|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
107-738 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1100.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 107 PDFQRVQITGDYASGVTVEDFEVVCKGLYRALCIREKYMqksfqrFPKTPSKYLRNIDGEALVGNESFYPVFTPPPKKGE 186
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSVQGEDSTPKENDEPVFHPPPKKGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 187 DPFRTEDLPANLGYHLKMKAGVIYIYPDEAAANrdepKPYPYPNLDDFLDDMNFLLALIAQGPVKTYAHRRLKFLSSKFQ 266
Cdd:pfam19326 75 DPYELFNFPPDLGYHLRMQDGVVHVYANKDALE----DSLPYPDLRDFYTDLEHLLALIADGPIKTFCHRRLQYLESKFN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 267 VHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYHIDADRVVYSTKEKSLTLKELFAKLNMHP 346
Cdd:pfam19326 151 LHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLKLTG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 347 YDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRS 426
Cdd:pfam19326 231 YDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESKYQMAEYRISIYGRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 427 PDEWNKLSSWFVCNRIYCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFLPVFEATINPQAHPDLSVFLKHITGFDSV 506
Cdd:pfam19326 311 PDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPELHVFLKRVIGFDSV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 507 DDESKHSGHMFsSKSPKPEEWTMENNPSYTYYAYYMYANITVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADNI 586
Cdd:pfam19326 391 DDESKPERRMF-RKSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGDIDHLVSAFLLAHGI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 587 SHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVF 666
Cdd:pfam19326 470 SHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVW 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907150345 667 KLSTCDMCEVARNSVLQCGISHEEKAKFLGNNYLEEGPVGNDIRRTNVAQIRMAYRYETWCYELNLIAEGLK 738
Cdd:pfam19326 550 KLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELALISDAVK 621
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
234-730 |
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: 908.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 234 FLDDMNFLLALIAQGPVKTYAHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFI 313
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 314 KKSYHIDADRVVYSTKEKSLTLKELFAKLNMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYIN 393
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 394 GEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWNKLSSWFVCNRIYCPNMTWMIQVPRIYDVFRSKNFLPHFGKML 473
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 474 ENIFLPVFEATINPQAHPDLSVFLKHITGFDSVDDESKhSGHMFSSKSPKPEEWTMENNPSYTYYAYYMYANITVLNSLR 553
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESK-SERRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 554 KERGMNTFLFRPHCGEAGALTHLMTAFMIADNISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQ 633
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 634 KGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKAKFLGNNYLEEGPVGNDIRRTN 713
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 1907150345 714 VAQIRMAYRYETWCYEL 730
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
125-733 |
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: 868.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 125 EDFEVVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEALVGNESFYPVFTPPPKKGEDPFRTEDL--PANLGYHL 202
Cdd:TIGR01429 1 EDLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQGYPESVPLEEGLPDFHPPPDPQEDPYCLDDDapPIELGYLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 203 KMKAGVIYIYPDEAAANRDEPKPYPYPNLDDFLDDMNFLLALIAQGPVKTYAHRRLKFLSSKFQVHQMLNEMDELKELKN 282
