|
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. ... |
350-537 |
1.98e-124 |
|
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: 362.21 E-value: 1.98e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 350 RKCKIIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASLG 429
Cdd:TIGR01360 1 AKCKIIFIVGGPGSGKGTQCEKIVEKYGFTHLSTGDLLRAEVASGSERGKQLQAIMESGDLVPLDTVLDLLKDAMVAALG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 430 DTRGFLIDGYPREVKQGEEFGRRIGDPQLVICMDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIAYYE 509
Cdd:TIGR01360 81 TSKGFLIDGYPREVKQGEEFERRIGPPTLVLYFDCSEDTMVKRLLKRAETSGRVDDNEKTIKKRLETYYKATEPVIAYYE 160
|
170 180
....*....|....*....|....*...
gi 530362359 510 TKTQLHKINAEGTPEDVFLQLCTAIDSI 537
Cdd:TIGR01360 161 TKGKLRKINAEGTVDDVFLQVCTAIDKL 188
|
|
| ADK |
cd01428 |
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ... |
354-526 |
1.76e-60 |
|
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: 197.84 E-value: 1.76e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 354 IIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMvASLGDTRG 433
Cdd:cd01428 1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTELGKKAKEYIDSGKLVPDEIVIKLLKERL-KKPDCKKG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 434 FLIDGYPREVKQGEEFGRRI---GDPQLVICMDCSADTMTNRLLQRSRSSLP-------------------VDDTTKTIA 491
Cdd:cd01428 80 FILDGFPRTVDQAEALDELLdegIKPDKVIELDVPDEVLIERILGRRICPVSgrvyhlgkddvtgeplsqrSDDNEETIK 159
|
170 180 190
....*....|....*....|....*....|....*
gi 530362359 492 KRLEAYYRASIPVIAYYETKTQLHKINAEGTPEDV 526
Cdd:cd01428 160 KRLEVYKEQTAPLIDYYKKKGKLVEIDGSGDIDEV 194
|
|
| UMP_CMP_kin_fam |
TIGR01359 |
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ... |
354-527 |
9.86e-58 |
|
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: 190.27 E-value: 9.86e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 354 IIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASE-SERSKLIRDIMERGDLVPSGIVLELLKEAMVASlGDTR 432
Cdd:TIGR01359 1 VVFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREgSENGSLIESYIKEGKIVPSEVTVELLKKAIQED-GSSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 433 GFLIDGYPREVKQGEEFGRRIG---DPQLVICMDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIAYYE 509
Cdd:TIGR01359 80 KFLIDGFPRNEENLEAWEKLMDnkvNFKFVLFFDCPEETMIKRLLKRGQTSGRVDDNIETLKKRFRTYNEETLPIIEHFE 159
|
170
....*....|....*...
gi 530362359 510 TKTQLHKINAEGTPEDVF 527
Cdd:TIGR01359 160 NKGKVKEINAEGSVEEVF 177
|
|
| ADK |
cd01428 |
Adenylate kinase (ADK) catalyzes the reversible phosphoryl transfer from adenosine ... |
110-283 |
3.37e-53 |
|
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: 178.97 E-value: 3.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 110 IILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNrkWSLIAKIITTGELAPQETTITEIKQKLMQIPDEE 189
Cdd:cd01428 1 RILLLGPPGSGKGTQAERLAKKYGLPHISTGDLLREEIASGTEL--GKKAKEYIDSGKLVPDEIVIKLLKERLKKPDCKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 190 GIVIDGFPRDVAQALSFEDQIC---TPDLVVFLACANQRLKERLLKR-------------------AEQQGRPDDNVKAT 247
Cdd:cd01428 79 GFILDGFPRTVDQAEALDELLDegiKPDKVIELDVPDEVLIERILGRricpvsgrvyhlgkddvtgEPLSQRSDDNEETI 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 530362359 248 QRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEV 283
Cdd:cd01428 159 KKRLEVYKEQTAPLIDYYKKKGKLVEIDGSGDIDEV 194
|
|
| aden_kin_iso1 |
TIGR01360 |
adenylate kinase, isozyme 1 subfamily; Members of this family are adenylate kinase, EC 2.7.4.3. ... |
109-292 |
2.16e-49 |
|
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: 168.46 E-value: 2.16e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 109 KIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwsLIAKIITTGELAPQETTITEIKQKLMQ-IPD 187
Cdd:TIGR01360 4 KIIFIVGGPGSGKGTQCEKIVEKYGFTHLSTGDLLRAEVASGSERGK--QLQAIMESGDLVPLDTVLDLLKDAMVAaLGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 188 EEGIVIDGFPRDVAQALSFEDQICTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQE 267
Cdd:TIGR01360 82 SKGFLIDGYPREVKQGEEFERRIGPPTLVLYFDCSEDTMVKRLLKRAETSGRVDDNEKTIKKRLETYYKATEPVIAYYET 161
|
170 180
....*....|....*....|....*
gi 530362359 268 KGLIMTFDADRDEDEVFYDISMAVD 292
Cdd:TIGR01360 162 KGKLRKINAEGTVDDVFLQVCTAID 186
|
|
| Adk |
COG0563 |
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ... |
353-534 |
1.77e-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: 166.84 E-value: 1.77e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 353 KIIFIiGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMvASLGDTR 432
Cdd:COG0563 2 RIILL-GPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAVKAGTELGKKAKEYMDAGELVPDEIVIGLVKERL-AQPDCAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 433 GFLIDGYPREVKQGE-------EFGRRIgdpQLVICMDCSADTMTNRLLQR-----------SRSSLPV----------- 483
Cdd:COG0563 80 GFILDGFPRTVAQAEaldellaELGIKL---DAVIELDVDDEELVERLSGRrvcpncgatyhVKFNPPKvegvcdkcgge 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 530362359 484 -----DDTTKTIAKRLEAYYRASIPVIAYYETKTQLHKINAEGTPEDVFLQLCTAI 534
Cdd:COG0563 157 lvqraDDNEETVRKRLEVYHEQTAPLIDYYRKKGKLVEIDGEGSIEEVTADILAIL 212
|
|
| ADK |
pfam00406 |
Adenylate kinase; |
357-511 |
2.95e-48 |
|
Adenylate kinase;
Pssm-ID: 395329 [Multi-domain] Cd Length: 184 Bit Score: 165.56 E-value: 2.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 357 IIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVAsLGDTRGFLI 436
Cdd:pfam00406 1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGKEAKEYMDKGELVPDEVVVGLVKERLEQ-NDCKNGFLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 437 DGYPREVKQGEEFGR---RIGDPQLVICMDCSADTMTNRLLQR---------------------------SRSSLPVDDT 486
Cdd:pfam00406 80 DGFPRTVPQAEALEElleRGIKLDYVIEFDVPDEVLVERLTGRrihpnsgrsyhlefnppkvpgkddvtgEPLVQRSDDN 159
|
170 180
....*....|....*....|....*
gi 530362359 487 TKTIAKRLEAYYRASIPVIAYYETK 511
Cdd:pfam00406 160 EETVKKRLETYHKQTKPLIDYYKKK 184
|
|
| PLN02200 |
PLN02200 |
adenylate kinase family protein |
354-530 |
3.59e-48 |
|
adenylate kinase family protein
Pssm-ID: 215125 [Multi-domain] Cd Length: 234 Bit Score: 166.99 E-value: 3.59e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 354 IIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASlgDTRG 433
Cdd:PLN02200 45 ITFVLGGPGSGKGTQCEKIVETFGFKHLSAGDLLRREIASNSEHGAMILNTIKEGKIVPSEVTVKLIQKEMESS--DNNK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 434 FLIDGYPREVKQGEEFGRRIG-DPQLVICMDCSADTMTNRLLQRSRSSlpVDDTTKTIAKRLEAYYRASIPVIAYYETKT 512
Cdd:PLN02200 123 FLIDGFPRTEENRIAFERIIGaEPNVVLFFDCPEEEMVKRVLNRNQGR--VDDNIDTIKKRLKVFNALNLPVIDYYSKKG 200
|
170
....*....|....*...
