|
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. ... |
365-552 |
1.53e-131 |
|
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: 381.09 E-value: 1.53e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 365 KNHKIIFVVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMVAKAD 444
Cdd:TIGR01360 1 AKCKIIFIVGGPGSGKGTQCEKIVEKYGFTHLSTGDLLRAEVASGSERGKQLQAIMESGDLVPLDTVLDLLKDAMVAALG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 445 SSKGYLIDGYPREVKQGEEFEKKIAPPTLLLYVDAGKETMVKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYE 524
Cdd:TIGR01360 81 TSKGFLIDGYPREVKQGEEFERRIGPPTLVLYFDCSEDTMVKRLLKRAETSGRVDDNEKTIKKRLETYYKATEPVIAYYE 160
|
170 180
....*....|....*....|....*...
gi 1622193232 525 KRGIVRKLNAEGSVDDVFQQVCTHLDAL 552
Cdd:TIGR01360 161 TKGKLRKINAEGTVDDVFLQVCTAIDKL 188
|
|
| ADK |
cd01428 |
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ... |
369-541 |
3.95e-73 |
|
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: 231.36 E-value: 3.95e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 369 IIFVVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMvAKADSSKG 448
Cdd:cd01428 1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKERL-KKPDCKKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 449 YLIDGYPREVKQGEEFEKKI---APPTLLLYVDAGKETMVKRLLKRGET-------------------SGRVDDNEETIK 506
Cdd:cd01428 80 FILDGFPRTVDQAEALDELLdegIKPDKVIELDVPDEVLIERILGRRICpvsgrvyhlgkddvtgeplSQRSDDNEETIK 159
|
170 180 190
....*....|....*....|....*....|....*
gi 1622193232 507 KRLETYYKATEPVIAFYEKRGIVRKLNAEGSVDDV 541
Cdd:cd01428 160 KRLEVYKEQTAPLIDYYKKKGKLVEIDGSGDIDEV 194
|
|
| ADK |
pfam00406 |
Adenylate kinase; |
372-526 |
6.18e-68 |
|
Adenylate kinase;
Pssm-ID: 395329 [Multi-domain] Cd Length: 184 Bit Score: 217.56 E-value: 6.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 372 VVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMvAKADSSKGYLI 451
Cdd:pfam00406 1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGKEAKEYMDKGELVPDEVVVGLVKERL-EQNDCKNGFLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 452 DGYPREVKQGEEFE---KKIAPPTLLLYVDAGKETMVKRLLKRGET---------------------------SGRVDDN 501
Cdd:pfam00406 80 DGFPRTVPQAEALEellERGIKLDYVIEFDVPDEVLVERLTGRRIHpnsgrsyhlefnppkvpgkddvtgeplVQRSDDN 159
|
170 180
....*....|....*....|....*
gi 1622193232 502 EETIKKRLETYYKATEPVIAFYEKR 526
Cdd:pfam00406 160 EETVKKRLETYHKQTKPLIDYYKKK 184
|
|
| Adk |
COG0563 |
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ... |
368-549 |
1.64e-65 |
|
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: 211.91 E-value: 1.64e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 368 KIIFVvGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMvAKADSSK 447
Cdd:COG0563 2 RIILL-GPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGKKAKEYMDAGELVPDEIVIGLVKERL-AQPDCAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 448 GYLIDGYPREVKQGEEFEKKIA----PPTLLLYVDAGKETMVKRLLKR---------------------------GETSG 496
Cdd:COG0563 80 GFILDGFPRTVAQAEALDELLAelgiKLDAVIELDVDDEELVERLSGRrvcpncgatyhvkfnppkvegvcdkcgGELVQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1622193232 497 RVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKLNAEGSVDDVFQQVCTHL 549
Cdd:COG0563 160 RADDNEETVRKRLEVYHEQTAPLIDYYRKKGKLVEIDGEGSIEEVTADILAIL 212
|
|
| UMP_CMP_kin_fam |
TIGR01359 |
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ... |
369-545 |
1.02e-64 |
|
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: 209.15 E-value: 1.02e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 369 IIFVVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVS-SGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMVAkADSSK 447
Cdd:TIGR01359 1 VVFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKrEGSENGSLIESYIKEGKIVPSEVTVELLKKAIQE-DGSSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 448 GYLIDGYPREVKQGEEFEKKI---APPTLLLYVDAGKETMVKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFYE 524
Cdd:TIGR01359 80 KFLIDGFPRNEENLEAWEKLMdnkVNFKFVLFFDCPEETMIKRLLKRGQTSGRVDDNIETLKKRFRTYNEETLPIIEHFE 159
|
170 180
....*....|....*....|.
gi 1622193232 525 KRGIVRKLNAEGSVDDVFQQV 545
Cdd:TIGR01359 160 NKGKVKEINAEGSVEEVFEDV 180
|
|
| adk |
PRK00279 |
adenylate kinase; Reviewed |
368-552 |
1.40e-63 |
|
adenylate kinase; Reviewed
Pssm-ID: 234711 [Multi-domain] Cd Length: 215 Bit Score: 207.31 E-value: 1.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 368 KIIFVvGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMvAKADSSK 447
Cdd:PRK00279 2 RLILL-GPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAGTELGKEAKSYMDAGELVPDEIVIGLVKERL-AQPDCKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 448 GYLIDGYPREVKQGEEFEKKIA----PPTLLLYVDAGKETMVKRLLKR---------------------------GETSG 496
Cdd:PRK00279 80 GFLLDGFPRTIPQAEALDEMLKelgiKLDAVIEIDVPDEELVERLSGRricpacgrtyhvkfnppkvegkcdvcgEELIQ 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622193232 497 RVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKLNAEGSVDDVFQQVCTHLDAL 552
Cdd:PRK00279 160 RADDNEETVRKRLEVYHKQTAPLIDYYKKKGKLKKIDGTGSIDEVFADILKALGKL 215
|
|
| adk |
TIGR01351 |
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ... |
368-545 |
1.65e-54 |
|
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: 183.20 E-value: 1.65e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 368 KIIFVvGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMVAKADSSK 447
Cdd:TIGR01351 1 RLVLL-GPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 448 GYLIDGYPREVKQGEEFEKKIA-PPTLLLYVDAGKETMVKRLLKRG--ETSGRV-------------------------D 499
Cdd:TIGR01351 80 GFILDGFPRTLSQAEALDALLEePIDAVIELDVPDEELVERLSGRRicPSCGRVyhlkfnppkvpgcddctgellvqreD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1622193232 500 DNEETIKKRLETYYKATEPVIAFYEKRGIVRKLNAEGSVDDVFQQV 545
Cdd:TIGR01351 160 DTEEVVKKRLEVYKEQTEPLIDYYKKRGILVQIDGNGPIDEVWKRI 205
|
|
| PLN02200 |
PLN02200 |
adenylate kinase family protein |
358-545 |
9.28e-50 |
|
adenylate kinase family protein
Pssm-ID: 215125 [Multi-domain] Cd Length: 234 Bit Score: 171.61 E-value: 9.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 358 RMAAEKLKNHKIIFVVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRD 437
Cdd:PLN02200 34 RGSSSKEKTPFITFVLGGPGSGKGTQCEKIVETFGFKHLSAGDLLRREIASNSEHGAMILNTIKEGKIVPSEVTVKLIQK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 438 AMvAKADSSKgYLIDGYPREVKQGEEFEKKI-APPTLLLYVDAGKETMVKRLLKRGEtsGRVDDNEETIKKRLETYYKAT 516
Cdd:PLN02200 114 EM-ESSDNNK-FLIDGFPRTEENRIAFERIIgAEPNVVLFFDCPEEEMVKRVLNRNQ--GRVDDNIDTIKKRLKVFNALN 189
|
170 180
....*....|....*....|....*....
