|
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: 357.63 E-value: 4.14e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVANKIIEALDVPWVVLLSMDSFYKVLSAEEQALAASNdyNFDHPGAFDFELLVTTLRKLKQGKSVK 174
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNN--NYDHPDAFDFDLLISHLQDLKNGKSVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 175 IPVYDFTTHGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERGRDIEGVIKQYNKF 254
Cdd:cd02023 79 IPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1624437681 255 VKPAFDQYIEPTMRLADIVVPRGGGNMVAIDLIVQHVHSQ 294
Cdd:cd02023 159 VKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
89-298 |
7.13e-94 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 283.20 E-value: 7.13e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 89 QSKEAFVIGLCGGSASGKTTVANKIIEALDVPWVVLLSMDSFYK---VLSAEEQALAasndyNFDHPGAFDFELLVTTLR 165
Cdd:PRK05480 2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLLIEHLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 166 KLKQGKSVKIPVYDFTTHGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERGRDIE 245
Cdd:PRK05480 77 ALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1624437681 246 GVIKQYNKFVKPAFDQYIEPTMRLADIVVPRGGGNMVAIDLIVQHVHSQLEER 298
Cdd:PRK05480 157 SVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
90-296 |
2.07e-83 |
|
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 272977 Cd Length: 207 Bit Score: 256.55 E-value: 2.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 90 SKEAFVIGLCGGSASGKTTVANKIIEALDVPWVVLLSMDSFYKvlSAEEQALAASNDYNFDHPGAFDFELLVTTLRKLKQ 169
Cdd:TIGR00235 3 KPKGIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYK--DQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 170 GKSVKIPVYDFTTHGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERGRDIEGVIK 249
Cdd:TIGR00235 81 GSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1624437681 250 QYNKFVKPAFDQYIEPTMRLADIVVPRGGGNMVAIDLIVQHVHSQLE 296
Cdd:TIGR00235 161 QYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
89-293 |
1.22e-81 |
|
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: 251.68 E-value: 1.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 89 QSKEAFVIGLCGGSASGKTTVANKIIEALDVPWVVLLSMDSFYKvlSAEEQALAASNDYNFDHPGAFDFELLVTTLRKLK 168
Cdd:COG0572 3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYK--DREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 169 QGKSVKIPVYDFTTHGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERGRDIEGVI 248
Cdd:COG0572 81 AGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1624437681 249 KQYNKFVKPAFDQYIEPTMRLADIVVPRGGG-NMVAIDLIVQHVHS 293
Cdd:COG0572 161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
95-283 |
2.37e-66 |
|
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop containing kinases: phosphoribulokinases, uridine kinases and bacterial pantothenate kinases(CoaA). Arabidopsis and other organizms have a dual uridine kinase/uracil phosphoribosyltransferase protein where the N-terminal region consists of a UK domain and the C-terminal region of a UPRT domain.
Pssm-ID: 425711 [Multi-domain] Cd Length: 196 Bit Score: 212.26 E-value: 2.37e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVANKIIEALDVPWV--------VLLSMDSFYKVLSAEEQALAASNDYNFDHPGAFDFELLVTTLRK 166
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 167 LKQGKSVKIPVYDFTTHGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERGRDIEG 246
Cdd:pfam00485 81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1624437681 247 VIKQYNkFVKPAFDQYIEPTMRLADIVVPRGGGNMVA 283
Cdd:pfam00485 161 VTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
95-234 |
4.80e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.74 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVANKIIEALDVP--WVVLLSMDSFYKVLSAEEQALAASNDYNFDHPGAfDFELLVTTLRKLKQGks 172
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGEL-RLRLALALARKLKPD-- 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624437681 173 vkipvydftthgrqkdwknvygasVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLR 234
Cdd:smart00382 81 ------------------------VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLT 118
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
313-488 |
4.93e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 39.42 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 313 SRP--SACPSQGAPGFGPPESAAPPDPQCPGEHAAGPRPA----RHHQKQGDQPRrvhlllqtpdaPPDRTCPDLPALAA 386
Cdd:PRK14086 106 SEPelPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARPAypayQQRPEPGAWPR-----------AADDYGWQQQRLGF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 387 lrcPDPARRGVRGAALPRQRDNRGVHFAGRGDHGAGpeggvQRRPHRQNPHPDQygfrraraalsaPAQRHQRRPRDthg 466
Cdd:PRK14086 175 ---PPRAPYASPASYAPEQERDREPYDAGRPEYDQR-----RRDYDHPRPDWDR------------PRRDRTDRPEP--- 231
|
170 180
....*....|....*....|..