Cdd:TIGR01429 81 RMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEMSELKEQKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 283 NPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYHIDADRVVYSTKEKSLTLKELFAKLNMHPYDLTVDSLDVHAGRQT 362
Cdd:TIGR01429 161 VPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTLDVHADRNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 363 FQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWNKLSSWFVCNRI 442
Cdd:TIGR01429 241 FHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLARWIIDHDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 443 YCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFLPVFEATINPQAHPDLSVFLKHITGFDSVDDESKHSGHMFSSKSP 522
Cdd:TIGR01429 321 FSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHEDHMFSRKFP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 523 KPEEWTMENNPSYTYYAYYMYANITVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADNISHGLNLKKSPVLQYLF 602
Cdd:TIGR01429 401 SPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRKVPVLQYLY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 603 FLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVL 682
Cdd:TIGR01429 481 YLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMCELARNSVL 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1907150345 683 QCGISHEEKAKFLGNNYLEEGPVGNDIRRTNVAQIRMAYRYETWCYELNLI 733
Cdd:TIGR01429 561 QSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
125-736 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 668.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 125 EDFEVVCKGLYRALCIREKYMQKsfqrfPKTPSKYLRNIDgealvgnesfypvfTPPPKKGEDPFRTEDLPANlGYHLKM 204
Cdd:PLN03055 6 DEEEEVCAMMQECLELRDKYLFR-----EKLPPWRKGIFE--------------SSTSKPNPDPFRYEPEPPS-QHVFRM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 205 KAGVIYIYPDEAAANrdepKPYPYPNLDDFLDDMNFLLALIAQGPVKTYAHRRLKFLSSKFQVHQMLNEMDELKELKNNP 284
Cdd:PLN03055 66 VDGVMHVYAPDDAKE----ELFPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 285 HRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYHIDADRVVYSTKEKSLTLKELFAKLNMHPYDLTVDSLDVHAGRQTFQ 364
Cdd:PLN03055 142 HRDFYNVRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 365 RFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWNKLSSWFVCNRIYC 444
Cdd:PLN03055 222 RFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 445 PNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFLPVFEATINPQAHPDLSVFLKHITGFDSVDDESK----HSGHMfssk 520
Cdd:PLN03055 302 ENVVWLIQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKperrPTKHM---- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 521 sPKPEEWTMENNPSYTYYAYYMYANITVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADNISHGLNLKKSPVLQY 600
Cdd:PLN03055 378 -QTPEQWDIPFNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQY 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 601 LFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNS 680
Cdd:PLN03055 457 LYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNS 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907150345 681 VLQCGISHEEKAKFLGNNYLEEGPVGNDIRRTNVAQIRMAYRYETWCYELNLIAEG 736
Cdd:PLN03055 537 VLQSGFPHASKKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYVFLG 592
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
565-695 |
9.23e-17 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 82.05 E-value: 9.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 565 PHCGEAG-------ALTHLMtafmiADNISHGLNLKKSP-VLQYLfflA--QIPIAMSPLSNNSL--FLEYAKNPFLDFL 632
Cdd:COG1816 186 AHAGEAGgpesiweALDLLG-----AERIGHGVRAIEDPaLVARL---AdrGIPLEVCPTSNVQLgvVPSLAEHPLRRLL 257