gi 1622193232 517 EPVIAFYEKRGIVRKLNAEGSVDDVFQQV 545
Cdd:PLN02200 190 LPVIDYYSKKGKLYTINAVGTVDEIFEQV 218
|
|
| aden_kin_iso1 |
TIGR01360 |
adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. ... |
125-308 |
5.71e-48 |
|
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: 164.99 E-value: 5.71e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 125 KIIFVIGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMihHANSDRKwELIAKIIANGELAPPETTIEELKQQFIKQPD 204
Cdd:TIGR01360 4 KIIFIVGGPGSGKGTQCEKIVEKYGFTHLSTGDLLRAEV--ASGSERG-KQLQAIMESGDLVPLDTVLDLLKDAMVAALG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 205 -AKGFVVDGFPRDIGQVLTFEEQIGSPDLVVFLACPSQKLRQRLEKRAQEQGRLDDNPHAIGRRLETFKQNVPLIVKYYQ 283
Cdd:TIGR01360 81 tSKGFLIDGYPREVKQGEEFERRIGPPTLVLYFDCSEDTMVKRLLKRAETSGRVDDNEKTIKKRLETYYKATEPVIAYYE 160
|
170 180
....*....|....*....|....*
gi 1622193232 284 EKGTIVRFAADREEEEIFEDIGSYV 308
Cdd:TIGR01360 161 TKGKLRKINAEGTVDDVFLQVCTAI 185
|
|
| ADK |
cd01428 |
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ... |
126-300 |
8.31e-47 |
|
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: 162.02 E-value: 8.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 126 IIFVIGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMihhANSDRKWELIAKIIANGELAPPETTIEELKQQFIKQPDA 205
Cdd:cd01428 1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEI---ASGTELGKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 206 KGFVVDGFPRDIGQVLTFEEQI---GSPDLVVFLACPSQKLRQRLEKRAQE-------------------QGRLDDNPHA 263
Cdd:cd01428 78 KGFILDGFPRTVDQAEALDELLdegIKPDKVIELDVPDEVLIERILGRRICpvsgrvyhlgkddvtgeplSQRSDDNEET 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622193232 264 IGRRLETFKQNVPLIVKYYQEKGTIVRFAADREEEEI 300
Cdd:cd01428 158 IKKRLEVYKEQTAPLIDYYKKKGKLVEIDGSGDIDEV 194
|
|
| PRK14531 |
PRK14531 |
adenylate kinase; Provisional |
367-550 |
1.01e-46 |
|
adenylate kinase; Provisional
Pssm-ID: 172997 [Multi-domain] Cd Length: 183 Bit Score: 161.52 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 367 HKIIFVvGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMvaKADSS 446
Cdd:PRK14531 3 QRLLFL-GPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVAAGSALGQEAEAVMNRGELVSDALVLAIVESQL--KALNS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 447 KGYLIDGYPREVKQGEEFE------KKIAPPTLLLYVDagKETMVKRLLKRgetsGRVDDNEETIKKRLETYYKATEPVI 520
Cdd:PRK14531 80 GGWLLDGFPRTVAQAEALEplleelKQPIEAVVLLELD--DAVLIERLLAR----GRADDNEAVIRNRLEVYREKTAPLI 153
|
170 180 190
....*....|....*....|....*....|
gi 1622193232 521 AFYEKRGIVRKLNAEGSVDDVFQQVCTHLD 550
Cdd:PRK14531 154 DHYRQRGLLQSVEAQGSIEAITERIEKVLA 183
|
|
| PRK14527 |
PRK14527 |
adenylate kinase; Provisional |
365-545 |
2.64e-45 |
|
adenylate kinase; Provisional
Pssm-ID: 237745 [Multi-domain] Cd Length: 191 Bit Score: 158.03 E-value: 2.64e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 365 KNHKIIFVvGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMVAKAD 444
Cdd:PRK14527 5 KNKVVIFL-GPPGAGKGTQAERLAQELGLKKLSTGDILRDHVARGTELGQRAKPIMEAGDLVPDELILALIRDELAGMEP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 445 SSkgYLIDGYPREVKQGEEFEKKI----APPTLLLYVDAGKETMVKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVI 520
Cdd:PRK14527 84 VR--VIFDGFPRTLAQAEALDRLLeelgARLLAVVLLEVPDEELIRRIVERARQEGRSDDNEETVRRRQQVYREQTQPLV 161
|
170 180
....*....|....*....|....*
gi 1622193232 521 AFYEKRGIVRKLNAEGSVDDVFQQV 545
Cdd:PRK14527 162 DYYEARGHLKRVDGLGTPDEVYARI 186
|
|
| UMP_CMP_kin_fam |
TIGR01359 |
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ... |
126-304 |
1.47e-43 |
|
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: 153.30 E-value: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 126 IIFVIGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMihHANSDRKWELIAKIIANGELAPPETTIEELKQQFIKQPDA 205
Cdd:TIGR01359 1 VVFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEI--KREGSENGSLIESYIKEGKIVPSEVTVELLKKAIQEDGSS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 206 KGFVVDGFPRDIGQVLTFEEQIGS---PDLVVFLACPSQKLRQRLEKRAQEQGRLDDNPHAIGRRLETFKQNVPLIVKYY 282
Cdd:TIGR01359 79 KKFLIDGFPRNEENLEAWEKLMDNkvnFKFVLFFDCPEETMIKRLLKRGQTSGRVDDNIETLKKRFRTYNEETLPIIEHF 158
|
170 180
....*....|....*....|..
gi 1622193232 283 QEKGTIVRFAADREEEEIFEDI 304
Cdd:TIGR01359 159 ENKGKVKEINAEGSVEEVFEDV 180
|
|
| PRK14532 |
PRK14532 |
adenylate kinase; Provisional |
369-541 |
5.47e-42 |
|
adenylate kinase; Provisional
Pssm-ID: 184729 [Multi-domain] Cd Length: 188 Bit Score: 149.20 E-value: 5.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 369 IIFvvGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMvAKADSSKG 448
Cdd:PRK14532 4 ILF--GPPAAGKGTQAKRLVEERGMVQLSTGDMLRAAIASGSELGQRVKGIMDRGELVSDEIVIALIEERL-PEAEAAGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 449 YLIDGYPREVKQGEEFEKKIAP------PTLLLYVDagKETMVKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAF 522
Cdd:PRK14532 81 AIFDGFPRTVAQAEALDKMLASrgqkidVVIRLKVD--DEALIERIVKRFEEQGRPDDNPEVFVTRLDAYNAQTAPLLPY 158
|
170
....*....|....*....
gi 1622193232 523 YEKRGIVRKLNAEGSVDDV 541
Cdd:PRK14532 159 YAGQGKLTEVDGMGSIEAV 177
|
|
| AAA_17 |
pfam13207 |
AAA domain; |
373-506 |
5.45e-40 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 141.61 E-value: 5.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 373 VGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSdrGKKLSAIMEKGELVPLDTVLDMLRDAMvAKADSSKGYLID 452
Cdd:pfam13207 1 TGVPGSGKTTQLKKLAEKLGFPHISAGDLLREEAKERG--LVEDRDEMRKLPLEPQKELQKLAAERI-AEEAGEGGVIVD 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 453 GYPREVKQGEEFEK------KIAPPTLLLYVDAGKETMVKRLLKRgETSGRVDDNEETIK 506
Cdd:pfam13207 78 GHPRIKTPAGYLPGlpvevlRELKPDAIILLEADPEEILERRLKD-RTRGRDDDSEEEIR 136
|
|
| PRK14528 |
PRK14528 |
adenylate kinase; Provisional |
368-541 |
5.54e-40 |
|
adenylate kinase; Provisional
Pssm-ID: 172994 [Multi-domain] Cd Length: 186 Bit Score: 143.61 E-value: 5.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 368 KIIFVvGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMVaKADSSK 447
Cdd:PRK14528 3 NIIFM-GPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMGIEAKRYMDAGDLVPDSVVIGIIKDRIR-EADCKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 448 GYLIDGYPREVKQGEEFEKKIAPPTL----LLYVDAGKETMVKRLLKRGETSGRVDDNEETIKKRLETYYKATEPVIAFY 523
Cdd:PRK14528 81 GFLLDGFPRTVEQADALDALLKNEGKsidkAINLEVPDGELLKRLLGRAEIEGRADDNEATIKNRLDNYNKKTLPLLDFY 160
|
170
....*....|....*...
