|
Name |
Accession |
Description |
Interval |
E-value |
| aden_kin_iso1 |
TIGR01360 |
adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. ... |
374-561 |
2.48e-115 |
|
adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. This clade is found only in eukaryotes and includes human adenylate kinase isozyme 1 (myokinase). Within the adenylate kinase superfamily, this set appears specifically closely related to a subfamily of eukaryotic UMP-CMP kinases (TIGR01359), rather than to the large clade of bacterial, archaeal, and eukaryotic adenylate kinase family members in TIGR01351.
Pssm-ID: 130427 [Multi-domain] Cd Length: 188 Bit Score: 339.87 E-value: 2.48e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 374 RKCKIIFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMVASLG 453
Cdd:TIGR01360 1 AKCKIIFIVGGPGSGKGTQCEKIVEKYGFTHLSTGDLLRAEVASGSERGKQLQAIMESGDLVPLDTVLDLLKDAMVAALG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 454 NTKGFLIDGYPREVKQGEEFGRRIGEPQLVICMDCSADTMTNRLLQRSQSSQRGEDSAKSVAKRLEAYHRASIPVIAYYE 533
Cdd:TIGR01360 81 TSKGFLIDGYPREVKQGEEFERRIGPPTLVLYFDCSEDTMVKRLLKRAETSGRVDDNEKTIKKRLETYYKATEPVIAYYE 160
|
170 180
....*....|....*....|....*...
gi 157822279 534 TKTQLQKVNAEGTPDQVFLQLCTAIDSV 561
Cdd:TIGR01360 161 TKGKLRKINAEGTVDDVFLQVCTAIDKL 188
|
|
| ADK |
cd01428 |
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ... |
378-550 |
1.06e-59 |
|
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.
Pssm-ID: 238713 [Multi-domain] Cd Length: 194 Bit Score: 196.30 E-value: 1.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 378 IIFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMvASLGNTKG 457
Cdd:cd01428 1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKERL-KKPDCKKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 458 FLIDGYPREVKQGEEFGRRIGE---PQLVICMDCSADTMTNRLLQRSQS-------------------SQRGEDSAKSVA 515
Cdd:cd01428 80 FILDGFPRTVDQAEALDELLDEgikPDKVIELDVPDEVLIERILGRRICpvsgrvyhlgkddvtgeplSQRSDDNEETIK 159
|
170 180 190
....*....|....*....|....*....|....*
gi 157822279 516 KRLEAYHRASIPVIAYYETKTQLQKVNAEGTPDQV 550
Cdd:cd01428 160 KRLEVYKEQTAPLIDYYKKKGKLVEIDGSGDIDEV 194
|
|
| UMP_CMP_kin_fam |
TIGR01359 |
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ... |
378-551 |
3.65e-56 |
|
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of UMP-CMP kinase, as well as others proteins with unknown specificity, some currently designated adenylate kinase. All known members are eukaryotic.
Pssm-ID: 273576 [Multi-domain] Cd Length: 185 Bit Score: 186.81 E-value: 3.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 378 IIFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSE-SERSKLIRDIMERGDLVPSGVVLELLKEAMVASlGNTK 456
Cdd:TIGR01359 1 VVFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREgSENGSLIESYIKEGKIVPSEVTVELLKKAIQED-GSSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 457 GFLIDGYPREVKQGEEFGRRIG---EPQLVICMDCSADTMTNRLLQRSQSSQRGEDSAKSVAKRLEAYHRASIPVIAYYE 533
Cdd:TIGR01359 80 KFLIDGFPRNEENLEAWEKLMDnkvNFKFVLFFDCPEETMIKRLLKRGQTSGRVDDNIETLKKRFRTYNEETLPIIEHFE 159
|
170
....*....|....*...
gi 157822279 534 TKTQLQKVNAEGTPDQVF 551
Cdd:TIGR01359 160 NKGKVKEINAEGSVEEVF 177
|
|
| ADK |
cd01428 |
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ... |
134-307 |
2.74e-52 |
|
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine triphosphates (ATP) to adenosine monophosphates (AMP) and to yield adenosine diphosphates (ADP). This enzyme is required for the biosynthesis of ADP and is essential for homeostasis of adenosine phosphates.
Pssm-ID: 238713 [Multi-domain] Cd Length: 194 Bit Score: 177.04 E-value: 2.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 134 IILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNrkWSLIAKIITNGELAPQETTITEIKQKLMQIPDEE 213
Cdd:cd01428 1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTEL--GKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 214 GIVIDGFPRDVAQALSFEDQIC---TPDLVVFLACANQRLKERLQKR-------------------AEQQGRPDDNLKAT 271
Cdd:cd01428 79 GFILDGFPRTVDQAEALDELLDegiKPDKVIELDVPDEVLIERILGRricpvsgrvyhlgkddvtgEPLSQRSDDNEETI 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 157822279 272 QRRLVNFKQNAAPLVKYFQEKGLIVTFDADRDEDAV 307
Cdd:cd01428 159 KKRLEVYKEQTAPLIDYYKKKGKLVEIDGSGDIDEV 194
|
|
| ADK |
pfam00406 |
Adenylate kinase; |
381-535 |
7.38e-51 |
|
Adenylate kinase;
Pssm-ID: 395329 [Multi-domain] Cd Length: 184 Bit Score: 172.88 E-value: 7.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 381 LMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMVAsLGNTKGFLI 460
Cdd:pfam00406 1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGKEAKEYMDKGELVPDEVVVGLVKERLEQ-NDCKNGFLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 461 DGYPREVKQGEEFGR---RIGEPQLVICMDCSADTMTNRLLQR---------------------------SQSSQRGEDS 510
Cdd:pfam00406 80 DGFPRTVPQAEALEElleRGIKLDYVIEFDVPDEVLVERLTGRrihpnsgrsyhlefnppkvpgkddvtgEPLVQRSDDN 159
|
170 180
....*....|....*....|....*
gi 157822279 511 AKSVAKRLEAYHRASIPVIAYYETK 535
Cdd:pfam00406 160 EETVKKRLETYHKQTKPLIDYYKKK 184
|
|
| Adk |
COG0563 |
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ... |
377-558 |
1.72e-48 |
|
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440329 [Multi-domain] Cd Length: 212 Bit Score: 167.23 E-value: 1.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 377 KIIfLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMvASLGNTK 456
Cdd:COG0563 2 RII-LLGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGKKAKEYMDAGELVPDEIVIGLVKERL-AQPDCAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 457 GFLIDGYPREVKQGE-------EFGRRIgepQLVICMDCSADTMTNRLLQR---------------------------SQ 502
Cdd:COG0563 80 GFILDGFPRTVAQAEaldellaELGIKL---DAVIELDVDDEELVERLSGRrvcpncgatyhvkfnppkvegvcdkcgGE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157822279 503 SSQRGEDSAKSVAKRLEAYHRASIPVIAYYETKTQLQKVNAEGTPDQVFLQLCTAI 558
Cdd:COG0563 157 LVQRADDNEETVRKRLEVYHEQTAPLIDYYRKKGKLVEIDGEGSIEEVTADILAIL 212
|
|
| aden_kin_iso1 |
TIGR01360 |
adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. ... |
133-316 |
1.20e-47 |
|
adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. This clade is found only in eukaryotes and includes human adenylate kinase isozyme 1 (myokinase). Within the adenylate kinase superfamily, this set appears specifically closely related to a subfamily of eukaryotic UMP-CMP kinases (TIGR01359), rather than to the large clade of bacterial, archaeal, and eukaryotic adenylate kinase family members in TIGR01351.