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907150345 633 QKGLMISLSTDDPMQFHFTkepLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKAKFL 695
Cdd:COG1816 258 DAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAALL 317
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
107-738 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1100.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 107 PDFQRVQITGDYASGVTVEDFEVVCKGLYRALCIREKYMqksfqrFPKTPSKYLRNIDGEALVGNESFYPVFTPPPKKGE 186
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSVQGEDSTPKENDEPVFHPPPKKGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 187 DPFRTEDLPANLGYHLKMKAGVIYIYPDEAAANrdepKPYPYPNLDDFLDDMNFLLALIAQGPVKTYAHRRLKFLSSKFQ 266
Cdd:pfam19326 75 DPYELFNFPPDLGYHLRMQDGVVHVYANKDALE----DSLPYPDLRDFYTDLEHLLALIADGPIKTFCHRRLQYLESKFN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 267 VHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYHIDADRVVYSTKEKSLTLKELFAKLNMHP 346
Cdd:pfam19326 151 LHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLKLTG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 347 YDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRS 426
Cdd:pfam19326 231 YDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESKYQMAEYRISIYGRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 427 PDEWNKLSSWFVCNRIYCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFLPVFEATINPQAHPDLSVFLKHITGFDSV 506
Cdd:pfam19326 311 PDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPELHVFLKRVIGFDSV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 507 DDESKHSGHMFsSKSPKPEEWTMENNPSYTYYAYYMYANITVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADNI 586
Cdd:pfam19326 391 DDESKPERRMF-RKSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGDIDHLVSAFLLAHGI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 587 SHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVF 666
Cdd:pfam19326 470 SHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVW 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907150345 667 KLSTCDMCEVARNSVLQCGISHEEKAKFLGNNYLEEGPVGNDIRRTNVAQIRMAYRYETWCYELNLIAEGLK 738
Cdd:pfam19326 550 KLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELALISDAVK 621
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
234-730 |
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: 908.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 234 FLDDMNFLLALIAQGPVKTYAHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFI 313
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 314 KKSYHIDADRVVYSTKEKSLTLKELFAKLNMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYIN 393
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 394 GEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWNKLSSWFVCNRIYCPNMTWMIQVPRIYDVFRSKNFLPHFGKML 473
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 474 ENIFLPVFEATINPQAHPDLSVFLKHITGFDSVDDESKhSGHMFSSKSPKPEEWTMENNPSYTYYAYYMYANITVLNSLR 553
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESK-SERRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 554 KERGMNTFLFRPHCGEAGALTHLMTAFMIADNISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQ 633
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 634 KGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKAKFLGNNYLEEGPVGNDIRRTN 713
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 1907150345 714 VAQIRMAYRYETWCYEL 730
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
125-733 |
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: 868.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 125 EDFEVVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEALVGNESFYPVFTPPPKKGEDPFRTEDL--PANLGYHL 202