gi 1622193232 524 EKRGIVRKLNAEGSVDDV 541
Cdd:PRK14528 161 AAQKKLSQVNGVGSLEEV 178
|
|
| Adk |
COG0563 |
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ... |
125-304 |
1.26e-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: 137.95 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 125 KIIFvIGGPGSGKGTQSNRIASHFGFTCISVGEILRKqmihHANSDRKWELIAK-IIANGELAPPETTIEELKQQfIKQP 203
Cdd:COG0563 2 RIIL-LGPPGAGKGTQAKRLAEKYGIPHISTGDMLRA----AVKAGTELGKKAKeYMDAGELVPDEIVIGLVKER-LAQP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 204 D-AKGFVVDGFPRDIGQVLTFEE---QIGSP-DLVVFLACPSQKLRQRLEKRA--------------------------- 251
Cdd:COG0563 76 DcANGFILDGFPRTVAQAEALDEllaELGIKlDAVIELDVDDEELVERLSGRRvcpncgatyhvkfnppkvegvcdkcgg 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622193232 252 QEQGRLDDNPHAIGRRLETF-KQNVPLIvKYYQEKGTIVRFAADREEEEIFEDI 304
Cdd:COG0563 156 ELVQRADDNEETVRKRLEVYhEQTAPLI-DYYRKKGKLVEIDGEGSIEEVTADI 208
|
|
| PLN02200 |
PLN02200 |
adenylate kinase family protein |
110-304 |
2.50e-37 |
|
adenylate kinase family protein
Pssm-ID: 215125 [Multi-domain] Cd Length: 234 Bit Score: 138.10 E-value: 2.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 110 LIQEYDVFVPGQPRPKIIFVIGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMIHHANSdrkWELIAKIIANGELAPPE 189
Cdd:PLN02200 29 ITLEERGSSSKEKTPFITFVLGGPGSGKGTQCEKIVETFGFKHLSAGDLLRREIASNSEH---GAMILNTIKEGKIVPSE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 190 TTIeELKQQFIKQPDAKGFVVDGFPRDIGQVLTFEEQIGS-PDLVVFLACPSQKLRQRLEKRaqEQGRLDDNPHAIGRRL 268
Cdd:PLN02200 106 VTV-KLIQKEMESSDNNKFLIDGFPRTEENRIAFERIIGAePNVVLFFDCPEEEMVKRVLNR--NQGRVDDNIDTIKKRL 182
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622193232 269 ETFKQ-NVPLIvKYYQEKGTIVRFAADREEEEIFEDI 304
Cdd:PLN02200 183 KVFNAlNLPVI-DYYSKKGKLYTINAVGTVDEIFEQV 218
|
|
| adk |
PRK02496 |
adenylate kinase; Provisional |
368-541 |
5.57e-37 |
|
adenylate kinase; Provisional
Pssm-ID: 179433 [Multi-domain] Cd Length: 184 Bit Score: 135.26 E-value: 5.57e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 368 KIIFVvGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMvAKADSSK 447
Cdd:PRK02496 3 RLIFL-GPPGAGKGTQAVVLAEHLHIPHISTGDILRQAIKEQTPLGIKAQGYMDKGELVPDQLVLDLVQERL-QQPDAAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 448 GYLIDGYPREVKQGEEFEK---KIAPP-TLLLYVDAGKETMVKRLLKRgetsGRVDDNEETIKKRLETYYKATEPVIAFY 523
Cdd:PRK02496 81 GWILDGFPRKVTQAAFLDEllqEIGQSgERVVNLDVPDDVVVERLLAR----GRKDDTEEVIRRRLEVYREQTAPLIDYY 156
|
170
....*....|....*...
gi 1622193232 524 EKRGIVRKLNAEGSVDDV 541
Cdd:PRK02496 157 RDRQKLLTIDGNQSVEAV 174
|
|
| PRK14530 |
PRK14530 |
adenylate kinase; Provisional |
367-551 |
1.51e-35 |
|
adenylate kinase; Provisional
Pssm-ID: 237747 [Multi-domain] Cd Length: 215 Bit Score: 132.60 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 367 HKIIFVVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRA-EVSSGSDRGKKLS---AIMEKGELVPlDTVLDMLRDAMVAK 442
Cdd:PRK14530 3 QPRILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALRAnKQMDISDMDTEYDtpgEYMDAGELVP-DAVVNEIVEEALSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 443 ADsskGYLIDGYPREVKQGEEFEKkIAPPTLLLYVDAGKETMVKRLLKR---------------------------GETS 495
Cdd:PRK14530 82 AD---GFVLDGYPRNLEQAEYLES-ITDLDVVLYLDVSEEELVDRLTGRrvcpdcganyhvefnqpeeegvcdecgGELI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622193232 496 GRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKLNAEGSVDDVFQQVCTHLDA 551
Cdd:PRK14530 158 QRDDDTEETVRERLDVFEENTEPVIEHYRDQGVLVEVDGEQTPDEVWADIQDAIDD 213
|
|
| PLN02842 |
PLN02842 |
nucleotide kinase |
372-550 |
2.70e-35 |
|
nucleotide kinase
Pssm-ID: 178435 [Multi-domain] Cd Length: 505 Bit Score: 138.84 E-value: 2.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 372 VVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMVAKADSSKGYLI 451
Cdd:PLN02842 2 ISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKRAKEFMNSGRLVPDEIVIAMVTGRLSREDAKEKGWLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 452 DGYPREVKQGEEFEKKIAPPTLLLYVDAGKETMVKRLLKR-------------------GETSGRV----DDNEETIKKR 508
Cdd:PLN02842 82 DGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRrldpvtgkiyhiknfppesEEIKARLitrpDDTEEKVKAR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1622193232 509 LETYYKATEPVIAFYEKrgIVRKLNAEGSVDDVFQQVCTHLD 550
Cdd:PLN02842 162 LQIYKKNAEAILSTYSD--IMVKIDGNRPKEVVFEEISSLLS 201
|
|
| adk |
TIGR01351 |
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ... |
125-304 |
1.06e-33 |
|
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: 127.35 E-value: 1.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 125 KIIFvIGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMihhANSDRKWELIAKIIANGELAPPETTIEELKQQFIKQPD 204
Cdd:TIGR01351 1 RLVL-LGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEI---KAGTPLGKKAKEYMEKGELVPDEIVNQLVKERLTQNDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 205 A-KGFVVDGFPRDIGQVLTFEEQI-GSPDLVVFLACPSQKLRQRLEKR---------------------------AQEQG 255
Cdd:TIGR01351 77 NeNGFILDGFPRTLSQAEALDALLeEPIDAVIELDVPDEELVERLSGRricpscgrvyhlkfnppkvpgcddctgELLVQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622193232 256 RLDDNPHAIGRRLETFKQNVPLIVKYYQEKGTIVRFAADREEEEIFEDI 304
Cdd:TIGR01351 157 REDDTEEVVKKRLEVYKEQTEPLIDYYKKRGILVQIDGNGPIDEVWKRI 205
|
|
| adk |
PRK00279 |
adenylate kinase; Reviewed |
125-304 |
9.97e-33 |
|
adenylate kinase; Reviewed
Pssm-ID: 234711 [Multi-domain] Cd Length: 215 Bit Score: 124.49 E-value: 9.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 125 KIIFvIGGPGSGKGTQSNRIASHFGFTCISVGEILRkqmihhANSDRKWEL---IAKIIANGELAPPETTIEELKqQFIK 201
Cdd:PRK00279 2 RLIL-LGPPGAGKGTQAKFIAEKYGIPHISTGDMLR------AAVKAGTELgkeAKSYMDAGELVPDEIVIGLVK-ERLA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 202 QPDAK-GFVVDGFPRDIGQVLTFEE---QIGSP-DLVVFLACPSQKLRQRLEKRA------------------------- 251
Cdd:PRK00279 74 QPDCKnGFLLDGFPRTIPQAEALDEmlkELGIKlDAVIEIDVPDEELVERLSGRRicpacgrtyhvkfnppkvegkcdvc 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1622193232 252 --QEQGRLDDNPHAIGRRLETF-KQNVPLIvKYYQEKGTIVRFAADREEEEIFEDI 304
Cdd:PRK00279 154 geELIQRADDNEETVRKRLEVYhKQTAPLI-DYYKKKGKLKKIDGTGSIDEVFADI 208
|
|
| ADK |
pfam00406 |
Adenylate kinase; |
129-285 |
1.32e-31 |
|
Adenylate kinase;
Pssm-ID: 395329 [Multi-domain] Cd Length: 184 Bit Score: 120.49 E-value: 1.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 129 VIGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMihhANSDRKWELIAKIIANGELAPPETTIEELKqQFIKQPD-AKG 207
Cdd:pfam00406 1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEI---KSGTELGKEAKEYMDKGELVPDEVVVGLVK-ERLEQNDcKNG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 208 FVVDGFPRDIGQVLTFE---EQIGSPDLVVFLACPSQKLRQRLEKRAQEQ---------------------------GRL 257
Cdd:pfam00406 77 FLLDGFPRTVPQAEALEellERGIKLDYVIEFDVPDEVLVERLTGRRIHPnsgrsyhlefnppkvpgkddvtgeplvQRS 156
|
170 180
....*....|....*....|....*...