Pssm-ID: 130427 [Multi-domain] Cd Length: 188 Bit Score: 164.22 E-value: 1.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 133 KIILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNRKwsLIAKIITNGELAPQETTITEIKQKLMQ-IPD 211
Cdd:TIGR01360 4 KIIFIVGGPGSGKGTQCEKIVEKYGFTHLSTGDLLRAEVASGSERGK--QLQAIMESGDLVPLDTVLDLLKDAMVAaLGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 212 EEGIVIDGFPRDVAQALSFEDQICTPDLVVFLACANQRLKERLQKRAEQQGRPDDNLKATQRRLVNFKQNAAPLVKYFQE 291
Cdd:TIGR01360 82 SKGFLIDGYPREVKQGEEFERRIGPPTLVLYFDCSEDTMVKRLLKRAETSGRVDDNEKTIKKRLETYYKATEPVIAYYET 161
|
170 180
....*....|....*....|....*
gi 157822279 292 KGLIVTFDADRDEDAVFHDISMAVD 316
Cdd:TIGR01360 162 KGKLRKINAEGTVDDVFLQVCTAID 186
|
|
| PLN02200 |
PLN02200 |
adenylate kinase family protein |
378-554 |
3.99e-45 |
|
adenylate kinase family protein
Pssm-ID: 215125 [Multi-domain] Cd Length: 234 Bit Score: 159.29 E-value: 3.99e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 378 IIFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMVASLGNTkg 457
Cdd:PLN02200 45 ITFVLGGPGSGKGTQCEKIVETFGFKHLSAGDLLRREIASNSEHGAMILNTIKEGKIVPSEVTVKLIQKEMESSDNNK-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 458 FLIDGYPREVKQGEEFGRRIG-EPQLVICMDCSADTMTNRLLQRSQSsqRGEDSAKSVAKRLEAYHRASIPVIAYYETKT 536
Cdd:PLN02200 123 FLIDGFPRTEENRIAFERIIGaEPNVVLFFDCPEEEMVKRVLNRNQG--RVDDNIDTIKKRLKVFNALNLPVIDYYSKKG 200
|
170
....*....|....*...
gi 157822279 537 QLQKVNAEGTPDQVFLQL 554
Cdd:PLN02200 201 KLYTINAVGTVDEIFEQV 218
|
|
| adk |
PRK00279 |
adenylate kinase; Reviewed |
379-560 |
1.60e-44 |
|
adenylate kinase; Reviewed
Pssm-ID: 234711 [Multi-domain] Cd Length: 215 Bit Score: 156.85 E-value: 1.60e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 379 IFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMvASLGNTKGF 458
Cdd:PRK00279 3 LILLGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAGTELGKEAKSYMDAGELVPDEIVIGLVKERL-AQPDCKNGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 459 LIDGYPREVKQGEEFGRRIGEPQL----VICMDCSADTMTNRLLQR---------------------------SQSSQRG 507
Cdd:PRK00279 82 LLDGFPRTIPQAEALDEMLKELGIkldaVIEIDVPDEELVERLSGRricpacgrtyhvkfnppkvegkcdvcgEELIQRA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 157822279 508 EDSAKSVAKRLEAYHRASIPVIAYYETKTQLQKVNAEGTPDQVFLQLCTAIDS 560
Cdd:PRK00279 162 DDNEETVRKRLEVYHKQTAPLIDYYKKKGKLKKIDGTGSIDEVFADILKALGK 214
|
|
| adk |
TIGR01351 |
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ... |
377-559 |
1.04e-40 |
|
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ATP as a phosphate donor for AMP. Most members of this family are known or believed to be adenylate kinase. However, some members accept other nucleotide triphosphates as donors, may be unable to use ATP, and may fail to complement adenylate kinase mutants. An example of a nucleoside-triphosphate--adenylate kinase (EC 2.7.4.10) is SP|Q9UIJ7, a GTP:AMP phosphotransferase. This family is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 273569 [Multi-domain] Cd Length: 210 Bit Score: 146.61 E-value: 1.04e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 377 KIIFLmGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMVASLGNTK 456
Cdd:TIGR01351 1 RLVLL-GPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 457 GFLIDGYPREVKQGEEFGRRIGEPQ-LVICMDCSADTMTNRLLQR---SQSS------------------------QRGE 508
Cdd:TIGR01351 80 GFILDGFPRTLSQAEALDALLEEPIdAVIELDVPDEELVERLSGRricPSCGrvyhlkfnppkvpgcddctgellvQRED 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 157822279 509 DSAKSVAKRLEAYHRASIPVIAYYETKTQLQKVNAEGTPDQVFLQLCTAID 559
Cdd:TIGR01351 160 DTEEVVKKRLEVYKEQTEPLIDYYKKRGILVQIDGNGPIDEVWKRILEALK 210
|
|
| UMP_CMP_kin_fam |
TIGR01359 |
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ... |
134-311 |
6.69e-38 |
|
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of UMP-CMP kinase, as well as others proteins with unknown specificity, some currently designated adenylate kinase. All known members are eukaryotic.
Pssm-ID: 273576 [Multi-domain] Cd Length: 185 Bit Score: 137.89 E-value: 6.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 134 IILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNRKwSLIAKIITNGELAPQETTITEIKQKLMQIPDEE 213
Cdd:TIGR01359 1 VVFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREGSENG-SLIESYIKEGKIVPSEVTVELLKKAIQEDGSSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 214 GIVIDGFPRDVAQALSFEDQICT---PDLVVFLACANQRLKERLQKRAEQQGRPDDNLKATQRRLVNFKQNAAPLVKYFQ 290
Cdd:TIGR01359 80 KFLIDGFPRNEENLEAWEKLMDNkvnFKFVLFFDCPEETMIKRLLKRGQTSGRVDDNIETLKKRFRTYNEETLPIIEHFE 159
|
170 180
....*....|....*....|.
gi 157822279 291 EKGLIVTFDADRDEDAVFHDI 311
Cdd:TIGR01359 160 NKGKVKEINAEGSVEEVFEDV 180
|
|
| Adk |
COG0563 |
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ... |
133-311 |
7.69e-37 |
|
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or related kinase is part of the Pathway/BioSystem: Pyrimidine biosynthesis
Pssm-ID: 440329 [Multi-domain] Cd Length: 212 Bit Score: 136.03 E-value: 7.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 133 KIILvIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNRKwsLIAKIITNGELAPQETTITEIKQKLMQIPDE 212
Cdd:COG0563 2 RIIL-LGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGK--KAKEYMDAGELVPDEIVIGLVKERLAQPDCA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 213 EGIVIDGFPRDVAQALSFEDQIC----TPDLVVFLACANQRLKERLQKRA---------------------------EQQ 261
Cdd:COG0563 79 NGFILDGFPRTVAQAEALDELLAelgiKLDAVIELDVDDEELVERLSGRRvcpncgatyhvkfnppkvegvcdkcggELV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 157822279 262 GRPDDNLKATQRRLVNFKQNAAPLVKYFQEKGLIVTFDADRDEDAVFHDI 311
Cdd:COG0563 159 QRADDNEETVRKRLEVYHEQTAPLIDYYRKKGKLVEIDGEGSIEEVTADI 208
|
|
| PLN02200 |
PLN02200 |
adenylate kinase family protein |
113-311 |
3.45e-36 |
|
adenylate kinase family protein
Pssm-ID: 215125 [Multi-domain] Cd Length: 234 Bit Score: 135.02 E-value: 3.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 113 SETAELIEEYEVFDPSRPR-PKIILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNrkWSLIAKIITNGE 191
Cdd:PLN02200 23 SFSTEIITLEERGSSSKEKtPFITFVLGGPGSGKGTQCEKIVETFGFKHLSAGDLLRREIASNSEH--GAMILNTIKEGK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 192 LAPQETTITEIKQKlMQIPDEEGIVIDGFPRDVAQALSFEDQI-CTPDLVVFLACANQRLKERLQKRaeQQGRPDDNLKA 270
Cdd:PLN02200 101 IVPSEVTVKLIQKE-MESSDNNKFLIDGFPRTEENRIAFERIIgAEPNVVLFFDCPEEEMVKRVLNR--NQGRVDDNIDT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 157822279 271 TQRRLVNFKQNAAPLVKYFQEKGLIVTFDADRDEDAVFHDI 311
Cdd:PLN02200 178 IKKRLKVFNALNLPVIDYYSKKGKLYTINAVGTVDEIFEQV 218
|
|
| ADK |
pfam00406 |
Adenylate kinase; |
137-292 |
1.93e-35 |
|
Adenylate kinase;
Pssm-ID: 395329 [Multi-domain] Cd Length: 184 Bit Score: 131.28 E-value: 1.93e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 137 VIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNRKwsLIAKIITNGELAPQETTITEIKQKLMQIPDEEGIV 216
Cdd:pfam00406 1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGK--EAKEYMDKGELVPDEVVVGLVKERLEQNDCKNGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 217 IDGFPRDVAQALSFED---QICTPDLVVFLACANQRLKERLQKRAEQQ---------------------------GRPDD 266
Cdd:pfam00406 79 LDGFPRTVPQAEALEElleRGIKLDYVIEFDVPDEVLVERLTGRRIHPnsgrsyhlefnppkvpgkddvtgeplvQRSDD 158
|
170 180
....*....|....*....|....*.
