|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
163-806 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1147.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 163 REFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMalslqsFCPTTRRYLQQLaekpletrtyeQGPD-TPVSADA 241
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSV-----------QGEDsTPKENDE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 242 PV-HPPALEQ-HPYEHCEPstmPGDLGLGLRMVRGVVHVYTRREpdehCSEVELPYPDLQEFVADVNVLMALIINGPIKS 319
Cdd:pfam19326 64 PVfHPPPKKGeDPYELFNF---PPDLGYHLRMQDGVVHVYANKD----ALEDSLPYPDLRDFYTDLEHLLALIADGPIKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 320 FCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGRE 399
Cdd:pfam19326 137 FCHRRLQYLESKFNLHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 400 QTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESK 479
Cdd:pfam19326 217 LTLREVFESLKLTGYDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 480 YQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPE 559
Cdd:pfam19326 297 YQMAEYRISIYGRSPDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 560 LHLFLEHVDGFDSVDDESKPENHVFNlESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGP 639
Cdd:pfam19326 377 LHVFLKRVIGFDSVDDESKPERRMFR-KSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 640 IHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTK 719
Cdd:pfam19326 456 IDHLVSAFLLAHGISHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 720 EPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELAL 799
Cdd:pfam19326 536 EPLMEEYSIAAQVWKLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELAL 615
|
....*..
gi 1584352064 800 ITQAVQS 806
Cdd:pfam19326 616 ISDAVKS 622
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
301-797 |
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: 937.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 301 FVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFI 380
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 381 KRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVS 460
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 461 GKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEML 540
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 541 ENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEnHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLR 620
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESKSE-RRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 621 RQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLS 700
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 701 RGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTN 780
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 1584352064 781 VPDIRVGYRYETLCQEL 797
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
182-800 |
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: 907.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 182 DLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAekPLETRTYEQGPDTPvsadapvHPPALEQHPYEHCEPSTM 261
Cdd:TIGR01429 2 DLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQG--YPESVPLEEGLPDF-------HPPPDPQEDPYCLDDDAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 262 PGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEM 341
Cdd:TIGR01429 73 PIELGYLVRMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 342 KELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTL 421
Cdd:TIGR01429 153 SELKEQKSVPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 422 DVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLA 501
Cdd:TIGR01429 233 DVHADRNTFHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 502 RWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEN 581
Cdd:TIGR01429 313 RWIIDHDVFSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 582 HVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRK 661
Cdd:TIGR01429 393 HMFSRKFPSPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 662 APVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMC 741
Cdd:TIGR01429 473 VPVLQYLYYLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMC 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1584352064 742 ELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 800
Cdd:TIGR01429 553 ELARNSVLQSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
198-800 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 770.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 198 EKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYehcepstmpgdlglglRMVRGVVH 277
Cdd:PLN03055 8 EEEVCAMMQECLELRDKYLFREKLPPWRKGIFESSTSKPNPDPFRYEPEPPSQHVF----------------RMVDGVMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 278 VYTrrePDEHCSEVeLPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYN 357
Cdd:PLN03055 72 VYA---PDDAKEEL-FPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAPHRDFYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 358 IRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFN 437
Cdd:PLN03055 148 VRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFHRFDKFN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 438 AKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWL 517
Cdd:PLN03055 228 LKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYSENVVWL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 518 VQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVfNLESPLPEAWVEE 597
Cdd:PLN03055 308 IQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKPERRP-TKHMQTPEQWDIP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 598 DNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIA 677
Cdd:PLN03055 387 FNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 678 MSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKV 757
Cdd:PLN03055 467 MSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNSVLQSGFPHAS 546
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1584352064 758 KSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 800
Cdd:PLN03055 547 KKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYV 589
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
596-762 |
5.59e-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: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 596 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSA--FMLAENISHGL-LLRKAPVLQYLyylA 672
Cdd:COG1816 162 ERGFPPEKFAEAFARA---------REAGLH---LTAHAGEAGGPESIWEAldLLGAERIGHGVrAIEDPALVARL---A 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 673 --QIGIAMSPLSNNSL--FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSV 748
Cdd:COG1816 227 drGIPLEVCPTSNVQLgvVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAI 303
|
170
....*....|....
