|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
109-741 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1131.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 109 PDFQRVQITGDYASGVTVEDFEIVCKGLYRALCIREKYMqksfqrFPKTPSKYLRNIDGEAWVANESFYPVFTPPVKKGE 188
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSVQGEDSTPKENDEPVFHPPPKKGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 189 DPFRTDNLPENLGYHLKMKDGVVYVYPNEAAVSKdepkPLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQ 268
Cdd:pfam19326 75 DPYELFNFPPDLGYHLRMQDGVVHVYANKDALED----SLPYPDLRDFYTDLEHLLALIADGPIKTFCHRRLQYLESKFN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 269 VHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHP 348
Cdd:pfam19326 151 LHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLKLTG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 349 YDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRS 428
Cdd:pfam19326 231 YDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESKYQMAEYRISIYGRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 429 PDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKHITGFDSV 508
Cdd:pfam19326 311 PDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPELHVFLKRVIGFDSV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 509 DDESKHSGHMFsSKSPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDI 588
Cdd:pfam19326 391 DDESKPERRMF-RKSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGDIDHLVSAFLLAHGI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 589 SHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVF 668
Cdd:pfam19326 470 SHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVW 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949468825 669 KLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLIAEGLKS 741
Cdd:pfam19326 550 KLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELALISDAVKS 622
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
236-732 |
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: 917.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 236 FLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFI 315
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 316 KKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYIN 395
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 396 GEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKML 475
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 476 ENIFMPVFEATINPQADPELSVFLKHITGFDSVDDESKhSGHMFSSKSPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLR 555
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESK-SERRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 556 KERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQ 635
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 636 KGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTN 715
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 1949468825 716 VAQIRMAYRYETWCYEL 732
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
127-735 |
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: 862.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 127 EDFEIVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEAWVANESFYPVFTPPVKKGEDP-FRTDNLPE-NLGYHL 204
Cdd:TIGR01429 1 EDLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQGYPESVPLEEGLPDFHPPPDPQEDPyCLDDDAPPiELGYLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 205 KMKDGVVYVYPNEAAVSKDEPKPLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKN 284
Cdd:TIGR01429 81 RMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEMSELKEQKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 285 NPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSLDVHAGRQT 364
Cdd:TIGR01429 161 VPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTLDVHADRNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 365 FQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWSKLSSWFVCNRI 444
Cdd:TIGR01429 241 FHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLARWIIDHDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 445 HCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKHITGFDSVDDESKHSGHMFSSKSP 524
Cdd:TIGR01429 321 FSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHEDHMFSRKFP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 525 KPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKKSPVLQYLF 604
Cdd:TIGR01429 401 SPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRKVPVLQYLY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 605 FLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVL 684
Cdd:TIGR01429 481 YLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMCELARNSVL 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1949468825 685 QCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLI 735
Cdd:TIGR01429 561 QSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
127-738 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 662.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 127 EDFEIVCKGLYRALCIREKYMQKsfqrfPKTPSkylrnidgEAWVANESFYPVFTPpvkkgeDPFRTDNLPENlGYHLKM 206
