|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02348 |
PLN02348 |
phosphoribulokinase |
1-395 |
0e+00 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 816.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 1 MAVSTIYSTQALNSTHFLTSSSSSKQVfLYRRQPQTNRRFNTLITCAQETIVIGLAADSGCGKSTFMRRLTSVFGGAAKP 80
Cdd:PLN02348 1 MAFATVSSTASLNATSSITTPTKSNLG-SRRSKSPAASSVVVALAADDGTVVIGLAADSGCGKSTFMRRLTSVFGGAAKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 81 PKGGNPDSNTLISDTTTVICLDDYHSLDRYGRKEQKVTALDPRANDFDLMYEQVKALKNGIAVEKPIYNHVTGLLDPPEL 160
Cdd:PLN02348 80 PKGGNPDSNTLISDTTTVICLDDYHSLDRTGRKEKGVTALDPRANNFDLMYEQVKALKEGKAVEKPIYNHVTGLLDPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 161 IQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQRDMAERGHSLESIKASIEARKPDFDAFIDPQKQYADA 240
Cdd:PLN02348 160 IEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAWKIQRDMAERGHSLESIKASIEARKPDFDAYIDPQKQYADV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 241 VIEVLPTTLIPDDNEGKVLRVRLIMKEGVKYFSPVYLFDEGSTISWIPCGRKLTCSYPGIKFNYEPDSYFDHEVSVLEMD 320
Cdd:PLN02348 240 VIEVLPTQLIPDDNEGKVLRVRLIMKEGVKNFDPVYLFDEGSTISWIPCGRKLTCSYPGIKFFYGPDTYFGHEVSVLEMD 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222551 321 GQFDRLDELIYVESHLSNLSTKFYGEVTQQMLKHADFPGSNNGTGLFQTIVGLKIRDLYEQLIANKATARAEAKA 395
Cdd:PLN02348 320 GQFDKLDELIYVESHLSNTSTKFYGEVTQQMLKHADFPGSNNGTGLFQTIVGLKIRDLYERIVAKRKVAAGEATA 394
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
52-341 |
0e+00 |
|
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: 541.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 52 VIGLAADSGCGKSTFMRRLTSVFGgaakppkggnpdsntliSDTTTVICLDDYHSLDRYGRKEQKVTALDPRANDFDLMY 131
Cdd:cd02026 1 IIGVAGDSGCGKSTFLRRLTSLFG-----------------SDLVTVICLDDYHSLDRKGRKETGITALDPRANNFDLMY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 132 EQVKALKNGIAVEKPIYNHVTGLLDPPELIQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQRDMAERGH 211
Cdd:cd02026 64 EQLKALKEGQAIEKPIYNHVTGLIDPPELIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 212 SLESIKASIEARKPDFDAFIDPQKQYADAVIEVLPTTLIPDDNEGKVLRVRLIMKEGVKYFSPVYLFDEGSTISWIPCGR 291
Cdd:cd02026 144 SLEDVLASIEARKPDFEAYIDPQKQYADVVIQVLPTQLIPDDTEGKVLRVRLIQKEGVKDFVPVYLFDEGSTISWIPCGR 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15222551 292 KLTCSYPGIKFNYEPDSYFDHEVSVLEMDGQFDRLDELIYVESHLSNLST 341
Cdd:cd02026 224 KLTCSYPGIKLAYGPDTYYGREVSVLEMDGQFDNLEELIYVESHLSNTST 273
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
52-251 |
7.66e-104 |
|
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: 305.09 E-value: 7.66e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 52 VIGLAADSGCGKSTFMRRLTSVFGGAAKPPKGGnpdsnTLISDTTTVICLDDYHSLDRYGRKEQKVTALDPRANDFDLMY 131
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGI-----EGDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 132 EQVKALKNGIAVEKPIYNHVTGLLDP-PELIQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQRDMAERG 210
