|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
99-742 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1142.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 99 REFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMalslqsFCPTTRRYLQQLaekpletrtyeQGPD-TPVSADA 177
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSV-----------QGEDsTPKENDE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 178 PV-HPPALEQ-HPYEHCEPstmPGDLGLGLRMVRGVVHVYTRREpdehCSEVELPYPDLQEFVADVNVLMALIINGPIKS 255
Cdd:pfam19326 64 PVfHPPPKKGeDPYELFNF---PPDLGYHLRMQDGVVHVYANKD----ALEDSLPYPDLRDFYTDLEHLLALIADGPIKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 256 FCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGRE 335
Cdd:pfam19326 137 FCHRRLQYLESKFNLHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 336 QTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESK 415
Cdd:pfam19326 217 LTLREVFESLKLTGYDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 416 YQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPE 495
Cdd:pfam19326 297 YQMAEYRISIYGRSPDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 496 LHLFLEHVDGFDSVDDESKPENHVFNlESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGP 575
Cdd:pfam19326 377 LHVFLKRVIGFDSVDDESKPERRMFR-KSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 576 IHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTK 655
Cdd:pfam19326 456 IDHLVSAFLLAHGISHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 656 EPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELAL 735
Cdd:pfam19326 536 EPLMEEYSIAAQVWKLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELAL 615
|
....*..
gi 383209660 736 ITQAVQS 742
Cdd:pfam19326 616 ISDAVKS 622
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
237-733 |
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: 932.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 237 FVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFI 316
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 317 KRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVS 396
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 397 GKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEML 476
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 477 ENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEnHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLR 556
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESKSE-RRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 557 RQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLS 636
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 637 RGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTN 716
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 383209660 717 VPDIRVGYRYETLCQEL 733
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
118-736 |
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: 903.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 118 DLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAekPLETRTYEQGPDTPvsadapvHPPALEQHPYEHCEPSTM 197
Cdd:TIGR01429 2 DLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQG--YPESVPLEEGLPDF-------HPPPDPQEDPYCLDDDAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 198 PGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEM 277
Cdd:TIGR01429 73 PIELGYLVRMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 278 KELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTL 357
Cdd:TIGR01429 153 SELKEQKSVPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 358 DVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLA 437
Cdd:TIGR01429 233 DVHADRNTFHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 438 RWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEN 517
Cdd:TIGR01429 313 RWIIDHDVFSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 518 HVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRK 597
Cdd:TIGR01429 393 HMFSRKFPSPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 598 APVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMC 677
Cdd:TIGR01429 473 VPVLQYLYYLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMC 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 383209660 678 ELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 736
Cdd:TIGR01429 553 ELARNSVLQSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
134-736 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 767.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 134 EKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYehcepstmpgdlglglRMVRGVVH 213
Cdd:PLN03055 8 EEEVCAMMQECLELRDKYLFREKLPPWRKGIFESSTSKPNPDPFRYEPEPPSQHVF----------------RMVDGVMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 214 VYTrrePDEHCSEVeLPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYN 293
Cdd:PLN03055 72 VYA---PDDAKEEL-FPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAPHRDFYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 294 IRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFN 373
Cdd:PLN03055 148 VRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFHRFDKFN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 374 AKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWL 453
Cdd:PLN03055 228 LKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYSENVVWL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 454 VQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPlPEAWVEE 533
Cdd:PLN03055 308 IQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKPERRPTKHMQT-PEQWDIP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 534 DNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIA 613
Cdd:PLN03055 387 FNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 614 MSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKV 693
Cdd:PLN03055 467 MSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNSVLQSGFPHAS 546
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 383209660 694 KSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 736
Cdd:PLN03055 547 KKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYV 589
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
532-698 |
6.18e-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: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 532 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSA--FMLAENISHGL-LLRKAPVLQYLyylA 608
Cdd:COG1816 162 ERGFPPEKFAEAFARA---------REAGLH---LTAHAGEAGGPESIWEAldLLGAERIGHGVrAIEDPALVARL---A 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 609 --QIGIAMSPLSNNSL--FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSV 684
Cdd:COG1816 227 drGIPLEVCPTSNVQLgvVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAI 303
|
170
....*....|....