gi 1622193232 258 DDNPHAIGRRLETFKQNVPLIVKYYQEK 285
Cdd:pfam00406 157 DDNEETVKKRLETYHKQTKPLIDYYKKK 184
|
|
| PRK13808 |
PRK13808 |
adenylate kinase; Provisional |
370-552 |
2.11e-31 |
|
adenylate kinase; Provisional
Pssm-ID: 172341 [Multi-domain] Cd Length: 333 Bit Score: 124.23 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 370 IFVVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDaMVAKADSSKGY 449
Cdd:PRK13808 3 LILLGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAVAAGTPVGLKAKDIMASGGLVPDEVVVGIISD-RIEQPDAANGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 450 LIDGYPREVKQGEEF-----EKKIAPPTLL-LYVDAGK-----ETMVKRLLKRGETSgRVDDNEETIKKRLETYYKATEP 518
Cdd:PRK13808 82 ILDGFPRTVPQAEALdallkDKQLKLDAVVeLRVNEGAllarvETRVAEMRARGEEV-RADDTPEVLAKRLASYRAQTEP 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1622193232 519 VIAFY-EKRGIvrkLNAEG--SVDDVFQQVCTHLDAL 552
Cdd:PRK13808 161 LVHYYsEKRKL---LTVDGmmTIDEVTREIGRVLAAV 194
|
|
| PLN02674 |
PLN02674 |
adenylate kinase |
358-545 |
1.04e-30 |
|
adenylate kinase
Pssm-ID: 178279 [Multi-domain] Cd Length: 244 Bit Score: 119.99 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 358 RMAAEKLKNHKIIFVvGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRD 437
Cdd:PLN02674 23 RMKCSSKPDKRLILI-GPPGSGKGTQSPIIKDEYCLCHLATGDMLRAAVAAKTPLGIKAKEAMDKGELVSDDLVVGIIDE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 438 AMvAKADSSKGYLIDGYPREV-----------KQGEEFEK------------------------------KIAPPTLLLY 476
Cdd:PLN02674 102 AM-KKPSCQKGFILDGFPRTVvqaqkldemlaKQGAKIDKvlnfaiddaileeritgrwihpssgrtyhtKFAPPKVPGV 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622193232 477 VDAGKETMVKrllkrgetsgRVDDNEETIKKRLETYYKATEPVIAFYEKRGIVRKLNAEGSVDDVFQQV 545
Cdd:PLN02674 181 DDVTGEPLIQ----------RKDDTAAVLKSRLEAFHKQTEPVIDYYAKKGVVANLHAEKPPKEVTAEV 239
|
|
| PLN02459 |
PLN02459 |
probable adenylate kinase |
362-527 |
1.99e-27 |
|
probable adenylate kinase
Pssm-ID: 215253 [Multi-domain] Cd Length: 261 Bit Score: 111.09 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 362 EKLKNHKIIFVvGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMVA 441
Cdd:PLN02459 25 AKGRNVNWVFL-GCPGVGKGTYASRLSKLLGVPHIATGDLVREEIKSSGPLGAQLKEIVNQGKLVPDEIIFSLLSKRLEA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 442 -KADSSKGYLIDGYPREVKQGEEFEkKIAPPTLLLYVDAGKETMVKRLLKR---GETSG--------------------- 496
Cdd:PLN02459 104 gEEEGESGFILDGFPRTVRQAEILE-GVTDIDLVVNLKLREEVLVEKCLGRricSECGKnfnvadidlkgedgrpgivmp 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1622193232 497 --------------RVDDNEETIKKRLETYYKATEPVIAFYEKRG 527
Cdd:PLN02459 183 pllpppecasklitRADDTEEVVKARLRVYKEESQPVEDFYRKRG 227
|
|
| PRK14532 |
PRK14532 |
adenylate kinase; Provisional |
126-289 |
5.83e-27 |
|
adenylate kinase; Provisional
Pssm-ID: 184729 [Multi-domain] Cd Length: 188 Bit Score: 107.60 E-value: 5.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 126 IIFviGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMIHHANSDRKwelIAKIIANGELAPPETTIEELKQQFIKQPDA 205
Cdd:PRK14532 4 ILF--GPPAAGKGTQAKRLVEERGMVQLSTGDMLRAAIASGSELGQR---VKGIMDRGELVSDEIVIALIEERLPEAEAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 206 KGFVVDGFPRDIGQ-------VLTFEEQIgspDLVVFLACPSQKLRQRLEKRAQEQGRLDDNPHAIGRRLETFKQNVPLI 278
Cdd:PRK14532 79 GGAIFDGFPRTVAQaealdkmLASRGQKI---DVVIRLKVDDEALIERIVKRFEEQGRPDDNPEVFVTRLDAYNAQTAPL 155
|
170
....*....|.
gi 1622193232 279 VKYYQEKGTIV 289
Cdd:PRK14532 156 LPYYAGQGKLT 166
|
|
| adk |
PRK02496 |
adenylate kinase; Provisional |
125-309 |
6.25e-26 |
|
adenylate kinase; Provisional
Pssm-ID: 179433 [Multi-domain] Cd Length: 184 Bit Score: 104.83 E-value: 6.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 125 KIIFvIGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMihhansDRKWELIAKI---IANGELAPPEtTIEELKQQFIK 201
Cdd:PRK02496 3 RLIF-LGPPGAGKGTQAVVLAEHLHIPHISTGDILRQAI------KEQTPLGIKAqgyMDKGELVPDQ-LVLDLVQERLQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 202 QPDAK-GFVVDGFPRDIGQVLTFEE---QIG-SPDLVVFLACPSQKLRQRLEKRaqeqGRLDDNPHAIGRRLETFKQNVP 276
Cdd:PRK02496 75 QPDAAnGWILDGFPRKVTQAAFLDEllqEIGqSGERVVNLDVPDDVVVERLLAR----GRKDDTEEVIRRRLEVYREQTA 150
|
170 180 190
....*....|....*....|....*....|...