Cdd:PLN03055 6 DEEEEVCAMMQECLELRDKYLFR-----EKLPP--------WRKGIFESSTSKPNP------DPFRYEPEPPS-QHVFRM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 207 KDGVVYVYPNEAAVSKdepkPLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNP 286
Cdd:PLN03055 66 VDGVMHVYAPDDAKEE----LFPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 287 HRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSLDVHAGRQTFQ 366
Cdd:PLN03055 142 HRDFYNVRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 367 RFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWSKLSSWFVCNRIHC 446
Cdd:PLN03055 222 RFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 447 PNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKHITGFDSVDDESK----HSGHMfssk 522
Cdd:PLN03055 302 ENVVWLIQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKperrPTKHM---- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 523 sPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKKSPVLQY 602
Cdd:PLN03055 378 -QTPEQWDIPFNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQY 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 603 LFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNS 682
Cdd:PLN03055 457 LYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNS 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949468825 683 VLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLIAEG 738
Cdd:PLN03055 537 VLQSGFPHASKKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYVFLG 592
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
567-693 |
8.40e-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: 78.97 E-value: 8.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 567 PHCGEAG-------ALTHLMtafmiADDISHGLNLKKSP-VLQYLfflA--QIPIAMSPLSNNSL--FLEYAKNPFLDFL 634
Cdd:COG1816 186 AHAGEAGgpesiweALDLLG-----AERIGHGVRAIEDPaLVARL---AdrGIPLEVCPTSNVQLgvVPSLAEHPLRRLL 257
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949468825 635 QKGLMISLSTDDPMQFHFTkepLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEK 693
Cdd:COG1816 258 DAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEK 313
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
109-741 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1131.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 109 PDFQRVQITGDYASGVTVEDFEIVCKGLYRALCIREKYMqksfqrFPKTPSKYLRNIDGEAWVANESFYPVFTPPVKKGE 188
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSVQGEDSTPKENDEPVFHPPPKKGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 189 DPFRTDNLPENLGYHLKMKDGVVYVYPNEAAVSKdepkPLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQ 268
Cdd:pfam19326 75 DPYELFNFPPDLGYHLRMQDGVVHVYANKDALED----SLPYPDLRDFYTDLEHLLALIADGPIKTFCHRRLQYLESKFN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 269 VHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHP 348
Cdd:pfam19326 151 LHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLKLTG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 349 YDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRS 428
Cdd:pfam19326 231 YDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESKYQMAEYRISIYGRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 429 PDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKHITGFDSV 508
Cdd:pfam19326 311 PDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPELHVFLKRVIGFDSV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 509 DDESKHSGHMFsSKSPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDI 588
Cdd:pfam19326 391 DDESKPERRMF-RKSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGDIDHLVSAFLLAHGI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 589 SHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVF 668
Cdd:pfam19326 470 SHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVW 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1949468825 669 KLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLIAEGLKS 741
Cdd:pfam19326 550 KLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELALISDAVKS 622
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
236-732 |
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: 917.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 236 FLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFI 315
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 316 KKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYIN 395
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 396 GEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKML 475
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 476 ENIFMPVFEATINPQADPELSVFLKHITGFDSVDDESKhSGHMFSSKSPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLR 555
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESK-SERRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 556 KERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQ 635
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 636 KGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTN 715
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 1949468825 716 VAQIRMAYRYETWCYEL 732
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
127-735 |
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: 862.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 127 EDFEIVCKGLYRALCIREKYMQKSFQRFPKTPSKYLRNIDGEAWVANESFYPVFTPPVKKGEDP-FRTDNLPE-NLGYHL 204