Cdd:TIGR01429 1 EDLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQGYPESVPLEEGLPDFHPPPDPQEDPYCLDDDapPIELGYLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 203 KMKAGVIYIYPDEAAANRDEPKPYPYPNLDDFLDDMNFLLALIAQGPVKTYAHRRLKFLSSKFQVHQMLNEMDELKELKN 282
Cdd:TIGR01429 81 RMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEMSELKEQKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 283 NPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYHIDADRVVYSTKEKSLTLKELFAKLNMHPYDLTVDSLDVHAGRQT 362
Cdd:TIGR01429 161 VPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTLDVHADRNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 363 FQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWNKLSSWFVCNRI 442
Cdd:TIGR01429 241 FHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLARWIIDHDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 443 YCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFLPVFEATINPQAHPDLSVFLKHITGFDSVDDESKHSGHMFSSKSP 522
Cdd:TIGR01429 321 FSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHEDHMFSRKFP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 523 KPEEWTMENNPSYTYYAYYMYANITVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADNISHGLNLKKSPVLQYLF 602
Cdd:TIGR01429 401 SPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRKVPVLQYLY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 603 FLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVL 682
Cdd:TIGR01429 481 YLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMCELARNSVL 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1907150345 683 QCGISHEEKAKFLGNNYLEEGPVGNDIRRTNVAQIRMAYRYETWCYELNLI 733
Cdd:TIGR01429 561 QSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
125-736 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 668.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 125 EDFEVVCKGLYRALCIREKYMQKsfqrfPKTPSKYLRNIDgealvgnesfypvfTPPPKKGEDPFRTEDLPANlGYHLKM 204
Cdd:PLN03055 6 DEEEEVCAMMQECLELRDKYLFR-----EKLPPWRKGIFE--------------SSTSKPNPDPFRYEPEPPS-QHVFRM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 205 KAGVIYIYPDEAAANrdepKPYPYPNLDDFLDDMNFLLALIAQGPVKTYAHRRLKFLSSKFQVHQMLNEMDELKELKNNP 284
Cdd:PLN03055 66 VDGVMHVYAPDDAKE----ELFPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 285 HRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYHIDADRVVYSTKEKSLTLKELFAKLNMHPYDLTVDSLDVHAGRQTFQ 364
Cdd:PLN03055 142 HRDFYNVRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 365 RFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWNKLSSWFVCNRIYC 444
Cdd:PLN03055 222 RFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 445 PNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFLPVFEATINPQAHPDLSVFLKHITGFDSVDDESK----HSGHMfssk 520
Cdd:PLN03055 302 ENVVWLIQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKperrPTKHM---- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 521 sPKPEEWTMENNPSYTYYAYYMYANITVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADNISHGLNLKKSPVLQY 600
Cdd:PLN03055 378 -QTPEQWDIPFNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQY 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 601 LFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNS 680
Cdd:PLN03055 457 LYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNS 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1907150345 681 VLQCGISHEEKAKFLGNNYLEEGPVGNDIRRTNVAQIRMAYRYETWCYELNLIAEG 736
Cdd:PLN03055 537 VLQSGFPHASKKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYVFLG 592
|
|
| PLN02768 |
PLN02768 |
AMP deaminase |
182-736 |
0e+00 |
|
AMP deaminase
Pssm-ID: 215411 Cd Length: 835 Bit Score: 655.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 182 PKKGEDPFrTEDLPANLGYHLKMKAGVIYIYPDEAAANRdepkPYPYPNLDDFLDDMNFLLALIAQGPVKTYAHRRLKFL 261
