|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
142-785 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1143.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 142 REFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMalslqsFCPTTRRYLQQLaekpletrtyeQGPD-TPVSADA 220
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSV-----------QGEDsTPKENDE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 221 PV-HPPALEQ-HPYEHCEPstmPGDLGLGLRMVRGVVHVYTRREpdehCSEVELPYPDLQEFVADVNVLMALIINGPIKS 298
Cdd:pfam19326 64 PVfHPPPKKGeDPYELFNF---PPDLGYHLRMQDGVVHVYANKD----ALEDSLPYPDLRDFYTDLEHLLALIADGPIKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 299 FCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGRE 378
Cdd:pfam19326 137 FCHRRLQYLESKFNLHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 379 QTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESK 458
Cdd:pfam19326 217 LTLREVFESLKLTGYDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 459 YQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPE 538
Cdd:pfam19326 297 YQMAEYRISIYGRSPDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 539 LHLFLEHVDGFDSVDDESKPENHVFNlESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGP 618
Cdd:pfam19326 377 LHVFLKRVIGFDSVDDESKPERRMFR-KSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 619 IHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTK 698
Cdd:pfam19326 456 IDHLVSAFLLAHGISHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 699 EPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELAL 778
Cdd:pfam19326 536 EPLMEEYSIAAQVWKLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELAL 615
|
....*..
gi 815890956 779 ITQAVQS 785
Cdd:pfam19326 616 ISDAVKS 622
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
280-776 |
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: 934.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 280 FVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFI 359
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 360 KRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVS 439
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 440 GKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEML 519
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 520 ENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEnHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLR 599
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESKSE-RRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 600 RQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLS 679
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 680 RGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTN 759
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 815890956 760 VPDIRVGYRYETLCQEL 776
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
161-779 |
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: 904.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 161 DLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAekPLETRTYEQGPDTPvsadapvHPPALEQHPYEHCEPSTM 240
Cdd:TIGR01429 2 DLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQG--YPESVPLEEGLPDF-------HPPPDPQEDPYCLDDDAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 241 PGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEM 320
Cdd:TIGR01429 73 PIELGYLVRMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 321 KELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTL 400
Cdd:TIGR01429 153 SELKEQKSVPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 401 DVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLA 480
Cdd:TIGR01429 233 DVHADRNTFHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 481 RWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEN 560
Cdd:TIGR01429 313 RWIIDHDVFSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 561 HVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRK 640
Cdd:TIGR01429 393 HMFSRKFPSPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 641 APVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMC 720
Cdd:TIGR01429 473 VPVLQYLYYLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMC 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 815890956 721 ELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 779
Cdd:TIGR01429 553 ELARNSVLQSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
177-779 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 767.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 177 EKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYehcepstmpgdlglglRMVRGVVH 256
Cdd:PLN03055 8 EEEVCAMMQECLELRDKYLFREKLPPWRKGIFESSTSKPNPDPFRYEPEPPSQHVF----------------RMVDGVMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 257 VYTrrePDEHCSEVeLPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYN 336
Cdd:PLN03055 72 VYA---PDDAKEEL-FPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAPHRDFYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 337 IRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFN 416
Cdd:PLN03055 148 VRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFHRFDKFN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 417 AKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWL 496
Cdd:PLN03055 228 LKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYSENVVWL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 497 VQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPlPEAWVEE 576
Cdd:PLN03055 308 IQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKPERRPTKHMQT-PEQWDIP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 577 DNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIA 656
Cdd:PLN03055 387 FNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 657 MSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKV 736
Cdd:PLN03055 467 MSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNSVLQSGFPHAS 546
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 815890956 737 KSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 779
Cdd:PLN03055 547 KKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYV 589
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
575-741 |
5.45e-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: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 575 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSA--FMLAENISHGL-LLRKAPVLQYLyylA 651
Cdd:COG1816 162 ERGFPPEKFAEAFARA---------REAGLH---LTAHAGEAGGPESIWEAldLLGAERIGHGVrAIEDPALVARL---A 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 652 --QIGIAMSPLSNNSL--FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSV 727
Cdd:COG1816 227 drGIPLEVCPTSNVQLgvVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAI 303
|
170
....*....|....
