|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
136-779 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1146.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 136 REFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMalslqsFCPTTRRYLQQLaekpletrtyeQGPD-TPVSADA 214
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSV-----------QGEDsTPKENDE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 215 PV-HPPALEQ-HPYEHCEPstmPGDLGLGLRMVRGVVHVYTRREpdehCSEVELPYPDLQEFVADVNVLMALIINGPIKS 292
Cdd:pfam19326 64 PVfHPPPKKGeDPYELFNF---PPDLGYHLRMQDGVVHVYANKD----ALEDSLPYPDLRDFYTDLEHLLALIADGPIKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 293 FCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGRE 372
Cdd:pfam19326 137 FCHRRLQYLESKFNLHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 373 QTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESK 452
Cdd:pfam19326 217 LTLREVFESLKLTGYDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 453 YQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPE 532
Cdd:pfam19326 297 YQMAEYRISIYGRSPDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 533 LHLFLEHVDGFDSVDDESKPENHVFNlESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGP 612
Cdd:pfam19326 377 LHVFLKRVIGFDSVDDESKPERRMFR-KSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 613 IHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTK 692
Cdd:pfam19326 456 IDHLVSAFLLAHGISHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 693 EPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELAL 772
Cdd:pfam19326 536 EPLMEEYSIAAQVWKLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELAL 615
|
....*..
gi 34147621 773 ITQAVQS 779
Cdd:pfam19326 616 ISDAVKS 622
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
274-770 |
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: 935.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 274 FVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFI 353
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 354 KRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVS 433
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 434 GKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEML 513
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 514 ENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEnHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLR 593
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESKSE-RRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 594 RQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLS 673
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 674 RGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTN 753
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 34147621 754 VPDIRVGYRYETLCQEL 770
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
155-773 |
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: 906.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 155 DLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAekPLETRTYEQGPDTPvsadapvHPPALEQHPYEHCEPSTM 234
Cdd:TIGR01429 2 DLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQG--YPESVPLEEGLPDF-------HPPPDPQEDPYCLDDDAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 235 PGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEM 314
Cdd:TIGR01429 73 PIELGYLVRMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 315 KELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTL 394
Cdd:TIGR01429 153 SELKEQKSVPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 395 DVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLA 474
Cdd:TIGR01429 233 DVHADRNTFHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 475 RWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEN 554
Cdd:TIGR01429 313 RWIIDHDVFSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 555 HVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRK 634
Cdd:TIGR01429 393 HMFSRKFPSPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 635 APVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMC 714
Cdd:TIGR01429 473 VPVLQYLYYLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMC 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 34147621 715 ELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 773
Cdd:TIGR01429 553 ELARNSVLQSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
171-773 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 769.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 171 EKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYehcepstmpgdlglglRMVRGVVH 250
Cdd:PLN03055 8 EEEVCAMMQECLELRDKYLFREKLPPWRKGIFESSTSKPNPDPFRYEPEPPSQHVF----------------RMVDGVMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 251 VYTrrePDEHCSEVeLPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYN 330
Cdd:PLN03055 72 VYA---PDDAKEEL-FPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAPHRDFYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 331 IRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFN 410
Cdd:PLN03055 148 VRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFHRFDKFN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 411 AKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWL 490
Cdd:PLN03055 228 LKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYSENVVWL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 491 VQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPlPEAWVEE 570
Cdd:PLN03055 308 IQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKPERRPTKHMQT-PEQWDIP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 571 DNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIA 650
Cdd:PLN03055 387 FNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 651 MSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKV 730
Cdd:PLN03055 467 MSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNSVLQSGFPHAS 546
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 34147621 731 KSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 773
Cdd:PLN03055 547 KKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYV 589
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
569-735 |
7.31e-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: 79.36 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 569 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSA--FMLAENISHGL-LLRKAPVLQYLyylA 645
Cdd:COG1816 162 ERGFPPEKFAEAFARA---------REAGLH---LTAHAGEAGGPESIWEAldLLGAERIGHGVrAIEDPALVARL---A 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 646 --QIGIAMSPLSNNSL--FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSV 721
Cdd:COG1816 227 drGIPLEVCPTSNVQLgvVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAI 303
|
170
....*....|....