gi 383209660 685 LMSGFSHKVKSHWL 698
Cdd:COG1816 304 EASFLPEEEKAALL 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
99-742 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1142.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 99 REFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMalslqsFCPTTRRYLQQLaekpletrtyeQGPD-TPVSADA 177
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSV-----------QGEDsTPKENDE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 178 PV-HPPALEQ-HPYEHCEPstmPGDLGLGLRMVRGVVHVYTRREpdehCSEVELPYPDLQEFVADVNVLMALIINGPIKS 255
Cdd:pfam19326 64 PVfHPPPKKGeDPYELFNF---PPDLGYHLRMQDGVVHVYANKD----ALEDSLPYPDLRDFYTDLEHLLALIADGPIKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 256 FCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGRE 335
Cdd:pfam19326 137 FCHRRLQYLESKFNLHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 336 QTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESK 415
Cdd:pfam19326 217 LTLREVFESLKLTGYDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 416 YQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPE 495
Cdd:pfam19326 297 YQMAEYRISIYGRSPDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 496 LHLFLEHVDGFDSVDDESKPENHVFNlESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGP 575
Cdd:pfam19326 377 LHVFLKRVIGFDSVDDESKPERRMFR-KSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 576 IHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTK 655
Cdd:pfam19326 456 IDHLVSAFLLAHGISHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 656 EPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELAL 735
Cdd:pfam19326 536 EPLMEEYSIAAQVWKLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELAL 615
|
....*..
gi 383209660 736 ITQAVQS 742
Cdd:pfam19326 616 ISDAVKS 622
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
237-733 |
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: 932.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 237 FVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFI 316
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 317 KRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVS 396
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 397 GKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEML 476
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 477 ENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEnHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLR 556
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESKSE-RRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 557 RQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLS 636
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 637 RGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTN 716
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 383209660 717 VPDIRVGYRYETLCQEL 733
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
118-736 |
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: 903.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 118 DLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAekPLETRTYEQGPDTPvsadapvHPPALEQHPYEHCEPSTM 197
Cdd:TIGR01429 2 DLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQG--YPESVPLEEGLPDF-------HPPPDPQEDPYCLDDDAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 198 PGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEM 277
Cdd:TIGR01429 73 PIELGYLVRMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 278 KELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTL 357
Cdd:TIGR01429 153 SELKEQKSVPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 358 DVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLA 437
Cdd:TIGR01429 233 DVHADRNTFHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 438 RWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEN 517
Cdd:TIGR01429 313 RWIIDHDVFSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 518 HVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRK 597
Cdd:TIGR01429 393 HMFSRKFPSPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 598 APVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMC 677
Cdd:TIGR01429 473 VPVLQYLYYLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMC 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 383209660 678 ELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 736
Cdd:TIGR01429 553 ELARNSVLQSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