gi 530362359 513 QLHKINAEGTPEDVFLQL 530
Cdd:PLN02200 201 KLYTINAVGTVDEIFEQV 218
|
|
| adk |
PRK00279 |
adenylate kinase; Reviewed |
355-537 |
8.19e-45 |
|
adenylate kinase; Reviewed
Pssm-ID: 234711 [Multi-domain] Cd Length: 215 Bit Score: 157.23 E-value: 8.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 355 IFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMvASLGDTRGF 434
Cdd:PRK00279 3 LILLGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAGTELGKEAKSYMDAGELVPDEIVIGLVKERL-AQPDCKNGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 435 LIDGYPREVKQGEEFGRRIGDPQL----VICMDCSADTMTNRLLQRS--RSSLPV------------------------- 483
Cdd:PRK00279 82 LLDGFPRTIPQAEALDEMLKELGIkldaVIEIDVPDEELVERLSGRRicPACGRTyhvkfnppkvegkcdvcgeeliqra 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530362359 484 DDTTKTIAKRLEAYYRASIPVIAYYETKTQLHKINAEGTPEDVFLQLCTAIDSI 537
Cdd:PRK00279 162 DDNEETVRKRLEVYHKQTAPLIDYYKKKGKLKKIDGTGSIDEVFADILKALGKL 215
|
|
| adk |
TIGR01351 |
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ... |
353-535 |
1.90e-42 |
|
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: 150.85 E-value: 1.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 353 KIIFIiGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASLGDTR 432
Cdd:TIGR01351 1 RLVLL-GPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGKKAKEYMEKGELVPDEIVNQLVKERLTQNDDNEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 433 GFLIDGYPREVKQGEEF--------------------------GRRI------------GDPQLVICMDCSADtmtnRLL 474
Cdd:TIGR01351 80 GFILDGFPRTLSQAEALdalleepidavieldvpdeelverlsGRRIcpscgrvyhlkfNPPKVPGCDDCTGE----LLV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530362359 475 QRSrsslpvDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHKINAEGTPEDVFLQLCTAID 535
Cdd:TIGR01351 156 QRE------DDTEEVVKKRLEVYKEQTEPLIDYYKKRGILVQIDGNGPIDEVWKRILEALK 210
|
|
| UMP_CMP_kin_fam |
TIGR01359 |
UMP-CMP kinase family; This subfamily of the adenylate kinase superfamily contains examples of ... |
110-287 |
8.48e-39 |
|
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: 140.20 E-value: 8.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 110 IILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwSLIAKIITTGELAPQETTITEIKQKLMQIPDEE 189
Cdd:TIGR01359 1 VVFVLGGPGSGKGTQCAKIVENFGFTHLSAGDLLRAEIKREGSENG-SLIESYIKEGKIVPSEVTVELLKKAIQEDGSSK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 190 GIVIDGFPRDVAQALSFEDQICT---PDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQ 266
Cdd:TIGR01359 80 KFLIDGFPRNEENLEAWEKLMDNkvnFKFVLFFDCPEETMIKRLLKRGQTSGRVDDNIETLKKRFRTYNEETLPIIEHFE 159
|
170 180
....*....|....*....|.
gi 530362359 267 EKGLIMTFDADRDEDEVFYDI 287
Cdd:TIGR01359 160 NKGKVKEINAEGSVEEVFEDV 180
|
|
| PLN02200 |
PLN02200 |
adenylate kinase family protein |
72-284 |
1.08e-38 |
|
adenylate kinase family protein
Pssm-ID: 215125 [Multi-domain] Cd Length: 234 Bit Score: 141.57 E-value: 1.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 72 GGQSRRSFlrnesDTDLSETAElieeyEVFDPTRPRPKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTS 151
Cdd:PLN02200 17 GLKIWESF-----STEIITLEE-----RGSSSKEKTPFITFVLGGPGSGKGTQCEKIVETFGFKHLSAGDLLRREIASNS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 152 SNrkWSLIAKIITTGELAPQETTITEIKQKlMQIPDEEGIVIDGFPRDVAQALSFEDQI-CTPDLVVFLACANQRLKERL 230
Cdd:PLN02200 87 EH--GAMILNTIKEGKIVPSEVTVKLIQKE-MESSDNNKFLIDGFPRTEENRIAFERIIgAEPNVVLFFDCPEEEMVKRV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530362359 231 LKRaeQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVF 284
Cdd:PLN02200 164 LNR--NQGRVDDNIDTIKKRLKVFNALNLPVIDYYSKKGKLYTINAVGTVDEIF 215
|
|
| Adk |
COG0563 |
Adenylate kinase or related kinase [Nucleotide transport and metabolism]; Adenylate kinase or ... |
109-287 |
2.02e-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: 137.18 E-value: 2.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 109 KIILvIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAK-IITTGELAPQETTITEIKQKLMQIPD 187
Cdd:COG0563 2 RIIL-LGPPGAGKGTQAKRLAEKYGIPHISTGDMLRAAV---KAGTELGKKAKeYMDAGELVPDEIVIGLVKERLAQPDC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 188 EEGIVIDGFPRDVAQALSFEDQIC----TPDLVVFLACANQRLKERLLKRA---------------------------EQ 236
Cdd:COG0563 78 ANGFILDGFPRTVAQAEALDELLAelgiKLDAVIELDVDDEELVERLSGRRvcpncgatyhvkfnppkvegvcdkcggEL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530362359 237 QGRPDDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDI 287
Cdd:COG0563 158 VQRADDNEETVRKRLEVYHEQTAPLIDYYRKKGKLVEIDGEGSIEEVTADI 208
|
|
| adk |
TIGR01351 |
adenylate kinase; Adenylate kinase (EC 2.7.4.3) converts ATP + AMP to ADP + ADP, that is, uses ... |
111-292 |
2.39e-36 |
|
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: 134.28 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 111 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwsLIAKIITTGELAPQETTITEIKQKLMQIPDEE- 189
Cdd:TIGR01351 2 LVLLGPPGSGKGTQAKRIAEKYGLPHISTGDLLRAEIKAGTPLGK--KAKEYMEKGELVPDEIVNQLVKERLTQNDDNEn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 190 GIVIDGFPRDVAQALSFEDQIC-TPDLVVFLACANQRLKERLLKR---------------------------AEQQGRPD 241
Cdd:TIGR01351 80 GFILDGFPRTLSQAEALDALLEePIDAVIELDVPDEELVERLSGRricpscgrvyhlkfnppkvpgcddctgELLVQRED 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 530362359 242 DNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDISMAVD 292
Cdd:TIGR01351 160 DTEEVVKKRLEVYKEQTEPLIDYYKKRGILVQIDGNGPIDEVWKRILEALK 210
|
|
| ADK |
pfam00406 |
Adenylate kinase; |
113-268 |
9.58e-36 |
|
Adenylate kinase;
Pssm-ID: 395329 [Multi-domain] Cd Length: 184 Bit Score: 131.66 E-value: 9.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 113 VIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwsLIAKIITTGELAPQETTITEIKQKLMQIPDEEGIV 192
Cdd:pfam00406 1 LLGPPGAGKGTQAEKIVQKYGLPHLSTGDLLRAEIKSGTELGK--EAKEYMDKGELVPDEVVVGLVKERLEQNDCKNGFL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 193 IDGFPRDVAQALSFED---QICTPDLVVFLACANQRLKERLLKRAEQQ---------------------------GRPDD 242
Cdd:pfam00406 79 LDGFPRTVPQAEALEElleRGIKLDYVIEFDVPDEVLVERLTGRRIHPnsgrsyhlefnppkvpgkddvtgeplvQRSDD 158
|
170 180
....*....|....*....|....*.