Cdd:PLN02768 277 PKPNPNPF-SYTPEGKSDHYFEMQDGVVHVYANKDSKEE----LFPVADATTFFTDLHHILRVIAAGNIRTLCHHRLNLL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 262 SSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYHIDADRVVYSTKEKSLTLKELFAK 341
Cdd:PLN02768 352 EQKFNLHLMLNADREFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGTYLTLKEVFES 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 342 LNMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLS 421
Cdd:PLN02768 432 LDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKQVFSDLEASKYQMAEYRIS 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 422 IYGRSPDEWNKLSSWFVCNRIYCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFLPVFEATINPQAHPDLSVFLKHIT 501
Cdd:PLN02768 512 IYGRKQSEWDQLASWIVNNELYSENVVWLIQLPRLYNVYKEMGIVTSFQNILDNIFIPLFEVTVDPDSHPQLHVFLKQVV 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 502 GFDSVDDESK----HSGHMfssksPKPEEWTMENNPSYTYYAYYMYANITVLNSLRKERGMNTFLFRPHCGEAGALTHLM 577
Cdd:PLN02768 592 GLDLVDDESKperrPTKHM-----PTPAQWTNVFNPAFSYYVYYCYANLYTLNKLRESKGMTTIKFRPHSGEAGDIDHLA 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 578 TAFMIADNISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLME 657
Cdd:PLN02768 667 ATFLTCHNIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFLRGLNVSLSTDDPLQIHLTKEPLVE 746
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907150345 658 EYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKAKFLGNNYLEEGPVGNDIRRTNVAQIRMAYRYETWCYELNLIAEG 736
Cdd:PLN02768 747 EYSIAASVWKLSSCDLCEIARNSVYQSGFSHALKSHWIGKEYYKRGPDGNDIHKTNVPHIRVEFRDTIWKEEMQQVYLG 825
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
1-735 |
5.46e-177 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 545.18 E-value: 5.46e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 1 MPLFKLTEIDD---AMRSFAEKVFASEVKDE--GGRH----EISPFDVDEICPISLHEMQAHIFHMENLSMDGRrkrrfq 71
Cdd:PTZ00310 583 MKLFSLSPLDTtelARNSVLNSSFPPEVKQQwlGERFqlgvEGNDFERSGVTNYRLAFREEAWALEEALLNDLL------ 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 72 grktVNLSIPQSETSSTKLSHIEefISSSPTYESVPDfQRVQITGDYASGVTVEDFEV-VCKGLYRALCIREKYmqksfq 150
Cdd:PTZ00310 657 ----LNVPSGDSGAGPSRWHYIS--NVQEVEYDTVLD-QRVRFPRTVLYGPHKSGKAVtAAPALARALDLRHKY------ 723
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 151 rfpktpskylrnidgealVGNESFYPVFTPPPKKGEDPFRTEDLPANLGYHLKMKAGVIYIYPdeaaANRDEPKPYPYPN 230
Cdd:PTZ00310 724 ------------------IWNPPPPWETTQRNVVEEDFQRTTRQFNEDQWTYAAYDGVFILSP----KGAVHAWPRFLPT 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 231 LDDFLDDMNFLLALIAQGPVKTYAHRRLKFLSSKFQVHQMLNEMDEL--KELKNNPHRDFYNCRKVDTHIHAAACMNQKH 308
Cdd:PTZ00310 782 LTEFIRDLSELRDICSSVEVKRLATKRLENLEHKFRLHLALNHSNEAgtTEERESSNRDFYQAYKVDTHIHMAAGMTARQ 861
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 309 LLRFIKKSYHIDADRVVYSTKEKSLTLKELFAKLNMHPyDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKT 388
Cdd:PTZ00310 862 LLEFVVDKLLESGDDIAFKRGDHIVTLGQLFSKYGITP-NLTVDQLNVQADHTLFERFDNFNSKYNPMENPDLRSLLLKT 940
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 389 DNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWNKLSSWFVCNRIYCPNMTWMIQVPRIYDVFRSKNFLPH 468
Cdd:PTZ00310 941 DNFMKGRYFAELIKDVFEQYSRDRFTYAENRLSIYGINVKEWDDLAHWFDTHGMASKHNKWMIQVPRVYKVFRAQNVIGS 1020
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 469 FGKMLENIFLPVFEATINPQAHPDLSVFLKHITGFDSVDDESKHSgHMFSSKSPkpEEWTMENNPSYTYYAYYMYANITV 548
Cdd:PTZ00310 1021 FGQYLDNIFQPLWEASLHPSKHPKFHYFLNHVSGFDSVDNEATID-LPFTDVSP--WAWTSVENPPYNYYLYYLYANIRT 1097
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 549 LNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADNISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPF 628