gi 157822279 267 NLKATQRRLVNFKQNAAPLVKYFQEK 292
Cdd:pfam00406 159 NEETVKKRLETYHKQTKPLIDYYKKK 184
|
|
| adk |
TIGR01351 |
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ... |
135-316 |
2.35e-35 |
|
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ATP as a phosphate donor for AMP. Most members of this family are known or believed to be adenylate kinase. However, some members accept other nucleotide triphosphates as donors, may be unable to use ATP, and may fail to complement adenylate kinase mutants. An example of a nucleoside-triphosphate--adenylate kinase (EC 2.7.4.10) is SP|Q9UIJ7, a GTP:AMP phosphotransferase. This family is designated subfamily rather than equivalog for this reason. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]
Pssm-ID: 273569 [Multi-domain] Cd Length: 210 Bit Score: 131.97 E-value: 2.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 135 ILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNRKwsLIAKIITNGELAPQETTITEIKQKLMQIPDEE- 213
Cdd:TIGR01351 2 LVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGK--KAKEYMEKGELVPDEIVNQLVKERLTQNDDNEn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 214 GIVIDGFPRDVAQALSFEDQIC-TPDLVVFLACANQRLKERLQKR---------------------------AEQQGRPD 265
Cdd:TIGR01351 80 GFILDGFPRTLSQAEALDALLEePIDAVIELDVPDEELVERLSGRricpscgrvyhlkfnppkvpgcddctgELLVQRED 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 157822279 266 DNLKATQRRLVNFKQNAAPLVKYFQEKGLIVTFDADRDEDAVFHDISMAVD 316
Cdd:TIGR01351 160 DTEEVVKKRLEVYKEQTEPLIDYYKKRGILVQIDGNGPIDEVWKRILEALK 210
|
|
| adk |
PRK00279 |
adenylate kinase; Reviewed |
133-318 |
3.20e-34 |
|
adenylate kinase; Reviewed
Pssm-ID: 234711 [Multi-domain] Cd Length: 215 Bit Score: 128.73 E-value: 3.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 133 KIILvIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNRKwsLIAKIITNGELAPQETTITEIKQKLMQIPDE 212
Cdd:PRK00279 2 RLIL-LGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAGTELGK--EAKSYMDAGELVPDEIVIGLVKERLAQPDCK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 213 EGIVIDGFPRDVAQALSFEDQIC----TPDLVVFLACANQRLKERLQKRA---------------------------EQQ 261
Cdd:PRK00279 79 NGFLLDGFPRTIPQAEALDEMLKelgiKLDAVIEIDVPDEELVERLSGRRicpacgrtyhvkfnppkvegkcdvcgeELI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157822279 262 GRPDDNLKATQRRLVNFKQNAAPLVKYFQEKGLIVTFDADRDEDAVFHDISMAVDNK 318
Cdd:PRK00279 159 QRADDNEETVRKRLEVYHKQTAPLIDYYKKKGKLKKIDGTGSIDEVFADILKALGKL 215
|
|
| PRK14527 |
PRK14527 |
adenylate kinase; Provisional |
375-551 |
4.07e-34 |
|
adenylate kinase; Provisional
Pssm-ID: 237745 [Multi-domain] Cd Length: 191 Bit Score: 127.98 E-value: 4.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 375 KCKIIFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAmVASLGN 454
Cdd:PRK14527 5 KNKVVIFLGPPGAGKGTQAERLAQELGLKKLSTGDILRDHVARGTELGQRAKPIMEAGDLVPDELILALIRDE-LAGMEP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 455 TKgFLIDGYPREVKQGEEFGRRIGEPQL----VICMDCSADTMTNRLLQRSQSSQRGEDSAKSVAKRLEAYHRASIPVIA 530
Cdd:PRK14527 84 VR-VIFDGFPRTLAQAEALDRLLEELGArllaVVLLEVPDEELIRRIVERARQEGRSDDNEETVRRRQQVYREQTQPLVD 162
|
170 180
....*....|....*....|.
gi 157822279 531 YYETKTQLQKVNAEGTPDQVF 551
Cdd:PRK14527 163 YYEARGHLKRVDGLGTPDEVY 183
|
|
| PRK14531 |
PRK14531 |
adenylate kinase; Provisional |
375-559 |
1.25e-32 |
|
adenylate kinase; Provisional
Pssm-ID: 172997 [Multi-domain] Cd Length: 183 Bit Score: 123.38 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 375 KCKIIFLmGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMVASlgN 454
Cdd:PRK14531 2 KQRLLFL-GPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVAAGSALGQEAEAVMNRGELVSDALVLAIVESQLKAL--N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 455 TKGFLIDGYPREVKQGEEFGRRIGE---P-QLVICMDCSADTMTNRLLQRSqssqRGEDSAKSVAKRLEAYHRASIPVIA 530
Cdd:PRK14531 79 SGGWLLDGFPRTVAQAEALEPLLEElkqPiEAVVLLELDDAVLIERLLARG----RADDNEAVIRNRLEVYREKTAPLID 154
|
170 180
....*....|....*....|....*....
gi 157822279 531 YYETKTQLQKVNAEGTPDQVFLQLCTAID 559
Cdd:PRK14531 155 HYRQRGLLQSVEAQGSIEAITERIEKVLA 183
|
|
| PRK14532 |
PRK14532 |
adenylate kinase; Provisional |
135-315 |
2.00e-31 |
|
adenylate kinase; Provisional
Pssm-ID: 184729 [Multi-domain] Cd Length: 188 Bit Score: 120.31 E-value: 2.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 135 ILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASS-NRKwslIAKIITNGELAPQETTITEIKQKLMQIPDEE 213
Cdd:PRK14532 3 LILFGPPAAGKGTQAKRLVEERGMVQLSTGDMLRAAIASGSElGQR---VKGIMDRGELVSDEIVIALIEERLPEAEAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 214 GIVIDGFPRDVAQALSFEDQICTP----DLVVFLACANQRLKERLQKRAEQQGRPDDNLKATQRRLVNFKQNAAPLVKYF 289
Cdd:PRK14532 80 GAIFDGFPRTVAQAEALDKMLASRgqkiDVVIRLKVDDEALIERIVKRFEEQGRPDDNPEVFVTRLDAYNAQTAPLLPYY 159
|
170 180
....*....|....*....|....*.
gi 157822279 290 QEKGLIVTFDADRDEDAVFHDISMAV 315
Cdd:PRK14532 160 AGQGKLTEVDGMGSIEAVAASIDAAL 185
|
|
| adk |
PRK02496 |
adenylate kinase; Provisional |
377-558 |
5.53e-31 |
|
adenylate kinase; Provisional
Pssm-ID: 179433 [Multi-domain] Cd Length: 184 Bit Score: 119.08 E-value: 5.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 377 KIIFLmGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMVASlGNTK 456
Cdd:PRK02496 3 RLIFL-GPPGAGKGTQAVVLAEHLHIPHISTGDILRQAIKEQTPLGIKAQGYMDKGELVPDQLVLDLVQERLQQP-DAAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 457 GFLIDGYPREVKQG---EEFGRRIGEP-QLVICMDCSADTMTNRLLQRSqssqRGEDSAKSVAKRLEAYHRASIPVIAYY 532
Cdd:PRK02496 81 GWILDGFPRKVTQAaflDELLQEIGQSgERVVNLDVPDDVVVERLLARG----RKDDTEEVIRRRLEVYREQTAPLIDYY 156
|
170 180
....*....|....*....|....*.