gi 815890956 728 LMSGFSHKVKSHWL 741
Cdd:COG1816 304 EASFLPEEEKAALL 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
142-785 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1143.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 142 REFQRVTISGEEKCGVPFTDLLDAAKSVVRALFIREKYMalslqsFCPTTRRYLQQLaekpletrtyeQGPD-TPVSADA 220
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSV-----------QGEDsTPKENDE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 221 PV-HPPALEQ-HPYEHCEPstmPGDLGLGLRMVRGVVHVYTRREpdehCSEVELPYPDLQEFVADVNVLMALIINGPIKS 298
Cdd:pfam19326 64 PVfHPPPKKGeDPYELFNF---PPDLGYHLRMQDGVVHVYANKD----ALEDSLPYPDLRDFYTDLEHLLALIADGPIKT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 299 FCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGRE 378
Cdd:pfam19326 137 FCHRRLQYLESKFNLHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKY 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 379 QTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESK 458
Cdd:pfam19326 217 LTLREVFESLKLTGYDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESK 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 459 YQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPE 538
Cdd:pfam19326 297 YQMAEYRISIYGRSPDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 539 LHLFLEHVDGFDSVDDESKPENHVFNlESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGP 618
Cdd:pfam19326 377 LHVFLKRVIGFDSVDDESKPERRMFR-KSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGD 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 619 IHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTK 698
Cdd:pfam19326 456 IDHLVSAFLLAHGISHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTK 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 699 EPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELAL 778
Cdd:pfam19326 536 EPLMEEYSIAAQVWKLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELAL 615
|
....*..
gi 815890956 779 ITQAVQS 785
Cdd:pfam19326 616 ISDAVKS 622
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
280-776 |
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: 934.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 280 FVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFI 359
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 360 KRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVS 439
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 440 GKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEML 519
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 520 ENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEnHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLR 599
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESKSE-RRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 600 RQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLS 679
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 680 RGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTN 759
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 815890956 760 VPDIRVGYRYETLCQEL 776
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
161-779 |
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: 904.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 161 DLLDAAKSVVRALFIREKYMALSLQSFCPTTRRYLQQLAekPLETRTYEQGPDTPvsadapvHPPALEQHPYEHCEPSTM 240
Cdd:TIGR01429 2 DLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQG--YPESVPLEEGLPDF-------HPPPDPQEDPYCLDDDAP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 241 PGDLGLGLRMVRGVVHVYTRREPDEHCSEVELPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEM 320
Cdd:TIGR01429 73 PIELGYLVRMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 321 KELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTL 400
Cdd:TIGR01429 153 SELKEQKSVPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 401 DVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLA 480
Cdd:TIGR01429 233 DVHADRNTFHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 481 RWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPEN 560
Cdd:TIGR01429 313 RWIIDHDVFSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHED 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 561 HVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRK 640
Cdd:TIGR01429 393 HMFSRKFPSPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRK 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 641 APVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMC 720
Cdd:TIGR01429 473 VPVLQYLYYLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMC 552
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 815890956 721 ELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 779