Cdd:PTZ00310 1098 LNEFRASRGFSTFALRPHCGESGSMDHLYGAFLCANSICHGINLRNDPPMQYLYYLAQIGLHVSPLSNNALFLAFLENPF 1177
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 629 LDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKAKFLGNNYLEEGPVGND 708
Cdd:PTZ00310 1178 PVFFHRGLNVSLSTDDPLMFHQTQEPLIEEYSIAARVWGLSLNDLCEIARNSVLQSGFDAAFKRNAIGDRWYLSSSLGND 1257
|
730 740
....*....|....*....|....*..
gi 1907150345 709 IRRTNVAQIRMAYRYETWCYELNLIAE 735
Cdd:PTZ00310 1258 SLRTHLSDIRVAFRFETYHTELNFLEL 1284
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
234-733 |
3.40e-76 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 268.60 E-value: 3.40e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 234 FLDDMNFLLALIAQGPVKTYAHRRLKFLSSKFQVHQMLN-EMDElkelKNNPHRD---FYNCRKVDTHIHAAACMNQKHL 309
Cdd:PTZ00310 148 YVRDVQAVYLTVGNGPCLSACRHRLTIIQERSRMFFLLNaEIEE----RADLYKAggvFSPCTKVDNAVLLSTSVDAQEL 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 310 LRFIKKSYHIDADRVVYSTKEKSLTLKELFAKLNMH-PYDLTVDSLDVHA--GRQTFQRFDKFnDKYNPVGA--SELRDL 384
Cdd:PTZ00310 224 LEFVVTTYREQPRAPLRLRDGSNSTLREYLEAHGVRdPRELTVEGLGWQPtkYRNKYGQYDLF-DAKNPMGAlgAELRQS 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 385 YLKTDNYINGeyfatiiKEVGADLVEAKY-----QHAEPRLSIYGRSPDEWNKLSSWFVCNRI--YCPNMtWMIQVpriy 457
Cdd:PTZ00310 303 FLSLHGNLCG-------KLLRRELERREYqkqqpQATEYSLPLYGHHPEELTDLAEWVRRQGFgpFSRNR-WILAI---- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 458 dvfRSKNFLPH--------FGKMLENIFLPVFEATINPQA--HPDLSVFLKHITGFdSVDDESKHSGHMFSSKSPKPEEW 527
Cdd:PTZ00310 371 ---SFKELGPFqvpsscttVQDQLDNIFLPLFKATLCPSDpqWSDVAWLLCQVGGL-QILTHAVVRSEDFDETAPDPDQV 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 528 TMENNPSYTYYAYYMYANITVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADNISHGLNLKKSPVLQYLFFLAQI 607
Cdd:PTZ00310 447 PYTAKCSDLYYFYYVYANLAVLNSLRKRKGLNTLQLRPSGEKAPAYDQLISSYLLGDVITRATSIADYPVLQYLCGLHRV 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 608 PIAMSPLSNNSL-FLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGI 686
Cdd:PTZ00310 527 GLTVSPLRDHALsITAYFDHPLPKFLHRCLRVSISTSDPLYFHHHSQPLIEEYATAMKLFSLSPLDTTELARNSVLNSSF 606
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1907150345 687 SHEEKAKFLGNNYlEEGPVGNDIRRTNVAQIRMAYRYETWCYELNLI 733
Cdd:PTZ00310 607 PPEVKQQWLGERF-QLGVEGNDFERSGVTNYRLAFREEAWALEEALL 652
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
291-696 |
3.91e-49 |
|
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: 174.84 E-value: 3.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 291 CRKVDTHIHAAACMNQKHLLRFIKKSYhidadrvvystkeksltlkelfaklnmhpydltvdsldvhagrqtFQRFDKFn 370
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKKEF---------------------------------------------FEKFLLV- 34
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 371 dkynpvgaselrdlylktDNY-INGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSP-DEWNKLSSWFVCNRIYCPNMT 448
Cdd:cd00443 35 ------------------HNLlQKGEALARALKEVIEEFAEDNVQYLELRTTPRLLETeKGLTKEQYWLLVIEGISEAKQ 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 449 W--MIQVPRIYDVFRSKnflphfgkmleniflPVFEATINPQAHPDLSVFLK-HITGFDSVDDESKHSGhmfsskspKPE 525
Cdd:cd00443 97 WfpPIKVRLILSVDRRG---------------PYVQNYLVASEILELAKFLSnYVVGIDLVGDESKGEN--------PLR 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 526 EWTMEnnpsytyyayymyanitvLNSLRKERGMNtflFRPHCGEAGALTHLMTAFM-IADNISHGLNLKKSPVLQYLFFL 604
Cdd:cd00443 154 DFYSY------------------YEYARRLGLLG---LTLHCGETGNREELLQALLlLPDRIGHGIFLLKHPELIYLVKL 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 605 AQIPIAMSPLSNNSLFL--EYAKNPFLDFLQKGLMISLSTDDPMQFHFtkePLMEEYAIAAQVFKLSTCDMCEVARNSVL 682
Cdd:cd00443 213 RNIPIEVCPTSNVVLGTvqSYEKHPFMRFFKAGLPVSLSTDDPGIFGT---SLSEEYSLAAKTFGLTFEDLCELNRNSVL 289
|
410
....*....|....