gi 530362359 243 NVKATQRRLMNFKQNAAPLVKYFQEK 268
Cdd:pfam00406 159 NEETVKKRLETYHKQTKPLIDYYKKK 184
|
|
| adk |
PRK00279 |
adenylate kinase; Reviewed |
111-294 |
1.23e-34 |
|
adenylate kinase; Reviewed
Pssm-ID: 234711 [Multi-domain] Cd Length: 215 Bit Score: 129.88 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 111 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwsLIAKIITTGELAPQETTITEIKQKLMQIPDEEG 190
Cdd:PRK00279 3 LILLGPPGAGKGTQAKFIAEKYGIPHISTGDMLRAAVKAGTELGK--EAKSYMDAGELVPDEIVIGLVKERLAQPDCKNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 191 IVIDGFPRDVAQALSFEDQIC----TPDLVVFLACANQRLKERLLKRA---------------------------EQQGR 239
Cdd:PRK00279 81 FLLDGFPRTIPQAEALDEMLKelgiKLDAVIEIDVPDEELVERLSGRRicpacgrtyhvkfnppkvegkcdvcgeELIQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530362359 240 PDDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDISMAVDNK 294
Cdd:PRK00279 161 ADDNEETVRKRLEVYHKQTAPLIDYYKKKGKLKKIDGTGSIDEVFADILKALGKL 215
|
|
| PRK14527 |
PRK14527 |
adenylate kinase; Provisional |
351-527 |
5.17e-34 |
|
adenylate kinase; Provisional
Pssm-ID: 237745 [Multi-domain] Cd Length: 191 Bit Score: 127.21 E-value: 5.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 351 KCKIIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAmVASLGD 430
Cdd:PRK14527 5 KNKVVIFLGPPGAGKGTQAERLAQELGLKKLSTGDILRDHVARGTELGQRAKPIMEAGDLVPDELILALIRDE-LAGMEP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 431 TRgFLIDGYPREVKQGEEFGRRIGDPQL----VICMDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIA 506
Cdd:PRK14527 84 VR-VIFDGFPRTLAQAEALDRLLEELGArllaVVLLEVPDEELIRRIVERARQEGRSDDNEETVRRRQQVYREQTQPLVD 162
|
170 180
....*....|....*....|.
gi 530362359 507 YYETKTQLHKINAEGTPEDVF 527
Cdd:PRK14527 163 YYEARGHLKRVDGLGTPDEVY 183
|
|
| PRK14531 |
PRK14531 |
adenylate kinase; Provisional |
351-535 |
1.20e-32 |
|
adenylate kinase; Provisional
Pssm-ID: 172997 [Multi-domain] Cd Length: 183 Bit Score: 123.38 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 351 KCKIIFIiGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASLGD 430
Cdd:PRK14531 2 KQRLLFL-GPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVAAGSALGQEAEAVMNRGELVSDALVLAIVESQLKALNSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 431 trGFLIDGYPREVKQGEEFGRRIGD---P-QLVICMDCSADTMTNRLLQRSRSslpvDDTTKTIAKRLEAYYRASIPVIA 506
Cdd:PRK14531 81 --GWLLDGFPRTVAQAEALEPLLEElkqPiEAVVLLELDDAVLIERLLARGRA----DDNEAVIRNRLEVYREKTAPLID 154
|
170 180
....*....|....*....|....*....
gi 530362359 507 YYETKTQLHKINAEGTPEDVFLQLCTAID 535
Cdd:PRK14531 155 HYRQRGLLQSVEAQGSIEAITERIEKVLA 183
|
|
| PRK14532 |
PRK14532 |
adenylate kinase; Provisional |
355-536 |
3.55e-31 |
|
adenylate kinase; Provisional
Pssm-ID: 184729 [Multi-domain] Cd Length: 188 Bit Score: 119.54 E-value: 3.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 355 IFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASLGdTRGF 434
Cdd:PRK14532 3 LILFGPPAAGKGTQAKRLVEERGMVQLSTGDMLRAAIASGSELGQRVKGIMDRGELVSDEIVIALIEERLPEAEA-AGGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 435 LIDGYPREVKQGEEF-------GRRIgdpQLVICMDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIAY 507
Cdd:PRK14532 82 IFDGFPRTVAQAEALdkmlasrGQKI---DVVIRLKVDDEALIERIVKRFEEQGRPDDNPEVFVTRLDAYNAQTAPLLPY 158
|
170 180
....*....|....*....|....*....
gi 530362359 508 YETKTQLHKINAEGTPEDVflqlCTAIDS 536
Cdd:PRK14532 159 YAGQGKLTEVDGMGSIEAV----AASIDA 183
|
|
| adk |
PRK02496 |
adenylate kinase; Provisional |
353-534 |
4.89e-31 |
|
adenylate kinase; Provisional
Pssm-ID: 179433 [Multi-domain] Cd Length: 184 Bit Score: 118.70 E-value: 4.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 353 KIIFIiGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASlgDTR 432
Cdd:PRK02496 3 RLIFL-GPPGAGKGTQAVVLAEHLHIPHISTGDILRQAIKEQTPLGIKAQGYMDKGELVPDQLVLDLVQERLQQP--DAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 433 -GFLIDGYPREVKQG---EEFGRRIGDP-QLVICMDCSADTMTNRLLQRSRSslpvDDTTKTIAKRLEAYYRASIPVIAY 507
Cdd:PRK02496 80 nGWILDGFPRKVTQAaflDELLQEIGQSgERVVNLDVPDDVVVERLLARGRK----DDTEEVIRRRLEVYREQTAPLIDY 155
|
170 180
....*....|....*....|....*..
gi 530362359 508 YETKTQLHKINAEGTPEDVFLQLCTAI 534
Cdd:PRK02496 156 YRDRQKLLTIDGNQSVEAVTTELKAAL 182
|
|
| PRK14532 |
PRK14532 |
adenylate kinase; Provisional |
111-291 |
1.64e-30 |
|
adenylate kinase; Provisional
Pssm-ID: 184729 [Multi-domain] Cd Length: 188 Bit Score: 117.62 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 111 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSS-NRKwslIAKIITTGELAPQETTITEIKQKLMQIPDEE 189
Cdd:PRK14532 3 LILFGPPAAGKGTQAKRLVEERGMVQLSTGDMLRAAIASGSElGQR---VKGIMDRGELVSDEIVIALIEERLPEAEAAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 190 GIVIDGFPRDVAQALSFEDQICTP----DLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKYF 265
Cdd:PRK14532 80 GAIFDGFPRTVAQAEALDKMLASRgqkiDVVIRLKVDDEALIERIVKRFEEQGRPDDNPEVFVTRLDAYNAQTAPLLPYY 159
|
170 180
....*....|....*....|....*.