gi 1624437681 467 qhrlHGGSCHDGRTGPTGPRRP 488
Cdd:PRK14086 232 ----PPGAGHVHRGGPGPPERD 249
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
95-294 |
4.14e-123 |
|
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: 357.63 E-value: 4.14e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVANKIIEALDVPWVVLLSMDSFYKVLSAEEQALAASNdyNFDHPGAFDFELLVTTLRKLKQGKSVK 174
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEEIIEQLGNPKVVIISQDSYYKDLSHEELEERKNN--NYDHPDAFDFDLLISHLQDLKNGKSVE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 175 IPVYDFTTHGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERGRDIEGVIKQYNKF 254
Cdd:cd02023 79 IPVYDFKTHSRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVERGRDLESVINQYLKF 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1624437681 255 VKPAFDQYIEPTMRLADIVVPRGGGNMVAIDLIVQHVHSQ 294
Cdd:cd02023 159 VKPMHEQFIEPTKRYADVIIPRGGDNHVAIDLIVQHIKSK 198
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
89-298 |
7.13e-94 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 283.20 E-value: 7.13e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 89 QSKEAFVIGLCGGSASGKTTVANKIIEALDVPWVVLLSMDSFYK---VLSAEEQALAasndyNFDHPGAFDFELLVTTLR 165
Cdd:PRK05480 2 MMKKPIIIGIAGGSGSGKTTVASTIYEELGDESIAVIPQDSYYKdqsHLSFEERVKT-----NYDHPDAFDHDLLIEHLK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 166 KLKQGKSVKIPVYDFTTHGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERGRDIE 245
Cdd:PRK05480 77 ALKAGKAIEIPVYDYTEHTRSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKRDVNERGRSLE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1624437681 246 GVIKQYNKFVKPAFDQYIEPTMRLADIVVPRGGGNMVAIDLIVQHVHSQLEER 298
Cdd:PRK05480 157 SVINQYLSTVRPMHLQFIEPSKRYADIIIPEGGKNRVAIDILKAKIRQLLEKN 209
|
|
| udk |
TIGR00235 |
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in ... |
90-296 |
2.07e-83 |
|
uridine kinase; Model contains a number of longer eukaryotic proteins and starts bringing in phosphoribulokinase hits at scores of 160 and below [Purines, pyrimidines, nucleosides, and nucleotides, Salvage of nucleosides and nucleotides]
Pssm-ID: 272977 Cd Length: 207 Bit Score: 256.55 E-value: 2.07e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 90 SKEAFVIGLCGGSASGKTTVANKIIEALDVPWVVLLSMDSFYKvlSAEEQALAASNDYNFDHPGAFDFELLVTTLRKLKQ 169
Cdd:TIGR00235 3 KPKGIIIGIGGGSGSGKTTVARKIYEQLGKLEIVIISQDNYYK--DQSHLEMAERKKTNFDHPDAFDNDLLYEHLKNLKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 170 GKSVKIPVYDFTTHGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERGRDIEGVIK 249
Cdd:TIGR00235 81 GSPIDVPVYDYVNHTRPKETVHIEPKDVVILEGIMPLFDERLRDLMDLKIFVDTPLDIRLIRRIERDINERGRSLDSVID 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1624437681 250 QYNKFVKPAFDQYIEPTMRLADIVVPRGGGNMVAIDLIVQHVHSQLE 296
Cdd:TIGR00235 161 QYRKTVRPMYEQFVEPTKQYADLIIPEGGRNEVAINVLDTKIKHLLE 207
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
89-293 |
1.22e-81 |
|
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: 251.68 E-value: 1.22e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 89 QSKEAFVIGLCGGSASGKTTVANKIIEALDVPWVVLLSMDSFYKvlSAEEQALAASNDYNFDHPGAFDFELLVTTLRKLK 168