gi 1584352064 749 LMSGFSHKVKSHWL 762
Cdd:COG1816 304 EASFLPEEEKAALL 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
163-806 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1147.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 163 REFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMalslqsFCPTTRRYLQQLaekpletrtyeQGPD-TPVSADA 241
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSV-----------QGEDsTPKENDE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 242 PV-HPPALEQ-HPYEHCEPstmPGDLGLGLRMVRGVVHVYTRREpdehCSEVELPYPDLQEFVADVNVLMALIINGPIKS 319
Cdd:pfam19326 64 PVfHPPPKKGeDPYELFNF---PPDLGYHLRMQDGVVHVYANKD----ALEDSLPYPDLRDFYTDLEHLLALIADGPIKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 320 FCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGRE 399
Cdd:pfam19326 137 FCHRRLQYLESKFNLHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 400 QTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESK 479
Cdd:pfam19326 217 LTLREVFESLKLTGYDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 480 YQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPE 559
Cdd:pfam19326 297 YQMAEYRISIYGRSPDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 560 LHLFLEHVDGFDSVDDESKPENHVFNlESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGP 639
Cdd:pfam19326 377 LHVFLKRVIGFDSVDDESKPERRMFR-KSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 640 IHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTK 719
Cdd:pfam19326 456 IDHLVSAFLLAHGISHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 720 EPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELAL 799
Cdd:pfam19326 536 EPLMEEYSIAAQVWKLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELAL 615
|
....*..
gi 1584352064 800 ITQAVQS 806
Cdd:pfam19326 616 ISDAVKS 622
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
301-797 |
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: 937.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 301 FVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFI 380
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 381 KRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVS 460
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 461 GKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEML 540
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 541 ENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEnHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLR 620
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESKSE-RRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 621 RQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLS 700
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 701 RGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTN 780
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 1584352064 781 VPDIRVGYRYETLCQEL 797
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
182-800 |
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: 907.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 182 DLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAekPLETRTYEQGPDTPvsadapvHPPALEQHPYEHCEPSTM 261
Cdd:TIGR01429 2 DLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQG--YPESVPLEEGLPDF-------HPPPDPQEDPYCLDDDAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 262 PGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEM 341
Cdd:TIGR01429 73 PIELGYLVRMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 342 KELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTL 421
Cdd:TIGR01429 153 SELKEQKSVPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 422 DVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLA 501
Cdd:TIGR01429 233 DVHADRNTFHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 502 RWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEN 581
Cdd:TIGR01429 313 RWIIDHDVFSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 582 HVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRK 661
Cdd:TIGR01429 393 HMFSRKFPSPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 662 APVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMC 741
Cdd:TIGR01429 473 VPVLQYLYYLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMC 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1584352064 742 ELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 800
Cdd:TIGR01429 553 ELARNSVLQSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