134-736 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 767.88 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 134 EKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYehcepstmpgdlglglRMVRGVVH 213
Cdd:PLN03055 8 EEEVCAMMQECLELRDKYLFREKLPPWRKGIFESSTSKPNPDPFRYEPEPPSQHVF----------------RMVDGVMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 214 VYTrrePDEHCSEVeLPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYN 293
Cdd:PLN03055 72 VYA---PDDAKEEL-FPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAPHRDFYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 294 IRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFN 373
Cdd:PLN03055 148 VRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFHRFDKFN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 374 AKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWL 453
Cdd:PLN03055 228 LKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYSENVVWL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 454 VQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPlPEAWVEE 533
Cdd:PLN03055 308 IQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKPERRPTKHMQT-PEQWDIP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 534 DNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIA 613
Cdd:PLN03055 387 FNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 614 MSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKV 693
Cdd:PLN03055 467 MSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNSVLQSGFPHAS 546
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 383209660 694 KSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 736
Cdd:PLN03055 547 KKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYV 589
|
|
| PLN02768 |
PLN02768 |
AMP deaminase |
95-736 |
0e+00 |
|
AMP deaminase
Pssm-ID: 215411 Cd Length: 835 Bit Score: 760.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 95 DVLERE-----FQRVTISGEEkcgVPFTDLLDAAKSVVRALFIREKYMalslqsfcpttrrYLQQLAekPLETRTyEQGP 169
Cdd:PLN02768 214 DILRKEpeqetFVRLNITPLE---VPSPDEVEAYKVLQECLELRKRYV-------------FREEVA--PWEKEI-ISDP 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 170 DTPVSADAPVH--PPALEQHPYEhcepstmpgdlglglrMVRGVVHVYtrrePDEHCSEVELPYPDLQEFVADVNVLMAL 247
Cdd:PLN02768 275 STPKPNPNPFSytPEGKSDHYFE----------------MQDGVVHVY----ANKDSKEELFPVADATTFFTDLHHILRV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 248 IINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEI 327
Cdd:PLN02768 335 IAAGNIRTLCHHRLNLLEQKFNLHLMLNADREFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 328 VHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEV 407
Cdd:PLN02768 415 VIFRDGTYLTLKEVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKQV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 408 MSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEAT 487
Cdd:PLN02768 495 FSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNELYSENVVWLIQLPRLYNVYKEMGIVTSFQNILDNIFIPLFEVT 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 488 VHPASHPELHLFLEHVDGFDSVDDESKPE----NHVfnlesPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHT 563
Cdd:PLN02768 575 VDPDSHPQLHVFLKQVVGLDLVDDESKPErrptKHM-----PTPAQWTNVFNPAFSYYVYYCYANLYTLNKLRESKGMTT 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 564 FVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSL 643
Cdd:PLN02768 650 IKFRPHSGEAGDIDHLAATFLTCHNIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFLRGLNVSL 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 644 STDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVG 723
Cdd:PLN02768 730 STDDPLQIHLTKEPLVEEYSIAASVWKLSSCDLCEIARNSVYQSGFSHALKSHWIGKEYYKRGPDGNDIHKTNVPHIRVE 809
|
650
....*....|...
gi 383209660 724 YRYETLCQELALI 736
Cdd:PLN02768 810 FRDTIWKEEMQQV 822
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
232-752 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 562.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 232 PDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAA--QKKVPHRDFYNIRKVDTHIHASSCMNQ 309
Cdd:PTZ00310 780 PTLTEFIRDLSELRDICSSVEVKRLATKRLENLEHKFRLHLALNHSNEAGTteERESSNRDFYQAYKVDTHIHMAAGMTA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 310 KHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAyDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFI 389
Cdd:PTZ00310 860 RQLLEFVVDKLLESGDDIAFKRGDHIVTLGQLFSKYGITP-NLTVDQLNVQADHTLFERFDNFNSKYNPMENPDLRSLLL 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 390 KTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQL 469