gi 530362359 266 QEKGLIMTFDADRDEDEVFYDISMAV 291
Cdd:PRK14532 160 AGQGKLTEVDGMGSIEAVAASIDAAL 185
|
|
| AAA_17 |
pfam13207 |
AAA domain; |
359-490 |
1.92e-30 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 115.41 E-value: 1.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 359 GGPGSGKGTQCEKLVEKYGFTHLSTGELLREElASESERSKlIRDIMERGDLVPSGIVLELLKEAMvASLGDTRGFLIDG 438
Cdd:pfam13207 2 GVPGSGKTTQLKKLAEKLGFPHISAGDLLREE-AKERGLVE-DRDEMRKLPLEPQKELQKLAAERI-AEEAGEGGVIVDG 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 530362359 439 YPREVKQGEEFGR------RIGDPQLVICMDCSADTMTNRLLQRsRSSLPVDDTTKTI 490
Cdd:pfam13207 79 HPRIKTPAGYLPGlpvevlRELKPDAIILLEADPEEILERRLKD-RTRGRDDDSEEEI 135
|
|
| PRK14530 |
PRK14530 |
adenylate kinase; Provisional |
355-536 |
1.42e-29 |
|
adenylate kinase; Provisional
Pssm-ID: 237747 [Multi-domain] Cd Length: 215 Bit Score: 115.66 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 355 IFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLReelaseSERSKLIRDI----------MERGDLVPSGIVLELLKEAm 424
Cdd:PRK14530 6 ILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALR------ANKQMDISDMdteydtpgeyMDAGELVPDAVVNEIVEEA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 425 vasLGDTRGFLIDGYPREVKQGEEFGR----------RIGDPQLV-------ICMDCSA---------------DTMTNR 472
Cdd:PRK14530 79 ---LSDADGFVLDGYPRNLEQAEYLESitdldvvlylDVSEEELVdrltgrrVCPDCGAnyhvefnqpeeegvcDECGGE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530362359 473 LLQRSrsslpvDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHKINAEGTPEDVFLQLCTAIDS 536
Cdd:PRK14530 156 LIQRD------DDTEETVRERLDVFEENTEPVIEHYRDQGVLVEVDGEQTPDEVWADIQDAIDD 213
|
|
| PRK14527 |
PRK14527 |
adenylate kinase; Provisional |
104-291 |
3.65e-28 |
|
adenylate kinase; Provisional
Pssm-ID: 237745 [Multi-domain] Cd Length: 191 Bit Score: 111.04 E-value: 3.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 104 TRPRPKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAK-IITTGELAPQETTITEIKQKL 182
Cdd:PRK14527 2 TQTKNKVVIFLGPPGAGKGTQAERLAQELGLKKLSTGDILRDHV---ARGTELGQRAKpIMEAGDLVPDELILALIRDEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 183 MQIPDEEgIVIDGFPRDVAQA----LSFEDQICTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNA 258
Cdd:PRK14527 79 AGMEPVR-VIFDGFPRTLAQAealdRLLEELGARLLAVVLLEVPDEELIRRIVERARQEGRSDDNEETVRRRQQVYREQT 157
|
170 180 190
....*....|....*....|....*....|...
gi 530362359 259 APLVKYFQEKGLIMTFDADRDEDEVFYDISMAV 291
Cdd:PRK14527 158 QPLVDYYEARGHLKRVDGLGTPDEVYARILKAL 190
|
|
| adk |
PRK02496 |
adenylate kinase; Provisional |
111-291 |
3.89e-27 |
|
adenylate kinase; Provisional
Pssm-ID: 179433 [Multi-domain] Cd Length: 184 Bit Score: 107.91 E-value: 3.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 111 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAKI-ITTGELAPQETTITEIKQKLMQIPDEE 189
Cdd:PRK02496 4 LIFLGPPGAGKGTQAVVLAEHLHIPHISTGDILRQAI---KEQTPLGIKAQGyMDKGELVPDQLVLDLVQERLQQPDAAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 190 GIVIDGFPRDVAQAlSFEDQICTP-----DLVVFLACANQRLKERLLKRaeqqGRPDDNVKATQRRLMNFKQNAAPLVKY 264
Cdd:PRK02496 81 GWILDGFPRKVTQA-AFLDELLQEigqsgERVVNLDVPDDVVVERLLAR----GRKDDTEEVIRRRLEVYREQTAPLIDY 155
|
170 180
....*....|....*....|....*..
gi 530362359 265 FQEKGLIMTFDADRDEDEVFYDISMAV 291
Cdd:PRK02496 156 YRDRQKLLTIDGNQSVEAVTTELKAAL 182
|
|
| PRK14528 |
PRK14528 |
adenylate kinase; Provisional |
353-526 |
5.95e-26 |
|
adenylate kinase; Provisional
Pssm-ID: 172994 [Multi-domain] Cd Length: 186 Bit Score: 104.71 E-value: 5.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 353 KIIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASlGDTR 432
Cdd:PRK14528 2 KNIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMGIEAKRYMDAGDLVPDSVVIGIIKDRIREA-DCKN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 433 GFLIDGYPREVKQGEEFGRRIGDPQL----VICMDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIAYY 508
Cdd:PRK14528 81 GFLLDGFPRTVEQADALDALLKNEGKsidkAINLEVPDGELLKRLLGRAEIEGRADDNEATIKNRLDNYNKKTLPLLDFY 160
|
170
....*....|....*...
gi 530362359 509 ETKTQLHKINAEGTPEDV 526
Cdd:PRK14528 161 AAQKKLSQVNGVGSLEEV 178
|
|
| AAA_17 |
pfam13207 |
AAA domain; |
115-244 |
7.10e-26 |
|
AAA domain;
Pssm-ID: 463810 [Multi-domain] Cd Length: 136 Bit Score: 102.70 E-value: 7.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 115 GGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstsSNRKWSLIAKIITTGELAPQETTITEIKQKLMQIPDEEGIVID 194
Cdd:pfam13207 2 GVPGSGKTTQLKKLAEKLGFPHISAGDLLREEA----KERGLVEDRDEMRKLPLEPQKELQKLAAERIAEEAGEGGVIVD 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 530362359 195 GFPRDVAQALSFED------QICTPDLVVFLACANQRLKERLLKRAEqQGRPDDNV 244
Cdd:pfam13207 78 GHPRIKTPAGYLPGlpvevlRELKPDAIILLEADPEEILERRLKDRT-RGRDDDSE 132
|
|
| PRK14530 |
PRK14530 |
adenylate kinase; Provisional |
111-295 |
1.91e-24 |
|
adenylate kinase; Provisional
Pssm-ID: 237747 [Multi-domain] Cd Length: 215 Bit Score: 101.40 E-value: 1.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 111 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLR--KKIHSTSSNRKWSLIAKIITTGELAPQEtTITEIKQKlmQIPDE 188
Cdd:PRK14530 6 ILLLGAPGAGKGTQSSNLAEEFGVEHVTTGDALRanKQMDISDMDTEYDTPGEYMDAGELVPDA-VVNEIVEE--ALSDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 189 EGIVIDGFPRDVAQALSFEDqICTPDLVVFLACANQRLKERLLKR----------------AEQQG-----------RPD 241