gi 157822279 533 ETKTQLQKVNAEGTPDQVFLQLCTAI 558
Cdd:PRK02496 157 RDRQKLLTIDGNQSVEAVTTELKAAL 182
|
|
| PRK14532 |
PRK14532 |
adenylate kinase; Provisional |
379-561 |
1.09e-30 |
|
adenylate kinase; Provisional
Pssm-ID: 184729 [Multi-domain] Cd Length: 188 Bit Score: 118.39 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 379 IFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMVASLGnTKGF 458
Cdd:PRK14532 3 LILFGPPAAGKGTQAKRLVEERGMVQLSTGDMLRAAIASGSELGQRVKGIMDRGELVSDEIVIALIEERLPEAEA-AGGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 459 LIDGYPREVKQGEEF-------GRRIgepQLVICMDCSADTMTNRLLQRSQSSQRGEDSAKSVAKRLEAYHRASIPVIAY 531
Cdd:PRK14532 82 IFDGFPRTVAQAEALdkmlasrGQKI---DVVIRLKVDDEALIERIVKRFEEQGRPDDNPEVFVTRLDAYNAQTAPLLPY 158
|
170 180 190
....*....|....*....|....*....|
gi 157822279 532 YETKTQLQKVNAEGTPDQVflqlCTAIDSV 561
Cdd:PRK14532 159 YAGQGKLTEVDGMGSIEAV----AASIDAA 184
|
|
| PRK14530 |
PRK14530 |
adenylate kinase; Provisional |
379-560 |
1.21e-30 |
|
adenylate kinase; Provisional
Pssm-ID: 237747 [Multi-domain] Cd Length: 215 Bit Score: 119.12 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 379 IFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLR-------QELTSESERSkliRDIMERGDLVPSGVVLELLKEAmvas 451
Cdd:PRK14530 6 ILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALRankqmdiSDMDTEYDTP---GEYMDAGELVPDAVVNEIVEEA---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 452 LGNTKGFLIDGYPREVKQGEEFgRRIGEPQLVICMDCSADTMTNRLLQRSQSS--------------------------- 504
Cdd:PRK14530 79 LSDADGFVLDGYPRNLEQAEYL-ESITDLDVVLYLDVSEEELVDRLTGRRVCPdcganyhvefnqpeeegvcdecggeli 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 157822279 505 QRGEDSAKSVAKRLEAYHRASIPVIAYYETKTQLQKVNAEGTPDQVFLQLCTAIDS 560
Cdd:PRK14530 158 QRDDDTEETVRERLDVFEENTEPVIEHYRDQGVLVEVDGEQTPDEVWADIQDAIDD 213
|
|
| AAA_17 |
pfam13207 |
AAA domain; |
382-514 |
2.14e-30 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 115.41 E-value: 2.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 382 MGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESerSKLIRDIMERGDLVPSGVVLELLKEAMVASLGNtKGFLID 461
Cdd:pfam13207 1 TGVPGSGKTTQLKKLAEKLGFPHISAGDLLREEAKERG--LVEDRDEMRKLPLEPQKELQKLAAERIAEEAGE-GGVIVD 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 157822279 462 GYPREVKQGEEFGR------RIGEPQLVICMDCSADTMTNRLLQRsQSSQRGEDSAKSV 514
Cdd:pfam13207 78 GHPRIKTPAGYLPGlpvevlRELKPDAIILLEADPEEILERRLKD-RTRGRDDDSEEEI 135
|
|
| PRK14528 |
PRK14528 |
adenylate kinase; Provisional |
377-550 |
4.17e-28 |
|
adenylate kinase; Provisional
Pssm-ID: 172994 [Multi-domain] Cd Length: 186 Bit Score: 110.87 E-value: 4.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 377 KIIFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMV-ASLGNt 455
Cdd:PRK14528 2 KNIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMGIEAKRYMDAGDLVPDSVVIGIIKDRIReADCKN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 456 kGFLIDGYPREVKQGEEFGRRIGEPQL----VICMDCSADTMTNRLLQRSQSSQRGEDSAKSVAKRLEAYHRASIPVIAY 531
Cdd:PRK14528 81 -GFLLDGFPRTVEQADALDALLKNEGKsidkAINLEVPDGELLKRLLGRAEIEGRADDNEATIKNRLDNYNKKTLPLLDF 159
|
170
....*....|....*....
gi 157822279 532 YETKTQLQKVNAEGTPDQV 550
Cdd:PRK14528 160 YAAQKKLSQVNGVGSLEEV 178
|
|
| PRK14527 |
PRK14527 |
adenylate kinase; Provisional |
132-315 |
6.95e-27 |
|
adenylate kinase; Provisional
Pssm-ID: 237745 [Multi-domain] Cd Length: 191 Bit Score: 107.57 E-value: 6.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 132 PKIILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKkiHSASSNRKWSLIAKIITNGELAPQETTITEIKQKLMQIPD 211
Cdd:PRK14527 6 NKVVIFLGPPGAGKGTQAERLAQELGLKKLSTGDILRD--HVARGTELGQRAKPIMEAGDLVPDELILALIRDELAGMEP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 212 EEgIVIDGFPRDVAQA----LSFEDQICTPDLVVFLACANQRLKERLQKRAEQQGRPDDNLKATQRRLVNFKQNAAPLVK 287
Cdd:PRK14527 84 VR-VIFDGFPRTLAQAealdRLLEELGARLLAVVLLEVPDEELIRRIVERARQEGRSDDNEETVRRRQQVYREQTQPLVD 162
|
170 180
....*....|....*....|....*...
gi 157822279 288 YFQEKGLIVTFDADRDEDAVFHDISMAV 315
Cdd:PRK14527 163 YYEARGHLKRVDGLGTPDEVYARILKAL 190
|
|
| adk |
PRK02496 |
adenylate kinase; Provisional |
135-315 |
4.49e-26 |
|
adenylate kinase; Provisional
Pssm-ID: 179433 [Multi-domain] Cd Length: 184 Bit Score: 105.22 E-value: 4.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 135 ILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIhsaSSNRKWSLIAKIITN-GELAPQETTITEIKQKLMQIPDEE 213
Cdd:PRK02496 4 LIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILRQAI---KEQTPLGIKAQGYMDkGELVPDQLVLDLVQERLQQPDAAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 214 GIVIDGFPRDVAQAlSFEDQICTP-----DLVVFLACANQRLKERLQKRaeqqGRPDDNLKATQRRLVNFKQNAAPLVKY 288
Cdd:PRK02496 81 GWILDGFPRKVTQA-AFLDELLQEigqsgERVVNLDVPDDVVVERLLAR----GRKDDTEEVIRRRLEVYREQTAPLIDY 155
|
170 180
....*....|....*....|....*..
gi 157822279 289 FQEKGLIVTFDADRDEDAVFHDISMAV 315
Cdd:PRK02496 156 YRDRQKLLTIDGNQSVEAVTTELKAAL 182
|
|
| AAA_17 |
pfam13207 |
AAA domain; |
139-268 |
2.67e-25 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 101.16 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 139 GGPGSGKGTQSLKIAERYGFQCISVGELLRKKIhsasSNRKWSLIAKIITNGELAPQETTITEIKQKLMQIPDEEGIVID 218
Cdd:pfam13207 2 GVPGSGKTTQLKKLAEKLGFPHISAGDLLREEA----KERGLVEDRDEMRKLPLEPQKELQKLAAERIAEEAGEGGVIVD 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 157822279 219 GFPRDVAQALSFED------QICTPDLVVFLACANQRLKERLQKRAEqQGRPDDNL 268
Cdd:pfam13207 78 GHPRIKTPAGYLPGlpvevlRELKPDAIILLEADPEEILERRLKDRT-RGRDDDSE 132
|
|
| PLN02842 |
PLN02842 |
nucleotide kinase |
383-561 |
1.51e-24 |
|
nucleotide kinase
Pssm-ID: 178435 [Multi-domain] Cd Length: 505 Bit Score: 107.25 E-value: 1.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 383 GGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMVASLGNTKGFLIDG 462
Cdd:PLN02842 4 GAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKRAKEFMNSGRLVPDEIVIAMVTGRLSREDAKEKGWLLDG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 463 YPREVKQGEEFGRRIGEPQLVICMDCSADTMTNRLLQR-----------------------SQSSQRGEDSAKSVAKRLE 519
Cdd:PLN02842 84 YPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRrldpvtgkiyhiknfppeseeikARLITRPDDTEEKVKARLQ 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157822279 520 AYHRASIPVIAYYEtkTQLQKVNAEGTPDQVFLQLCTAIDSV 561
Cdd:PLN02842 164 IYKKNAEAILSTYS--DIMVKIDGNRPKEVVFEEISSLLSQI 203
|
|
| PRK13808 |
PRK13808 |
adenylate kinase; Provisional |
379-550 |
2.33e-24 |
|
adenylate kinase; Provisional
Pssm-ID: 172341 [Multi-domain] Cd Length: 333 Bit Score: 104.20 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 379 IFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMVASlGNTKGF 458
Cdd:PRK13808 3 LILLGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAVAAGTPVGLKAKDIMASGGLVPDEVVVGIISDRIEQP-DAANGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 459 LIDGYPREVKQGEEFGRRIGEPQL----VICMDCSADTMTNRLLQR-SQSSQRGE-----DSAKSVAKRLEAYHRASIPV 528
Cdd:PRK13808 82 ILDGFPRTVPQAEALDALLKDKQLkldaVVELRVNEGALLARVETRvAEMRARGEevradDTPEVLAKRLASYRAQTEPL 161
|
170 180
....*....|....*....|..