Cdd:PTZ00310 939 KTDNFMKGRYFAELIKDVFEQYSRDRFTYAENRLSIYGINVKEWDDLAHWFDTHGMASKHNKWMIQVPRVYKVFRAQNVI 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 470 ANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKpenhvfnLESPL----PEAWVEEDNPPYAYYLYYT 545
Cdd:PTZ00310 1019 GSFGQYLDNIFQPLWEASLHPSKHPKFHYFLNHVSGFDSVDNEAT-------IDLPFtdvsPWAWTSVENPPYNYYLYYL 1091
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 546 FANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLS 625
Cdd:PTZ00310 1092 YANIRTLNEFRASRGFSTFALRPHCGESGSMDHLYGAFLCANSICHGINLRNDPPMQYLYYLAQIGLHVSPLSNNALFLA 1171
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 626 YHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKE 705
Cdd:PTZ00310 1172 FLENPFPVFFHRGLNVSLSTDDPLMFHQTQEPLIEEYSIAARVWGLSLNDLCEIARNSVLQSGFDAAFKRNAIGDRWYLS 1251
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 383209660 706 GPEGNDIRRTNVPDIRVGYRYETLCQELALI----TQAVQSEMLETIPEEA 752
Cdd:PTZ00310 1252 SSLGNDSLRTHLSDIRVAFRFETYHTELNFLelcsGRPIPRAMKTLEEELA 1302
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
184-738 |
9.55e-92 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 314.06 E-value: 9.55e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 184 LEQHPYEHCEPST-----MPGDLGLGLRmvRGVVHVytrrepDEHCSEVELPYPdLQEFVADVNVLMALIINGPIKSFCY 258
Cdd:PTZ00310 99 TDTKVPEGEREQPsdstpMPSLVTIVQR--DGVYRF------SGMDTSVVLPPP-WEQYVRDVQAVYLTVGNGPCLSACR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 259 RRLQYLSSKFQMHVLLN-EMKELAAqkkvPHRD---FYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGR 334
Cdd:PTZ00310 170 HRLTIIQERSRMFFLLNaEIEERAD----LYKAggvFSPCTKVDNAVLLSTSVDAQELLEFVVTTYREQPRAPLRLRDGS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 335 EQTLREVFESMNL-TAYDLSVDTLDVHA--DRNTFHRFDKFNAKyNPIGE--SVLREIFIKTDNRVSGKyfahIIKEVMS 409
Cdd:PTZ00310 246 NSTLREYLEAHGVrDPRELTVEGLGWQPtkYRNKYGQYDLFDAK-NPMGAlgAELRQSFLSLHGNLCGK----LLRRELE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 410 DLEESKY--QNAELRLSIYGRSRDEWDKLARWavMHRVHS---PNVRWLVQV--PRL--FDVYRTkgqLANFQEMLENIF 480
Cdd:PTZ00310 321 RREYQKQqpQATEYSLPLYGHHPEELTDLAEW--VRRQGFgpfSRNRWILAIsfKELgpFQVPSS---CTTVQDQLDNIF 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 481 LPLFEATVHPA--SHPELHLFLEHVDGFdSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQ 558
Cdd:PTZ00310 396 LPLFKATLCPSdpQWSDVAWLLCQVGGL-QILTHAVVRSEDFDETAPDPDQVPYTAKCSDLYYFYYVYANLAVLNSLRKR 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 559 RGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSL-FLSYHRNPLPEYLSR 637
Cdd:PTZ00310 475 KGLNTLQLRPSGEKAPAYDQLISSYLLGDVITRATSIADYPVLQYLCGLHRVGLTVSPLRDHALsITAYFDHPLPKFLHR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 638 GLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKeGPEGNDIRRTNV 717
Cdd:PTZ00310 555 CLRVSISTSDPLYFHHHSQPLIEEYATAMKLFSLSPLDTTELARNSVLNSSFPPEVKQQWLGERFQL-GVEGNDFERSGV 633
|
570 580
....*....|....*....|.
gi 383209660 718 PDIRVGYRYETLCQELALITQ 738
Cdd:PTZ00310 634 TNYRLAFREEAWALEEALLND 654
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
294-701 |
2.74e-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: 216.44 E-value: 2.74e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 294 IRKVDTHIHASSCMNQKHLLRFIKRAmkrhleeivhveqgreqtlrevfesmnltaydlsvdtldvhadrntfhrfdkfn 373
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKKE------------------------------------------------------ 26
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 374 akynpigesvLREIFIKTDN-RVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRS-RDEWDKLARWAVMHRVHSPNVR 451
Cdd:cd00443 27 ----------FFEKFLLVHNlLQKGEALARALKEVIEEFAEDNVQYLELRTTPRLLEtEKGLTKEQYWLLVIEGISEAKQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 452 WL--VQVPRLFDVYRTKgqlanfqemleniflPLFEATVHPASHPELHLFL-EHVDGFDSVDDESKPENhvfnlesplpe 528
Cdd:cd00443 97 WFppIKVRLILSVDRRG---------------PYVQNYLVASEILELAKFLsNYVVGIDLVGDESKGEN----------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 529 awveednPPYAYYLYYtfanmamlNHLRRqrgFHTFVLRPHCGEAGPIHHLVSAFML-AENISHGLLLRKAPVLQYLYYL 607
Cdd:cd00443 151 -------PLRDFYSYY--------EYARR---LGLLGLTLHCGETGNREELLQALLLlPDRIGHGIFLLKHPELIYLVKL 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 608 AQIGIAMSPLSNNSLFL--SYHRNPLPEYLSRGLMVSLSTDDPLQFHFtkePLMEEYSIATQVWKLSSCDMCELARNSVL 685
Cdd:cd00443 213 RNIPIEVCPTSNVVLGTvqSYEKHPFMRFFKAGLPVSLSTDDPGIFGT---SLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
|
410
....*....|....*.