198-800 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 770.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 198 EKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYehcepstmpgdlglglRMVRGVVH 277
Cdd:PLN03055 8 EEEVCAMMQECLELRDKYLFREKLPPWRKGIFESSTSKPNPDPFRYEPEPPSQHVF----------------RMVDGVMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 278 VYTrrePDEHCSEVeLPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYN 357
Cdd:PLN03055 72 VYA---PDDAKEEL-FPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAPHRDFYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 358 IRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFN 437
Cdd:PLN03055 148 VRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFHRFDKFN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 438 AKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWL 517
Cdd:PLN03055 228 LKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYSENVVWL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 518 VQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVfNLESPLPEAWVEE 597
Cdd:PLN03055 308 IQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKPERRP-TKHMQTPEQWDIP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 598 DNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIA 677
Cdd:PLN03055 387 FNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 678 MSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKV 757
Cdd:PLN03055 467 MSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNSVLQSGFPHAS 546
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1584352064 758 KSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 800
Cdd:PLN03055 547 KKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYV 589
|
|
| PLN02768 |
PLN02768 |
AMP deaminase |
159-800 |
0e+00 |
|
AMP deaminase
Pssm-ID: 215411 Cd Length: 835 Bit Score: 761.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 159 DVLERE-----FQRVTISGEEkcgVPFTDLLDAAKSVVRALFIREKYMalslqsfcpttrrYLQQLAekPLETRTyEQGP 233
Cdd:PLN02768 214 DILRKEpeqetFVRLNITPLE---VPSPDEVEAYKVLQECLELRKRYV-------------FREEVA--PWEKEI-ISDP 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 234 DTPVSADAPVH--PPALEQHPYEhcepstmpgdlglglrMVRGVVHVYtrrePDEHCSEVELPYPDLQEFVADVNVLMAL 311
Cdd:PLN02768 275 STPKPNPNPFSytPEGKSDHYFE----------------MQDGVVHVY----ANKDSKEELFPVADATTFFTDLHHILRV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 312 IINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEI 391
Cdd:PLN02768 335 IAAGNIRTLCHHRLNLLEQKFNLHLMLNADREFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 392 VHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEV 471
Cdd:PLN02768 415 VIFRDGTYLTLKEVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKQV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 472 MSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEAT 551
Cdd:PLN02768 495 FSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNELYSENVVWLIQLPRLYNVYKEMGIVTSFQNILDNIFIPLFEVT 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 552 VHPASHPELHLFLEHVDGFDSVDDESKPE----NHVfnlesPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHT 627
Cdd:PLN02768 575 VDPDSHPQLHVFLKQVVGLDLVDDESKPErrptKHM-----PTPAQWTNVFNPAFSYYVYYCYANLYTLNKLRESKGMTT 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 628 FVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSL 707
Cdd:PLN02768 650 IKFRPHSGEAGDIDHLAATFLTCHNIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFLRGLNVSL 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 708 STDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVG 787
Cdd:PLN02768 730 STDDPLQIHLTKEPLVEEYSIAASVWKLSSCDLCEIARNSVYQSGFSHALKSHWIGKEYYKRGPDGNDIHKTNVPHIRVE 809
|
650
....*....|...
gi 1584352064 788 YRYETLCQELALI 800
Cdd:PLN02768 810 FRDTIWKEEMQQV 822
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
296-816 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 564.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 296 PDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAA--QKKVPHRDFYNIRKVDTHIHASSCMNQ 373
Cdd:PTZ00310 780 PTLTEFIRDLSELRDICSSVEVKRLATKRLENLEHKFRLHLALNHSNEAGTteERESSNRDFYQAYKVDTHIHMAAGMTA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 374 KHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAyDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFI 453
Cdd:PTZ00310 860 RQLLEFVVDKLLESGDDIAFKRGDHIVTLGQLFSKYGITP-NLTVDQLNVQADHTLFERFDNFNSKYNPMENPDLRSLLL 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 454 KTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQL 533