gi 157822279 529 IAYYETKTQLQKVNAEGTPDQV 550
Cdd:PRK13808 162 VHYYSEKRKLLTVDGMMTIDEV 183
|
|
| PRK14530 |
PRK14530 |
adenylate kinase; Provisional |
128-319 |
9.21e-24 |
|
adenylate kinase; Provisional
Pssm-ID: 237747 [Multi-domain] Cd Length: 215 Bit Score: 99.48 E-value: 9.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 128 SRPRpkiILVIGGPGSGKGTQSLKIAERYGFQCISVGELLR--KKIHSASSNRKWSLIAKIITNGELAPQEtTITEIKQK 205
Cdd:PRK14530 2 SQPR---ILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALRanKQMDISDMDTEYDTPGEYMDAGELVPDA-VVNEIVEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 206 lmQIPDEEGIVIDGFPRDVAQALSFEDqICTPDLVVFLACANQRLKERLQKR----------------AEQQG------- 262
Cdd:PRK14530 78 --ALSDADGFVLDGYPRNLEQAEYLES-ITDLDVVLYLDVSEEELVDRLTGRrvcpdcganyhvefnqPEEEGvcdecgg 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822279 263 ----RPDDNLKATQRRLVNFKQNAAPLVKYFQEKGLIVTFDADRDEDAVFHDISMAVDNKL 319
Cdd:PRK14530 155 eliqRDDDTEETVRERLDVFEENTEPVIEHYRDQGVLVEVDGEQTPDEVWADIQDAIDDAT 215
|
|
| PRK14531 |
PRK14531 |
adenylate kinase; Provisional |
135-300 |
6.80e-23 |
|
adenylate kinase; Provisional
Pssm-ID: 172997 [Multi-domain] Cd Length: 183 Bit Score: 96.03 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 135 ILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNRKWSliAKIITNGELAPQETTITEIKQKlMQIPDEEG 214
Cdd:PRK14531 5 LLFLGPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVAAGSALGQEA--EAVMNRGELVSDALVLAIVESQ-LKALNSGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 215 IVIDGFPRDVAQALSFE---DQICTP-DLVVFLACANQRLKERLQKRaeqqGRPDDNLKATQRRLVNFKQNAAPLVKYFQ 290
Cdd:PRK14531 82 WLLDGFPRTVAQAEALEpllEELKQPiEAVVLLELDDAVLIERLLAR----GRADDNEAVIRNRLEVYREKTAPLIDHYR 157
|
170
....*....|
gi 157822279 291 EKGLIVTFDA 300
Cdd:PRK14531 158 QRGLLQSVEA 167
|
|
| PLN02674 |
PLN02674 |
adenylate kinase |
377-550 |
8.90e-23 |
|
adenylate kinase
Pssm-ID: 178279 [Multi-domain] Cd Length: 244 Bit Score: 97.65 E-value: 8.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 377 KIIFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMVASlGNTK 456
Cdd:PLN02674 32 KRLILIGPPGSGKGTQSPIIKDEYCLCHLATGDMLRAAVAAKTPLGIKAKEAMDKGELVSDDLVVGIIDEAMKKP-SCQK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 457 GFLIDGYPREVKQGEEF-------GRRIgEPQLVICMDCS--ADTMTNRLLQRSQSS----------------------- 504
Cdd:PLN02674 111 GFILDGFPRTVVQAQKLdemlakqGAKI-DKVLNFAIDDAilEERITGRWIHPSSGRtyhtkfappkvpgvddvtgepli 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 157822279 505 QRGEDSAKSVAKRLEAYHRASIPVIAYYETKTQLQKVNAEGTPDQV 550
Cdd:PLN02674 190 QRKDDTAAVLKSRLEAFHKQTEPVIDYYAKKGVVANLHAEKPPKEV 235
|
|
| PRK13808 |
PRK13808 |
adenylate kinase; Provisional |
133-299 |
2.06e-22 |
|
adenylate kinase; Provisional
Pssm-ID: 172341 [Multi-domain] Cd Length: 333 Bit Score: 98.42 E-value: 2.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 133 KIILvIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNrkwSLIAK-IITNGELAPQETTITEIKQKLMQIPD 211
Cdd:PRK13808 2 RLIL-LGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAVAAGTPV---GLKAKdIMASGGLVPDEVVVGIISDRIEQPDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 212 EEGIVIDGFPRDVAQALSFE----DQICTPDLVVFLACANQRLKERLQKR-AEQQG-----RPDDNLKATQRRLVNFKQN 281
Cdd:PRK13808 78 ANGFILDGFPRTVPQAEALDallkDKQLKLDAVVELRVNEGALLARVETRvAEMRArgeevRADDTPEVLAKRLASYRAQ 157
|
170
....*....|....*...
gi 157822279 282 AAPLVKYFQEKGLIVTFD 299
Cdd:PRK13808 158 TEPLVHYYSEKRKLLTVD 175
|
|
| PRK14528 |
PRK14528 |
adenylate kinase; Provisional |
133-295 |
6.34e-21 |
|
adenylate kinase; Provisional
Pssm-ID: 172994 [Multi-domain] Cd Length: 186 Bit Score: 90.46 E-value: 6.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 133 KIILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNRKWSliAKIITNGELAPQETTITEIKQKLMQIPDE 212
Cdd:PRK14528 2 KNIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMGIEA--KRYMDAGDLVPDSVVIGIIKDRIREADCK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 213 EGIVIDGFPRDVAQALSFEDQI----CTPDLVVFLACANQRLKERLQKRAEQQGRPDDNLKATQRRLVNFKQNAAPLVKY 288
Cdd:PRK14528 80 NGFLLDGFPRTVEQADALDALLknegKSIDKAINLEVPDGELLKRLLGRAEIEGRADDNEATIKNRLDNYNKKTLPLLDF 159
|
....*..
gi 157822279 289 FQEKGLI 295
Cdd:PRK14528 160 YAAQKKL 166
|
|
| PRK14526 |
PRK14526 |
adenylate kinase; Provisional |
377-550 |
8.71e-21 |
|
adenylate kinase; Provisional
Pssm-ID: 172992 [Multi-domain] Cd Length: 211 Bit Score: 90.68 E-value: 8.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 377 KIIFLmGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLkEAMVASLGNTK 456
Cdd:PRK14526 2 KLVFL-GPPGSGKGTIAKILSNELNYYHISTGDLFRENILNSTPLGKEIKQIVENGQLVPDSITIKIV-EDKINTIKNND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 457 GFLIDGYPREVKQGEEFGRRIGEPQLV-----------------ICMDC-------SADTMTNRLLQRSQSS--QRGEDS 510
Cdd:PRK14526 80 NFILDGFPRNINQAKALDKFLPNIKIInflideellikrlsgrrICKSCnnifniyTLPTKEKGICDVCKGDlyQRKDDK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 157822279 511 AKSVAKRLEAYHRASIPVIAYYETKTQLQKVNAEGTPDQV 550
Cdd:PRK14526 160 EESLKTRLQEYKLQTKPLIEFYSKCNRLNNIDASKDIDEV 199
|
|
| DD_AK5 |
cd22978 |
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar ... |
3-46 |
1.80e-20 |
|
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar proteins; AK5 (EC 2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 5, acts as a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It is active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. It also displays broad nucleoside diphosphate kinase activity. AK5 contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438547 Cd Length: 44 Bit Score: 84.51 E-value: 1.80e-20
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 157822279 3 TNEAKEYLARRDIPQLFESLLNGLMCSKPEDPIEYLETCLQKVK 46
Cdd:cd22978 1 SEDAKDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLEDCLEKIR 44
|
|
| PLN02459 |
PLN02459 |
probable adenylate kinase |
374-538 |
1.24e-19 |
|
probable adenylate kinase
Pssm-ID: 215253 [Multi-domain] Cd Length: 261 Bit Score: 88.75 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 374 RKCKIIFLmGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMVASLG 453
Cdd:PLN02459 28 RNVNWVFL-GCPGVGKGTYASRLSKLLGVPHIATGDLVREEIKSSGPLGAQLKEIVNQGKLVPDEIIFSLLSKRLEAGEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 454 N-TKGFLIDGYPREVKQGEEF------------------------GRRI----GEPQLVICMDCSADTMTNRLLQ----- 499
Cdd:PLN02459 107 EgESGFILDGFPRTVRQAEILegvtdidlvvnlklreevlvekclGRRIcsecGKNFNVADIDLKGEDGRPGIVMppllp 186
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 157822279 500 ----RSQSSQRGEDSAKSVAKRLEAYHRASIPVIAYYETKTQL 538
Cdd:PLN02459 187 ppecASKLITRADDTEEVVKARLRVYKEESQPVEDFYRKRGKL 229
|
|
| PTZ00088 |
PTZ00088 |
adenylate kinase 1; Provisional |
379-533 |
1.33e-19 |
|
adenylate kinase 1; Provisional
Pssm-ID: 240262 [Multi-domain] Cd Length: 229 Bit Score: 87.93 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 379 IFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGVVLELLKEAMVASL-GNTKG 457
Cdd:PTZ00088 9 IVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGKEIQKVVTSGNLVPDNLVIAIVKDEIAKVTdDCFKG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 458 FLIDGYPREVKQGEEFGrRIGEPQLV------------------ICMDCSADTMTNRLLQRS------------------ 501
Cdd:PTZ00088 89 FILDGFPRNLKQCKELG-KITNIDLFvniylprnilikkllgrrICNTCNRNFNIAHIRSDPydmppilppadcegckgn 167
|
170 180 190
....*....|....*....|....*....|...