Cdd:TIGR01429 553 ELARNSVLQSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
177-779 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 767.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 177 EKYMALSLQSFCPTTRRYLQQLAEKPLETRTYEQGPDTPVSADAPVHPPALEQHPYehcepstmpgdlglglRMVRGVVH 256
Cdd:PLN03055 8 EEEVCAMMQECLELRDKYLFREKLPPWRKGIFESSTSKPNPDPFRYEPEPPSQHVF----------------RMVDGVMH 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 257 VYTrrePDEHCSEVeLPYPDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYN 336
Cdd:PLN03055 72 VYA---PDDAKEEL-FPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAPHRDFYN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 337 IRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFN 416
Cdd:PLN03055 148 VRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFHRFDKFN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 417 AKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWL 496
Cdd:PLN03055 228 LKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYSENVVWL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 497 VQVPRLFDVYRTKGQLANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKPENHVFNLESPlPEAWVEE 576
Cdd:PLN03055 308 IQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKPERRPTKHMQT-PEQWDIP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 577 DNPPYAYYLYYTFANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIA 656
Cdd:PLN03055 387 FNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYLAQIGLA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 657 MSPLSNNSLFLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKV 736
Cdd:PLN03055 467 MSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNSVLQSGFPHAS 546
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 815890956 737 KSHWLGPNYTKEGPEGNDIRRTNVPDIRVGYRYETLCQELALI 779
Cdd:PLN03055 547 KKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYV 589
|
|
| PLN02768 |
PLN02768 |
AMP deaminase |
138-779 |
0e+00 |
|
AMP deaminase
Pssm-ID: 215411 Cd Length: 835 Bit Score: 759.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 138 DVLERE-----FQRVTISGEEkcgVPFTDLLDAAKSVVRALFIREKYMalslqsfcpttrrYLQQLAekPLETRTyEQGP 212
Cdd:PLN02768 214 DILRKEpeqetFVRLNITPLE---VPSPDEVEAYKVLQECLELRKRYV-------------FREEVA--PWEKEI-ISDP 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 213 DTPVSADAPVH--PPALEQHPYEhcepstmpgdlglglrMVRGVVHVYtrrePDEHCSEVELPYPDLQEFVADVNVLMAL 290
Cdd:PLN02768 275 STPKPNPNPFSytPEGKSDHYFE----------------MQDGVVHVY----ANKDSKEELFPVADATTFFTDLHHILRV 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 291 IINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAAQKKVPHRDFYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEI 370
Cdd:PLN02768 335 IAAGNIRTLCHHRLNLLEQKFNLHLMLNADREFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEV 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 371 VHVEQGREQTLREVFESMNLTAYDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFIKTDNRVSGKYFAHIIKEV 450
Cdd:PLN02768 415 VIFRDGTYLTLKEVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKQV 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 451 MSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQLANFQEMLENIFLPLFEAT 530
Cdd:PLN02768 495 FSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNELYSENVVWLIQLPRLYNVYKEMGIVTSFQNILDNIFIPLFEVT 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 531 VHPASHPELHLFLEHVDGFDSVDDESKPE----NHVfnlesPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQRGFHT 606
Cdd:PLN02768 575 VDPDSHPQLHVFLKQVVGLDLVDDESKPErrptKHM-----PTPAQWTNVFNPAFSYYVYYCYANLYTLNKLRESKGMTT 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 607 FVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLSYHRNPLPEYLSRGLMVSL 686
Cdd:PLN02768 650 IKFRPHSGEAGDIDHLAATFLTCHNIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFLRGLNVSL 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 687 STDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKEGPEGNDIRRTNVPDIRVG 766
Cdd:PLN02768 730 STDDPLQIHLTKEPLVEEYSIAASVWKLSSCDLCEIARNSVYQSGFSHALKSHWIGKEYYKRGPDGNDIHKTNVPHIRVE 809
|
650
....*....|...
gi 815890956 767 YRYETLCQELALI 779
Cdd:PLN02768 810 FRDTIWKEEMQQV 822
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
275-795 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 561.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 275 PDLQEFVADVNVLMALIINGPIKSFCYRRLQYLSSKFQMHVLLNEMKELAA--QKKVPHRDFYNIRKVDTHIHASSCMNQ 352
Cdd:PTZ00310 780 PTLTEFIRDLSELRDICSSVEVKRLATKRLENLEHKFRLHLALNHSNEAGTteERESSNRDFYQAYKVDTHIHMAAGMTA 859
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 353 KHLLRFIKRAMKRHLEEIVHVEQGREQTLREVFESMNLTAyDLSVDTLDVHADRNTFHRFDKFNAKYNPIGESVLREIFI 432