Cdd:pfam00485 76 EQFKELKEGGSVDKPIYNHVTHERDPtPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15222551 211 HSLESIKASIEARKPDFDAFIDPQKQYADAVIEVLPTTLIP 251
Cdd:pfam00485 156 HSLEGVTDSILFRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
48-263 |
2.07e-59 |
|
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: 191.59 E-value: 2.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 48 QETIVIGLAADSGCGKSTFMRRLTSVFGgaakppkggnpdsntliSDTTTVICLDDYHSLDRYGRKEQ--KVTALDPRAN 125
Cdd:COG0572 5 GKPRIIGIAGPSGSGKTTFARRLAEQLG-----------------ADKVVVISLDDYYKDREHLPLDErgKPNFDHPEAF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 126 DFDLMYEQVKALKNGIAVEKPIYNHVTG-LLDPPELIQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQR 204
Cdd:COG0572 68 DLDLLNEHLEPLKAGESVELPVYDFATGtRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 205 DMAERGHSLES-IKASIEARKPDFDAFIDPQKQYADAVIevlPTTLIPDDNEGKVLRVRL 263
Cdd:COG0572 148 DGEERGRTAESvIEQYWATVRPGHEQYIEPTKEYADIVI---PNGGPLNPVALDLLVARL 204
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02348 |
PLN02348 |
phosphoribulokinase |
1-395 |
0e+00 |
|
phosphoribulokinase
Pssm-ID: 215198 Cd Length: 395 Bit Score: 816.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 1 MAVSTIYSTQALNSTHFLTSSSSSKQVfLYRRQPQTNRRFNTLITCAQETIVIGLAADSGCGKSTFMRRLTSVFGGAAKP 80
Cdd:PLN02348 1 MAFATVSSTASLNATSSITTPTKSNLG-SRRSKSPAASSVVVALAADDGTVVIGLAADSGCGKSTFMRRLTSVFGGAAKP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 81 PKGGNPDSNTLISDTTTVICLDDYHSLDRYGRKEQKVTALDPRANDFDLMYEQVKALKNGIAVEKPIYNHVTGLLDPPEL 160
Cdd:PLN02348 80 PKGGNPDSNTLISDTTTVICLDDYHSLDRTGRKEKGVTALDPRANNFDLMYEQVKALKEGKAVEKPIYNHVTGLLDPPEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 161 IQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQRDMAERGHSLESIKASIEARKPDFDAFIDPQKQYADA 240
Cdd:PLN02348 160 IEPPKILVIEGLHPMYDERVRDLLDFSIYLDISDDVKFAWKIQRDMAERGHSLESIKASIEARKPDFDAYIDPQKQYADV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 241 VIEVLPTTLIPDDNEGKVLRVRLIMKEGVKYFSPVYLFDEGSTISWIPCGRKLTCSYPGIKFNYEPDSYFDHEVSVLEMD 320
Cdd:PLN02348 240 VIEVLPTQLIPDDNEGKVLRVRLIMKEGVKNFDPVYLFDEGSTISWIPCGRKLTCSYPGIKFFYGPDTYFGHEVSVLEMD 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15222551 321 GQFDRLDELIYVESHLSNLSTKFYGEVTQQMLKHADFPGSNNGTGLFQTIVGLKIRDLYEQLIANKATARAEAKA 395
Cdd:PLN02348 320 GQFDKLDELIYVESHLSNTSTKFYGEVTQQMLKHADFPGSNNGTGLFQTIVGLKIRDLYERIVAKRKVAAGEATA 394
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
52-341 |
0e+00 |
|
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: 541.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 52 VIGLAADSGCGKSTFMRRLTSVFGgaakppkggnpdsntliSDTTTVICLDDYHSLDRYGRKEQKVTALDPRANDFDLMY 131
Cdd:cd02026 1 IIGVAGDSGCGKSTFLRRLTSLFG-----------------SDLVTVICLDDYHSLDRKGRKETGITALDPRANNFDLMY 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 132 EQVKALKNGIAVEKPIYNHVTGLLDPPELIQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQRDMAERGH 211