gi 157822279 502 -QSSQRGEDSAKSVAKRLEAYHRASIPVIAYYE 533
Cdd:PTZ00088 168 pKLQKRSDDTEEIVAHRLNTYESTNSPIIQFFK 200
|
|
| PLN02842 |
PLN02842 |
nucleotide kinase |
136-312 |
5.25e-19 |
|
nucleotide kinase
Pssm-ID: 178435 [Multi-domain] Cd Length: 505 Bit Score: 90.31 E-value: 5.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 136 LVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNRKWSliAKIITNGELAPQETTITEIKQKLmQIPD--EE 213
Cdd:PLN02842 1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKRA--KEFMNSGRLVPDEIVIAMVTGRL-SREDakEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 214 GIVIDGFPRDVAQALSFEDQICTPDLVVFLACANQRLKERLQKR-----------------------AEQQGRPDDNLKA 270
Cdd:PLN02842 78 GWLLDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRrldpvtgkiyhiknfppeseeikARLITRPDDTEEK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157822279 271 TQRRLVNFKQNAAPLVKYFQEkgLIVTFDADRDEDAVFHDIS 312
Cdd:PLN02842 158 VKARLQIYKKNAEAILSTYSD--IMVKIDGNRPKEVVFEEIS 197
|
|
| PRK14526 |
PRK14526 |
adenylate kinase; Provisional |
135-307 |
1.86e-13 |
|
adenylate kinase; Provisional
Pssm-ID: 172992 [Multi-domain] Cd Length: 211 Bit Score: 69.49 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 135 ILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNRKWslIAKIITNGELAPQETTITEIKQKLMQIPDEEG 214
Cdd:PRK14526 3 LVFLGPPGSGKGTIAKILSNELNYYHISTGDLFRENILNSTPLGKE--IKQIVENGQLVPDSITIKIVEDKINTIKNNDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 215 IVIDGFPRDVAQALSFEDQICTPDLVVFLaCANQRLKERLQKR----------------AEQQG-----------RPDDN 267
Cdd:PRK14526 81 FILDGFPRNINQAKALDKFLPNIKIINFL-IDEELLIKRLSGRrickscnnifniytlpTKEKGicdvckgdlyqRKDDK 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 157822279 268 LKATQRRLVNFKQNAAPLVKYFQEKGLIVTFDADRDEDAV 307
Cdd:PRK14526 160 EESLKTRLQEYKLQTKPLIEFYSKCNRLNNIDASKDIDEV 199
|
|
| PTZ00088 |
PTZ00088 |
adenylate kinase 1; Provisional |
131-293 |
3.91e-13 |
|
adenylate kinase 1; Provisional
Pssm-ID: 240262 [Multi-domain] Cd Length: 229 Bit Score: 69.06 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 131 RPKIILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIHSASSNRKwsLIAKIITNGELAPQETTITEIKQKLMQIP 210
Cdd:PTZ00088 5 GPLKIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGK--EIQKVVTSGNLVPDNLVIAIVKDEIAKVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 211 DE--EGIVIDGFPRDVAQALSFEdQICTPDLVVFLACANQRLKERLQKR------------------------------- 257
Cdd:PTZ00088 83 DDcfKGFILDGFPRNLKQCKELG-KITNIDLFVNIYLPRNILIKKLLGRricntcnrnfniahirsdpydmppilppadc 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 157822279 258 ------AEQQGRPDDNLKATQRRLVNFKQNAAPLVKYFQEKG 293
Cdd:PTZ00088 162 egckgnPKLQKRSDDTEEIVAHRLNTYESTNSPIIQFFKNEN 203
|
|
| PLN02674 |
PLN02674 |
adenylate kinase |
128-315 |
9.50e-13 |
|
adenylate kinase
Pssm-ID: 178279 [Multi-domain] Cd Length: 244 Bit Score: 68.37 E-value: 9.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 128 SRPRPKIILvIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIhsaSSNRKWSLIAK-IITNGELAPQETTITEIKQKL 206
Cdd:PLN02674 28 SKPDKRLIL-IGPPGSGKGTQSPIIKDEYCLCHLATGDMLRAAV---AAKTPLGIKAKeAMDKGELVSDDLVVGIIDEAM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 207 MQIPDEEGIVIDGFPRDVAQALSFED----QICTPDLVVFLACANQRLKERLQKR----------------------AEQ 260
Cdd:PLN02674 104 KKPSCQKGFILDGFPRTVVQAQKLDEmlakQGAKIDKVLNFAIDDAILEERITGRwihpssgrtyhtkfappkvpgvDDV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 261 QGRP-----DDNLKATQRRLVNFKQNAAPLVKYFQEKGLIVTFDADRDEDAVFHDISMAV 315
Cdd:PLN02674 184 TGEPliqrkDDTAAVLKSRLEAFHKQTEPVIDYYAKKGVVANLHAEKPPKEVTAEVQKAL 243
|
|
| PRK14529 |
PRK14529 |
adenylate kinase; Provisional |
379-471 |
2.50e-12 |
|
adenylate kinase; Provisional
Pssm-ID: 237746 [Multi-domain] Cd Length: 223 Bit Score: 66.67 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 379 IFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELTSESERSKLIRDIMERGDLVPSGV----VLELLKEAmvaslgN 454
Cdd:PRK14529 3 ILIFGPNGSGKGTQGALVKKKYDLAHIESGAIFREHIGGGTELGKKAKEYIDRGDLVPDDItipmILETLKQD------G 76
|
90
....*....|....*..
gi 157822279 455 TKGFLIDGYPREVKQGE 471
Cdd:PRK14529 77 KNGWLLDGFPRNKVQAE 93
|
|
| PLN02459 |
PLN02459 |
probable adenylate kinase |
108-299 |
4.81e-12 |
|
probable adenylate kinase
Pssm-ID: 215253 [Multi-domain] Cd Length: 261 Bit Score: 66.41 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 108 SDTDLSETAELIEEYEV-FDPSRPRPKII--LVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIhsASSNRKWSLIA 184
Cdd:PLN02459 2 SERDAKSTSALADDLASaCDRSLAKGRNVnwVFLGCPGVGKGTYASRLSKLLGVPHIATGDLVREEI--KSSGPLGAQLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 185 KIITNGELAPQETTITEIKQKLMQIPD--EEGIVIDGFPRDVAQALSFEDqICTPDLVVFLACANQRLKER-LQKR---- 257
Cdd:PLN02459 80 EIVNQGKLVPDEIIFSLLSKRLEAGEEegESGFILDGFPRTVRQAEILEG-VTDIDLVVNLKLREEVLVEKcLGRRicse 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822279 258 ------------AEQQGRP---------------------DDNLKATQRRLVNFKQNAAPLVKYFQEKGLIVTFD 299
Cdd:PLN02459 159 cgknfnvadidlKGEDGRPgivmppllpppecasklitraDDTEEVVKARLRVYKEESQPVEDFYRKRGKLLEFE 233
|
|
| DD_TEX55-like |
cd22961 |
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ... |
5-44 |
1.43e-11 |
|
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55)-like family; The TEX55-like family includes TEX55, F-box/LRR-repeat protein 13 (FBXL13), adenylate kinase isoenzymes AK5 and AK8, as well as uncharacterized EF-hand calcium-binding domain-containing protein 10 (EFCAB10), and protein VEST-1. TEX55, also called testis-specific conserved cAMP-dependent type II PK-anchoring protein (TSCPA), is a putative A-kinase anchoring protein (AKAP) that is dispensable for male fertility. FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6 (DRC6), is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. AK5 and AK8 act as nucleoside monophosphate (NMP) kinases that catalyze the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Members of this family contain a conserved helical bundle domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438530 Cd Length: 43 Bit Score: 59.35 E-value: 1.43e-11
10 20 30 40
....*....|....*....|....*....|....*....|
gi 157822279 5 EAKEYLARRDIPQLFESLLNGLMCSKPEDPIEYLETCLQK 44
Cdd:cd22961 3 DAEEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQ 42
|
|
| PRK14529 |
PRK14529 |
adenylate kinase; Provisional |
135-227 |
1.23e-09 |
|
adenylate kinase; Provisional
Pssm-ID: 237746 [Multi-domain] Cd Length: 223 Bit Score: 58.58 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 135 ILVIGGPGSGKGTQSLKIAERYGFQCISVGELLRKKIhsaSSNRKWSLIAK-IITNGELAPQETTITEIKQKLmQIPDEE 213
Cdd:PRK14529 3 ILIFGPNGSGKGTQGALVKKKYDLAHIESGAIFREHI---GGGTELGKKAKeYIDRGDLVPDDITIPMILETL-KQDGKN 78
|
90
....*....|....