Cdd:TIGR01429 1 EDLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQGYPESVPLEEGLPDFHPPPDPQEDPyCLDDDAPPiELGYLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 205 KMKDGVVYVYPNEAAVSKDEPKPLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKN 284
Cdd:TIGR01429 81 RMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEMSELKEQKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 285 NPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSLDVHAGRQT 364
Cdd:TIGR01429 161 VPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTLDVHADRNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 365 FQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWSKLSSWFVCNRI 444
Cdd:TIGR01429 241 FHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLARWIIDHDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 445 HCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKHITGFDSVDDESKHSGHMFSSKSP 524
Cdd:TIGR01429 321 FSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHEDHMFSRKFP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 525 KPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKKSPVLQYLF 604
Cdd:TIGR01429 401 SPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRKVPVLQYLY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 605 FLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVL 684
Cdd:TIGR01429 481 YLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMCELARNSVL 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1949468825 685 QCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLI 735
Cdd:TIGR01429 561 QSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
127-738 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 662.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 127 EDFEIVCKGLYRALCIREKYMQKsfqrfPKTPSkylrnidgEAWVANESFYPVFTPpvkkgeDPFRTDNLPENlGYHLKM 206
Cdd:PLN03055 6 DEEEEVCAMMQECLELRDKYLFR-----EKLPP--------WRKGIFESSTSKPNP------DPFRYEPEPPS-QHVFRM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 207 KDGVVYVYPNEAAVSKdepkPLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLNEMDELKELKNNP 286
Cdd:PLN03055 66 VDGVMHVYAPDDAKEE----LFPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 287 HRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMHPYDLTVDSLDVHAGRQTFQ 366
Cdd:PLN03055 142 HRDFYNVRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 367 RFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSPDEWSKLSSWFVCNRIHC 446
Cdd:PLN03055 222 RFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 447 PNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFLKHITGFDSVDDESK----HSGHMfssk 522
Cdd:PLN03055 302 ENVVWLIQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKperrPTKHM---- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 523 sPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKKSPVLQY 602
Cdd:PLN03055 378 -QTPEQWDIPFNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQY 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 603 LFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVARNS 682
Cdd:PLN03055 457 LYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNS 536
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949468825 683 VLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLIAEG 738
Cdd:PLN03055 537 VLQSGFPHASKKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYVFLG 592
|
|
| PLN02768 |
PLN02768 |
AMP deaminase |
181-738 |
0e+00 |
|
AMP deaminase
Pssm-ID: 215411 Cd Length: 835 Bit Score: 650.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 181 TPpvKKGEDPFRTDNLPENlGYHLKMKDGVVYVYPNeaavsKDEPKPL-PYPNLDTFLDDMNFLLALIAQGPVKTYTHRR 259
Cdd:PLN02768 276 TP--KPNPNPFSYTPEGKS-DHYFEMQDGVVHVYAN-----KDSKEELfPVADATTFFTDLHHILRVIAAGNIRTLCHHR 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 260 LKFLSSKFQVHQMLNEMDELKELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKE 339
Cdd:PLN02768 348 LNLLEQKFNLHLMLNADREFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGTYLTLKE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 340 LFAKLKMHPYDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLVEAKYQHAE 419
Cdd:PLN02768 428 VFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKQVFSDLEASKYQMAE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 420 PRLSIYGRSPDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQADPELSVFL 499
Cdd:PLN02768 508 YRISIYGRKQSEWDQLASWIVNNELYSENVVWLIQLPRLYNVYKEMGIVTSFQNILDNIFIPLFEVTVDPDSHPQLHVFL 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 500 KHITGFDSVDDESK----HSGHMfssksPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGAL 575
Cdd:PLN02768 588 KQVVGLDLVDDESKperrPTKHM-----PTPAQWTNVFNPAFSYYVYYCYANLYTLNKLRESKGMTTIKFRPHSGEAGDI 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 576 THLMTAFMIADDISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKE 655
Cdd:PLN02768 663 DHLAATFLTCHNIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFLRGLNVSLSTDDPLQIHLTKE 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 656 PLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLI 735
Cdd:PLN02768 743 PLVEEYSIAASVWKLSSCDLCEIARNSVYQSGFSHALKSHWIGKEYYKRGPDGNDIHKTNVPHIRVEFRDTIWKEEMQQV 822
|
...