Cdd:cd02026 64 EQLKALKEGQAIEKPIYNHVTGLIDPPELIKPTKIVVIEGLHPLYDERVRELLDFSVYLDISDEVKFAWKIQRDMAERGH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 212 SLESIKASIEARKPDFDAFIDPQKQYADAVIEVLPTTLIPDDNEGKVLRVRLIMKEGVKYFSPVYLFDEGSTISWIPCGR 291
Cdd:cd02026 144 SLEDVLASIEARKPDFEAYIDPQKQYADVVIQVLPTQLIPDDTEGKVLRVRLIQKEGVKDFVPVYLFDEGSTISWIPCGR 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 15222551 292 KLTCSYPGIKFNYEPDSYFDHEVSVLEMDGQFDRLDELIYVESHLSNLST 341
Cdd:cd02026 224 KLTCSYPGIKLAYGPDTYYGREVSVLEMDGQFDNLEELIYVESHLSNTST 273
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
51-391 |
1.05e-172 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 484.90 E-value: 1.05e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 51 IVIGLAADSGCGKSTFMRRLTSVFGgaakppkggnpdsntliSDTTTVICLDDYHSLDRYGRKEQKVTALDPRANDFDLM 130
Cdd:PRK07429 9 VLLGVAGDSGCGKTTFLRGLADLLG-----------------EELVTVICTDDYHSYDRKQRKELGITALDPRANNLDIM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 131 YEQVKALKNGIAVEKPIYNHVTGLLDPPELIQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQRDMAERG 210
Cdd:PRK07429 72 YEHLKALKTGQPILKPIYNHETGTFDPPEYIEPNKIVVVEGLHPLYDERVRELYDFKVYLDPPEEVKIAWKIKRDMAKRG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 211 HSLESIKASIEARKPDFDAFIDPQKQYADAVIEVLPTTLIPDDNEGKVLRVRLIMKEGVKYFSPVYLFDEGstiswipcg 290
Cdd:PRK07429 152 HTYEQVLAEIEAREPDFEAYIRPQRQWADVVIQFLPTQLIDNDEENKVLRVRLVLRPGIPHPDPAYLFDEG--------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 291 rKLTCSYPGIKFNYEPDSYFDHEVSVLEMDG-----QFDRLDELIYVESHLSNLSTKFYGEVTQQMLKHADFPGSNNGTG 365
Cdd:PRK07429 223 -KLTCSYPGIALRYGPDRYMGKPVDVLEVDGhatleQFDNLEEMIYIEPHLSNTSTKYYGELTGLLLGHTDYPGSSNGLA 301
|
330 340
....*....|....*....|....*.
gi 15222551 366 LFQTIVGLKIRDLYEQLIANKATARA 391
Cdd:PRK07429 302 LFQLLIGYKMRAAYERLTAKEAKLAV 327
|
|
| PRK |
pfam00485 |
Phosphoribulokinase / Uridine kinase family; This family matches three types of P-loop ... |
52-251 |
7.66e-104 |
|
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: 305.09 E-value: 7.66e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 52 VIGLAADSGCGKSTFMRRLTSVFGGAAKPPKGGnpdsnTLISDTTTVICLDDYHSLDRYGRKEQKVTALDPRANDFDLMY 131
Cdd:pfam00485 1 VIGVAGSSGSGKTTVARRIVSIFGREGVPAVGI-----EGDSFHSTDRFYMDLHPEDRKRAGNNGYSFDGPEANDFDLLY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 132 EQVKALKNGIAVEKPIYNHVTGLLDP-PELIQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQRDMAERG 210
Cdd:pfam00485 76 EQFKELKEGGSVDKPIYNHVTHERDPtPELIEGADVLVIEGLHALYDERVAQLLDLKIYVDPDIDLELARKIQRDMAERG 155
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 15222551 211 HSLESIKASIEARKPDFDAFIDPQKQYADAVIEVLPTTLIP 251
Cdd:pfam00485 156 HSLEGVTDSILFRKPDYVNYIDPQFSYADLIIQRVPTNDTA 196
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
48-263 |
2.07e-59 |
|
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: 191.59 E-value: 2.07e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 48 QETIVIGLAADSGCGKSTFMRRLTSVFGgaakppkggnpdsntliSDTTTVICLDDYHSLDRYGRKEQ--KVTALDPRAN 125