gi 34147621 722 LMSGFSHKVKSHWL 735
Cdd:COG1816 304 EASFLPEEEKAALL 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
136-779 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1146.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 136 REFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMalslqsFCPTTRRYLQQLaekpletrtyeQGPD-TPVSADA 214
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSV-----------QGEDsTPKENDE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 215 PV-HPPALEQ-HPYEHCEPstmPGDLGLGLRMVRGVVHVYTRREpdehCSEVELPYPDLQEFVADVNVLMALIINGPIKS 292
Cdd:pfam19326 64 PVfHPPPKKGeDPYELFNF---PPDLGYHLRMQDGVVHVYANKD----ALEDSLPYPDLRDFYTDLEHLLALIADGPIKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 293 FCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGRE 372
Cdd:pfam19326 137 FCHRRLQYLESKFNLHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 373 QTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESK 452
Cdd:pfam19326 217 LTLREVFESLKLTGYDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 453 YQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPE 532
Cdd:pfam19326 297 YQMAEYRISIYGRSPDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 533 LHLFLEHVDGFDSVDDESKPENHVFNlESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGP 612
Cdd:pfam19326 377 LHVFLKRVIGFDSVDDESKPERRMFR-KSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 613 IHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTK 692
Cdd:pfam19326 456 IDHLVSAFLLAHGISHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 693 EPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELAL 772
Cdd:pfam19326 536 EPLMEEYSIAAQVWKLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELAL 615
|
....*..
gi 34147621 773 ITQAVQS 779
Cdd:pfam19326 616 ISDAVKS 622
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
274-770 |
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: 935.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 274 FVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFI 353
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 354 KRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVS 433
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 434 GKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEML 513
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 514 ENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEnHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLR 593
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESKSE-RRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 594 RQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLS 673
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 674 RGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTN 753
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 34147621 754 VPDIRVGYRYETLCQEL 770
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
155-773 |
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: 906.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 155 DLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAekPLETRTYEQGPDTPvsadapvHPPALEQHPYEHCEPSTM 234
Cdd:TIGR01429 2 DLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQG--YPESVPLEEGLPDF-------HPPPDPQEDPYCLDDDAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 235 PGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEM 314
Cdd:TIGR01429 73 PIELGYLVRMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 315 KELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTL 394
Cdd:TIGR01429 153 SELKEQKSVPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 395 DVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLA 474
Cdd:TIGR01429 233 DVHADRNTFHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 475 RWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEN 554
Cdd:TIGR01429 313 RWIIDHDVFSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 555 HVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRK 634
Cdd:TIGR01429 393 HMFSRKFPSPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 635 APVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMC 714
Cdd:TIGR01429 473 VPVLQYLYYLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMC 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 34147621 715 ELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 773
Cdd:TIGR01429 553 ELARNSVLQSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