gi 1949468825 736 AEG 738
Cdd:PLN02768 823 YLG 825
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
98-737 |
2.55e-176 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 543.64 E-value: 2.55e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 98 YIS--SSPTYQTVPDfQRVQITGDYASGVTVEDFEI-VCKGLYRALCIREKYMQKsfqrfPKTPskylrnidgeaWVANE 174
Cdd:PTZ00310 673 YISnvQEVEYDTVLD-QRVRFPRTVLYGPHKSGKAVtAAPALARALDLRHKYIWN-----PPPP-----------WETTQ 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 175 SfYPVFtppvkkgEDPFR-TDNLPENLgYHLKMKDGVVYVYPNEAAVSKdepkPLPYPNLDTFLDDMNFLLALIAQGPVK 253
Cdd:PTZ00310 736 R-NVVE-------EDFQRtTRQFNEDQ-WTYAAYDGVFILSPKGAVHAW----PRFLPTLTEFIRDLSELRDICSSVEVK 802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 254 TYTHRRLKFLSSKFQVHQMLNEMDEL--KELKNNPHRDFYNCRKVDTHIHAAACMNQKHLLRFIKKSYQIDADRVVYSTK 331
Cdd:PTZ00310 803 RLATKRLENLEHKFRLHLALNHSNEAgtTEERESSNRDFYQAYKVDTHIHMAAGMTARQLLEFVVDKLLESGDDIAFKRG 882
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 332 EKNLTLKELFAKLKMHPyDLTVDSLDVHAGRQTFQRFDKFNDKYNPVGASELRDLYLKTDNYINGEYFATIIKEVGADLV 411
Cdd:PTZ00310 883 DHIVTLGQLFSKYGITP-NLTVDQLNVQADHTLFERFDNFNSKYNPMENPDLRSLLLKTDNFMKGRYFAELIKDVFEQYS 961
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 412 EAKYQHAEPRLSIYGRSPDEWSKLSSWFVCNRIHCPNMTWMIQVPRIYDVFRSKNFLPHFGKMLENIFMPVFEATINPQA 491
Cdd:PTZ00310 962 RDRFTYAENRLSIYGINVKEWDDLAHWFDTHGMASKHNKWMIQVPRVYKVFRAQNVIGSFGQYLDNIFQPLWEASLHPSK 1041
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 492 DPELSVFLKHITGFDSVDDESKHSgHMFSSKSPkpQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGE 571
Cdd:PTZ00310 1042 HPKFHYFLNHVSGFDSVDNEATID-LPFTDVSP--WAWTSVENPPYNYYLYYLYANIRTLNEFRASRGFSTFALRPHCGE 1118
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 572 AGALTHLMTAFMIADDISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAKNPFLDFLQKGLMISLSTDDPMQFH 651
Cdd:PTZ00310 1119 SGSMDHLYGAFLCANSICHGINLRNDPPMQYLYYLAQIGLHVSPLSNNALFLAFLENPFPVFFHRGLNVSLSTDDPLMFH 1198
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 652 FTKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFLGDNYLEEGPAGNDIRRTNVAQIRMAYRYETWCYE 731
Cdd:PTZ00310 1199 QTQEPLIEEYSIAARVWGLSLNDLCEIARNSVLQSGFDAAFKRNAIGDRWYLSSSLGNDSLRTHLSDIRVAFRFETYHTE 1278
|
....*.
gi 1949468825 732 LNLIAE 737
Cdd:PTZ00310 1279 LNFLEL 1284
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
227-735 |
1.10e-75 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 267.06 E-value: 1.10e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 227 PLPYPNLDTFLDDMNFLLALIAQGPVKTYTHRRLKFLSSKFQVHQMLN-EMDElkelKNNPHRD---FYNCRKVDTHIHA 302
Cdd:PTZ00310 139 VVLPPPWEQYVRDVQAVYLTVGNGPCLSACRHRLTIIQERSRMFFLLNaEIEE----RADLYKAggvFSPCTKVDNAVLL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 303 AACMNQKHLLRFIKKSYQIDADRVVYSTKEKNLTLKELFAKLKMH-PYDLTVDSLDVHA--GRQTFQRFDKFnDKYNPVG 379