Cdd:COG0572 5 GKPRIIGIAGPSGSGKTTFARRLAEQLG-----------------ADKVVVISLDDYYKDREHLPLDErgKPNFDHPEAF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 126 DFDLMYEQVKALKNGIAVEKPIYNHVTG-LLDPPELIQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQR 204
Cdd:COG0572 68 DLDLLNEHLEPLKAGESVELPVYDFATGtRSGETVKVEPADVIIVEGIHALNDELLRDLLDLKIYVDADTDVRLIRRIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 205 DMAERGHSLES-IKASIEARKPDFDAFIDPQKQYADAVIevlPTTLIPDDNEGKVLRVRL 263
Cdd:COG0572 148 DGEERGRTAESvIEQYWATVRPGHEQYIEPTKEYADIVI---PNGGPLNPVALDLLVARL 204
|
|
| UMPK |
cd02023 |
Uridine monophosphate kinase (UMPK, EC 2.7.1.48), also known as uridine kinase or ... |
52-242 |
4.03e-39 |
|
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: 138.46 E-value: 4.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 52 VIGLAADSGCGKSTFMRRLTSVFGGaakppkggnpdsntlisDTTTVICLDD-YHSLDRYGRKEQKVTALD-PRANDFDL 129
Cdd:cd02023 1 IIGIAGGSGSGKTTVAEEIIEQLGN-----------------PKVVIISQDSyYKDLSHEELEERKNNNYDhPDAFDFDL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 130 MYEQVKALKNGIAVEKPIYNHVTG-LLDPPELIQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQRDMAE 208
Cdd:cd02023 64 LISHLQDLKNGKSVEIPVYDFKTHsRLKETVTVYPADVIILEGILALYDKELRDLMDLKIFVDTDADVRLIRRIERDIVE 143
|
170 180 190
....*....|....*....|....*....|....*
gi 15222551 209 RGHSLESIKASIEAR-KPDFDAFIDPQKQYADAVI 242
Cdd:cd02023 144 RGRDLESVINQYLKFvKPMHEQFIEPTKRYADVII 178
|
|
| PRK05480 |
PRK05480 |
uridine/cytidine kinase; Provisional |
48-242 |
5.10e-39 |
|
uridine/cytidine kinase; Provisional
Pssm-ID: 235492 [Multi-domain] Cd Length: 209 Bit Score: 138.75 E-value: 5.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 48 QETIVIGLAADSGCGKSTFMRRLTSVFGGaakppkggnpdsntlisDTTTVICLDDY-HSLDRYGRKEQKVTALD-PRAN 125
Cdd:PRK05480 4 KKPIIIGIAGGSGSGKTTVASTIYEELGD-----------------ESIAVIPQDSYyKDQSHLSFEERVKTNYDhPDAF 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 126 DFDLMYEQVKALKNGIAVEKPIYNHVTGL-LDPPELIQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQR 204
Cdd:PRK05480 67 DHDLLIEHLKALKAGKAIEIPVYDYTEHTrSKETIRVEPKDVIILEGILLLEDERLRDLMDIKIFVDTPLDIRLIRRLKR 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 15222551 205 DMAERGHSLES-IKASIEARKPDFDAFIDPQKQYADAVI 242
Cdd:PRK05480 147 DVNERGRSLESvINQYLSTVRPMHLQFIEPSKRYADIII 185
|
|
| UMPK_like |
cd02028 |
Uridine monophosphate kinase_like (UMPK_like) is a family of proteins highly similar to the ... |
52-242 |
5.68e-14 |
|
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: 69.64 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 52 VIGLAADSGCGKSTFMRRLtsvfgGAAKPPKGGNPdsntlisdttTVICLDDYHSLDRYGRKEQKvTALDPRANDFDLMY 131
Cdd:cd02028 1 VVGIAGPSGSGKTTFAKKL-----SNQLRVNGIGP----------VVISLDDYYVPRKTPRDEDG-NYDFESILDLDLLN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 132 EQVKALKNGIAVEKPIYNHVTG-LLDPPELIQPP-KILVIEGLHPMFdERVRDLLDFSIYldISNEVKFAWKIQRDMAER 209
Cdd:cd02028 65 KNLHDLLNGKEVELPIYDFRTGkRRGYRKLKLPPsGVVILEGIYALN-ERLRSLLDIRVA--VSGGVHLNRLLRRVVRDI 141
|
170 180 190