171-773 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 769.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 171 EKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYehcepstmpgdlglglRMVRGVVH 250
Cdd:PLN03055 8 EEEVCAMMQECLELRDKYLFREKLPPWRKGIFESSTSKPNPDPFRYEPEPPSQHVF----------------RMVDGVMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 251 VYTrrePDEHCSEVeLPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYN 330
Cdd:PLN03055 72 VYA---PDDAKEEL-FPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAPHRDFYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 331 IRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFN 410
Cdd:PLN03055 148 VRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFHRFDKFN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 411 AKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWL 490
Cdd:PLN03055 228 LKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYSENVVWL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 491 VQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPlPEAWVEE 570
Cdd:PLN03055 308 IQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKPERRPTKHMQT-PEQWDIP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 571 DNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIA 650
Cdd:PLN03055 387 FNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 651 MSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKV 730
Cdd:PLN03055 467 MSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNSVLQSGFPHAS 546
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 34147621 731 KSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 773
Cdd:PLN03055 547 KKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYV 589
|
|
| PLN02768 |
PLN02768 |
AMP deaminase |
132-773 |
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 34147621 132 DVLERE-----FQRVTISGEEkcgVPFTDLLDAAKSVVRALFIREKYMalslqsfcpttrrYLQQLAekPLETRTyEQGP 206
Cdd:PLN02768 214 DILRKEpeqetFVRLNITPLE---VPSPDEVEAYKVLQECLELRKRYV-------------FREEVA--PWEKEI-ISDP 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 207 DTPVSADAPVH--PPALEQHPYEhcepstmpgdlglglrMVRGVVHVYtrrePDEHCSEVELPYPDLQEFVADVNVLMAL 284
Cdd:PLN02768 275 STPKPNPNPFSytPEGKSDHYFE----------------MQDGVVHVY----ANKDSKEELFPVADATTFFTDLHHILRV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 285 IINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEI 364
Cdd:PLN02768 335 IAAGNIRTLCHHRLNLLEQKFNLHLMLNADREFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 365 VHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEV 444
Cdd:PLN02768 415 VIFRDGTYLTLKEVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKQV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 445 MSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEAT 524
Cdd:PLN02768 495 FSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNELYSENVVWLIQLPRLYNVYKEMGIVTSFQNILDNIFIPLFEVT 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 525 VHPASHPELHLFLEHVDGFDSVDDESKPE----NHVfnlesPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHT 600
Cdd:PLN02768 575 VDPDSHPQLHVFLKQVVGLDLVDDESKPErrptKHM-----PTPAQWTNVFNPAFSYYVYYCYANLYTLNKLRESKGMTT 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 601 FVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSL 680
Cdd:PLN02768 650 IKFRPHSGEAGDIDHLAATFLTCHNIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFLRGLNVSL 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 681 STDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVG 760
Cdd:PLN02768 730 STDDPLQIHLTKEPLVEEYSIAASVWKLSSCDLCEIARNSVYQSGFSHALKSHWIGKEYYKRGPDGNDIHKTNVPHIRVE 809
|
650
....*....|...
gi 34147621 761 YRYETLCQELALI 773
Cdd:PLN02768 810 FRDTIWKEEMQQV 822
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
269-789 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 563.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 269 PDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAA--QKKVPHRDFYNIRKVDTHIHASSCMNQ 346
Cdd:PTZ00310 780 PTLTEFIRDLSELRDICSSVEVKRLATKRLENLEHKFRLHLALNHSNEAGTteERESSNRDFYQAYKVDTHIHMAAGMTA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 347 KHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAyDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFI 426
Cdd:PTZ00310 860 RQLLEFVVDKLLESGDDIAFKRGDHIVTLGQLFSKYGITP-NLTVDQLNVQADHTLFERFDNFNSKYNPMENPDLRSLLL 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 427 KTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQL 506