gi 1907150345 683 QCGISHEEKAKFLG 696
Cdd:cd00443 290 SSFAKDEEKKSLLE 303
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
565-695 |
9.23e-17 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 82.05 E-value: 9.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 565 PHCGEAG-------ALTHLMtafmiADNISHGLNLKKSP-VLQYLfflA--QIPIAMSPLSNNSL--FLEYAKNPFLDFL 632
Cdd:COG1816 186 AHAGEAGgpesiweALDLLG-----AERIGHGVRAIEDPaLVARL---AdrGIPLEVCPTSNVQLgvVPSLAEHPLRRLL 257
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907150345 633 QKGLMISLSTDDPMQFHFTkepLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKAKFL 695
Cdd:COG1816 258 DAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAALL 317
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
554-695 |
4.85e-16 |
|
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: 79.94 E-value: 4.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 554 KERGMNtflFRPHCGEAGALTHLMTAF--MIADNISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNnsLFL----EYAKNP 627
Cdd:cd01320 183 REAGLR---LTAHAGEAGGPESVRDALdlLGAERIGHGIRAIEDPELVKRLAERNIPLEVCPTSN--VQTgavkSLAEHP 257
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907150345 628 FLDFLQKGLMISLSTDDPMQFHFTkepLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKAKFL 695
Cdd:cd01320 258 LRELLDAGVKVTINTDDPTVFGTY---LTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEKAELL 322
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
561-695 |
1.10e-14 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 75.98 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 561 FLFRPHCGEAGALTHLMTA--FMIADNISHGLNLKKSPVLqyLFFLA--QIPIAMSPLSNNSL--FLEYAKNPFLDFLQK 634
Cdd:PRK09358 196 LRLTAHAGEAGGPESIWEAldELGAERIGHGVRAIEDPAL--MARLAdrRIPLEVCPTSNVQTgaVPSLAEHPLKTLLDA 273
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907150345 635 GLMISLSTDDPMQFHFTkepLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKAKFL 695
Cdd:PRK09358 274 GVRVTINTDDPLVFGTT---LTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEEEKAALL 331
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
562-695 |
1.93e-09 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 59.75 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 562 LFRPHCGEAGALTHLMTA--FMIADNISHGLNLKKSPVLqyLFFLA--QIPIAMSPLSN--NSLFLEYAKNPFLDFLQKG 635
Cdd:pfam00962 190 HLTVHAGEAGGPQSVWEAldDLGAERIGHGVRSAEDPRL--LDRLAdrQIPLEICPTSNvqTGAVASLAEHPLKTFLRAG 267
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 636 LMISLSTDDPMQFhftKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKAKFL 695
Cdd:pfam00962 268 VPVSLNTDDPLMF---GSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPADEKRALL 324
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
552-677 |
1.05e-06 |
|
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: 50.79 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 552 LRKERGMntfLFRPHCGEAGALTHLMTAFM------IADNISHGLNLkkSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAK 625
Cdd:cd01292 141 EARKLGL---PVVIHAGELPDPTRALEDLVallrlgGRVVIGHVSHL--DPELLELLKEAGVSLEVCPLSNYLLGRDGEG 215
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1907150345 626 NPFLD-FLQKGLMISLSTDDPmqFHFTKEPLMEEYAIAAQVFKL--STCDMCEVA 677
Cdd:cd01292 216 AEALRrLLELGIRVTLGTDGP--PHPLGTDLLALLRLLLKVLRLglSLEEALRLA 268
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
545-695 |
2.32e-04 |
|
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: 44.19 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 545 NITVLNSLRKERGMNTFLFrpHCGE-----AGALTHLMTAFMI-ADNISHGLNLKKSPVLQYLFFLAQIPIAMSPLSN-- 616
Cdd:cd01321 181 FLPQLLWFPKQCAEIPFFF--HAGEtngdgTETDENLVDALLLnTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNqv 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907150345 617 NSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTkePLMEEY-----AIAAQVFKLSTCDMceVARNSVLQCGISHEEK 691
Cdd:cd01321 259 LGLVSDLRNHPAAALLARGVPVVISSDDPGFWGAK--GLSHDFyqafmGLAPADAGLRGLKQ--LAENSIRYSALSDQEK 334
|
....
gi 1907150345 692 AKFL 695
Cdd:cd01321 335 DEAV 338
|
|
| |
