|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
137-780 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1141.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 137 REFQRVIISGEEKCGVPFTDLLDAAKSVVRALFIREKYMalslqsFCPTTRRYLQQLaekpletrtyEQSPDTPVSADAP 216
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSV----------QGEDSTPKENDEP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 217 V-HPPALEQ-HPYEHCEPsamPGDLGLGLRMVRGVVHVYTRRDpdehCPEVELPYPDLQEFVADVNVLMALIINGPIKSF 294
Cdd:pfam19326 65 VfHPPPKKGeDPYELFNF---PPDLGYHLRMQDGVVHVYANKD----ALEDSLPYPDLRDFYTDLEHLLALIADGPIKTF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 295 CYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQ 374
Cdd:pfam19326 138 CHRRLQYLESKFNLHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKYL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 375 TLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNKISGKYFAHIIKEVMADLEESKY 454
Cdd:pfam19326 218 TLREVFESLKLTGYDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESKY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 455 QNAELRLSIYGRSRDEWDKLARWAVNHKVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPEL 534
Cdd:pfam19326 298 QMAEYRISIYGRSPDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPEL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 535 HLFLEHVDGFDSVDDESKPENHVFNlESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPI 614
Cdd:pfam19326 378 HVFLKRVIGFDSVDDESKPERRMFR-KSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGDI 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 615 HHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKE 694
Cdd:pfam19326 457 DHLVSAFLLAHGISHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTKE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 695 PLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 774
Cdd:pfam19326 537 PLMEEYSIAAQVWKLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELALI 616
|
....*.
gi 21311925 775 TQAVQS 780
Cdd:pfam19326 617 SDAVKS 622
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
275-771 |
0e+00 |
|
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at position 6 of the adenine nucleotide ring. AMPD is a diverse and highly regulated eukaryotic key enzyme of the adenylate catabolic pathway.
Pssm-ID: 238644 Cd Length: 496 Bit Score: 937.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 275 FVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFI 354
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 355 KRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNKIS 434
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 435 GKYFAHIIKEVMADLEESKYQNAELRLSIYGRSRDEWDKLARWAVNHKVHSPNVRWLVQVPRLFDVYRTKGQLANFQEML 514
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 515 ENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEnHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLR 594
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESKSE-RRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 595 RQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLS 674
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 675 RGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTN 754
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 21311925 755 VPDIRVGYRYETLCQEL 771
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
156-774 |
0e+00 |
|
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein involved in energy metabolism. Most members of the family have an additional, poorly alignable region of 150 amino acids or more N-terminal to the region included in the model.
Pssm-ID: 273618 [Multi-domain] Cd Length: 611 Bit Score: 908.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 156 DLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAeKPLETRTYEQSPDTpvsadapvHPPALEQHPYEHCEPSAM 235
Cdd:TIGR01429 2 DLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQG-YPESVPLEEGLPDF--------HPPPDPQEDPYCLDDDAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 236 PGDLGLGLRMVRGVVHVYTRRDPDEHCPEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEM 315
Cdd:TIGR01429 73 PIELGYLVRMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 316 KELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTL 395
Cdd:TIGR01429 153 SELKEQKSVPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 396 DVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNKISGKYFAHIIKEVMADLEESKYQNAELRLSIYGRSRDEWDKLA 475
Cdd:TIGR01429 233 DVHADRNTFHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 476 RWAVNHKVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEN 555
Cdd:TIGR01429 313 RWIIDHDVFSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 556 HVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRK 635
Cdd:TIGR01429 393 HMFSRKFPSPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 636 APVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMC 715
Cdd:TIGR01429 473 VPVLQYLYYLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMC 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 21311925 716 ELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 774
Cdd:TIGR01429 553 ELARNSVLQSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
172-774 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 772.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 172 EKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQSPDTPVSADAPVHPPALEQHPYehcepsampgdlglglRMVRGVVH 251
Cdd:PLN03055 8 EEEVCAMMQECLELRDKYLFREKLPPWRKGIFESSTSKPNPDPFRYEPEPPSQHVF----------------RMVDGVMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 252 VYTRRDPDEHCpeveLPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYN 331
Cdd:PLN03055 72 VYAPDDAKEEL----FPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAPHRDFYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 332 IRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFN 411
Cdd:PLN03055 148 VRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFHRFDKFN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 412 AKYNPIGESVLREIFIKTDNKISGKYFAHIIKEVMADLEESKYQNAELRLSIYGRSRDEWDKLARWAVNHKVHSPNVRWL 491
Cdd:PLN03055 228 LKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYSENVVWL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 492 VQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPlPEAWVEE 571
Cdd:PLN03055 308 IQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKPERRPTKHMQT-PEQWDIP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 572 DNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIA 651
Cdd:PLN03055 387 FNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 652 MSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKV 731
Cdd:PLN03055 467 MSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNSVLQSGFPHAS 546
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 21311925 732 KSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 774
Cdd:PLN03055 547 KKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYV 589
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
570-736 |
6.25e-16 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 79.74 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 570 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSA--FMLAENISHGL-LLRKAPVLQYLyylA 646
Cdd:COG1816 162 ERGFPPEKFAEAFARA---------REAGLH---LTAHAGEAGGPESIWEAldLLGAERIGHGVrAIEDPALVARL---A 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 647 --QIGIAMSPLSNNSL--FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSV 722
Cdd:COG1816 227 drGIPLEVCPTSNVQLgvVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAI 303
|
170
....*....|....