gi 383209660 686 MSGFSHKVKSHWLGPN 701
Cdd:cd00443 290 SSFAKDEEKKSLLEVL 305
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
532-698 |
6.18e-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: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 532 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSA--FMLAENISHGL-LLRKAPVLQYLyylA 608
Cdd:COG1816 162 ERGFPPEKFAEAFARA---------REAGLH---LTAHAGEAGGPESIWEAldLLGAERIGHGVrAIEDPALVARL---A 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 609 --QIGIAMSPLSNNSL--FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSV 684
Cdd:COG1816 227 drGIPLEVCPTSNVQLgvVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAI 303
|
170
....*....|....
gi 383209660 685 LMSGFSHKVKSHWL 698
Cdd:COG1816 304 EASFLPEEEKAALL 317
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
532-698 |
7.10e-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: 70.31 E-value: 7.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 532 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSAF--MLAENISHGLLLRKAPVLqyLYYLA- 608
Cdd:cd01320 167 EVGFPPEKFVRAFQRA---------REAGLR---LTAHAGEAGGPESVRDALdlLGAERIGHGIRAIEDPEL--VKRLAe 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 609 -QIGIAMSPLSNnsLFL----SYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNS 683
Cdd:cd01320 233 rNIPLEVCPTSN--VQTgavkSLAEHPLRELLDAGVKVTINTDDPTVFGTY---LTDEYELLAEAFGLTEEELKKLARNA 307
|
170
....*....|....*
gi 383209660 684 VLMSGFSHKVKSHWL 698
Cdd:cd01320 308 VEASFLSEEEKAELL 322
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
557-698 |
5.90e-11 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 64.81 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 557 RQRGFHtfvLRPHCGEAGP---IHHLVsAFMLAENISHGL-------LLRkapvlqylyYLA--QIGIAMSPLSNNSL-- 622
Cdd:PRK09358 192 RDAGLR---LTAHAGEAGGpesIWEAL-DELGAERIGHGVraiedpaLMA---------RLAdrRIPLEVCPTSNVQTga 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 383209660 623 FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWL 698
Cdd:PRK09358 259 VPSLAEHPLKTLLDAGVRVTINTDDPLVFGTT---LTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEEEKAALL 331
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
540-680 |
2.46e-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: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 540 YYLYYTFANMAMLNHlrrqrgfhtfVLRPHCGEAGPIHHLVSAFMLA------ENISHGLLLrkAPVLQYLYYLAQIGIA 613
Cdd:cd01292 133 ESLRRVLEEARKLGL----------PVVIHAGELPDPTRALEDLVALlrlggrVVIGHVSHL--DPELLELLKEAGVSLE 200
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 614 MSPLSNNSLFL-SYHRNPLPEYLSRGLMVSLSTDDPlqFHFTKEPLMEEYSIATQVWKL--SSCDMCELA 680
Cdd:cd01292 201 VCPLSNYLLGRdGEGAEALRRLLELGIRVTLGTDGP--PHPLGTDLLALLRLLLKVLRLglSLEEALRLA 268
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
569-690 |
4.03e-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: 55.74 E-value: 4.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 383209660 569 HCGE-----AGPIHHLVSAFML-AENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSN--NSLFLSYHRNPLPEYLSRGLM 640
Cdd:cd01321 200 HAGEtngdgTETDENLVDALLLnTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNqvLGLVSDLRNHPAAALLARGVP 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 383209660 641 VSLSTDDPLQFHFTkePLMEEYSIATQVWKLSSCDMC---ELARNSVLMSGFS 690
Cdd:cd01321 280 VVISSDDPGFWGAK--GLSHDFYQAFMGLAPADAGLRglkQLAENSIRYSALS 330
|
|
| |