Cdd:PRK14530 83 DGFVLDGYPRNLEQAEYLES-ITDLDVVLYLDVSEEELVDRLTGRrvcpdcganyhvefnqPEEEGvcdecggeliqRDD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 530362359 242 DNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDISMAVDNKL 295
Cdd:PRK14530 162 DTEETVRERLDVFEENTEPVIEHYRDQGVLVEVDGEQTPDEVWADIQDAIDDAT 215
|
|
| PLN02842 |
PLN02842 |
nucleotide kinase |
357-537 |
8.85e-24 |
|
nucleotide kinase
Pssm-ID: 178435 [Multi-domain] Cd Length: 505 Bit Score: 104.56 E-value: 8.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 357 IIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASLGDTRGFLI 436
Cdd:PLN02842 2 ISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKRAKEFMNSGRLVPDEIVIAMVTGRLSREDAKEKGWLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 437 DGYPREVKQGEEFGRRIGDPQLVICMDCSADTMTNRLLQR-----------------------SRSSLPVDDTTKTIAKR 493
Cdd:PLN02842 82 DGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRrldpvtgkiyhiknfppeseeikARLITRPDDTEEKVKAR 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530362359 494 LEAYYRASIPVIAYYETKtqLHKINAEGTPEDVFLQLCTAIDSI 537
Cdd:PLN02842 162 LQIYKKNAEAILSTYSDI--MVKIDGNRPKEVVFEEISSLLSQI 203
|
|
| PRK14531 |
PRK14531 |
adenylate kinase; Provisional |
111-276 |
1.36e-23 |
|
adenylate kinase; Provisional
Pssm-ID: 172997 [Multi-domain] Cd Length: 183 Bit Score: 97.96 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 111 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKWSliAKIITTGELAPQETTITEIKQKlMQIPDEEG 190
Cdd:PRK14531 5 LLFLGPPGAGKGTQAARLCAAHGLRHLSTGDLLRSEVAAGSALGQEA--EAVMNRGELVSDALVLAIVESQ-LKALNSGG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 191 IVIDGFPRDVAQALSFE---DQICTP-DLVVFLACANQRLKERLLKRaeqqGRPDDNVKATQRRLMNFKQNAAPLVKYFQ 266
Cdd:PRK14531 82 WLLDGFPRTVAQAEALEpllEELKQPiEAVVLLELDDAVLIERLLAR----GRADDNEAVIRNRLEVYREKTAPLIDHYR 157
|
170
....*....|
gi 530362359 267 EKGLIMTFDA 276
Cdd:PRK14531 158 QRGLLQSVEA 167
|
|
| PRK13808 |
PRK13808 |
adenylate kinase; Provisional |
355-526 |
4.22e-23 |
|
adenylate kinase; Provisional
Pssm-ID: 172341 [Multi-domain] Cd Length: 333 Bit Score: 100.35 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 355 IFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASlGDTRGF 434
Cdd:PRK13808 3 LILLGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAVAAGTPVGLKAKDIMASGGLVPDEVVVGIISDRIEQP-DAANGF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 435 LIDGYPREVKQGEEFGRRIGDPQL----VICMDCSADTMTNRLLQR-----SRSSLP-VDDTTKTIAKRLEAYYRASIPV 504
Cdd:PRK13808 82 ILDGFPRTVPQAEALDALLKDKQLkldaVVELRVNEGALLARVETRvaemrARGEEVrADDTPEVLAKRLASYRAQTEPL 161
|
170 180
....*....|....*....|..
gi 530362359 505 IAYYETKTQLHKINAEGTPEDV 526
Cdd:PRK13808 162 VHYYSEKRKLLTVDGMMTIDEV 183
|
|
| PRK13808 |
PRK13808 |
adenylate kinase; Provisional |
109-287 |
1.63e-22 |
|
adenylate kinase; Provisional
Pssm-ID: 172341 [Multi-domain] Cd Length: 333 Bit Score: 98.42 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 109 KIILvIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAK-IITTGELAPQETTITEIKQKLMQIPD 187
Cdd:PRK13808 2 RLIL-LGPPGAGKGTQAQRLVQQYGIVQLSTGDMLRAAV---AAGTPVGLKAKdIMASGGLVPDEVVVGIISDRIEQPDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 188 EEGIVIDGFPRDVAQALSFE----DQICTPDLVVFLACANQRLKERLLKR-AEQQG-----RPDDNVKATQRRLMNFKQN 257
Cdd:PRK13808 78 ANGFILDGFPRTVPQAEALDallkDKQLKLDAVVELRVNEGALLARVETRvAEMRArgeevRADDTPEVLAKRLASYRAQ 157
|
170 180 190
....*....|....*....|....*....|
gi 530362359 258 AAPLVKYFQEKGLIMTFDADRDEDEVFYDI 287
Cdd:PRK13808 158 TEPLVHYYSEKRKLLTVDGMMTIDEVTREI 187
|
|
| PLN02674 |
PLN02674 |
adenylate kinase |
353-526 |
3.74e-22 |
|
adenylate kinase
Pssm-ID: 178279 [Multi-domain] Cd Length: 244 Bit Score: 95.72 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 353 KIIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASlGDTR 432
Cdd:PLN02674 32 KRLILIGPPGSGKGTQSPIIKDEYCLCHLATGDMLRAAVAAKTPLGIKAKEAMDKGELVSDDLVVGIIDEAMKKP-SCQK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 433 GFLIDGYPREVKQGEEF-------GRRIgDPQLVICMDCS--ADTMTNR-----------------------------LL 474
Cdd:PLN02674 111 GFILDGFPRTVVQAQKLdemlakqGAKI-DKVLNFAIDDAilEERITGRwihpssgrtyhtkfappkvpgvddvtgepLI 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530362359 475 QRSrsslpvDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHKINAEGTPEDV 526
Cdd:PLN02674 190 QRK------DDTAAVLKSRLEAFHKQTEPVIDYYAKKGVVANLHAEKPPKEV 235
|
|
| PRK14528 |
PRK14528 |
adenylate kinase; Provisional |
109-271 |
4.55e-22 |
|
adenylate kinase; Provisional
Pssm-ID: 172994 [Multi-domain] Cd Length: 186 Bit Score: 93.54 E-value: 4.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 109 KIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKWSliAKIITTGELAPQETTITEIKQKLMQIPDE 188
Cdd:PRK14528 2 KNIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMGIEA--KRYMDAGDLVPDSVVIGIIKDRIREADCK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 189 EGIVIDGFPRDVAQALSFEDQI----CTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKY 264
Cdd:PRK14528 80 NGFLLDGFPRTVEQADALDALLknegKSIDKAINLEVPDGELLKRLLGRAEIEGRADDNEATIKNRLDNYNKKTLPLLDF 159
|
....*..