....*....|....*....|....*....|....*
gi 15222551 210 GHSLESIKASIEARK--PDFDAFIDPQKQYADAVI 242
Cdd:cd02028 142 QFRGYSAELTILMWPsvPSGEEFIIPPLQEAAIVM 176
|
|
| PLN02318 |
PLN02318 |
phosphoribulokinase/uridine kinase |
50-238 |
5.08e-12 |
|
phosphoribulokinase/uridine kinase
Pssm-ID: 177952 [Multi-domain] Cd Length: 656 Bit Score: 67.58 E-value: 5.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 50 TIVIGLAADSGCGKSTFMRRLTSVFGGAAkppkggnpdsntlisdtttVICLDDYHSLDRY--GRKEqkvtalDPRANDF 127
Cdd:PLN02318 65 IILVGVAGPSGAGKTVFTEKVLNFMPSIA-------------------VISMDNYNDSSRIidGNFD------DPRLTDY 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 128 DLMYEQVKALKNGIAVEKPIYNHVTG------LLDPPEliqpPKILVIEGLHPMfDERVRDLLDFSIylDISNEVKF--A 199
Cdd:PLN02318 120 DTLLDNIHDLKAGKSVQVPIYDFKSSsrvgyrTLEVPS----SRIVIIEGIYAL-SEKLRPLLDLRV--SVTGGVHFdlV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 15222551 200 WKIQRDMAERGHSLESIKASI-EARKPDFDAFIDPQKQYA 238
Cdd:PLN02318 193 KRVLRDIQRAGQEPEEIIHQIsETVYPMYKAFIEPDLQTA 232
|
|
| PTZ00301 |
PTZ00301 |
uridine kinase; Provisional |
52-242 |
5.98e-11 |
|
uridine kinase; Provisional
Pssm-ID: 140322 [Multi-domain] Cd Length: 210 Bit Score: 61.56 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 52 VIGLAADSGCGKSTFMRRLTSVFGGAAKPPKGGnpdsntlisdtttVICLDDYHSlDRYGRKEQKVTALD---PRANDFD 128
Cdd:PTZ00301 5 VIGISGASGSGKSSLSTNIVSELMAHCGPVSIG-------------VICEDFYYR-DQSNIPESERAYTNydhPKSLEHD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 129 LMYEQVKALKNGIAVEKPIYNHVT-GLLDPPELIQPPKILVIEGLHPMFDERVRDLLDFSIYLDISNEVKFAWKIQRDMA 207
Cdd:PTZ00301 71 LLTTHLRELKSGKTVQIPQYDYVHhTRSDTAVTMTPKSVLIVEGILLFTNAELRNEMDCLIFVDTPLDICLIRRAKRDMR 150
|
170 180 190
....*....|....*....|....*....|....*.
gi 15222551 208 ERGHSLESIKASIEAR-KPDFDAFIDPQKQYADAVI 242
Cdd:PTZ00301 151 ERGRTFESVIEQYEATvRPMYYAYVEPSKVYADIIV 186
|
|
| PRK_like |
cd02029 |
Phosphoribulokinase-like (PRK-like) is a family of proteins similar to phosphoribulokinase ... |
52-247 |
6.99e-10 |
|
Phosphoribulokinase-like (PRK-like) is a family of proteins similar to phosphoribulokinase (PRK), the enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. PRK 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: 238987 Cd Length: 277 Bit Score: 59.43 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 52 VIGLAADSGCGKSTFMRRLTSVFGgaakpPKGGNPdsntlisdttTVICLDDYHSLDRYGRKEQKVTALD---------P 122
Cdd:cd02029 1 VIAVTGSSGAGTTTVKRAFEHIFA-----REGIHP----------AVVEGDSFHRYERMEMKMAIAEALDagrnfshfgP 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 123 RANDFDLMYEQVKALKNGIAVEKPIYNH----------VTGLLDPPELIQPPK-ILVIEGLHPMFderVRDLLDFSIYLD 191
Cdd:cd02029 66 EANLFDLLEELFRTYGETGRGRSRYYLHsdeeaapfnqEPGTFTPWEDLPEDTdLLFYEGLHGGV---VTEGYNVAQHAD 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15222551 192 ISNEV----KFAW--KIQRDMAERGHSLESIKASIEARKPDFDAFIDPQKQYADAVIEVLPT 247
Cdd:cd02029 143 LLVGVvpiiNLEWiqKIHRDTAERGYSAEAVMDTILRRMPDYINYICPQFSRTDINFQRVPT 204
|
|
| CoaA |
COG1072 |