Cdd:PTZ00310 939 KTDNFMKGRYFAELIKDVFEQYSRDRFTYAENRLSIYGINVKEWDDLAHWFDTHGMASKHNKWMIQVPRVYKVFRAQNVI 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 534 ANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKpenhvfnLESPL----PEAWVEEDNPPYAYYLYYT 609
Cdd:PTZ00310 1019 GSFGQYLDNIFQPLWEASLHPSKHPKFHYFLNHVSGFDSVDNEAT-------IDLPFtdvsPWAWTSVENPPYNYYLYYL 1091
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 610 FANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLS 689
Cdd:PTZ00310 1092 YANIRTLNEFRASRGFSTFALRPHCGESGSMDHLYGAFLCANSICHGINLRNDPPMQYLYYLAQIGLHVSPLSNNALFLA 1171
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 690 YHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKE 769
Cdd:PTZ00310 1172 FLENPFPVFFHRGLNVSLSTDDPLMFHQTQEPLIEEYSIAARVWGLSLNDLCEIARNSVLQSGFDAAFKRNAIGDRWYLS 1251
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1584352064 770 GPEGNDIRRTNVPDIRVGYRYETLCQELALI----TQAVQSEMLETIPEEA 816
Cdd:PTZ00310 1252 SSLGNDSLRTHLSDIRVAFRFETYHTELNFLelcsGRPIPRAMKTLEEELA 1302
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
248-802 |
1.75e-91 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 315.21 E-value: 1.75e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 248 LEQHPYEHCEPST-----MPGDLGLGLRmvRGVVHVytrrepDEHCSEVELPYPdLQEFVADVNVLMALIINGPIKSFCY 322
Cdd:PTZ00310 99 TDTKVPEGEREQPsdstpMPSLVTIVQR--DGVYRF------SGMDTSVVLPPP-WEQYVRDVQAVYLTVGNGPCLSACR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 323 RRLQYLSSKFQMHVLLN-EMKELAAqkkvPHRD---FYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGR 398
Cdd:PTZ00310 170 HRLTIIQERSRMFFLLNaEIEERAD----LYKAggvFSPCTKVDNAVLLSTSVDAQELLEFVVTTYREQPRAPLRLRDGS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 399 EQTLREVFESMNL-TAYDLSVDTLDVHA--DRNTFHRFDKFNAKyNPIGE--SVLREIFIKTDNRVSGKyfahIIKEVMS 473
Cdd:PTZ00310 246 NSTLREYLEAHGVrDPRELTVEGLGWQPtkYRNKYGQYDLFDAK-NPMGAlgAELRQSFLSLHGNLCGK----LLRRELE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 474 DLEESKY--QNAELRLSIYGRSRDEWDKLARWavMHRVHS---PNVRWLVQV--PRL--FDVYRTkgqLANFQEMLENIF 544
Cdd:PTZ00310 321 RREYQKQqpQATEYSLPLYGHHPEELTDLAEW--VRRQGFgpfSRNRWILAIsfKELgpFQVPSS---CTTVQDQLDNIF 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 545 LPLFEATVHPA--SHPELHLFLEHVDGFdSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQ 622
Cdd:PTZ00310 396 LPLFKATLCPSdpQWSDVAWLLCQVGGL-QILTHAVVRSEDFDETAPDPDQVPYTAKCSDLYYFYYVYANLAVLNSLRKR 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 623 RGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSL-FLSYHRNPLPEYLSR 701
Cdd:PTZ00310 475 KGLNTLQLRPSGEKAPAYDQLISSYLLGDVITRATSIADYPVLQYLCGLHRVGLTVSPLRDHALsITAYFDHPLPKFLHR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 702 GLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKeGPEGNDIRRTNV 781
Cdd:PTZ00310 555 CLRVSISTSDPLYFHHHSQPLIEEYATAMKLFSLSPLDTTELARNSVLNSSFPPEVKQQWLGERFQL-GVEGNDFERSGV 633
|
570 580
....*....|....*....|.
gi 1584352064 782 PDIRVGYRYETLCQELALITQ 802
Cdd:PTZ00310 634 TNYRLAFREEAWALEEALLND 654
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
358-765 |
8.12e-65 |
|
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: 219.14 E-value: 8.12e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 358 IRKVDTHIHASSCMNQKHLLRFIKRAmkrhleeivhveqgreqtlrevfesmnltaydlsvdtldvhadrntfhrfdkfn 437
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKKE------------------------------------------------------ 26
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 438 akynpigesvLREIFIKTDN-RVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRS-RDEWDKLARWAVMHRVHSPNVR 515
Cdd:cd00443 27 ----------FFEKFLLVHNlLQKGEALARALKEVIEEFAEDNVQYLELRTTPRLLEtEKGLTKEQYWLLVIEGISEAKQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 516 WL--VQVPRLFDVYRTKgqlanfqemleniflPLFEATVHPASHPELHLFL-EHVDGFDSVDDESKPENhvfnlesplpe 592
Cdd:cd00443 97 WFppIKVRLILSVDRRG---------------PYVQNYLVASEILELAKFLsNYVVGIDLVGDESKGEN----------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 593 awveednPPYAYYLYYtfanmamlNHLRRqrgFHTFVLRPHCGEAGPIHHLVSAFML-AENISHGLLLRKAPVLQYLYYL 671
Cdd:cd00443 151 -------PLRDFYSYY--------EYARR---LGLLGLTLHCGETGNREELLQALLLlPDRIGHGIFLLKHPELIYLVKL 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 672 AQIGIAMSPLSNNSLFL--SYHRNPLPEYLSRGLMVSLSTDDPLQFHFtkePLMEEYSIATQVWKLSSCDMCELARNSVL 749
Cdd:cd00443 213 RNIPIEVCPTSNVVLGTvqSYEKHPFMRFFKAGLPVSLSTDDPGIFGT---SLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
|
410
....*....|....*.