Cdd:COG0572 3 RSGKPRIIGIAGPSGSGKTTFARRLAEQLGADKVVVISLDDYYK--DREHLPLDERGKPNFDHPEAFDLDLLNEHLEPLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 169 QGKSVKIPVYDFTTHGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERGRDIEGVI 248
Cdd:COG0572 81 AGESVELPVYDFATGTRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVRDGEERGRTAESVI 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1624437681 249 KQYNKFVKPAFDQYIEPTMRLADIVVPRGGG-NMVAIDLIVQHVHS 293
Cdd:COG0572 161 EQYWATVRPGHEQYIEPTKEYADIVIPNGGPlNPVALDLLVARLLS 206
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
95-283 |
2.37e-66 |
|
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop containing kinases: phosphoribulokinases, uridine kinases and bacterial pantothenate kinases(CoaA). Arabidopsis and other organizms have a dual uridine kinase/uracil phosphoribosyltransferase protein where the N-terminal region consists of a UK domain and the C-terminal region of a UPRT domain.
Pssm-ID: 425711 [Multi-domain] Cd Length: 196 Bit Score: 212.26 E-value: 2.37e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVANKIIEALDVPWV--------VLLSMDSFYKVLSAEEQALAASNDYNFDHPGAFDFELLVTTLRK 166
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVpavgiegdSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLYEQFKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 167 LKQGKSVKIPVYDFTTHGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERGRDIEG 246
Cdd:pfam00485 81 LKEGGSVDKPIYNHVTHERDPTPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERGHSLEG 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1624437681 247 VIKQYNkFVKPAFDQYIEPTMRLADIVVPRGGGNMVA 283
Cdd:pfam00485 161 VTDSIL-FRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| PTZ00301 |
PTZ00301 |
uridine kinase; Provisional |
95-287 |
3.72e-34 |
|
uridine kinase; Provisional
Pssm-ID: 140322 [Multi-domain] Cd Length: 210 Bit Score: 127.81 E-value: 3.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVANKIIEALDV---PWVV-LLSMDSFYKVLSAEEQALAASNDYnfDHPGAFDFELLVTTLRKLKQG 170
Cdd:PTZ00301 5 VIGISGASGSGKSSLSTNIVSELMAhcgPVSIgVICEDFYYRDQSNIPESERAYTNY--DHPKSLEHDLLTTHLRELKSG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 171 KSVKIPVYDFTTHGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERGRDIEGVIKQ 250
Cdd:PTZ00301 83 KTVQIPQYDYVHHTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMRERGRTFESVIEQ 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 1624437681 251 YNKFVKPAFDQYIEPTMRLADIVVPRGGGNMVAIDLI 287
Cdd:PTZ00301 163 YEATVRPMYYAYVEPSKVYADIIVPSWKDNSVAVGVL 199
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
95-274 |
1.31e-29 |
|
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: 114.32 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVANKIIEALDV--PWVVLLSMDSFYKVLSAEEQAlaasnDYNFDHPGAFDFELLVTTLRKLKQGKS 172
Cdd:cd02028 1 VVGIAGPSGSGKTTFAKKLSNQLRVngIGPVVISLDDYYVPRKTPRDE-----DGNYDFESILDLDLLNKNLHDLLNGKE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 173 VKIPVYDFTTHGRQKDWKNVYGAS-VIIFEGIMAFADKeLLRLLDMKIFVDT-DSDIRLVRRLRRDITERGRDIEGVIKQ 250
Cdd:cd02028 76 VELPIYDFRTGKRRGYRKLKLPPSgVVILEGIYALNER-LRSLLDIRVAVSGgVHLNRLLRRVVRDIQFRGYSAELTILM 154
|
170 180
....*....|....*....|....