Cdd:PTZ00310 939 KTDNFMKGRYFAELIKDVFEQYSRDRFTYAENRLSIYGINVKEWDDLAHWFDTHGMASKHNKWMIQVPRVYKVFRAQNVI 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 507 ANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKpenhvfnLESPL----PEAWVEEDNPPYAYYLYYT 582
Cdd:PTZ00310 1019 GSFGQYLDNIFQPLWEASLHPSKHPKFHYFLNHVSGFDSVDNEAT-------IDLPFtdvsPWAWTSVENPPYNYYLYYL 1091
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 583 FANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLS 662
Cdd:PTZ00310 1092 YANIRTLNEFRASRGFSTFALRPHCGESGSMDHLYGAFLCANSICHGINLRNDPPMQYLYYLAQIGLHVSPLSNNALFLA 1171
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 663 YHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKE 742
Cdd:PTZ00310 1172 FLENPFPVFFHRGLNVSLSTDDPLMFHQTQEPLIEEYSIAARVWGLSLNDLCEIARNSVLQSGFDAAFKRNAIGDRWYLS 1251
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 34147621 743 GPEGNDIRRTNVPDIRVGYRYETLCQELALI----TQAVQSEMLETIPEEA 789
Cdd:PTZ00310 1252 SSLGNDSLRTHLSDIRVAFRFETYHTELNFLelcsGRPIPRAMKTLEEELA 1302
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
221-775 |
1.89e-91 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 314.44 E-value: 1.89e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 221 LEQHPYEHCEPST-----MPGDLGLGLRmvRGVVHVytrrepDEHCSEVELPYPdLQEFVADVNVLMALIINGPIKSFCY 295
Cdd:PTZ00310 99 TDTKVPEGEREQPsdstpMPSLVTIVQR--DGVYRF------SGMDTSVVLPPP-WEQYVRDVQAVYLTVGNGPCLSACR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 296 RRLQYLSSKFQMHVLLN-EMKELAAqkkvPHRD---FYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGR 371
Cdd:PTZ00310 170 HRLTIIQERSRMFFLLNaEIEERAD----LYKAggvFSPCTKVDNAVLLSTSVDAQELLEFVVTTYREQPRAPLRLRDGS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 372 EQTLREVFESMNL-TAYDLSVDTLDVHA--DRNTFHRFDKFNAKyNPIGE--SVLREIFIKTDNRVSGKyfahIIKEVMS 446
Cdd:PTZ00310 246 NSTLREYLEAHGVrDPRELTVEGLGWQPtkYRNKYGQYDLFDAK-NPMGAlgAELRQSFLSLHGNLCGK----LLRRELE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 447 DLEESKY--QNAELRLSIYGRSRDEWDKLARWavMHRVHS---PNVRWLVQV--PRL--FDVYRTkgqLANFQEMLENIF 517
Cdd:PTZ00310 321 RREYQKQqpQATEYSLPLYGHHPEELTDLAEW--VRRQGFgpfSRNRWILAIsfKELgpFQVPSS---CTTVQDQLDNIF 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 518 LPLFEATVHPA--SHPELHLFLEHVDGFdSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQ 595
Cdd:PTZ00310 396 LPLFKATLCPSdpQWSDVAWLLCQVGGL-QILTHAVVRSEDFDETAPDPDQVPYTAKCSDLYYFYYVYANLAVLNSLRKR 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 596 RGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSL-FLSYHRNPLPEYLSR 674
Cdd:PTZ00310 475 KGLNTLQLRPSGEKAPAYDQLISSYLLGDVITRATSIADYPVLQYLCGLHRVGLTVSPLRDHALsITAYFDHPLPKFLHR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 675 GLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKeGPEGNDIRRTNV 754
Cdd:PTZ00310 555 CLRVSISTSDPLYFHHHSQPLIEEYATAMKLFSLSPLDTTELARNSVLNSSFPPEVKQQWLGERFQL-GVEGNDFERSGV 633
|
570 580
....*....|....*....|.
gi 34147621 755 PDIRVGYRYETLCQELALITQ 775
Cdd:PTZ00310 634 TNYRLAFREEAWALEEALLND 654
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
331-738 |
1.41e-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: 217.99 E-value: 1.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 331 IRKVDTHIHASSCMNQKHLLRFIKRAmkrhleeivhveqgreqtlrevfesmnltaydlsvdtldvhadrntfhrfdkfn 410
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKKE------------------------------------------------------ 26
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 411 akynpigesvLREIFIKTDN-RVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRS-RDEWDKLARWAVMHRVHSPNVR 488
Cdd:cd00443 27 ----------FFEKFLLVHNlLQKGEALARALKEVIEEFAEDNVQYLELRTTPRLLEtEKGLTKEQYWLLVIEGISEAKQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 489 WL--VQVPRLFDVYRTKgqlanfqemleniflPLFEATVHPASHPELHLFL-EHVDGFDSVDDESKPENhvfnlesplpe 565
Cdd:cd00443 97 WFppIKVRLILSVDRRG---------------PYVQNYLVASEILELAKFLsNYVVGIDLVGDESKGEN----------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 566 awveednPPYAYYLYYtfanmamlNHLRRqrgFHTFVLRPHCGEAGPIHHLVSAFML-AENISHGLLLRKAPVLQYLYYL 644
Cdd:cd00443 151 -------PLRDFYSYY--------EYARR---LGLLGLTLHCGETGNREELLQALLLlPDRIGHGIFLLKHPELIYLVKL 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 645 AQIGIAMSPLSNNSLFL--SYHRNPLPEYLSRGLMVSLSTDDPLQFHFtkePLMEEYSIATQVWKLSSCDMCELARNSVL 722
Cdd:cd00443 213 RNIPIEVCPTSNVVLGTvqSYEKHPFMRFFKAGLPVSLSTDDPGIFGT---SLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
|
410
....*....|....*.