gi 21311925 723 LMSGFSHKVKSHWL 736
Cdd:COG1816 304 EASFLPEEEKAALL 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
137-780 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1141.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 137 REFQRVIISGEEKCGVPFTDLLDAAKSVVRALFIREKYMalslqsFCPTTRRYLQQLaekpletrtyEQSPDTPVSADAP 216
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSV----------QGEDSTPKENDEP 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 217 V-HPPALEQ-HPYEHCEPsamPGDLGLGLRMVRGVVHVYTRRDpdehCPEVELPYPDLQEFVADVNVLMALIINGPIKSF 294
Cdd:pfam19326 65 VfHPPPKKGeDPYELFNF---PPDLGYHLRMQDGVVHVYANKD----ALEDSLPYPDLRDFYTDLEHLLALIADGPIKTF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 295 CYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQ 374
Cdd:pfam19326 138 CHRRLQYLESKFNLHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKYL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 375 TLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNKISGKYFAHIIKEVMADLEESKY 454
Cdd:pfam19326 218 TLREVFESLKLTGYDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESKY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 455 QNAELRLSIYGRSRDEWDKLARWAVNHKVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPEL 534
Cdd:pfam19326 298 QMAEYRISIYGRSPDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPEL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 535 HLFLEHVDGFDSVDDESKPENHVFNlESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPI 614
Cdd:pfam19326 378 HVFLKRVIGFDSVDDESKPERRMFR-KSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGDI 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 615 HHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKE 694
Cdd:pfam19326 457 DHLVSAFLLAHGISHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTKE 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 695 PLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 774
Cdd:pfam19326 537 PLMEEYSIAAQVWKLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELALI 616
|
....*.
gi 21311925 775 TQAVQS 780
Cdd:pfam19326 617 SDAVKS 622
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
275-771 |
0e+00 |
|
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at position 6 of the adenine nucleotide ring. AMPD is a diverse and highly regulated eukaryotic key enzyme of the adenylate catabolic pathway.
Pssm-ID: 238644 Cd Length: 496 Bit Score: 937.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 275 FVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFI 354
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 355 KRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNKIS 434
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 435 GKYFAHIIKEVMADLEESKYQNAELRLSIYGRSRDEWDKLARWAVNHKVHSPNVRWLVQVPRLFDVYRTKGQLANFQEML 514
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 515 ENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEnHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLR 594
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESKSE-RRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 595 RQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLS 674
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 675 RGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTN 754
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 21311925 755 VPDIRVGYRYETLCQEL 771
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
156-774 |
0e+00 |
|
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein involved in energy metabolism. Most members of the family have an additional, poorly alignable region of 150 amino acids or more N-terminal to the region included in the model.