gi 530362359 265 FQEKGLI 271
Cdd:PRK14528 160 YAAQKKL 166
|
|
| PLN02459 |
PLN02459 |
probable adenylate kinase |
358-524 |
1.15e-20 |
|
probable adenylate kinase
Pssm-ID: 215253 [Multi-domain] Cd Length: 261 Bit Score: 91.83 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 358 IGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASLGD-TRGFLI 436
Cdd:PLN02459 35 LGCPGVGKGTYASRLSKLLGVPHIATGDLVREEIKSSGPLGAQLKEIVNQGKLVPDEIIFSLLSKRLEAGEEEgESGFIL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 437 DGYPREVKQGEEF------------------------GRRI----GDPQLVICMDCSADTMTNRLLQRSRSSLP------ 482
Cdd:PLN02459 115 DGFPRTVRQAEILegvtdidlvvnlklreevlvekclGRRIcsecGKNFNVADIDLKGEDGRPGIVMPPLLPPPecaskl 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530362359 483 ---VDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHKIN-AEGTPE 524
Cdd:PLN02459 195 itrADDTEEVVKARLRVYKEESQPVEDFYRKRGKLLEFElPGGIPE 240
|
|
| DD_AK5 |
cd22978 |
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 5 (AK5) and similar ... |
3-46 |
1.18e-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: 84.89 E-value: 1.18e-20
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 530362359 3 TNDAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVK 46
Cdd:cd22978 1 SEDAKDYLSRKEIPQLFESLMTGLMYNRPDDPIEFLEDCLEKIR 44
|
|
| PLN02842 |
PLN02842 |
nucleotide kinase |
112-288 |
3.09e-20 |
|
nucleotide kinase
Pssm-ID: 178435 [Multi-domain] Cd Length: 505 Bit Score: 93.77 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 112 LVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKWSliAKIITTGELAPQETTITEIKQKLmQIPD--EE 189
Cdd:PLN02842 1 MISGAPASGKGTQCELIVHKFGLVHISTGDLLRAEVSAGTDIGKRA--KEFMNSGRLVPDEIVIAMVTGRL-SREDakEK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 190 GIVIDGFPRDVAQALSFEDQICTPDLVVFLACANQRLKERLLKR-----------------------AEQQGRPDDNVKA 246
Cdd:PLN02842 78 GWLLDGYPRSFAQAQSLEKLKIRPDIFILLDVPDEILIDRCVGRrldpvtgkiyhiknfppeseeikARLITRPDDTEEK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530362359 247 TQRRLMNFKQNAAPLVKYFQEkgLIMTFDADRDEDEVFYDIS 288
Cdd:PLN02842 158 VKARLQIYKKNAEAILSTYSD--IMVKIDGNRPKEVVFEEIS 197
|
|
| PTZ00088 |
PTZ00088 |
adenylate kinase 1; Provisional |
346-509 |
1.00e-19 |
|
adenylate kinase 1; Provisional
Pssm-ID: 240262 [Multi-domain] Cd Length: 229 Bit Score: 88.32 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 346 MEDLRKCKIIFIiGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMV 425
Cdd:PTZ00088 1 MKLKGPLKIVLF-GAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGKEIQKVVTSGNLVPDNLVIAIVKDEIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 426 ASLGDT-RGFLIDGYPREVKQGEEFGrRIGDPQLV------------------ICMDCSADTMTNRLLQRSRSSLPV--- 483
Cdd:PTZ00088 80 KVTDDCfKGFILDGFPRNLKQCKELG-KITNIDLFvniylprnilikkllgrrICNTCNRNFNIAHIRSDPYDMPPIlpp 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530362359 484 ----------------DDTTKTIAKRLEAYYRASIPVIAYYE 509
Cdd:PTZ00088 159 adcegckgnpklqkrsDDTEEIVAHRLNTYESTNSPIIQFFK 200
|
|
| PRK14526 |
PRK14526 |
adenylate kinase; Provisional |
353-526 |
4.45e-18 |
|
adenylate kinase; Provisional
Pssm-ID: 172992 [Multi-domain] Cd Length: 211 Bit Score: 82.98 E-value: 4.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 353 KIIFIiGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLkEAMVASLGDTR 432
Cdd:PRK14526 2 KLVFL-GPPGSGKGTIAKILSNELNYYHISTGDLFRENILNSTPLGKEIKQIVENGQLVPDSITIKIV-EDKINTIKNND 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 433 GFLIDGYPREVKQGEEFGRRIGDPQLV-----------------ICMDCS---------------ADTMTNRLLQRSrss 480
Cdd:PRK14526 80 NFILDGFPRNINQAKALDKFLPNIKIInflideellikrlsgrrICKSCNnifniytlptkekgiCDVCKGDLYQRK--- 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 530362359 481 lpvDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHKINAEGTPEDV 526
Cdd:PRK14526 157 ---DDKEESLKTRLQEYKLQTKPLIEFYSKCNRLNNIDASKDIDEV 199
|
|
| PTZ00088 |
PTZ00088 |
adenylate kinase 1; Provisional |
107-269 |
9.69e-15 |
|
adenylate kinase 1; Provisional
Pssm-ID: 240262 [Multi-domain] Cd Length: 229 Bit Score: 73.68 E-value: 9.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 107 RPKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKwsLIAKIITTGELAPQETTITEIKQKLMQIP 186
Cdd:PTZ00088 5 GPLKIVLFGAPGVGKGTFAEILSKKENLKHINMGNILREEIKAKTTIGK--EIQKVVTSGNLVPDNLVIAIVKDEIAKVT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 187 DE--EGIVIDGFPRDVAQALSFEdQICTPDLVVFLACANQRLKERLLKR------------------------------- 233
Cdd:PTZ00088 83 DDcfKGFILDGFPRNLKQCKELG-KITNIDLFVNIYLPRNILIKKLLGRricntcnrnfniahirsdpydmppilppadc 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 530362359 234 ------AEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQEKG 269
Cdd:PTZ00088 162 egckgnPKLQKRSDDTEEIVAHRLNTYESTNSPIIQFFKNEN 203
|
|
| PRK14526 |
PRK14526 |
adenylate kinase; Provisional |
111-283 |
6.66e-14 |
|
adenylate kinase; Provisional
Pssm-ID: 172992 [Multi-domain] Cd Length: 211 Bit Score: 70.65 E-value: 6.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 111 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKWslIAKIITTGELAPQETTITEIKQKLMQIPDEEG 190
Cdd:PRK14526 3 LVFLGPPGSGKGTIAKILSNELNYYHISTGDLFRENILNSTPLGKE--IKQIVENGQLVPDSITIKIVEDKINTIKNNDN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 191 IVIDGFPRDVAQALSFEDQICTPDLVVFL---ACANQRLKERLLKRA------------EQQG-----------RPDDNV 244
Cdd:PRK14526 81 FILDGFPRNINQAKALDKFLPNIKIINFLideELLIKRLSGRRICKScnnifniytlptKEKGicdvckgdlyqRKDDKE 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 530362359 245 KATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEV 283
Cdd:PRK14526 161 ESLKTRLQEYKLQTKPLIEFYSKCNRLNNIDASKDIDEV 199
|
|
| PRK14529 |
PRK14529 |
adenylate kinase; Provisional |
355-447 |
1.05e-13 |
|
adenylate kinase; Provisional
Pssm-ID: 237746 [Multi-domain] Cd Length: 223 Bit Score: 70.52 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 355 IFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGI----VLELLKEAmvaslgD 430
Cdd:PRK14529 3 ILIFGPNGSGKGTQGALVKKKYDLAHIESGAIFREHIGGGTELGKKAKEYIDRGDLVPDDItipmILETLKQD------G 76
|
90
....*....|....*..
gi 530362359 431 TRGFLIDGYPREVKQGE 447
Cdd:PRK14529 77 KNGWLLDGFPRNKVQAE 93
|
|
| PLN02674 |
PLN02674 |
adenylate kinase |
104-291 |
1.26e-13 |
|
adenylate kinase
Pssm-ID: 178279 [Multi-domain] Cd Length: 244 Bit Score: 70.68 E-value: 1.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 104 TRPRPKIILvIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAK-IITTGELAPQETTITEIKQKL 182
Cdd:PLN02674 28 SKPDKRLIL-IGPPGSGKGTQSPIIKDEYCLCHLATGDMLRAAV---AAKTPLGIKAKeAMDKGELVSDDLVVGIIDEAM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 183 MQIPDEEGIVIDGFPRDVAQALSFED----QICTPDLVVFLACANQRLKERLLKR----------------------AEQ 236
Cdd:PLN02674 104 KKPSCQKGFILDGFPRTVVQAQKLDEmlakQGAKIDKVLNFAIDDAILEERITGRwihpssgrtyhtkfappkvpgvDDV 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 237 QGRP-----DDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDISMAV 291
Cdd:PLN02674 184 TGEPliqrkDDTAAVLKSRLEAFHKQTEPVIDYYAKKGVVANLHAEKPPKEVTAEVQKAL 243
|
|
| PLN02459 |
PLN02459 |
probable adenylate kinase |
84-275 |
6.22e-13 |
|
probable adenylate kinase
Pssm-ID: 215253 [Multi-domain] Cd Length: 261 Bit Score: 69.11 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 84 SDTDLSETAELIEEYEV-FDPTRPRPKII--LVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSnrKWSLIA 160
Cdd:PLN02459 2 SERDAKSTSALADDLASaCDRSLAKGRNVnwVFLGCPGVGKGTYASRLSKLLGVPHIATGDLVREEIKSSGP--LGAQLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 161 KIITTGELAPQETTITEIKQKLMQIPD--EEGIVIDGFPRDVAQALSFEDqICTPDLVVFLACANQRLKERLLKR----- 233
Cdd:PLN02459 80 EIVNQGKLVPDEIIFSLLSKRLEAGEEegESGFILDGFPRTVRQAEILEG-VTDIDLVVNLKLREEVLVEKCLGRricse 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530362359 234 ------------AEQQGRP---------------------DDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFD 275
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 |
4.58e-12 |
|
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: 60.51 E-value: 4.58e-12
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530362359 5 DAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQK 44
Cdd:cd22961 3 DAEEYLEKHKIPELFESLLTALLIEKPEDPIEFLIDKLQQ 42
|
|
| PRK14529 |
PRK14529 |
adenylate kinase; Provisional |
111-203 |
5.50e-10 |
|
adenylate kinase; Provisional
Pssm-ID: 237746 [Multi-domain] Cd Length: 223 Bit Score: 59.35 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 111 ILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIhstSSNRKWSLIAK-IITTGELAPQETTITEIKQKLmQIPDEE 189
Cdd:PRK14529 3 ILIFGPNGSGKGTQGALVKKKYDLAHIESGAIFREHI---GGGTELGKKAKeYIDRGDLVPDDITIPMILETL-KQDGKN 78
|
90
....*....|....