Panthothenate kinase [Coenzyme transport and metabolism]; Panthothenate kinase is part of the ... |
24-204 |
8.11e-07 |
|
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: 50.29 E-value: 8.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 24 SKQVFLYRRQPQTnrRFntlitcaqetiVIGLAADSGCGKSTFMRRLTSVFGGAAKPPKGGnpdsntLIsdtTTviclDD 103
Cdd:COG1072 73 ATSAFLGQADKKT--PF-----------IIGIAGSVAVGKSTTARLLQALLSRWPEHPKVE------LV---TT----DG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 104 YH----SLDRYGRKEQK---VTaldprandFDL--MYEQVKALKNGIA-VEKPIYNHVTglldppELIQP--------PK 165
Cdd:COG1072 127 FLypnaVLERRGLMDRKgfpES--------YDRrgLLRFLARVKSGDPeVRAPVYSHLL------YDIVPgaivvvdqPD 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 15222551 166 ILVIEGLHPMFDER-----VRDLLDFSIYLDISNEVKFAWKIQR 204
Cdd:COG1072 193 ILIVEGNNVLQDEPnpwlfVSDFFDFSIYVDADEEDLREWYVER 236
|
|
| PanK |
cd02025 |
Pantothenate kinase (PanK) catalyzes the phosphorylation of pantothenic acid to form 4 ... |
122-204 |
4.63e-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: 47.31 E-value: 4.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 122 PRANDFDLMYEQVKALKNGIA-VEKPIYNH----VTGLLDppELIQPPKILVIEGLHPMFDER-----VRDLLDFSIYLD 191
Cdd:cd02025 59 PESYDMEALLKFLKDIKSGKKnVKIPVYSHltydVIPGEK--QTVDQPDILIIEGLNVLQTGQnprlfVSDFFDFSIYVD 136
|
90
....*....|...
gi 15222551 192 ISNEVKFAWKIQR 204
Cdd:cd02025 137 ADEDDIEKWYIKR 149
|
|
| PRK06696 |
PRK06696 |
uridine kinase; Validated |
60-243 |
8.07e-06 |
|
uridine kinase; Validated
Pssm-ID: 180660 Cd Length: 223 Bit Score: 46.51 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 60 GCGKSTFMRRLTSVFGGAAKPpkggnpdsntlisdtttVIC--LDDYHS--LDRYGRKEqkvtaLDPRA---NDFDlmYE 132
Cdd:PRK06696 32 ASGKTTFADELAEEIKKRGRP-----------------VIRasIDDFHNprVIRYRRGR-----ESAEGyyeDAYD--YT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 133 QVKAL------KNG-IAVEKPIYNHVTG--LLDPPELIQPPKILVIEGLHPMFDErVRDLLDFSIYLDISNEVKFAWKIQ 203
Cdd:PRK06696 88 ALRRLlldplgPNGdRQYRTASHDLKTDipVHNPPLLAAPNAVLIVDGTFLLRPE-LRDLWDYKIFLDTDFEVSRRRGAK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 15222551 204 RDMAERGhslesikASIEARKPDFDAFIDPQKQY---------ADAVIE 243
Cdd:PRK06696 167 RDTEAFG-------SYEEAEKMYLARYHPAQKLYiaeanpkerADVVID 208
|
|
| PRK15453 |
PRK15453 |
phosphoribulokinase; Provisional |
102-234 |
1.72e-05 |
|
phosphoribulokinase; Provisional
Pssm-ID: 237970 Cd Length: 290 Bit Score: 45.96 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 102 DDYHSLDRYGRKEQKVTALD---------PRANDFDLMYEQVKAL-KNGI---------AVEKPIYNHVTGLLDPPELIQ 162
Cdd:PRK15453 42 DSFHRYTRPEMKAAIAKARAagrhfshfgPEANLFDELEQLFREYgETGTgktrkylhtDDEAVPYNQVPGTFTPWEPLP 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15222551 163 PPK-ILVIEGLHPMFderVRDLLDFSIYLD-------ISNevkFAW--KIQRDMAERGHSLESIKASIEARKPDFDAFID 232
Cdd:PRK15453 122 EGTdLLFYEGLHGGV---VTDQVDVAQHVDlligvvpIVN---LEWiqKIHRDTSERGYSREAVMDTILRRMPDYINYIT 195
|
..
gi 15222551 233 PQ 234
Cdd:PRK15453 196 PQ 197
|
|
| |