Cdd:PTZ00310 215 STSVDAQELLEFVVTTYREQPRAPLRLRDGSNSTLREYLEAHGVRdPRELTVEGLGWQPtkYRNKYGQYDLF-DAKNPMG 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 380 A--SELRDLYLKTDNYINGeyfatiiKEVGADLVEAKY-----QHAEPRLSIYGRSPDEWSKLSSWFVCNRIHC-PNMTW 451
Cdd:PTZ00310 294 AlgAELRQSFLSLHGNLCG-------KLLRRELERREYqkqqpQATEYSLPLYGHHPEELTDLAEWVRRQGFGPfSRNRW 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 452 MIQVpriydvfRSKNFLPH--------FGKMLENIFMPVFEATINPQaDPE---LSVFLKHITGFdSVDDESKHSGHMFS 520
Cdd:PTZ00310 367 ILAI-------SFKELGPFqvpsscttVQDQLDNIFLPLFKATLCPS-DPQwsdVAWLLCQVGGL-QILTHAVVRSEDFD 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 521 SKSPKPQEWTLEKNPSYTYYAYYMYANIMVLNSLRKERGMNTFLFRPHCGEAGALTHLMTAFMIADDISHGLNLKKSPVL 600
Cdd:PTZ00310 438 ETAPDPDQVPYTAKCSDLYYFYYVYANLAVLNSLRKRKGLNTLQLRPSGEKAPAYDQLISSYLLGDVITRATSIADYPVL 517
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 601 QYLFFLAQIPIAMSPLSNNSL-FLEYAKNPFLDFLQKGLMISLSTDDPMQFHFTKEPLMEEYAIAAQVFKLSTCDMCEVA 679
Cdd:PTZ00310 518 QYLCGLHRVGLTVSPLRDHALsITAYFDHPLPKFLHRCLRVSISTSDPLYFHHHSQPLIEEYATAMKLFSLSPLDTTELA 597
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1949468825 680 RNSVLQCGISHEEKVKFLGDNYlEEGPAGNDIRRTNVAQIRMAYRYETWCYELNLI 735
Cdd:PTZ00310 598 RNSVLNSSFPPEVKQQWLGERF-QLGVEGNDFERSGVTNYRLAFREEAWALEEALL 652
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
293-698 |
9.06e-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: 174.07 E-value: 9.06e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 293 CRKVDTHIHAAACMNQKHLLRFIKKSYQidadrvvystkeknltlkELFAKLkmHPYDltvdsldvhagrqtfqrfdkfn 372
Cdd:cd00443 1 LPKVELHAHLSGSISPETLLELIKKEFF------------------EKFLLV--HNLL---------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 373 dkynpvgaselrdlylktdnyINGEYFATIIKEVGADLVEAKYQHAEPRLSIYGRSP-DEWSKLSSWFVCNRIHCPNMTW 451
Cdd:cd00443 39 ---------------------QKGEALARALKEVIEEFAEDNVQYLELRTTPRLLETeKGLTKEQYWLLVIEGISEAKQW 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 452 --MIQVPRIYDVFRSknflphfgkmlenifMPVFEATINPQADPELSVFLK-HITGFDSVDDESKHSghmfsskSPKPqE 528
Cdd:cd00443 98 fpPIKVRLILSVDRR---------------GPYVQNYLVASEILELAKFLSnYVVGIDLVGDESKGE-------NPLR-D 154
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 529 WTleknpsytyyayymyaniMVLNSLRKERGMNtflFRPHCGEAGALTHLMTAFM-IADDISHGLNLKKSPVLQYLFFLA 607
Cdd:cd00443 155 FY------------------SYYEYARRLGLLG---LTLHCGETGNREELLQALLlLPDRIGHGIFLLKHPELIYLVKLR 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 608 QIPIAMSPLSNNSLFL--EYAKNPFLDFLQKGLMISLSTDDPMQFHFtkePLMEEYAIAAQVFKLSTCDMCEVARNSVLQ 685
Cdd:cd00443 214 NIPIEVCPTSNVVLGTvqSYEKHPFMRFFKAGLPVSLSTDDPGIFGT---SLSEEYSLAAKTFGLTFEDLCELNRNSVLS 290
|
410
....*....|...