Pssm-ID: 273618 [Multi-domain] Cd Length: 611 Bit Score: 908.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 156 DLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAeKPLETRTYEQSPDTpvsadapvHPPALEQHPYEHCEPSAM 235
Cdd:TIGR01429 2 DLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQG-YPESVPLEEGLPDF--------HPPPDPQEDPYCLDDDAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 236 PGDLGLGLRMVRGVVHVYTRRDPDEHCPEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEM 315
Cdd:TIGR01429 73 PIELGYLVRMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 316 KELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTL 395
Cdd:TIGR01429 153 SELKEQKSVPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 396 DVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNKISGKYFAHIIKEVMADLEESKYQNAELRLSIYGRSRDEWDKLA 475
Cdd:TIGR01429 233 DVHADRNTFHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 476 RWAVNHKVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEN 555
Cdd:TIGR01429 313 RWIIDHDVFSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 556 HVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRK 635
Cdd:TIGR01429 393 HMFSRKFPSPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 636 APVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMC 715
Cdd:TIGR01429 473 VPVLQYLYYLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMC 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 21311925 716 ELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 774
Cdd:TIGR01429 553 ELARNSVLQSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
172-774 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 772.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 172 EKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQSPDTPVSADAPVHPPALEQHPYehcepsampgdlglglRMVRGVVH 251
Cdd:PLN03055 8 EEEVCAMMQECLELRDKYLFREKLPPWRKGIFESSTSKPNPDPFRYEPEPPSQHVF----------------RMVDGVMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 252 VYTRRDPDEHCpeveLPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYN 331
Cdd:PLN03055 72 VYAPDDAKEEL----FPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAPHRDFYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 332 IRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFN 411
Cdd:PLN03055 148 VRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFHRFDKFN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 412 AKYNPIGESVLREIFIKTDNKISGKYFAHIIKEVMADLEESKYQNAELRLSIYGRSRDEWDKLARWAVNHKVHSPNVRWL 491
Cdd:PLN03055 228 LKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYSENVVWL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 492 VQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPlPEAWVEE 571
Cdd:PLN03055 308 IQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKPERRPTKHMQT-PEQWDIP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 572 DNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIA 651
Cdd:PLN03055 387 FNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 652 MSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKV 731
Cdd:PLN03055 467 MSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNSVLQSGFPHAS 546
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 21311925 732 KSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 774
Cdd:PLN03055 547 KKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYV 589
|
|
| PLN02768 |
PLN02768 |
AMP deaminase |
139-774 |
0e+00 |
|
AMP deaminase
Pssm-ID: 215411 Cd Length: 835 Bit Score: 762.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 139 FQRVIISGEEkcgVPFTDLLDAAKSVVRALFIREKYMalslqsfcpttrrYLQQLAekPLETRTyEQSPDTPVSADAPVH 218
Cdd:PLN02768 225 FVRLNITPLE---VPSPDEVEAYKVLQECLELRKRYV-------------FREEVA--PWEKEI-ISDPSTPKPNPNPFS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 219 --PPALEQHPYEhcepsampgdlglglrMVRGVVHVYtrrdPDEHCPEVELPYPDLQEFVADVNVLMALIINGPIKSFCY 296
Cdd:PLN02768 286 ytPEGKSDHYFE----------------MQDGVVHVY----ANKDSKEELFPVADATTFFTDLHHILRVIAAGNIRTLCH 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 297 RRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTL 376
Cdd:PLN02768 346 HRLNLLEQKFNLHLMLNADREFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGTYLTL 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 377 REVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNKISGKYFAHIIKEVMADLEESKYQN 456
Cdd:PLN02768 426 KEVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKQVFSDLEASKYQM 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 457 AELRLSIYGRSRDEWDKLARWAVNHKVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHL 536
Cdd:PLN02768 506 AEYRISIYGRKQSEWDQLASWIVNNELYSENVVWLIQLPRLYNVYKEMGIVTSFQNILDNIFIPLFEVTVDPDSHPQLHV 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 537 FLEHVDGFDSVDDESKPE----NHVfnlesPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAG 612
Cdd:PLN02768 586 FLKQVVGLDLVDDESKPErrptKHM-----PTPAQWTNVFNPAFSYYVYYCYANLYTLNKLRESKGMTTIKFRPHSGEAG 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 613 PIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFT 692
Cdd:PLN02768 661 DIDHLAATFLTCHNIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFLRGLNVSLSTDDPLQIHLT 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 693 KEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELA 772
Cdd:PLN02768 741 KEPLVEEYSIAASVWKLSSCDLCEIARNSVYQSGFSHALKSHWIGKEYYKRGPDGNDIHKTNVPHIRVEFRDTIWKEEMQ 820
|
..