gi 1622193232 277 LIVKYYQEKGTIVRFAADREEEEIFEDIGSYVQ 309
Cdd:PRK02496 151 PLIDYYRDRQKLLTIDGNQSVEAVTTELKAALA 183
|
|
| PRK14527 |
PRK14527 |
adenylate kinase; Provisional |
121-304 |
1.47e-25 |
|
adenylate kinase; Provisional
Pssm-ID: 237745 [Multi-domain] Cd Length: 191 Bit Score: 103.72 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 121 QPRPKIIFVIGGPGSGKGTQSNRIASHFGFTCISVGEILRKqmiHHANSDRKWELIAKIIANGELAPPETTIEELKQQFI 200
Cdd:PRK14527 3 QTKNKVVIFLGPPGAGKGTQAERLAQELGLKKLSTGDILRD---HVARGTELGQRAKPIMEAGDLVPDELILALIRDELA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 201 KQPDAKgFVVDGFPRDIGQVLTFE---EQIGSPDL-VVFLACPSQKLRQRLEKRAQEQGRLDDNPHAIGRRLETFKQNVP 276
Cdd:PRK14527 80 GMEPVR-VIFDGFPRTLAQAEALDrllEELGARLLaVVLLEVPDEELIRRIVERARQEGRSDDNEETVRRRQQVYREQTQ 158
|
170 180
....*....|....*....|....*...
gi 1622193232 277 LIVKYYQEKGTIVRFAADREEEEIFEDI 304
Cdd:PRK14527 159 PLVDYYEARGHLKRVDGLGTPDEVYARI 186
|
|
| AAA_17 |
pfam13207 |
AAA domain; |
131-264 |
4.52e-25 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 100.78 E-value: 4.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 131 GGPGSGKGTQSNRIASHFGFTCISVGEILRKQMihhanSDRKWELIAKIIANGELAPPETTIEELKQQFIKQPDAKGFVV 210
Cdd:pfam13207 2 GVPGSGKTTQLKKLAEKLGFPHISAGDLLREEA-----KERGLVEDRDEMRKLPLEPQKELQKLAAERIAEEAGEGGVIV 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 211 DGFPRDI---GQVLTFEEQIGS---PDLVVFLACPSQKLRQRLEKRaQEQGRLDDNPHAI 264
Cdd:pfam13207 77 DGHPRIKtpaGYLPGLPVEVLRelkPDAIILLEADPEEILERRLKD-RTRGRDDDSEEEI 135
|
|
| PRK14526 |
PRK14526 |
adenylate kinase; Provisional |
368-541 |
3.59e-24 |
|
adenylate kinase; Provisional
Pssm-ID: 172992 [Multi-domain] Cd Length: 211 Bit Score: 100.70 E-value: 3.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 368 KIIFVvGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAmVAKADSSK 447
Cdd:PRK14526 2 KLVFL-GPPGSGKGTIAKILSNELNYYHISTGDLFRENILNSTPLGKEIKQIVENGQLVPDSITIKIVEDK-INTIKNND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 448 GYLIDGYPREVKQGEEFEkKIAPPTLLLYVDAGKETMVKRLLKR---------------------------GETSGRVDD 500
Cdd:PRK14526 80 NFILDGFPRNINQAKALD-KFLPNIKIINFLIDEELLIKRLSGRrickscnnifniytlptkekgicdvckGDLYQRKDD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1622193232 501 NEETIKKRLETYYKATEPVIAFYEKRGIVRKLNAEGSVDDV 541
Cdd:PRK14526 159 KEESLKTRLQEYKLQTKPLIEFYSKCNRLNNIDASKDIDEV 199
|
|
| PTZ00088 |
PTZ00088 |
adenylate kinase 1; Provisional |
363-528 |
1.60e-22 |
|
adenylate kinase 1; Provisional
Pssm-ID: 240262 [Multi-domain] Cd Length: 229 Bit Score: 96.41 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 363 KLKNHKIIFVVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMVAK 442
Cdd:PTZ00088 2 KLKGPLKIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGKEIQKVVTSGNLVPDNLVIAIVKDEIAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 443 ADS-SKGYLIDGYPREVKQGEEFeKKIAPPTLLLYVDAGKETMVKRLLKR----------------------------GE 493
Cdd:PTZ00088 82 TDDcFKGFILDGFPRNLKQCKEL-GKITNIDLFVNIYLPRNILIKKLLGRricntcnrnfniahirsdpydmppilppAD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1622193232 494 TSG---------RVDDNEETIKKRLETYYKATEPVIAFYEKRGI 528
Cdd:PTZ00088 161 CEGckgnpklqkRSDDTEEIVAHRLNTYESTNSPIIQFFKNENC 204
|
|
| DD_AK5 |
cd22978 |
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar ... |
4-47 |
1.22e-21 |
|
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: 87.97 E-value: 1.22e-21
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622193232 4 TADARDYVSRREIPQLFESMLTGLMYYRPEDPVSYLEHCLQKVR 47
Cdd:cd22978 1 SEDAKDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLEDCLEKIR 44
|
|
| PRK14530 |
PRK14530 |
adenylate kinase; Provisional |
121-312 |
2.26e-21 |
|
adenylate kinase; Provisional
Pssm-ID: 237747 [Multi-domain] Cd Length: 215 Bit Score: 92.54 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 121 QPRpkiIFVIGGPGSGKGTQSNRIASHFGFTCISVGEILR--KQMiHHANSDRKWELIAKIIANGELAPPETTIEELKQQ 198
Cdd:PRK14530 3 QPR---ILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALRanKQM-DISDMDTEYDTPGEYMDAGELVPDAVVNEIVEEA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 199 FikqPDAKGFVVDGFPRDIGQVLTFEEqIGSPDLVVFLACPSQKLRQRLEKR----------------AQEQG------- 255
Cdd:PRK14530 79 L---SDADGFVLDGYPRNLEQAEYLES-ITDLDVVLYLDVSEEELVDRLTGRrvcpdcganyhvefnqPEEEGvcdecgg 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622193232 256 ----RLDDNPHAIGRRLETFKQNVPLIVKYYQEKGTIVRFAADREEEEIFEDIGSYVQQRL 312
Cdd:PRK14530 155 eliqRDDDTEETVRERLDVFEENTEPVIEHYRDQGVLVEVDGEQTPDEVWADIQDAIDDAT 215
|
|
| PRK14529 |
PRK14529 |
adenylate kinase; Provisional |
370-541 |
6.86e-20 |
|
adenylate kinase; Provisional
Pssm-ID: 237746 [Multi-domain] Cd Length: 223 Bit Score: 88.62 E-value: 6.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 370 IFVVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGELVPLDTVLDMLRDAMvaKADSSKGY 449
Cdd:PRK14529 3 ILIFGPNGSGKGTQGALVKKKYDLAHIESGAIFREHIGGGTELGKKAKEYIDRGDLVPDDITIPMILETL--KQDGKNGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 450 LIDGYPREVKQGEEFEKKIAPPTLLL-YV--------DAGKETMVKRLLKR------------------------GETSG 496
Cdd:PRK14529 81 LLDGFPRNKVQAEKLWEALQKEGMKLdYVieillpreVAKNRIMGRRLCKNdnnhpnnifidaikpdgdvcrvcgGELST 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622193232 497 RVDD-NEETIKKRLETYYKATEPVIA---FYE---KRGIVR--KLNAEGSVDDV 541
Cdd:PRK14529 161 RADDqDEEAINKRHDIYYDTETGTLAaayFFKdlaAKGSTKyiELDGEGSIDEI 214
|
|
| PRK13808 |
PRK13808 |
adenylate kinase; Provisional |
127-285 |
7.64e-20 |
|
adenylate kinase; Provisional
Pssm-ID: 172341 [Multi-domain] Cd Length: 333 Bit Score: 90.72 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 127 IFVIGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMihhaNSDRKWELIAK-IIANGELAPPETTIEELKQQfIKQPDA 205
Cdd:PRK13808 3 LILLGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAV----AAGTPVGLKAKdIMASGGLVPDEVVVGIISDR-IEQPDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 206 K-GFVVDGFPRDIGQV-----LTFEEQIGSpDLVVFLACPSQKLRQRLEKRA---QEQG---RLDDNPHAIGRRLETFK- 272
Cdd:PRK13808 78 AnGFILDGFPRTVPQAealdaLLKDKQLKL-DAVVELRVNEGALLARVETRVaemRARGeevRADDTPEVLAKRLASYRa 156
|
170
....*....|...