gi 34147621 723 MSGFSHKVKSHWLGPN 738
Cdd:cd00443 290 SSFAKDEEKKSLLEVL 305
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
569-735 |
7.31e-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: 79.36 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 569 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSA--FMLAENISHGL-LLRKAPVLQYLyylA 645
Cdd:COG1816 162 ERGFPPEKFAEAFARA---------REAGLH---LTAHAGEAGGPESIWEAldLLGAERIGHGVrAIEDPALVARL---A 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 646 --QIGIAMSPLSNNSL--FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSV 721
Cdd:COG1816 227 drGIPLEVCPTSNVQLgvVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAI 303
|
170
....*....|....
gi 34147621 722 LMSGFSHKVKSHWL 735
Cdd:COG1816 304 EASFLPEEEKAALL 317
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
569-735 |
6.73e-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: 6.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 569 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSAF--MLAENISHGLLLRKAPVLqyLYYLA- 645
Cdd:cd01320 167 EVGFPPEKFVRAFQRA---------REAGLR---LTAHAGEAGGPESVRDALdlLGAERIGHGIRAIEDPEL--VKRLAe 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 646 -QIGIAMSPLSNnsLFL----SYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNS 720
Cdd:cd01320 233 rNIPLEVCPTSN--VQTgavkSLAEHPLRELLDAGVKVTINTDDPTVFGTY---LTDEYELLAEAFGLTEEELKKLARNA 307
|
170
....*....|....*
gi 34147621 721 VLMSGFSHKVKSHWL 735
Cdd:cd01320 308 VEASFLSEEEKAELL 322
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
594-735 |
6.53e-11 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 64.43 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 594 RQRGFHtfvLRPHCGEAGP---IHHLVsAFMLAENISHGL-------LLRkapvlqylyYLA--QIGIAMSPLSNNSL-- 659
Cdd:PRK09358 192 RDAGLR---LTAHAGEAGGpesIWEAL-DELGAERIGHGVraiedpaLMA---------RLAdrRIPLEVCPTSNVQTga 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 34147621 660 FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWL 735
Cdd:PRK09358 259 VPSLAEHPLKTLLDAGVRVTINTDDPLVFGTT---LTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEEEKAALL 331
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
577-717 |
2.84e-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: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 577 YYLYYTFANMAMLNHlrrqrgfhtfVLRPHCGEAGPIHHLVSAFMLA------ENISHGLLLrkAPVLQYLYYLAQIGIA 650
Cdd:cd01292 133 ESLRRVLEEARKLGL----------PVVIHAGELPDPTRALEDLVALlrlggrVVIGHVSHL--DPELLELLKEAGVSLE 200
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 651 MSPLSNNSLFL-SYHRNPLPEYLSRGLMVSLSTDDPlqFHFTKEPLMEEYSIATQVWKL--SSCDMCELA 717
Cdd:cd01292 201 VCPLSNYLLGRdGEGAEALRRLLELGIRVTLGTDGP--PHPLGTDLLALLRLLLKVLRLglSLEEALRLA 268
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
606-727 |
3.62e-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: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 34147621 606 HCGE-----AGPIHHLVSAFML-AENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSN--NSLFLSYHRNPLPEYLSRGLM 677
Cdd:cd01321 200 HAGEtngdgTETDENLVDALLLnTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNqvLGLVSDLRNHPAAALLARGVP 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 34147621 678 VSLSTDDPLQFHFTkePLMEEYSIATQVWKLSSCDMC---ELARNSVLMSGFS 727
Cdd:cd01321 280 VVISSDDPGFWGAK--GLSHDFYQAFMGLAPADAGLRglkQLAENSIRYSALS 330
|
|
| |