gi 21311925 773 LI 774
Cdd:PLN02768 821 QV 822
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
270-771 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 566.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 270 PDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAA--QKKVPHRDFYNIRKVDTHIHASSCMNQ 347
Cdd:PTZ00310 780 PTLTEFIRDLSELRDICSSVEVKRLATKRLENLEHKFRLHLALNHSNEAGTteERESSNRDFYQAYKVDTHIHMAAGMTA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 348 KHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAyDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFI 427
Cdd:PTZ00310 860 RQLLEFVVDKLLESGDDIAFKRGDHIVTLGQLFSKYGITP-NLTVDQLNVQADHTLFERFDNFNSKYNPMENPDLRSLLL 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 428 KTDNKISGKYFAHIIKEVMADLEESKYQNAELRLSIYGRSRDEWDKLARWAVNHKVHSPNVRWLVQVPRLFDVYRTKGQL 507
Cdd:PTZ00310 939 KTDNFMKGRYFAELIKDVFEQYSRDRFTYAENRLSIYGINVKEWDDLAHWFDTHGMASKHNKWMIQVPRVYKVFRAQNVI 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 508 ANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKpenhvfnLESPL----PEAWVEEDNPPYAYYLYYT 583
Cdd:PTZ00310 1019 GSFGQYLDNIFQPLWEASLHPSKHPKFHYFLNHVSGFDSVDNEAT-------IDLPFtdvsPWAWTSVENPPYNYYLYYL 1091
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 584 FANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLS 663
Cdd:PTZ00310 1092 YANIRTLNEFRASRGFSTFALRPHCGESGSMDHLYGAFLCANSICHGINLRNDPPMQYLYYLAQIGLHVSPLSNNALFLA 1171
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 664 YHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKE 743
Cdd:PTZ00310 1172 FLENPFPVFFHRGLNVSLSTDDPLMFHQTQEPLIEEYSIAARVWGLSLNDLCEIARNSVLQSGFDAAFKRNAIGDRWYLS 1251
|
490 500
....*....|....*....|....*...
gi 21311925 744 GPEGNDIRRTNVPDIRVGYRYETLCQEL 771
Cdd:PTZ00310 1252 SSLGNDSLRTHLSDIRVAFRFETYHTEL 1279
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
124-776 |
1.20e-92 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 317.91 E-value: 1.20e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 124 GDRGLWERDVVLEREFQRVIISGEEKcGVpftDLLDAAKSVVRALFIREKYmalslqsfcpttrrylqqlaeKPLETRTY 203
Cdd:PTZ00310 50 GHGAPEVSLAAVASTMFRVVIDGDDG-GV---DMRKVHGRIAAAIRVRQLY---------------------KPTDTKVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 204 EQSPDTPVSAdapvhppaleqhpyehcepSAMPGDLGLGLRmvRGVvhvYTRRDPDEHcpeVELPYPdLQEFVADVNVLM 283
Cdd:PTZ00310 105 EGEREQPSDS-------------------TPMPSLVTIVQR--DGV---YRFSGMDTS---VVLPPP-WEQYVRDVQAVY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 284 ALIINGPIKSFCYRRLQYLSSKFQMHVLLN-EMKELAAqkkvPHRD---FYNIRKVDTHIHASSCMNQKHLLRFIKRAMK 359
Cdd:PTZ00310 157 LTVGNGPCLSACRHRLTIIQERSRMFFLLNaEIEERAD----LYKAggvFSPCTKVDNAVLLSTSVDAQELLEFVVTTYR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 360 RHLEEIVHVEQGREQTLREVFESMNL-TAYDLSVDTLDVHA--DRNTFHRFDKFNAKyNPIGE--SVLREIFIKTDNKIS 434
Cdd:PTZ00310 233 EQPRAPLRLRDGSNSTLREYLEAHGVrDPRELTVEGLGWQPtkYRNKYGQYDLFDAK-NPMGAlgAELRQSFLSLHGNLC 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 435 GKyfahIIKEVMADLEESKY--QNAELRLSIYGRSRDEWDKLARWAVNHKVHS-PNVRWLVQV--PRL--FDVYRTkgqL 507
Cdd:PTZ00310 312 GK----LLRRELERREYQKQqpQATEYSLPLYGHHPEELTDLAEWVRRQGFGPfSRNRWILAIsfKELgpFQVPSS---C 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 508 ANFQEMLENIFLPLFEATVHPA--SHPELHLFLEHVDGFdSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFA 585
Cdd:PTZ00310 385 TTVQDQLDNIFLPLFKATLCPSdpQWSDVAWLLCQVGGL-QILTHAVVRSEDFDETAPDPDQVPYTAKCSDLYYFYYVYA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 586 NMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSL-FLSY 664