gi 530362359 190 GIVIDGFPRDVAQA 203
Cdd:PRK14529 79 GWLLDGFPRNKVQA 92
|
|
| DD_FBXL13 |
cd22977 |
dimerization/docking (D/D) domain found in F-box/LRR-repeat protein 13 (FBXL13) and similar ... |
7-45 |
2.72e-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: 47.16 E-value: 2.72e-07
10 20 30
....*....|....*....|....*....|....*....
gi 530362359 7 KEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKV 45
Cdd:cd22977 5 RKYLRKHKLPDVYEALLTGLAVMCPEDPLRFIEEKLKEL 43
|
|
| DD_EFCAB10 |
cd22976 |
dimerization/docking (D/D) domain found in EF-hand calcium-binding domain-containing protein ... |
5-47 |
9.18e-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: 45.56 E-value: 9.18e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 530362359 5 DAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKE 47
Cdd:cd22976 3 EAEEYLEKHKIPELFENLTSLLLYHRPEDPKAFLIEQLEKLKE 45
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
354-418 |
1.24e-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: 48.25 E-value: 1.24e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530362359 354 IIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREE---LASESERSKLIRDIM---ERGDLVPSGIVLE 418
Cdd:cd02020 1 IIAIDGPAGSGKSTVAKLLAKKLGLPYLDTGGIRTEEvgkLASEVAAIPEVRKALderQRELAKKPGIVLE 71
|
|
| DD_AK8 |
cd22979 |
dimerization/docking (D/D) domain found in adenylate kinase isoenzyme 8 (AK8) and similar ... |
8-44 |
4.86e-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: 43.61 E-value: 4.86e-06
10 20 30
....*....|....*....|....*....|....*..
gi 530362359 8 EYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQK 44
Cdd:cd22979 8 AYAEKHRIFELFQDLLKQLLIHKPEDPLQFLIDYLQK 44
|
|
| DD_TbAK-like |
cd22981 |
dimerization/docking (D/D) domain found in Trypanosoma brucei adenylate kinase (AK) and ... |
5-44 |
1.23e-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: 42.40 E-value: 1.23e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 530362359 5 DAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQK 44
Cdd:cd22981 4 DAQKYLKEKNIPQLFEFLLRHLLLDKPENPLEYLHDLLER 43
|
|
| CMPK |
cd02020 |
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ... |
111-142 |
2.17e-05 |
|
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: 44.40 E-value: 2.17e-05
10 20 30
....*....|....*....|....*....|...
gi 530362359 111 ILVIGGP-GSGKGTQSLKIAERYGFQYISVGEL 142
Cdd:cd02020 1 IIAIDGPaGSGKSTVAKLLAKKLGLPYLDTGGI 33
|
|
| COG0645 |
COG0645 |
Predicted kinase, contains AAA domain [General function prediction only]; |
354-497 |
2.51e-05 |
|
Predicted kinase, contains AAA domain [General function prediction only];
Pssm-ID: 440410 [Multi-domain] Cd Length: 164 Bit Score: 44.52 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 354 IIFIIGGPGSGKGTQCEKLVEKYGFTHLST----GELLREELASE---SERSKLIRDIMERgdlvpsgIVLELLKEamva 426
Cdd:COG0645 1 LILVCGLPGSGKSTLARALAERLGAVRLRSdvvrKRLFGAGLAPLersPEATARTYARLLA-------LARELLAA---- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530362359 427 slgdtrGF--LIDG---YPREVKQGEEFGRRIGDPQLVICMDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAY 497
Cdd:COG0645 70 ------GRsvILDAtflRRAQREAFRALAEEAGAPFVLIWLDAPEEVLRERLEARNAEGGDSDATWEVLERQLAFE 139
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
354-394 |
3.09e-05 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 44.80 E-value: 3.09e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 530362359 354 IIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLReELASE 394
Cdd:PRK04182 2 IITISGPPGSGKTTVARLLAEKLGLKHVSAGEIFR-ELAKE 41
|
|
| PRK04182 |
PRK04182 |
cytidylate kinase; Provisional |
111-145 |
3.52e-05 |
|
cytidylate kinase; Provisional
Pssm-ID: 235244 [Multi-domain] Cd Length: 180 Bit Score: 44.41 E-value: 3.52e-05
10 20 30
....*....|....*....|....*....|....*.
gi 530362359 111 ILVIGG-PGSGKGTQSLKIAERYGFQYISVGELLRK 145
Cdd:PRK04182 2 IITISGpPGSGKTTVARLLAEKLGLKHVSAGEIFRE 37
|
|
| PRK01184 |
PRK01184 |
flagellar hook-basal body complex protein FliE; |
108-242 |
4.58e-05 |
|
flagellar hook-basal body complex protein FliE;
Pssm-ID: 234914 [Multi-domain] Cd Length: 184 Bit Score: 44.17 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 108 PKIILVIGGPGSGKGTQSlKIAERYGFQYISVGELLRKK-----IHSTSSNrkwslIAKIITT-----GELAPQETTITE 177
Cdd:PRK01184 1 MKIIGVVGMPGSGKGEFS-KIAREMGIPVVVMGDVIREEvkkrgLEPTDEN-----IGKVAIDlrkelGMDAVAKRTVPK 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530362359 178 IKQKLMQIpdeegIVIDGFpRDVAQALSFEDQI-CTPDLVVFLACANQRLkERLLKRaeqqGRPDD 242
Cdd:PRK01184 75 IREKGDEV-----VVIDGV-RGDAEVEYFRKEFpEDFILIAIHAPPEVRF-ERLKKR----GRSDD 129
|
|
| DD_CrRSP_unchar |
cd22964 |
dimerization/docking (D/D) domain of an uncharacterized subunit found in Chlamydomonas ... |
4-47 |
4.88e-05 |
|
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: 40.68 E-value: 4.88e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 530362359 4 NDAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKE 47
Cdd:cd22964 3 EEKKEYLQQKVINPILEQLVTDLLQEKPEDPVPFMIQWLRKKRS 46
|
|
| Pgk2 |
COG2074 |
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and ... |
105-255 |
9.61e-05 |
|
2-phosphoglycerate kinase/Mevalonate-3-phosphate 5-kinase [Carbohydrate transport and metabolism, Lipid transport and metabolism];
Pssm-ID: 441677 Cd Length: 207 Bit Score: 43.78 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 105 RPRPKIILVIGGPGSGKGTQSLKIAERYGFQYI----SVGELLRK--------KIHsTSSNRKW-SLIAKIITTGELAPQ 171
Cdd:COG2074 3 MKRPRIILIGGASGVGKSTIAAELARRLGIPRVistdSIREVMRPiiskelvpTLH-TSSYEAYkSLSEEEIIAGFLDQA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 172 ETTITEIKQklMQ---IPDEEGIVIDG---FPRDVAQALSFEDQICtpdLVVFLACANQRLKERLLKRAEQQGRpddnvK 245
Cdd:COG2074 82 EAVSPGIEA--VIeraLKEGESLVIEGvhlVPGFLAELKFNGGNVV---MLVLLVSDEELHRERFYSRARYTHA-----N 151
|
170
....*....|.