gi 1624437681 251 yNKFVkPAFDQYIEPTMRLADIVV 274
Cdd:cd02028 155 -WPSV-PSGEEFIIPPLQEAAIVM 176
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
95-274 |
2.76e-24 |
|
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: 102.03 E-value: 2.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVANKIIEALDVPWVVLLSMDSFYKvLSAEEQALAASNDYnfdHPGAFDFELLVTTLRKLKQGKSVK 174
Cdd:cd02026 1 IIGVAGDSGCGKSTFLRRLTSLFGSDLVTVICLDDYHS-LDRKGRKETGITAL---DPRANNFDLMYEQLKALKEGQAIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 175 IPVYDFTThGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERGRDIEGVIKQYNKf 254
Cdd:cd02026 77 KPIYNHVT-GLIDPPELIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGHSLEDVLASIEA- 154
|
170 180
....*....|....*....|
gi 1624437681 255 VKPAFDQYIEPTMRLADIVV 274
Cdd:cd02026 155 RKPDFEAYIDPQKQYADVVI 174
|
|
| PLN02318 |
PLN02318 |
phosphoribulokinase/uridine kinase |
95-274 |
1.48e-21 |
|
phosphoribulokinase/uridine kinase
Pssm-ID: 177952 [Multi-domain] Cd Length: 656 Bit Score: 98.01 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVANKIIEALdvPWVVLLSMDSF---YKVLsaeeqalaasnDYNFDHPGAFDFELLVTTLRKLKQGK 171
Cdd:PLN02318 67 LVGVAGPSGAGKTVFTEKVLNFM--PSIAVISMDNYndsSRII-----------DGNFDDPRLTDYDTLLDNIHDLKAGK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 172 SVKIPVYDFTTHGRQKDWK-NVYGASVIIFEGIMAFADKelLR-LLDMKIFVDTDSDIRLVRRLRRDITERGRDIEGVIK 249
Cdd:PLN02318 134 SVQVPIYDFKSSSRVGYRTlEVPSSRIVIIEGIYALSEK--LRpLLDLRVSVTGGVHFDLVKRVLRDIQRAGQEPEEIIH 211
|
170 180
....*....|....*....|....*
gi 1624437681 250 QYNKFVKPAFDQYIEPTMRLADIVV 274
Cdd:PLN02318 212 QISETVYPMYKAFIEPDLQTAHIKI 236
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
87-274 |
4.39e-20 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 90.84 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 87 GTQSKEAFVIGLCGGSASGKTTVANKIIEALDVPWVVLLSMDSFYKVLSAEEQ-----ALaasndynfdHPGAFDFELLV 161
Cdd:PRK07429 2 TSMPDRPVLLGVAGDSGCGKTTFLRGLADLLGEELVTVICTDDYHSYDRKQRKelgitAL---------DPRANNLDIMY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 162 TTLRKLKQGKSVKIPVYDFTThGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITERG 241
Cdd:PRK07429 73 EHLKALKTGQPILKPIYNHET-GTFDPPEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRG 151
|
170 180 190
....*....|....*....|....*....|...