Cdd:PTZ00310 464 NLAVLNSLRKRKGLNTLQLRPSGEKAPAYDQLISSYLLGDVITRATSIADYPVLQYLCGLHRVGLTVSPLRDHALsITAY 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 665 HRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKeG 744
Cdd:PTZ00310 544 FDHPLPKFLHRCLRVSISTSDPLYFHHHSQPLIEEYATAMKLFSLSPLDTTELARNSVLNSSFPPEVKQQWLGERFQL-G 622
|
650 660 670
....*....|....*....|....*....|..
gi 21311925 745 PEGNDIRRTNVPDIRVGYRYETLCQELALITQ 776
Cdd:PTZ00310 623 VEGNDFERSGVTNYRLAFREEAWALEEALLND 654
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
332-739 |
6.92e-64 |
|
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic organisms and catalyze the zinc dependent irreversible deamination of adenosine nucleosides to inosine nucleosides and ammonia. The eukaryotic AMP deaminase catalyzes a similar reaction leading to the hydrolytic removal of an amino group at the 6 position of the adenine nucleotide ring, a branch point in the adenylate catabolic pathway.
Pssm-ID: 238250 Cd Length: 305 Bit Score: 216.06 E-value: 6.92e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 332 IRKVDTHIHASSCMNQKHLLRFIKRAmkrhleeivhveqgreqtlrevfesmnltaydlsvdtldvhadrntfhrfdkfn 411
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKKE------------------------------------------------------ 26
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 412 akynpigesvLREIFIKTDN-KISGKYFAHIIKEVMADLEESKYQNAELRLSIYGRS-RDEWDKLARWAVNHKVHSPNVR 489
Cdd:cd00443 27 ----------FFEKFLLVHNlLQKGEALARALKEVIEEFAEDNVQYLELRTTPRLLEtEKGLTKEQYWLLVIEGISEAKQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 490 WL--VQVPRLFDVYRTKgqlanfqemleniflPLFEATVHPASHPELHLFL-EHVDGFDSVDDESKPENhvfnlesplpe 566
Cdd:cd00443 97 WFppIKVRLILSVDRRG---------------PYVQNYLVASEILELAKFLsNYVVGIDLVGDESKGEN----------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 567 awveednPPYAYYLYYtfanmamlNHLRRqrgFHTFVLRPHCGEAGPIHHLVSAFML-AENISHGLLLRKAPVLQYLYYL 645
Cdd:cd00443 151 -------PLRDFYSYY--------EYARR---LGLLGLTLHCGETGNREELLQALLLlPDRIGHGIFLLKHPELIYLVKL 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 646 AQIGIAMSPLSNNSLFL--SYHRNPLPEYLSRGLMVSLSTDDPLQFHFtkePLMEEYSIATQVWKLSSCDMCELARNSVL 723
Cdd:cd00443 213 RNIPIEVCPTSNVVLGTvqSYEKHPFMRFFKAGLPVSLSTDDPGIFGT---SLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
|
410
....*....|....*.
gi 21311925 724 MSGFSHKVKSHWLGPN 739
Cdd:cd00443 290 SSFAKDEEKKSLLEVL 305
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
570-736 |
6.25e-16 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 79.74 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 570 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSA--FMLAENISHGL-LLRKAPVLQYLyylA 646
Cdd:COG1816 162 ERGFPPEKFAEAFARA---------REAGLH---LTAHAGEAGGPESIWEAldLLGAERIGHGVrAIEDPALVARL---A 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 647 --QIGIAMSPLSNNSL--FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSV 722
Cdd:COG1816 227 drGIPLEVCPTSNVQLgvVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAI 303
|
170
....*....|....
gi 21311925 723 LMSGFSHKVKSHWL 736
Cdd:COG1816 304 EASFLPEEEKAALL 317
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
570-736 |
6.55e-13 |
|
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the irreversible hydrolytic deamination of both adenosine, as well as desoxyadenosine, to ammonia and inosine or desoxyinosine, respectively. ADA plays an important role in the purine pathway. Low, as well as high levels of ADA activity have been linked to several diseases.