gi 157822279 214 GIVIDGFPRDVAQA 227
Cdd:PRK14529 79 GWLLDGFPRNKVQA 92
|
|
| DD_FBXL13 |
cd22977 |
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ... |
5-45 |
1.26e-07 |
|
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar proteins; FBXL13, also called F-box and leucine-rich repeat protein 13, or dynein regulatory complex subunit 6 (DRC6), is a component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes. It may also function as a substrate-recognition component of an SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex. It contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438546 Cd Length: 43 Bit Score: 47.93 E-value: 1.26e-07
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 157822279 5 EAKEYLARRDIPQLFESLLNGLMCSKPEDPIEYLETCLQKV 45
Cdd:cd22977 3 ELRKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
|
|
| DD_EFCAB10 |
cd22976 |
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein ... |
5-47 |
7.58e-07 |
|
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein 10 (EFCAB10) and similar proteins; The subfamily includes uncharacterized EF-hand calcium-binding domain-containing protein 10 (EFCAB10), which contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438545 Cd Length: 47 Bit Score: 45.94 E-value: 7.58e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 157822279 5 EAKEYLARRDIPQLFESLLNGLMCSKPEDPIEYLETCLQKVKE 47
Cdd:cd22976 3 EAEEYLEKHKIPELFENLTSLLLYHRPEDPKAFLIEQLEKLKE 45
|
|
| DD_AK8 |
cd22979 |
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ... |
8-44 |
2.53e-06 |
|
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar proteins; AK8 (EC 2.7.4.3/EC 2.7.4.6), also called ATP-AMP transphosphorylase 8, acts as a nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. It has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. It also displays broad nucleoside diphosphate kinase activity. AK8 contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438548 Cd Length: 45 Bit Score: 44.38 E-value: 2.53e-06
10 20 30
....*....|....*....|....*....|....*..
gi 157822279 8 EYLARRDIPQLFESLLNGLMCSKPEDPIEYLETCLQK 44
Cdd:cd22979 8 AYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
378-442 |
3.43e-06 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 47.10 E-value: 3.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822279 378 IIFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQELT---SESERSKLIRDIM---ERGDLVPSGVVLE 442
Cdd:cd02020 1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTGGIRTEEVGklaSEVAAIPEVRKALderQRELAKKPGIVLE 71
|
|
| PRK01184 |
PRK01184 |
flagellar hook-basal body complex protein FliE; |
132-266 |
3.55e-06 |
|
flagellar hook-basal body complex protein FliE;
Pssm-ID: 234914 [Multi-domain] Cd Length: 184 Bit Score: 47.63 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 132 PKIILVIGGPGSGKGTQSlKIAERYGFQCISVGELLRKKIHSASSNRKWSLIAKIITN-----GELAPQETTITEIKQKL 206
Cdd:PRK01184 1 MKIIGVVGMPGSGKGEFS-KIAREMGIPVVVMGDVIREEVKKRGLEPTDENIGKVAIDlrkelGMDAVAKRTVPKIREKG 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822279 207 MQIpdeegIVIDGFpRDVAQALSFEDQI-CTPDLVVFLACANQRLkERLQKRaeqqGRPDD 266
Cdd:PRK01184 80 DEV-----VVIDGV-RGDAEVEYFRKEFpEDFILIAIHAPPEVRF-ERLKKR----GRSDD 129
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
379-521 |
5.32e-06 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 46.83 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 379 IFLMGG-PGSGKGTQCEKLAEKYGFTHLST----GELLRQELTSE---SERSKLIRDIMER--GDLVPSG--VVLELlke 446
Cdd:COG0645 1 LILVCGlPGSGKSTLARALAERLGAVRLRSdvvrKRLFGAGLAPLersPEATARTYARLLAlaRELLAAGrsVILDA--- 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822279 447 amvaslgntkGFLidgYPREVKQGEEFGRRIGEPQLVICMDCSADTMTNRLLQRSQSSQRGEDSAKSVAKRLEAY 521
Cdd:COG0645 78 ----------TFL---RRAQREAFRALAEEAGAPFVLIWLDAPEEVLRERLEARNAEGGDSDATWEVLERQLAFE 139
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
135-287 |
6.51e-06 |
|
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.
Pssm-ID: 238978 [Multi-domain] Cd Length: 147 Bit Score: 45.94 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 135 ILVIGGP-GSGKGTQSLKIAERYGFQCISVGELLRKKIHS-ASSNRKWSLIAKIITNgelapqettiteiKQKLMQIPDe 212
Cdd:cd02020 1 IIAIDGPaGSGKSTVAKLLAKKLGLPYLDTGGIRTEEVGKlASEVAAIPEVRKALDE-------------RQRELAKKP- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 213 eGIVIDGfpRDVAqALSFEDqictPDLVVFLAC-----ANQRLKERLQKRAEqqGRPDDNLKATQRR-LVNFKQNAAPLV 286
Cdd:cd02020 67 -GIVLEG--RDIG-TVVFPD----ADLKIFLTAspevrAKRRAKQLQAKGEG--VDLEEILAEIIERdERDSTRYVAPLK 136
|
.
gi 157822279 287 K 287
Cdd:cd02020 137 L 137
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
378-413 |
1.56e-05 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 45.57 E-value: 1.56e-05
10 20 30
....*....|....*....|....*....|....*.
gi 157822279 378 IIFLMGGPGSGKGTQCEKLAEKYGFTHLSTGELLRQ 413
Cdd:PRK04182 2 IITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFRE 37
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
135-169 |
4.79e-05 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 44.41 E-value: 4.79e-05
10 20 30
....*....|....*....|....*....|....*.
gi 157822279 135 ILVIGG-PGSGKGTQSLKIAERYGFQCISVGELLRK 169
Cdd:PRK04182 2 IITISGpPGSGKTTVARLLAEKLGLKHVSAGEIFRE 37
|
|
| DD_TbAK-like |
cd22981 |
dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and ... |
5-44 |
5.32e-05 |
|
dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and similar proteins; AK (EC 2.7.4.3), also called ATP-AMP transphosphorylase, ATP:AMP phosphotransferase, or adenylate monophosphate kinase, catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. It plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Members of this subfamily contain an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438550 Cd Length: 44 Bit Score: 40.48 E-value: 5.32e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 157822279 5 EAKEYLARRDIPQLFESLLNGLMCSKPEDPIEYLETCLQK 44
Cdd:cd22981 4 DAQKYLKEKNIPQLFEFLLRHLLLDKPENPLEYLHDLLER 43
|
|
| DD_CrRSP_unchar |
cd22964 |
dimerization/docking (D/D) domain of an uncharacterized subunit found in Chlamydomonas ... |
4-47 |
1.53e-04 |
|
dimerization/docking (D/D) domain of an uncharacterized subunit found in Chlamydomonas reinhardtii radial spoke 1; Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules. This subfamily includes an uncharacterized protein found in Chlamydomonas reinhardtii radial spoke 1. It contains a conserved domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438533 Cd Length: 46 Bit Score: 39.52 E-value: 1.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 157822279 4 NEAKEYLARRDIPQLFESLLNGLMCSKPEDPIEYLETCLQKVKE 47
Cdd:cd22964 3 EEKKEYLQQKVINPILEQLVTDLLQEKPEDPVPFMIQWLRKKRS 46
|
|
| DD_VEST1 |
cd22980 |
dimerization/docking (D/D) domain found in protein VEST-1 and similar proteins; VEST-1 (also ... |
5-47 |
4.52e-04 |
|
dimerization/docking (D/D) domain found in protein VEST-1 and similar proteins; VEST-1 (also called protein C8orf34) is an uncharacterized protein which contains an N-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438549 Cd Length: 45 Bit Score: 38.00 E-value: 4.52e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 157822279 5 EAKEYLARRDIPQLFESLLNGLMCSKPEDPIEYLETCLQKVKE 47
Cdd:cd22980 3 RIQAYLEKHKIGALFEDLMAKLIRDTPDEPIPYLIKVLQKKAG 45
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
378-428 |
5.72e-04 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 38.47 E-value: 5.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 157822279 378 IIFLMGGPGSGKGTQCEKLAEKYG---FTHLSTGELLRQELTSESERSKLIRDI 428
Cdd:cd02019 1 IIAITGGSGSGKSTVAKKLAEQLGgrsVVVLDEIVILEGLYASYKSRDARIRDL 54
|
|
| Pgk2 |
COG2074 |
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and ... |
128-258 |
9.45e-04 |
|
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 441677 Cd Length: 207 Bit Score: 40.70 E-value: 9.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 128 SRPRPKIILVIGGPGSGKGTQSLKIAERYGFQ-CIS---VGELLRK--------KIHsASSNRKW-SLIAKIITNGELAP 194
Cdd:COG2074 2 RMKRPRIILIGGASGVGKSTIAAELARRLGIPrVIStdsIREVMRPiiskelvpTLH-TSSYEAYkSLSEEEIIAGFLDQ 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 195 QETTITEIKQklMQ---IPDEEGIVIDG---FPRDVAQALSFEDQICtpdLVVFLACANQRLKERLQKRA 258
Cdd:COG2074 81 AEAVSPGIEA--VIeraLKEGESLVIEGvhlVPGFLAELKFNGGNVV---MLVLLVSDEELHRERFYSRA 145
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
135-272 |
1.01e-03 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 39.33 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 135 ILVIGGPGSGKGTQSLKIAERYGFQcISVGELLRKkihsassnRKWSLIAKIITNGELAPQETTITEIKQKLMQIPDEEG 214
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGFG-DNVRDLALE--------NGLVLGDDPETRESKRLDEDKLDRLLDLLEENAALEE 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157822279 215 ---IVIDGFPrdvAQALSFEDqicTPDLVVFLACANQRLKERLQKRAEQQGRPDDNLKATQ 272
Cdd:pfam13238 72 ggnLIIDGHL---AELEPERA---KDLVGIVLRASPEELLERLEKRGYEEAKIKENEEAEI 126
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
135-285 |
1.08e-03 |
|
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the AAA superfamily. Many of the proteins in this family are just short fragments so there is no Walker B motif.