Cdd:PTZ00310 860 RQLLEFVVDKLLESGDDIAFKRGDHIVTLGQLFSKYGITP-NLTVDQLNVQADHTLFERFDNFNSKYNPMENPDLRSLLL 938
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 433 KTDNRVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRSRDEWDKLARWAVMHRVHSPNVRWLVQVPRLFDVYRTKGQL 512
Cdd:PTZ00310 939 KTDNFMKGRYFAELIKDVFEQYSRDRFTYAENRLSIYGINVKEWDDLAHWFDTHGMASKHNKWMIQVPRVYKVFRAQNVI 1018
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 513 ANFQEMLENIFLPLFEATVHPASHPELHLFLEHVDGFDSVDDESKpenhvfnLESPL----PEAWVEEDNPPYAYYLYYT 588
Cdd:PTZ00310 1019 GSFGQYLDNIFQPLWEASLHPSKHPKFHYFLNHVSGFDSVDNEAT-------IDLPFtdvsPWAWTSVENPPYNYYLYYL 1091
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 589 FANMAMLNHLRRQRGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSLFLS 668
Cdd:PTZ00310 1092 YANIRTLNEFRASRGFSTFALRPHCGESGSMDHLYGAFLCANSICHGINLRNDPPMQYLYYLAQIGLHVSPLSNNALFLA 1171
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 669 YHRNPLPEYLSRGLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKE 748
Cdd:PTZ00310 1172 FLENPFPVFFHRGLNVSLSTDDPLMFHQTQEPLIEEYSIAARVWGLSLNDLCEIARNSVLQSGFDAAFKRNAIGDRWYLS 1251
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 815890956 749 GPEGNDIRRTNVPDIRVGYRYETLCQELALI----TQAVQSEMLETIPEEA 795
Cdd:PTZ00310 1252 SSLGNDSLRTHLSDIRVAFRFETYHTELNFLelcsGRPIPRAMKTLEEELA 1302
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
227-781 |
5.29e-91 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 313.29 E-value: 5.29e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 227 LEQHPYEHCEPST-----MPGDLGLGLRmvRGVVHVytrrepDEHCSEVELPYPdLQEFVADVNVLMALIINGPIKSFCY 301
Cdd:PTZ00310 99 TDTKVPEGEREQPsdstpMPSLVTIVQR--DGVYRF------SGMDTSVVLPPP-WEQYVRDVQAVYLTVGNGPCLSACR 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 302 RRLQYLSSKFQMHVLLN-EMKELAAqkkvPHRD---FYNIRKVDTHIHASSCMNQKHLLRFIKRAMKRHLEEIVHVEQGR 377
Cdd:PTZ00310 170 HRLTIIQERSRMFFLLNaEIEERAD----LYKAggvFSPCTKVDNAVLLSTSVDAQELLEFVVTTYREQPRAPLRLRDGS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 378 EQTLREVFESMNL-TAYDLSVDTLDVHA--DRNTFHRFDKFNAKyNPIGE--SVLREIFIKTDNRVSGKyfahIIKEVMS 452
Cdd:PTZ00310 246 NSTLREYLEAHGVrDPRELTVEGLGWQPtkYRNKYGQYDLFDAK-NPMGAlgAELRQSFLSLHGNLCGK----LLRRELE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 453 DLEESKY--QNAELRLSIYGRSRDEWDKLARWavMHRVHS---PNVRWLVQV--PRL--FDVYRTkgqLANFQEMLENIF 523
Cdd:PTZ00310 321 RREYQKQqpQATEYSLPLYGHHPEELTDLAEW--VRRQGFgpfSRNRWILAIsfKELgpFQVPSS---CTTVQDQLDNIF 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 524 LPLFEATVHPA--SHPELHLFLEHVDGFdSVDDESKPENHVFNLESPLPEAWVEEDNPPYAYYLYYTFANMAMLNHLRRQ 601
Cdd:PTZ00310 396 LPLFKATLCPSdpQWSDVAWLLCQVGGL-QILTHAVVRSEDFDETAPDPDQVPYTAKCSDLYYFYYVYANLAVLNSLRKR 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 602 RGFHTFVLRPHCGEAGPIHHLVSAFMLAENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSNNSL-FLSYHRNPLPEYLSR 680
Cdd:PTZ00310 475 KGLNTLQLRPSGEKAPAYDQLISSYLLGDVITRATSIADYPVLQYLCGLHRVGLTVSPLRDHALsITAYFDHPLPKFLHR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 681 GLMVSLSTDDPLQFHFTKEPLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWLGPNYTKeGPEGNDIRRTNV 760
Cdd:PTZ00310 555 CLRVSISTSDPLYFHHHSQPLIEEYATAMKLFSLSPLDTTELARNSVLNSSFPPEVKQQWLGERFQL-GVEGNDFERSGV 633
|
570 580
....*....|....*....|.
gi 815890956 761 PDIRVGYRYETLCQELALITQ 781
Cdd:PTZ00310 634 TNYRLAFREEAWALEEALLND 654
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
337-744 |
8.80e-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: 218.76 E-value: 8.80e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 337 IRKVDTHIHASSCMNQKHLLRFIKRAmkrhleeivhveqgreqtlrevfesmnltaydlsvdtldvhadrntfhrfdkfn 416
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKKE------------------------------------------------------ 26
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 417 akynpigesvLREIFIKTDN-RVSGKYFAHIIKEVMSDLEESKYQNAELRLSIYGRS-RDEWDKLARWAVMHRVHSPNVR 494
Cdd:cd00443 27 ----------FFEKFLLVHNlLQKGEALARALKEVIEEFAEDNVQYLELRTTPRLLEtEKGLTKEQYWLLVIEGISEAKQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 495 WL--VQVPRLFDVYRTKgqlanfqemleniflPLFEATVHPASHPELHLFL-EHVDGFDSVDDESKPENhvfnlesplpe 571
Cdd:cd00443 97 WFppIKVRLILSVDRRG---------------PYVQNYLVASEILELAKFLsNYVVGIDLVGDESKGEN----------- 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 572 awveednPPYAYYLYYtfanmamlNHLRRqrgFHTFVLRPHCGEAGPIHHLVSAFML-AENISHGLLLRKAPVLQYLYYL 650
Cdd:cd00443 151 -------PLRDFYSYY--------EYARR---LGLLGLTLHCGETGNREELLQALLLlPDRIGHGIFLLKHPELIYLVKL 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 651 AQIGIAMSPLSNNSLFL--SYHRNPLPEYLSRGLMVSLSTDDPLQFHFtkePLMEEYSIATQVWKLSSCDMCELARNSVL 728
Cdd:cd00443 213 RNIPIEVCPTSNVVLGTvqSYEKHPFMRFFKAGLPVSLSTDDPGIFGT---SLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
|
410
....*....|....*.