Pssm-ID: 238645 Cd Length: 325 Bit Score: 70.70 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 570 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSAF--MLAENISHGLLLRKAPVLqyLYYLA- 646
Cdd:cd01320 167 EVGFPPEKFVRAFQRA---------REAGLR---LTAHAGEAGGPESVRDALdlLGAERIGHGIRAIEDPEL--VKRLAe 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 647 -QIGIAMSPLSNnsLFL----SYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNS 721
Cdd:cd01320 233 rNIPLEVCPTSN--VQTgavkSLAEHPLRELLDAGVKVTINTDDPTVFGTY---LTDEYELLAEAFGLTEEELKKLARNA 307
|
170
....*....|....*
gi 21311925 722 VLMSGFSHKVKSHWL 736
Cdd:cd01320 308 VEASFLSEEEKAELL 322
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
595-736 |
6.13e-11 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 64.81 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 595 RQRGFHtfvLRPHCGEAGP---IHHLVsAFMLAENISHGL-------LLRkapvlqylyYLA--QIGIAMSPLSNNSL-- 660
Cdd:PRK09358 192 RDAGLR---LTAHAGEAGGpesIWEAL-DELGAERIGHGVraiedpaLMA---------RLAdrRIPLEVCPTSNVQTga 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21311925 661 FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWL 736
Cdd:PRK09358 259 VPSLAEHPLKTLLDAGVRVTINTDDPLVFGTT---LTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEEEKAALL 331
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
578-718 |
2.74e-09 |
|
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a conserved metal binding site, involving four histidines and one aspartic acid residue. In the common reaction mechanism, the metal ion (or ions) deprotonate a water molecule for a nucleophilic attack on the substrate. The family includes urease alpha, adenosine deaminase, phosphotriesterase dihydroorotases, allantoinases, hydantoinases, AMP-, adenine and cytosine deaminases, imidazolonepropionase, aryldialkylphosphatase, chlorohydrolases, formylmethanofuran dehydrogenases and others.
Pssm-ID: 238617 [Multi-domain] Cd Length: 275 Bit Score: 58.88 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 578 YYLYYTFANMAMLNHlrrqrgfhtfVLRPHCGEAGPIHHLVSAFMLA------ENISHGLLLrkAPVLQYLYYLAQIGIA 651
Cdd:cd01292 133 ESLRRVLEEARKLGL----------PVVIHAGELPDPTRALEDLVALlrlggrVVIGHVSHL--DPELLELLKEAGVSLE 200
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 652 MSPLSNNSLFL-SYHRNPLPEYLSRGLMVSLSTDDPlqFHFTKEPLMEEYSIATQVWKL--SSCDMCELA 718
Cdd:cd01292 201 VCPLSNYLLGRdGEGAEALRRLLELGIRVTLGTDGP--PHPLGTDLLALLRLLLKVLRLglSLEEALRLA 268
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
607-728 |
4.18e-08 |
|
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors with sequence similarty to adenosine deaminase.
Pssm-ID: 238646 Cd Length: 345 Bit Score: 56.13 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21311925 607 HCGE-----AGPIHHLVSAFML-AENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSN--NSLFLSYHRNPLPEYLSRGLM 678
Cdd:cd01321 200 HAGEtngdgTETDENLVDALLLnTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNqvLGLVSDLRNHPAAALLARGVP 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 21311925 679 VSLSTDDPLQFHFTkePLMEEYSIATQVWKLSSCDMC---ELARNSVLMSGFS 728
Cdd:cd01321 280 VVISSDDPGFWGAK--GLSHDFYQAFMGLAPADAGLRglkQLAENSIRYSALS 330
|
|
| |