gi 1624437681 242 RDIEGVIKQYNKfVKPAFDQYIEPTMRLADIVV 274
Cdd:PRK07429 152 HTYEQVLAEIEA-REPDFEAYIRPQRQWADVVI 183
|
|
| PLN02348 |
PLN02348 |
phosphoribulokinase |
151-274 |
1.10e-18 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 87.98 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 151 HPGAFDFELLVTTLRKLKQGKSVKIPVYDFTThGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLV 230
Cdd:PLN02348 120 DPRANNFDLMYEQVKALKEGKAVEKPIYNHVT-GLLDPPELIEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFA 198
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1624437681 231 RRLRRDITERGRDIEGvIKQYNKFVKPAFDQYIEPTMRLADIVV 274
Cdd:PLN02348 199 WKIQRDMAERGHSLES-IKASIEARKPDFDAYIDPQKQYADVVI 241
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
95-232 |
3.42e-12 |
|
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: 65.04 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVANKIIEALdvPWVVLLSMDSFYKvlSAEEQALAASNDYNFDHPGAFDFELLVTTLR-KLKQGKSV 173
Cdd:cd02024 1 IVGISGVTNSGKTTLAKLLQRIL--PNCCVIHQDDFFK--PEDEIPVDENGFKQWDVLEALDMEAMMSTLDyWRETGHFP 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624437681 174 K-------------IPVYDFTTHGRQKDWKNVYGASVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRR 232
Cdd:cd02024 77 KflrshgnendpekEFIEDAQIEETKADLLGAEDLHILIVDGFLLYNYKPLVDLFDIRYFLRVPYETCKRRR 148
|
|
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
94-235 |
1.41e-10 |
|
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440690 Cd Length: 309 Bit Score: 62.23 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 94 FVIGLCGGSASGKTTVAnKIIEAL-----DVPWVVLLSMDSF-Y--KVLsaEEQALAasndynfDHPGA---FDFELLVT 162
Cdd:COG1072 87 FIIGIAGSVAVGKSTTA-RLLQALlsrwpEHPKVELVTTDGFlYpnAVL--ERRGLM-------DRKGFpesYDRRGLLR 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 163 TLRKLKQGKS-VKIPVYDFTTH---------GRQKDwknvygasVIIFEGIMAFADKELLR-----LLDMKIFVDTD-SD 226
Cdd:COG1072 157 FLARVKSGDPeVRAPVYSHLLYdivpgaivvVDQPD--------ILIVEGNNVLQDEPNPWlfvsdFFDFSIYVDADeED 228
|
170
....*....|.
gi 1624437681 227 I--RLVRRLRR 235
Cdd:COG1072 229 LreWYVERFLK 239
|
|
| PRK08233 |
PRK08233 |
hypothetical protein; Provisional |
91-302 |
2.44e-10 |
|
hypothetical protein; Provisional
Pssm-ID: 181310 [Multi-domain] Cd Length: 182 Bit Score: 59.76 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 91 KEAFVIGLCGGSASGKTTVANKIIEalDVPWVVLLSMDSFYKVLSAEE--QALAASNDYNfdhpgAFDFELLVTTLRKLK 168
Cdd:PRK08233 1 KKTKIITIAAVSGGGKTTLTERLTH--KLKNSKALYFDRYDFDNCPEDicKWIDKGANYS-----EWVLTPLIKDIQELI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 169 QGksvkipvydftthgRQKDWknvygasvIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLRRDITER-GRDIEGV 247
Cdd:PRK08233 74 AK--------------SNVDY--------IIVDYPFAYLNSEMRQFIDVTIFIDTPLDIAMARRILRDFKEDtGNEIHND 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1624437681 248 IKQYNKFVKPAFDQYIEPTMRLADIVVprgGGNMvAIDLIVQHVHSQLEERELSV 302
Cdd:PRK08233 132 LKHYLNYARPLYLEALHTVKPNADIVL---DGAL-SVEEIINQIEEELYRREVIV 182
|
|
| PLN03046 |
PLN03046 |
D-glycerate 3-kinase; Provisional |
85-204 |
1.72e-07 |
|
D-glycerate 3-kinase; Provisional