Pssm-ID: 463952 [Multi-domain] Cd Length: 143 Bit Score: 39.60 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 135 ILVIGGPGSGKGTQSLKIAERYGFQCISVgELLRKKIHSASSNRkwslIAKIITNGELAPQetTITEIKQKLMQIPDeeG 214
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEELGAVRLSS-DDERKRLFGEGRPS----ISYYTDATDRTYE--RLHELARIALRAGR--P 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157822279 215 IVIDG---FPRDVAQALS-FEDQICTPDLVVFLACANQrLKERLQKRAEQQGRPDDnlkATQRRLVNFKQNAAPL 285
Cdd:pfam13671 73 VILDAtnlRRDERARLLAlAREYGVPVRIVVFEAPEEV-LRERLAARARAGGDPSD---VPEEVLDRQKARFEPP 143
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
377-560 |
1.21e-03 |
|
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).
Pssm-ID: 238835 Cd Length: 200 Bit Score: 40.33 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 377 KIIFLMGGPGSGKGTQCEKLAE---KYGFTHLSTGELlrqeltSESERSKLIRDIMERGDLVPSGVVLELL--------- 444
Cdd:cd01672 1 MFIVFEGIDGAGKTTLIELLAErleARGYEVVLTREP------GGTPIGEAIRELLLDPEDEKMDPRAELLlfaadraqh 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 445 -KEAMVASLGNTKGFLID----------GYPR-----EVKQGEEFGRRIGEPQLVICMDCSADTmtnrLLQRSQSSQRGE 508
Cdd:cd01672 75 vEEVIKPALARGKIVLSDrfvdsslayqGAGRglgeaLIEALNDLATGGLKPDLTILLDIDPEV----GLARIEARGRDD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 157822279 509 DSaksvAKRLEAYHRAsipVIAYY-----ETKTQLQKVNAEGTPDQVFLQLCTAIDS 560
Cdd:cd01672 151 RD----EQEGLEFHER---VREGYlelaaQEPERIIVIDASQPLEEVLAEILKAILE 200
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
134-219 |
1.43e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 39.81 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 134 IILVIGG-PGSGKGTQSLKIAERYGFQCISvGELLRKkihsASSNRKWSLI--------AKIITNGELAPQETTITEIKQ 204
Cdd:COG1102 1 MVITISRePGSGGTTIAKRLAEKLGLPLYD-GEILRE----AAKERGLSEEefekldekAPSLLYRDTAEEDEIDRALDK 75
|
90
....*....|....*
gi 157822279 205 KLMQIPDEEGIVIDG 219
Cdd:COG1102 76 VIRELARKGNCVIVG 90
|
|
| DD_TEX55 |
cd22975 |
dimerization/docking (D/D) domain found in testis-specific expressed protein 55 (TEX55) and ... |
5-47 |
2.67e-03 |
|
dimerization/docking (D/D) domain found in testis-specific expressed protein 55 (TEX55) and similar proteins; TEX55, also called testis-specific conserved cAMP-dependent type II PK-anchoring protein (TSCPA), is a putative A-kinase anchoring protein (AKAP) that is dispensable for male fertility. It contains a C-terminal domain that shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438544 Cd Length: 50 Bit Score: 36.00 E-value: 2.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 157822279 5 EAKEYLARRDIPQLFESLLNGLMCSKPEDPIEYLETCLQKVKE 47
Cdd:cd22975 6 KAVKYLEKHNILQLFQELTAGLVYERPDDPIQFMIDEIEKIIK 48
|
|
| PRK03839 |
PRK03839 |
putative kinase; Provisional |
134-270 |
2.76e-03 |
|
putative kinase; Provisional
Pssm-ID: 179660 Cd Length: 180 Bit Score: 38.93 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 134 IILVIGGPGSGKGTQSLKIAERYGFQCISVGEL-LRKKIHSassnrkwsliakiITNGELapqETTITEIKQKLMQIPDE 212
Cdd:PRK03839 2 IIAITGTPGVGKTTVSKLLAEKLGYEYVDLTEFaLKKGIGE-------------EKDDEM---EIDFDKLAYFIEEEFKE 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 157822279 213 EGIVIDGFprdvaqaLSfedQICTPDLVVFLACANQRLKERLQKRAEQQGRPDDNLKA 270
Cdd:PRK03839 66 KNVVLDGH-------LS---HLLPVDYVIVLRAHPKIIKERLKERGYSKKKILENVEA 113
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
383-435 |
5.22e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 38.27 E-value: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822279 383 GGPGSGKGTQCEKLAEKYGFTHLStGELLRQ------------------------ELTSESER-----SKLIRDIMERGD 433
Cdd:COG1102 7 REPGSGGTTIAKRLAEKLGLPLYD-GEILREaakerglseeefekldekapsllyRDTAEEDEidralDKVIRELARKGN 85
|
..
gi 157822279 434 LV 435
Cdd:COG1102 86 CV 87
|
|
| DD_AtENO3-like |
cd22962 |
dimerization/docking (D/D) domain found in Arabidopsis thaliana cytosolic enolase 3 (ENO3) and ... |
5-44 |
7.34e-03 |
|
dimerization/docking (D/D) domain found in Arabidopsis thaliana cytosolic enolase 3 (ENO3) and similar proteins; Enolase (EC 4.2.1.11), also known as phosphopyruvate hydratase, is a metalloenzyme responsible for catalyzing the conversion of 2-phosphoglycerate (2-PG) to phosphoenolpyruvate (PEP), the ninth and penultimate step of glycolysis. The subfamily includes Arabidopsis thaliana ENO3, also called ENOC, 2-phospho-D-glycerate hydro-lyase 3, or 2-phosphoglycerate dehydratase 3. It contains an N-terminal domain which shows high sequence similarity to the dimerization/docking (D/D) domains of regulatory subunit of cAMP-dependent protein kinase (PKA) and protein DPY-30/SDC1.
Pssm-ID: 438531 Cd Length: 45 Bit Score: 34.48 E-value: 7.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 157822279 5 EAKEYLARRDIPQLFESLLNGLMCSKPEDPIEYLETCLQK 44
Cdd:cd22962 2 SVQEYLEKHKLEEKLEEAVNAVVKEKPEDPFGFLAQLLRK 41
|
|
| Cmk |
COG0283 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
384-408 |
7.54e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440052 [Multi-domain] Cd Length: 220 Bit Score: 38.08 E-value: 7.54e-03
10 20
....*....|....*....|....*.
gi 157822279 384 GP-GSGKGTQCEKLAEKYGFTHLSTG 408
Cdd:COG0283 7 GPaGSGKSTVAKALAKRLGYHYLDTG 32
|
|
| |