gi 815890956 729 MSGFSHKVKSHWLGPN 744
Cdd:cd00443 290 SSFAKDEEKKSLLEVL 305
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
575-741 |
5.45e-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: 5.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 575 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSA--FMLAENISHGL-LLRKAPVLQYLyylA 651
Cdd:COG1816 162 ERGFPPEKFAEAFARA---------REAGLH---LTAHAGEAGGPESIWEAldLLGAERIGHGVrAIEDPALVARL---A 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 652 --QIGIAMSPLSNNSL--FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSV 727
Cdd:COG1816 227 drGIPLEVCPTSNVQLgvVPSLAEHPLRRLLDAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAI 303
|
170
....*....|....
gi 815890956 728 LMSGFSHKVKSHWL 741
Cdd:COG1816 304 EASFLPEEEKAALL 317
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
575-741 |
4.04e-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: 4.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 575 EEDNPPYAYYLYYTFAnmamlnhlrRQRGFHtfvLRPHCGEAGPIHHLVSAF--MLAENISHGLLLRKAPVLqyLYYLA- 651
Cdd:cd01320 167 EVGFPPEKFVRAFQRA---------REAGLR---LTAHAGEAGGPESVRDALdlLGAERIGHGIRAIEDPEL--VKRLAe 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 652 -QIGIAMSPLSNnsLFL----SYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNS 726
Cdd:cd01320 233 rNIPLEVCPTSN--VQTgavkSLAEHPLRELLDAGVKVTINTDDPTVFGTY---LTDEYELLAEAFGLTEEELKKLARNA 307
|
170
....*....|....*
gi 815890956 727 VLMSGFSHKVKSHWL 741
Cdd:cd01320 308 VEASFLSEEEKAELL 322
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
600-741 |
4.56e-11 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 65.20 E-value: 4.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 600 RQRGFHtfvLRPHCGEAGP---IHHLVsAFMLAENISHGL-------LLRkapvlqylyYLA--QIGIAMSPLSNNSL-- 665
Cdd:PRK09358 192 RDAGLR---LTAHAGEAGGpesIWEAL-DELGAERIGHGVraiedpaLMA---------RLAdrRIPLEVCPTSNVQTga 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 815890956 666 FLSYHRNPLPEYLSRGLMVSLSTDDPLQFHFTkepLMEEYSIATQVWKLSSCDMCELARNSVLMSGFSHKVKSHWL 741
Cdd:PRK09358 259 VPSLAEHPLKTLLDAGVRVTINTDDPLVFGTT---LTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEEEKAALL 331
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
583-723 |
2.77e-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: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 583 YYLYYTFANMAMLNHlrrqrgfhtfVLRPHCGEAGPIHHLVSAFMLA------ENISHGLLLrkAPVLQYLYYLAQIGIA 656
Cdd:cd01292 133 ESLRRVLEEARKLGL----------PVVIHAGELPDPTRALEDLVALlrlggrVVIGHVSHL--DPELLELLKEAGVSLE 200
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 657 MSPLSNNSLFL-SYHRNPLPEYLSRGLMVSLSTDDPlqFHFTKEPLMEEYSIATQVWKL--SSCDMCELA 723
Cdd:cd01292 201 VCPLSNYLLGRdGEGAEALRRLLELGIRVTLGTDGP--PHPLGTDLLALLRLLLKVLRLglSLEEALRLA 268
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
612-733 |
3.86e-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: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 815890956 612 HCGE-----AGPIHHLVSAFML-AENISHGLLLRKAPVLQYLYYLAQIGIAMSPLSN--NSLFLSYHRNPLPEYLSRGLM 683
Cdd:cd01321 200 HAGEtngdgTETDENLVDALLLnTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNqvLGLVSDLRNHPAAALLARGVP 279
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 815890956 684 VSLSTDDPLQFHFTkePLMEEYSIATQVWKLSSCDMC---ELARNSVLMSGFS 733
Cdd:cd01321 280 VVISSDDPGFWGAK--GLSHDFYQAFMGLAPADAGLRglkQLAENSIRYSALS 330
|
|
| |