Pssm-ID: 178608 Cd Length: 460 Bit Score: 53.38 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 85 EHGTQSKEA-----FVIGLCGGSASGKTTvankIIEALDVPWVV------LLSMDSFYkvLSAEEQA-LAASNDYNF--- 149
Cdd:PLN03046 199 EHRSKFKDGddippLVIGFSAPQGCGKTT----LVFALDYLFRVtgrksaTLSIDDFY--LTAEGQAeLRERNPGNAlle 272
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1624437681 150 --DHPGAFDFELLVTTLRKL----KQGKSVKIPVYDFTTHGRQKD------WKNVYGA-SVIIFEGIM 204
Cdd:PLN03046 273 lrGNAGSHDLQFSVETLEALskltKEGIKMKVPRYDKSAYSGRGDradpstWPEVEGPlEVILFEGWM 340
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
95-277 |
2.18e-06 |
|
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: 48.46 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVAnKIIEAL-----DVPWVVLLSMDSF-YKVLSAEEQALAASNDYnfdhPGAFDFELLVTTLRKLK 168
Cdd:cd02025 1 IIGIAGSVAVGKSTTA-RVLQALlsrwpDHPNVELITTDGFlYPNKELIERGLMDRKGF----PESYDMEALLKFLKDIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 169 QGKS-VKIPVYDFTTHGRQKDWK-NVYGASVIIFEGIMAFADKELLR-----LLDMKIFVDTD-SDIR--LVRRLRRDIT 238
Cdd:cd02025 76 SGKKnVKIPVYSHLTYDVIPGEKqTVDQPDILIIEGLNVLQTGQNPRlfvsdFFDFSIYVDADeDDIEkwYIKRFLKLRE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1624437681 239 ERGRDIEGVIKQYNKFV----------------KPAFDQYIEPTMRLADIVVPRG 277
Cdd:cd02025 156 TAFSDPDSYFHRYAKMSeeeaiafarevwkninLKNLRENILPTRNRADLILEKG 210
|
|
| PRK09270 |
PRK09270 |
nucleoside triphosphate hydrolase domain-containing protein; Reviewed |
94-235 |
1.02e-05 |
|
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
Pssm-ID: 236442 Cd Length: 229 Bit Score: 46.85 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 94 FVIGLCGGSASGKTTVANKIIEALD----VPWVVlLSMDSFY---KVLsaEEQALAASNdynfdhpGA---FDFELLVTT 163
Cdd:PRK09270 34 TIVGIAGPPGAGKSTLAEFLEALLQqdgeLPAIQ-VPMDGFHldnAVL--DAHGLRPRK-------GApetFDVAGLAAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 164 LRKLKQGKS-VKIPVYDftthgRQKDwKNVYGASVI-------IFEGIMAFAD----KELLRLLDMKIFVDTDSDIrLVR 231
Cdd:PRK09270 104 LRRLRAGDDeVYWPVFD-----RSLE-DPVADAIVVpptarlvIVEGNYLLLDeepwRRLAGLFDFTIFLDAPAEV-LRE 176
|
....
gi 1624437681 232 RLRR 235
Cdd:PRK09270 177 RLVA 180
|
|
| PRK06696 |
PRK06696 |
uridine kinase; Validated |
96-274 |
7.20e-05 |
|
uridine kinase; Validated
Pssm-ID: 180660 Cd Length: 223 Bit Score: 44.20 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 96 IGLCGGSASGKTTVANKI---IEALDVPwVVLLSMDSFYKV---------LSAEeqalaasnDYNFDhpgAFDFELLVT- 162
Cdd:PRK06696 25 VAIDGITASGKTTFADELaeeIKKRGRP-VIRASIDDFHNPrviryrrgrESAE--------GYYED---AYDYTALRRl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 163 TLRKLKQGKS--VKIPVYDFTTHGRQKD-WKNVYGASVIIFEGIMAFADkELLRLLDMKIFVDTDSDIRLVRRLRRDITE 239
Cdd:PRK06696 93 LLDPLGPNGDrqYRTASHDLKTDIPVHNpPLLAAPNAVLIVDGTFLLRP-ELRDLWDYKIFLDTDFEVSRRRGAKRDTEA 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 1624437681 240 RGRDIEgVIKQYNKFVKPAFDQYIE---PtMRLADIVV 274
Cdd:PRK06696 172 FGSYEE-AEKMYLARYHPAQKLYIAeanP-KERADVVI 207
|
|
| CoaE |
COG0237 |
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the ... |
94-122 |
2.46e-03 |
|
Dephospho-CoA kinase [Coenzyme transport and metabolism]; Dephospho-CoA kinase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 440007 Cd Length: 193 Bit Score: 39.28 E-value: 2.46e-03
10 20
....*....|....*....|....*....