gi 1622193232 273 QNVPLiVKYYQEK 285
Cdd:PRK13808 157 QTEPL-VHYYSEK 168
|
|
| PRK14528 |
PRK14528 |
adenylate kinase; Provisional |
125-300 |
1.16e-19 |
|
adenylate kinase; Provisional
Pssm-ID: 172994 [Multi-domain] Cd Length: 186 Bit Score: 86.99 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 125 KIIFvIGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMihhANSDRKWELIAKIIANGELAPPETTIEELKQQFIKQPD 204
Cdd:PRK14528 3 NIIF-MGPPGAGKGTQAKILCERLSIPQISTGDILREAV---KNQTAMGIEAKRYMDAGDLVPDSVVIGIIKDRIREADC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 205 AKGFVVDGFPRDIGQVLTFEEQIG----SPDLVVFLACPSQKLRQRLEKRAQEQGRLDDNPHAIGRRLETF-KQNVPLIv 279
Cdd:PRK14528 79 KNGFLLDGFPRTVEQADALDALLKnegkSIDKAINLEVPDGELLKRLLGRAEIEGRADDNEATIKNRLDNYnKKTLPLL- 157
|
170 180
....*....|....*....|.
gi 1622193232 280 KYYQEKGTIVRFAADREEEEI 300
Cdd:PRK14528 158 DFYAAQKKLSQVNGVGSLEEV 178
|
|
| PRK14531 |
PRK14531 |
adenylate kinase; Provisional |
130-304 |
1.25e-18 |
|
adenylate kinase; Provisional
Pssm-ID: 172997 [Multi-domain] Cd Length: 183 Bit Score: 83.71 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 130 IGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMihHANSDRKWELIAkIIANGELAPPETTIEELKQQfIKQPDAKGFV 209
Cdd:PRK14531 8 LGPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEV--AAGSALGQEAEA-VMNRGELVSDALVLAIVESQ-LKALNSGGWL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 210 VDGFPRDIGQVLTFE---EQIGSP-DLVVFLACPSQKLRQRLEKRaqeqGRLDDNPHAIGRRLETFKQNVPLIVKYYQEK 285
Cdd:PRK14531 84 LDGFPRTVAQAEALEpllEELKQPiEAVVLLELDDAVLIERLLAR----GRADDNEAVIRNRLEVYREKTAPLIDHYRQR 159
|
170
....*....|....*....
gi 1622193232 286 GTIVRFAADREEEEIFEDI 304
Cdd:PRK14531 160 GLLQSVEAQGSIEAITERI 178
|
|
| PLN02842 |
PLN02842 |
nucleotide kinase |
131-338 |
7.52e-18 |
|
nucleotide kinase
Pssm-ID: 178435 [Multi-domain] Cd Length: 505 Bit Score: 86.45 E-value: 7.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 131 GGPGSGKGTQSNRIASHFGFTCISVGEILRKQMIHHANSDRKweliAKIIAN-GELAPPETTIEELKQQfIKQPDAK--G 207
Cdd:PLN02842 4 GAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKR----AKEFMNsGRLVPDEIVIAMVTGR-LSREDAKekG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 208 FVVDGFPRDIGQVLTFEEQIGSPDLVVFLACPSQKLRQRL-----------------------EKRAQEQGRLDDNPHAI 264
Cdd:PLN02842 79 WLLDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCvgrrldpvtgkiyhiknfppeseEIKARLITRPDDTEEKV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622193232 265 GRRLETFKQNVPLIVKYYQEkgTIVRFAADREEEEIFEDIGSYVQQ-RLHLERMEFPEspllasldnLFSPSQDS 338
Cdd:PLN02842 159 KARLQIYKKNAEAILSTYSD--IMVKIDGNRPKEVVFEEISSLLSQiQKDATKMIKTK---------KASPVQDK 222
|
|
| PTZ00088 |
PTZ00088 |
adenylate kinase 1; Provisional |
123-312 |
9.46e-14 |
|
adenylate kinase 1; Provisional
Pssm-ID: 240262 [Multi-domain] Cd Length: 229 Bit Score: 70.98 E-value: 9.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 123 RPKIIFVIGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMIHHANSDRKwelIAKIIANGELAPPETTIEELKQQFIKQ 202
Cdd:PTZ00088 5 GPLKIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGKE---IQKVVTSGNLVPDNLVIAIVKDEIAKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 203 PD--AKGFVVDGFPRDIGQVLTFEEqIGSPDLVVFLACPSQKLRQRLEKR------------------------------ 250
Cdd:PTZ00088 82 TDdcFKGFILDGFPRNLKQCKELGK-ITNIDLFVNIYLPRNILIKKLLGRricntcnrnfniahirsdpydmppilppad 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 251 -------AQEQGRLDDNPHAIGRRLETFK-QNVPLIVKYYQEKGTIVRFAADREEEEiFEDIGSYVQQRL 312
Cdd:PTZ00088 161 cegckgnPKLQKRSDDTEEIVAHRLNTYEsTNSPIIQFFKNENCNLVDFEITRGLRD-FDDFYRIVLQRL 229
|
|
| DD_TEX55-like |
cd22961 |
dimerization/docking (D/D) domain found in the testis-specific expressed protein 55 (TEX55) ... |
4-45 |
1.09e-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: 1.09e-11
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1622193232 4 TADARDYVSRREIPQLFESMLTGLMYYRPEDPVSYLEHCLQK 45
Cdd:cd22961 1 LEDAEEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQ 42
|
|
| PLN02674 |
PLN02674 |
adenylate kinase |
121-300 |
2.93e-11 |
|
adenylate kinase
Pssm-ID: 178279 [Multi-domain] Cd Length: 244 Bit Score: 63.75 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 121 QPRPKIIFvIGGPGSGKGTQSNRIASHFGFTCISVGEILRkqmihhANSDRKWELIAK---IIANGELAPPETTIEELKQ 197
Cdd:PLN02674 29 KPDKRLIL-IGPPGSGKGTQSPIIKDEYCLCHLATGDMLR------AAVAAKTPLGIKakeAMDKGELVSDDLVVGIIDE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 198 QFIKQPDAKGFVVDGFPRDIGQVLTFEE----QIGSPDLVVFLACPSQKLRQRLEKR----------------AQEQG-- 255
Cdd:PLN02674 102 AMKKPSCQKGFILDGFPRTVVQAQKLDEmlakQGAKIDKVLNFAIDDAILEERITGRwihpssgrtyhtkfapPKVPGvd 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1622193232 256 ---------RLDDNPHAIGRRLETFKQNVPLIVKYYQEKGTIVRFAADREEEEI 300
Cdd:PLN02674 182 dvtgepliqRKDDTAAVLKSRLEAFHKQTEPVIDYYAKKGVVANLHAEKPPKEV 235
|
|
| PRK14526 |
PRK14526 |
adenylate kinase; Provisional |
125-236 |
3.30e-11 |
|
adenylate kinase; Provisional
Pssm-ID: 172992 [Multi-domain] Cd Length: 211 Bit Score: 62.95 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 125 KIIFvIGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMihhANSDRKWELIAKIIANGELAPPETTIEELKQQFIKQPD 204
Cdd:PRK14526 2 KLVF-LGPPGSGKGTIAKILSNELNYYHISTGDLFRENI---LNSTPLGKEIKQIVENGQLVPDSITIKIVEDKINTIKN 77
|
90 100 110
....*....|....*....|....*....|..