gi 530362359 246 ATQRRLM-NFK 255
Cdd:COG2074 152 RPGERYLdHFE 162
|
|
| AAA_18 |
pfam13238 |
AAA domain; |
111-248 |
2.43e-04 |
|
AAA domain;
Pssm-ID: 433052 [Multi-domain] Cd Length: 128 Bit Score: 41.26 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 111 ILVIGGPGSGKGTQSLKIAERYGFqYISVGELLRKKIHSTSSNRKWSLiAKIITTGELApqettitEIKQKLMQIPDEEG 190
Cdd:pfam13238 1 ILITGTPGVGKTTLAKELSKRLGF-GDNVRDLALENGLVLGDDPETRE-SKRLDEDKLD-------RLLDLLEENAALEE 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530362359 191 ---IVIDGFPrdvAQALSFEDqicTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQ 248
Cdd:pfam13238 72 ggnLIIDGHL---AELEPERA---KDLVGIVLRASPEELLERLEKRGYEEAKIKENEEAEI 126
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
354-404 |
3.87e-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: 38.86 E-value: 3.87e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 530362359 354 IIFIIGGPGSGKGTQCEKLVEKYG---FTHLSTGELLREELASESERSKLIRDI 404
Cdd:cd02019 1 IIAITGGSGSGKSTVAKKLAEQLGgrsVVVLDEIVILEGLYASYKSRDARIRDL 54
|
|
| PRK03839 |
PRK03839 |
putative kinase; Provisional |
110-332 |
6.12e-04 |
|
putative kinase; Provisional
Pssm-ID: 179660 Cd Length: 180 Bit Score: 40.86 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 110 IILVIGGPGSGKGTQSLKIAERYGFQYISVGEL-LRKKIHSTSSNrkwsliakiittgELapqETTITEIKQKLMQIPDE 188
Cdd:PRK03839 2 IIAITGTPGVGKTTVSKLLAEKLGYEYVDLTEFaLKKGIGEEKDD-------------EM---EIDFDKLAYFIEEEFKE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 189 EGIVIDGFprdvaqaLSfedQICTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKAtqrRLMNfkqnaAPLVKYFQEK 268
Cdd:PRK03839 66 KNVVLDGH-------LS---HLLPVDYVIVLRAHPKIIKERLKERGYSKKKILENVEA---ELVD-----VCLCEALEEK 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530362359 269 GLIMTFD-ADRDEDEVFYDISMAVDNKlfpnKEAAAGssdldpsmILDTGEIIDTGSDYEDQGDD 332
Cdd:PRK03839 128 EKVIEVDtTGKTPEEVVEEILELIKSG----KKRKVG--------IVDWSEVYDEIFPYLRLGID 180
|
|
| DD_VEST1 |
cd22980 |
dimerization/docking (D/D) domain found in protein VEST-1 and similar proteins; VEST-1 (also ... |
9-47 |
7.88e-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: 37.23 E-value: 7.88e-04
10 20 30
....*....|....*....|....*....|....*....
gi 530362359 9 YLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKE 47
Cdd:cd22980 7 YLEKHKIGALFEDLMAKLIRDTPDEPIPYLIKVLQKKAG 45
|
|
| PRK12337 |
PRK12337 |
2-phosphoglycerate kinase; Provisional |
76-202 |
3.16e-03 |
|
2-phosphoglycerate kinase; Provisional
Pssm-ID: 183452 [Multi-domain] Cd Length: 475 Bit Score: 40.14 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 76 RRSFLRNESDTDLSETA--ELIEEYEVFDPTR--PRPKIILVIGGPGSGKGTQSLKIAERYGFQYI----SVGELLRKKI 147
Cdd:PRK12337 219 RRDQLRRKVEALLLEEAgeEVARRYRLLRSIRrpPRPLHVLIGGVSGVGKSVLASALAYRLGITRIvstdAVREVLRAMV 298
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530362359 148 HS-------TSSNRKWsliakiitTGELAPQETTITEIKQKLmqipdeegiVIDGFPRDVAQ 202
Cdd:PRK12337 299 SKdllptlhASTFNAW--------RALLPPGEGLPAEPTRAE---------VLRGFRDQVQQ 343
|
|
| BREX_3_BrxF |
NF033453 |
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino ... |
109-163 |
6.11e-03 |
|
BREX-3 system P-loop-containing protein BrxF; This family of proteins that are about 150 amino acids in length includes BrxF from type 3 BREX (bacteriophage exclusion) systems. Most members have the P-loop motif GxxGxGKT, but the region is surprisingly poorly conserved in a sizable fraction of otherwise strongly similar proteins.
Pssm-ID: 468038 Cd Length: 149 Bit Score: 37.47 E-value: 6.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 530362359 109 KIILVIGGPGSGKgTQSL-KIAERYGFQYISVGELLRKKIHSTSSNRKWSLIAKII 163
Cdd:NF033453 17 KLILLVGPPGSGK-TALLrELAAKRGAPVINVNLELSRRLLELPEKQRALRAPRLL 71
|
|
| CmkB |
COG1102 |
Cytidylate kinase [Nucleotide transport and metabolism]; |
110-195 |
6.85e-03 |
|
Cytidylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 440719 [Multi-domain] Cd Length: 188 Bit Score: 37.88 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530362359 110 IILVIGG-PGSGKGTQSLKIAERYGFQYISvGELLRKkihsTSSNRKWSLI--------AKIITTGELAPQETTITEIKQ 180
Cdd:COG1102 1 MVITISRePGSGGTTIAKRLAEKLGLPLYD-GEILRE----AAKERGLSEEefekldekAPSLLYRDTAEEDEIDRALDK 75
|
90
....*....|....*
gi 530362359 181 KLMQIPDEEGIVIDG 195
Cdd:COG1102 76 VIRELARKGNCVIVG 90
|
|
| DD_TEX55 |
cd22975 |
dimerization/docking (D/D) domain found in testis-specific expressed protein 55 (TEX55) and ... |
6-47 |
7.06e-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: 34.85 E-value: 7.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 530362359 6 AKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKE 47
Cdd:cd22975 7 AVKYLEKHNILQLFQELTAGLVYERPDDPIQFMIDEIEKIIK 48
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
353-420 |
8.95e-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: 37.63 E-value: 8.95e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530362359 353 KIIFIIGGPGSGKGTQCEKLVE---KYGFTHLSTGELlreelaSESERSKLIRDIMERGDLVPSGIVLELL 420
Cdd:cd01672 1 MFIVFEGIDGAGKTTLIELLAErleARGYEVVLTREP------GGTPIGEAIRELLLDPEDEKMDPRAELL 65
|
|
| |