gi 1584352064 750 MSGFSHKVKSHWLGPN 765
Cdd:cd00443 290 SSFAKDEEKKSLLEVL 305
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
596-762 |
5.59e-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: 5.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 596 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSA--FMLAENISHGL-LLRKAPVLQYLyylA 672
Cdd:COG1816 162 ERGFPPEKFAEAFARA---------REAGLH---LTAHAGEAGGPESIWEAldLLGAERIGHGVrAIEDPALVARL---A 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 673 --QIGIAMSPLSNNSL--FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSV 748
Cdd:COG1816 227 drGIPLEVCPTSNVQLgvVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAI 303
|
170
....*....|....
gi 1584352064 749 LMSGFSHKVKSHWL 762
Cdd:COG1816 304 EASFLPEEEKAALL 317
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
596-762 |
5.21e-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: 71.08 E-value: 5.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 596 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSAF--MLAENISHGLLLRKAPVLqyLYYLA- 672
Cdd:cd01320 167 EVGFPPEKFVRAFQRA---------REAGLR---LTAHAGEAGGPESVRDALdlLGAERIGHGIRAIEDPEL--VKRLAe 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 673 -QIGIAMSPLSNnsLFL----SYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNS 747
Cdd:cd01320 233 rNIPLEVCPTSN--VQTgavkSLAEHPLRELLDAGVKVTINTDDPTVFGTY---LTDEYELLAEAFGLTEEELKKLARNA 307
|
170
....*....|....*
gi 1584352064 748 VLMSGFSHKVKSHWL 762
Cdd:cd01320 308 VEASFLSEEEKAELL 322
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
621-762 |
5.50e-11 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 64.81 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 621 RQRGFHtfvLRPHCGEAGP---IHHLVsAFMLAENISHGL-------LLRkapvlqylyYLA--QIGIAMSPLSNNSL-- 686
Cdd:PRK09358 192 RDAGLR---LTAHAGEAGGpesIWEAL-DELGAERIGHGVraiedpaLMA---------RLAdrRIPLEVCPTSNVQTga 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1584352064 687 FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWL 762
Cdd:PRK09358 259 VPSLAEHPLKTLLDAGVRVTINTDDPLVFGTT---LTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEEEKAALL 331
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
604-744 |
2.15e-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: 59.27 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 604 YYLYYTFANMAMLNHlrrqrgfhtfVLRPHCGEAGPIHHLVSAFMLA------ENISHGLLLrkAPVLQYLYYLAQIGIA 677
Cdd:cd01292 133 ESLRRVLEEARKLGL----------PVVIHAGELPDPTRALEDLVALlrlggrVVIGHVSHL--DPELLELLKEAGVSLE 200
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 678 MSPLSNNSLFL-SYHRNPLPEYLSRGLMVSLSTDDPlqFHFTKEPLMEEYSIATQVWKL--SSCDMCELA 744
Cdd:cd01292 201 VCPLSNYLLGRdGEGAEALRRLLELGIRVTLGTDGP--PHPLGTDLLALLRLLLKVLRLglSLEEALRLA 268
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
633-754 |
3.43e-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: 3.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1584352064 633 HCGE-----AGPIHHLVSAFML-AENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSN--NSLFLSYHRNPLPEYLSRGLM 704
Cdd:cd01321 200 HAGEtngdgTETDENLVDALLLnTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNqvLGLVSDLRNHPAAALLARGVP 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1584352064 705 VSLSTDDPLQFHFTkePLMEEYSIATQVWKLSSCDMC---ELARNSVLMSGFS 754
Cdd:cd01321 280 VVISSDDPGFWGAK--GLSHDFYQAFMGLAPADAGLRglkQLAENSIRYSALS 330
|
|
| |