gi 1622193232 205 AKGFVVDGFPRDIGQVLTFEEQIGSPDLVVFL 236
Cdd:PRK14526 78 NDNFILDGFPRNINQAKALDKFLPNIKIINFL 109
|
|
| PLN02459 |
PLN02459 |
probable adenylate kinase |
130-291 |
8.50e-10 |
|
probable adenylate kinase
Pssm-ID: 215253 [Multi-domain] Cd Length: 261 Bit Score: 59.48 E-value: 8.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 130 IGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMihhANSDRKWELIAKIIANGELAPPETTIEELKQ--QFIKQPDAKG 207
Cdd:PLN02459 35 LGCPGVGKGTYASRLSKLLGVPHIATGDLVREEI---KSSGPLGAQLKEIVNQGKLVPDEIIFSLLSKrlEAGEEEGESG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 208 FVVDGFPR------------DIGQV--LTFEEQI-----------------------------GSPDLVVFLACPSQKLR 244
Cdd:PLN02459 112 FILDGFPRtvrqaeilegvtDIDLVvnLKLREEVlvekclgrricsecgknfnvadidlkgedGRPGIVMPPLLPPPECA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1622193232 245 QRLEKRAqeqgrlDDNPHAIGRRLETFKQNVPLIVKYYQEKGTIVRF 291
Cdd:PLN02459 192 SKLITRA------DDTEEVVKARLRVYKEESQPVEDFYRKRGKLLEF 232
|
|
| PRK14529 |
PRK14529 |
adenylate kinase; Provisional |
127-262 |
2.71e-08 |
|
adenylate kinase; Provisional
Pssm-ID: 237746 [Multi-domain] Cd Length: 223 Bit Score: 54.73 E-value: 2.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 127 IFVIGGPGSGKGTQSNRIASHFGFTCISVGEILRKqmihHANSDRKWELIAK-IIANGELAPPETTIEELKQQfIKQPDA 205
Cdd:PRK14529 3 ILIFGPNGSGKGTQGALVKKKYDLAHIESGAIFRE----HIGGGTELGKKAKeYIDRGDLVPDDITIPMILET-LKQDGK 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622193232 206 KGFVVDGFPRDIGQVLTFEEQIGSP----DLVVFLACPSQKLRQRLEKRaqeqgRL--DDNPH 262
Cdd:PRK14529 78 NGWLLDGFPRNKVQAEKLWEALQKEgmklDYVIEILLPREVAKNRIMGR-----RLckNDNNH 135
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
368-551 |
3.04e-08 |
|
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: 53.81 E-value: 3.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 368 KIIFVVGGPGSGKGTQCERIVQ---KYGYTHLSTGDLlraevsSGSDRGKKLSAIMEKGELVPLDTVLDML-----RDAM 439
Cdd:cd01672 1 MFIVFEGIDGAGKTTLIELLAErleARGYEVVLTREP------GGTPIGEAIRELLLDPEDEKMDPRAELLlfaadRAQH 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 440 VAK-----------------ADSS---KGYLIDGYPREVKQGEEFEKKIAPPTLLLYVDAGKETMVKRLLKRGETSGRVD 499
Cdd:cd01672 75 VEEvikpalargkivlsdrfVDSSlayQGAGRGLGEALIEALNDLATGGLKPDLTILLDIDPEVGLARIEARGRDDRDEQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1622193232 500 DNEETIKKRLETYYKatepVIAFYEKRGIVrkLNAEGSVDDVFQQVCTHLDA 551
Cdd:cd01672 155 EGLEFHERVREGYLE----LAAQEPERIIV--IDASQPLEEVLAEILKAILE 200
|
|
| DD_EFCAB10 |
cd22976 |
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein ... |
5-48 |
3.37e-08 |
|
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: 49.79 E-value: 3.37e-08
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622193232 5 ADARDYVSRREIPQLFESMLTGLMYYRPEDPVSYLEHCLQKVRE 48
Cdd:cd22976 2 EEAEEYLEKHKIPELFENLTSLLLYHRPEDPKAFLIEQLEKLKE 45
|
|
| DD_FBXL13 |
cd22977 |
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ... |
8-46 |
1.91e-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: 47.55 E-value: 1.91e-07
10 20 30
....*....|....*....|....*....|....*....
gi 1622193232 8 RDYVSRREIPQLFESMLTGLMYYRPEDPVSYLEHCLQKV 46
Cdd:cd22977 5 RKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
370-512 |
7.62e-07 |
|
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: 48.85 E-value: 7.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 370 IFVVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAImekGELVPlDTVLDMLRDAMVAKADsskgY 449
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEELGAVRLSSDDERKRLFGEGRPSISYYTDA---TDRTY-ERLHELARIALRAGRP----V 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622193232 450 LIDG---YPREVKQGEEFEKKIAPPTLLLYVDAGKETMVKRLLKRGETSG-RVDDNEETIKKRLETY 512
Cdd:pfam13671 74 ILDAtnlRRDERARLLALAREYGVPVRIVVFEAPEEVLRERLAARARAGGdPSDVPEEVLDRQKARF 140
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
130-269 |
7.92e-07 |
|
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: 48.64 E-value: 7.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 130 IGGP-GSGKGTQSNRIASHFGFTCISVGEIlRKQMIhhansdrkwELIAKIIAngelAPPEttI-EELKQQFIKQPDAKG 207
Cdd:cd02020 4 IDGPaGSGKSTVAKLLAKKLGLPYLDTGGI-RTEEV---------GKLASEVA----AIPE--VrKALDERQRELAKKPG 67
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622193232 208 FVVDGfpRDIGQVLtFEEqigsPDLVVFLACPSQklrQRLEKRAQE--QGRLDDNPHAIGRRLE 269
Cdd:cd02020 68 IVLEG--RDIGTVV-FPD----ADLKIFLTASPE---VRAKRRAKQlqAKGEGVDLEEILAEII 121
|
|
| PRK01184 |
PRK01184 |
flagellar hook-basal body complex protein FliE; |
368-508 |
7.05e-06 |
|
flagellar hook-basal body complex protein FliE;
Pssm-ID: 234914 [Multi-domain] Cd Length: 184 Bit Score: 46.86 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 368 KIIFVVGGPGSGKGtQCERIVQKYGYTHLSTGDLLRAEVSSG----SDRGKKLSAIMEKGELVPlDTVldMLRDAMVAKA 443
Cdd:PRK01184 2 KIIGVVGMPGSGKG-EFSKIAREMGIPVVVMGDVIREEVKKRglepTDENIGKVAIDLRKELGM-DAV--AKRTVPKIRE 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622193232 444 DSSKGYLIDGYpREVKQGEEFEKKIAPPTLLLYVDAGKETMVKRLLKRgetsGRVDDNE--ETIKKR 508
Cdd:PRK01184 78 KGDEVVVIDGV-RGDAEVEYFRKEFPEDFILIAIHAPPEVRFERLKKR----GRSDDPKswEELEER 139
|
|
| DD_AK8 |
cd22979 |
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ... |
9-45 |
1.36e-05 |
|
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: 42.45 E-value: 1.36e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1622193232 9 DYVSRREIPQLFESMLTGLMYYRPEDPVSYLEHCLQK 45
Cdd:cd22979 8 AYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
127-260 |
2.09e-05 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 44.34 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 127 IFVIGGPGSGKGTQSNRIASHFGFTcISVGEILRKQMIHHANSDRKWEliAKIIANGELAPpetTIEELKQQfIKQPDAK 206
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGFG-DNVRDLALENGLVLGDDPETRE--SKRLDEDKLDR---LLDLLEEN-AALEEGG 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1622193232 207 GFVVDGFprdigqvLTFEEQIGSPDLV-VFLACPSQKLRQRLEKRAQEQGRLDDN 260
Cdd:pfam13238 74 NLIIDGH-------LAELEPERAKDLVgIVLRASPEELLERLEKRGYEEAKIKEN 121
|
|
| DD_TEX55 |
cd22975 |
dimerization/docking (D/D) domain found in testis-specific expressed protein 55 (TEX55) and ... |
7-48 |
3.39e-05 |
|
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: 41.40 E-value: 3.39e-05