gi 1949468825 686 CGISHEEKVKFLG 698
Cdd:cd00443 291 SFAKDEEKKSLLE 303
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
567-693 |
8.40e-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: 78.97 E-value: 8.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 567 PHCGEAG-------ALTHLMtafmiADDISHGLNLKKSP-VLQYLfflA--QIPIAMSPLSNNSL--FLEYAKNPFLDFL 634
Cdd:COG1816 186 AHAGEAGgpesiweALDLLG-----AERIGHGVRAIEDPaLVARL---AdrGIPLEVCPTSNVQLgvVPSLAEHPLRRLL 257
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1949468825 635 QKGLMISLSTDDPMQFHFTkepLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEK 693
Cdd:COG1816 258 DAGVRVTLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEK 313
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
556-697 |
2.63e-15 |
|
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: 77.63 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 556 KERGMNtflFRPHCGEAGALTHLMTAF--MIADDISHGLNLKKSPVLQYLFFLAQIPIAMSPLSNnsLFL----EYAKNP 629
Cdd:cd01320 183 REAGLR---LTAHAGEAGGPESVRDALdlLGAERIGHGIRAIEDPELVKRLAERNIPLEVCPTSN--VQTgavkSLAEHP 257
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949468825 630 FLDFLQKGLMISLSTDDPMQFHFTkepLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFL 697
Cdd:cd01320 258 LRELLDAGVKVTINTDDPTVFGTY---LTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEKAELL 322
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
563-693 |
7.55e-14 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 73.29 E-value: 7.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 563 FLFRPHCGEAGALTHLMTA--FMIADDISHGLNLKKSPVLqyLFFLA--QIPIAMSPLSNNSL--FLEYAKNPFLDFLQK 636
Cdd:PRK09358 196 LRLTAHAGEAGGPESIWEAldELGAERIGHGVRAIEDPAL--MARLAdrRIPLEVCPTSNVQTgaVPSLAEHPLKTLLDA 273
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1949468825 637 GLMISLSTDDPMQFHFTkepLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEK 693
Cdd:PRK09358 274 GVRVTINTDDPLVFGTT---LTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEEEK 327
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
494-697 |
4.45e-09 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 58.60 E-value: 4.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 494 ELSVFLKH--ITGFDSVDDESKHSGHMFSSkspkpqewtleknpsytyyaYYMYANIMVLNSLRkergmntflFRPHCGE 571
Cdd:pfam00962 147 ELAPRYRDqgIVAFGLAGDEKGFPPSLFRD--------------------HVEAFARARDAGLH---------LTVHAGE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 572 AGALTHLMTA--FMIADDISHGLNLKKSPVLqyLFFLA--QIPIAMSPLSN--NSLFLEYAKNPFLDFLQKGLMISLSTD 645
Cdd:pfam00962 198 AGGPQSVWEAldDLGAERIGHGVRSAEDPRL--LDRLAdrQIPLEICPTSNvqTGAVASLAEHPLKTFLRAGVPVSLNTD 275
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1949468825 646 DPMQFhftKEPLMEEYAIAAQVFKLSTCDMCEVARNSVLQCGISHEEKVKFL 697
Cdd:pfam00962 276 DPLMF---GSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPADEKRALL 324
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
554-679 |
3.48e-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: 49.25 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 554 LRKERGMntfLFRPHCGEAGALTHLMTAFMIADD------ISHGLNLkkSPVLQYLFFLAQIPIAMSPLSNNSLFLEYAK 627
Cdd:cd01292 141 EARKLGL---PVVIHAGELPDPTRALEDLVALLRlggrvvIGHVSHL--DPELLELLKEAGVSLEVCPLSNYLLGRDGEG 215
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1949468825 628 NPFLD-FLQKGLMISLSTDDPmqFHFTKEPLMEEYAIAAQVFKL--STCDMCEVA 679
Cdd:cd01292 216 AEALRrLLELGIRVTLGTDGP--PHPLGTDLLALLRLLLKVLRLglSLEEALRLA 268
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
563-697 |
5.59e-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: 42.64 E-value: 5.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949468825 563 FLFrpHCGE-----AGALTHLMTAFMI-ADDISHGLNLKKSPVLQYLFFLAQIPIAMSPLSN--NSLFLEYAKNPFLDFL 634
Cdd:cd01321 197 FFF--HAGEtngdgTETDENLVDALLLnTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNqvLGLVSDLRNHPAAALL 274
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949468825 635 QKGLMISLSTDDPMQFHFTkePLMEEY-----AIAAQVFKLSTCDMceVARNSVLQCGISHEEKVKFL 697
Cdd:cd01321 275 ARGVPVVISSDDPGFWGAK--GLSHDFyqafmGLAPADAGLRGLKQ--LAENSIRYSALSDQEKDEAV 338
|
|
| |