gi 1624437681 94 FVIGLCGGSASGKTTVAnKIIEALDVPWV 122
Cdd:COG0237 2 LIIGLTGGIGSGKSTVA-RMFAELGAPVI 29
|
|
| CPT |
pfam07931 |
Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to ... |
95-154 |
3.24e-03 |
|
Chloramphenicol phosphotransferase-like protein; The members of this family are all similar to chloramphenicol 3-O phosphotransferase (CPT) expressed by Streptomyces venezuelae. Chloramphenicol (Cm) is a metabolite produced by this bacterium that can inhibit ribosomal peptidyl transferase activity and therefore protein production. By transferring a phosphate group to the C-3 hydroxyl group of Cm, CPT inactivates this potentially lethal metabolite.
Pssm-ID: 400334 Cd Length: 172 Bit Score: 38.59 E-value: 3.24e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVANKIIEALDVPWVVlLSMDSFYKVLSAEEQALAASNDYNFDHPGA 154
Cdd:pfam07931 3 IILLNGGSSSGKSSIARALQDVLDGPWMH-FGVDAFVEAMPPKRQNSGGGLEWSTDGPGP 61
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
96-252 |
3.71e-03 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 37.41 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 96 IGLCGGSASGKTTVAnKIIEALDVPWVVLLSMdsfykvlsAEEQALAASNDYNFDHPGAFDFELLVTTLRKLKQgksvki 175
Cdd:pfam13238 1 ILITGTPGVGKTTLA-KELSKRLGFGDNVRDL--------ALENGLVLGDDPETRESKRLDEDKLDRLLDLLEE------ 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1624437681 176 pvydftthgrqkdWKNVYGASVIIFEGIMAFADKELLRLLdMKIFVDTDSDIRLVRRLRRDITERGRDIEGVIKQYN 252
Cdd:pfam13238 66 -------------NAALEEGGNLIIDGHLAELEPERAKDL-VGIVLRASPEELLERLEKRGYEEAKIKENEEAEILG 128
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
95-234 |
4.80e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.74 E-value: 4.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 95 VIGLCGGSASGKTTVANKIIEALDVP--WVVLLSMDSFYKVLSAEEQALAASNDYNFDHPGAfDFELLVTTLRKLKQGks 172
Cdd:smart00382 4 VILIVGPPGSGKTTLARALARELGPPggGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGEL-RLRLALALARKLKPD-- 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1624437681 173 vkipvydftthgrqkdwknvygasVIIFEGIMAFADKELLRLLDMKIFVDTDSDIRLVRRLR 234
Cdd:smart00382 81 ------------------------VLILDEITSLLDAEQEALLLLLEELRLLLLLKSEKNLT 118
|
|
| dnaA |
PRK14086 |
chromosomal replication initiator protein DnaA; |
313-488 |
4.93e-03 |
|
chromosomal replication initiator protein DnaA;
Pssm-ID: 237605 [Multi-domain] Cd Length: 617 Bit Score: 39.42 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 313 SRP--SACPSQGAPGFGPPESAAPPDPQCPGEHAAGPRPA----RHHQKQGDQPRrvhlllqtpdaPPDRTCPDLPALAA 386
Cdd:PRK14086 106 SEPelPRPGRRPYEGYGGPRADDRPPGLPRQDQLPTARPAypayQQRPEPGAWPR-----------AADDYGWQQQRLGF 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1624437681 387 lrcPDPARRGVRGAALPRQRDNRGVHFAGRGDHGAGpeggvQRRPHRQNPHPDQygfrraraalsaPAQRHQRRPRDthg 466
Cdd:PRK14086 175 ---PPRAPYASPASYAPEQERDREPYDAGRPEYDQR-----RRDYDHPRPDWDR------------PRRDRTDRPEP--- 231
|
170 180
....*....|....*....|..
gi 1624437681 467 qhrlHGGSCHDGRTGPTGPRRP 488
Cdd:PRK14086 232 ----PPGAGHVHRGGPGPPERD 249
|
|
|