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1622193232 7 ARDYVSRREIPQLFESMLTGLMYYRPEDPVSYLEHCLQKVRE 48
Cdd:cd22975 7 AVKYLEKHNILQLFQELTAGLVYERPDDPIQFMIDEIEKIIK 48
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
126-161 |
6.58e-05 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 43.64 E-value: 6.58e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1622193232 126 IIFVIGGPGSGKGTQSNRIASHFGFTCISVGEILRK 161
Cdd:PRK04182 2 IITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFRE 37
|
|
| PRK01184 |
PRK01184 |
flagellar hook-basal body complex protein FliE; |
124-259 |
8.01e-05 |
|
flagellar hook-basal body complex protein FliE;
Pssm-ID: 234914 [Multi-domain] Cd Length: 184 Bit Score: 43.78 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 124 PKIIFVIGGPGSGKGTQSnRIASHFGFTCISVGEILRKQMIHH------------ANSDRKWE---LIAKIIAngelapp 188
Cdd:PRK01184 1 MKIIGVVGMPGSGKGEFS-KIAREMGIPVVVMGDVIREEVKKRgleptdenigkvAIDLRKELgmdAVAKRTV------- 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622193232 189 ettieelkqQFIKQPDAKGFVVDGFpRDIGQVLTFEEQIGSPDLVVFLACPsqkLRQRLEkRAQEQGRLDD 259
Cdd:PRK01184 73 ---------PKIREKGDEVVVIDGV-RGDAEVEYFRKEFPEDFILIAIHAP---PEVRFE-RLKKRGRSDD 129
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
369-408 |
1.19e-04 |
|
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: 42.47 E-value: 1.19e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1622193232 369 IIFVVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSS 408
Cdd:cd02020 1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTGGIRTEEVGK 40
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
369-508 |
1.90e-04 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 42.49 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 369 IIFVVGGPGSGKGTQCERIVQKYGYTHLSTGDLLR--AEvssgsDRGKKLSAIMEKGELVP-LDTVLD-MLRDAMVAKAD 444
Cdd:PRK04182 2 IITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFRelAK-----ERGMSLEEFNKYAEEDPeIDKEIDrRQLEIAEKEDN 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622193232 445 S---SK--GYLIDGYprevkqgeefekkiapPTLLLYVDAGKETMVKRLLKRGETSgrVDDNEETIKKR 508
Cdd:PRK04182 77 VvleGRlaGWMAKDY----------------ADLKIWLKAPLEVRAERIAEREGIS--VEEALEETIER 127
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
125-310 |
3.72e-04 |
|
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: 41.87 E-value: 3.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 125 KIIFVIGGPGSGKGTQSNRIASHFG-------FTC----ISVGEILRKqmIHHANSDRKWELIAKIIAngELAPPETTIE 193
Cdd:cd01672 1 MFIVFEGIDGAGKTTLIELLAERLEargyevvLTRepggTPIGEAIRE--LLLDPEDEKMDPRAELLL--FAADRAQHVE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 194 ELkqqfIKQPDAKGFVV--D----------GFPR-----DIGQVLTFEEQIGSPDLVVFLACPSQKLRQRLEKRAQEQgR 256
Cdd:cd01672 77 EV----IKPALARGKIVlsDrfvdsslayqGAGRglgeaLIEALNDLATGGLKPDLTILLDIDPEVGLARIEARGRDD-R 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1622193232 257 LDDNPHAIGRRL-ETFKQNVPlivkyyQEKGTIVRFAADREEEEIFEDIGSYVQQ 310
Cdd:cd01672 152 DEQEGLEFHERVrEGYLELAA------QEPERIIVIDASQPLEEVLAEILKAILE 200
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
370-503 |
4.29e-04 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 40.49 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 370 IFVVGGPGSGKGTQCERIVQKYGYTHLSTGDLLRAEVSSGSDRGKKLSAIMEKGElvpLDTVLDMLRDAmvAKADSSKGY 449
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGFGDNVRDLALENGLVLGDDPETRESKRLDEDK---LDRLLDLLEEN--AALEEGGNL 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1622193232 450 LIDGYPreVKQGEEFEKKIAPptllLYVDAGKETMVKRLLKRGETSGRVDDNEE 503
Cdd:pfam13238 76 IIDGHL--AELEPERAKDLVG----IVLRASPEELLERLEKRGYEEAKIKENEE 123
|
|
| AAA_33 |
pfam13671 |
AAA domain; This family of domains contain only a P-loop motif, that is characteriztic of the ... |
127-274 |
1.43e-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: 39.22 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 127 IFVIGGPGSGKGTQSNRIASHFGFTCISVGEILRKQMIHHANSDRKWELIAKIIANgelappetTIEELKQQFIKQPdaK 206
Cdd:pfam13671 2 ILLVGLPGSGKSTLARRLLEELGAVRLSSDDERKRLFGEGRPSISYYTDATDRTYE--------RLHELARIALRAG--R 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622193232 207 GFVVDG---FPRDIGQVLTFEEQIGSPDLVVFLACPSQKLRQRLEKRAqeqGRLDDNPHAIGRRLETFKQN 274
Cdd:pfam13671 72 PVILDAtnlRRDERARLLALAREYGVPVRIVVFEAPEEVLRERLAARA---RAGGDPSDVPEEVLDRQKAR 139
|
|
| DD_TbAK-like |
cd22981 |
dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and ... |
3-45 |
2.06e-03 |
|
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: 36.24 E-value: 2.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1622193232 3 ETADARDYVSRREIPQLFESMLTGLMYYRPEDPVSYLEHCLQK 45
Cdd:cd22981 1 LSEDAQKYLKEKNIPQLFEFLLRHLLLDKPENPLEYLHDLLER 43
|
|
| DD_CrRSP_unchar |
cd22964 |
dimerization/docking (D/D) domain of an uncharacterized subunit found in Chlamydomonas ... |
5-48 |
2.40e-03 |
|
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: 36.05 E-value: 2.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1622193232 5 ADARDYVSRREIPQLFESMLTGLMYYRPEDPVSYLEHCLQKVRE 48
Cdd:cd22964 3 EEKKEYLQQKVINPILEQLVTDLLQEKPEDPVPFMIQWLRKKRS 46
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
119-322 |
4.67e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 38.50 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 119 PGQPRPKIIFVIGGPGSGKGTQSNRIASHFGFT--CISVGEILRKQMIHHANSDRKweliAKIIANGELAPPETTI--EE 194
Cdd:pfam06414 6 TSQERPKAILLGGQPGAGKTELARALLDELGRQgnVVRIDPDDFRELHPHYRELQA----ADPKTASEYTQPDASRwvEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622193232 195 LKQQFIKQpdakgfvvdgfprdiGQVLTFEEQIGSPDLVvflacpsQKLRQRLEKRaqeqgrlddnphaiGRRLETFkqn 274
Cdd:pfam06414 82 LLQHAIEN---------------GYNIILEGTLRSPDVA-------KKIARALKAA--------------GYRVEVA--- 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1622193232 275 vplIVkyYQEKGTIVRFAADREEEEIFEdiGSYVQQRLHLERME-FPES 322
Cdd:pfam06414 123 ---AV--AAPPELSWLGVLDRYEEEVAE--GRYVPKEHHDEAFNgLRES 164
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
468-514 |
9.93e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 37.36 E-value: 9.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1622193232 468 IAPPTLllyvdagkETMVKRLLKRGetsgrvDDNEETIKKRLETYYK 514
Cdd:COG0194 119 ILPPSL--------EELERRLRGRG------TDSEEVIERRLAKARE 151
|
|
| |
