|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
139-771 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1069.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 139 PEFQRVTISGDYCAGITVEDYEQAAKSLLTALFIREKYSrlayhrFPRTAAKFLRSANNEKWSEDEEVLPDICPSPSEGE 218
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSVQGEDSTPKENDEPVFHPPPKKGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 219 DPYSMEDLPQNLNYSLKMKDGIIYVYDNEDALKQdlprSLPYPDLETFAIDLSHVLAMIADGPTKTYCHRRLNFLTSKFQ 298
Cdd:pfam19326 75 DPYELFNFPPDLGYHLRMQDGVVHVYANKDALED----SLPYPDLRDFYTDLEHLLALIADGPIKTFCHRRLQYLESKFN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 299 LHEMLNEMAELKELKCVPHRDFYNVRKVDTHIHAAACMNQKHLLKFIQDSYQTEADRVVLEKGGKKFTLKQVFENLKMDP 378
Cdd:pfam19326 151 LHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLKLTG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 379 YDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGANELREIYLKTDNYINGEYFARLIKEVAHDLEESKYQHAEPRLSIYGRA 458
Cdd:pfam19326 231 YDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESKYQMAEYRISIYGRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 459 PEEWESLSKWFIMQKLHSPNMRWMIQVPRIYDIFRSKKIIANFAKMLENIFLPLFQATVNPQKHKEMHVFLKHVTGFDSV 538
Cdd:pfam19326 311 PDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPELHVFLKRVIGFDSV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 539 DDESKHSDHIFNyKSPKPEEWTSEENPPYTYYLFHMYANIMVLNNLRKERGLNTFLFRPHCGEAGSITHLVSAFLTADNI 618
Cdd:pfam19326 391 DDESKPERRMFR-KSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGDIDHLVSAFLLAHGI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 619 SHGLNLKKSPVLQYLYYLAQVPIAMSPLSNNSLFLEYSKNPLREFLQKGLCVSLSTDDPLQFHYTKEALMEEYAIAAQLW 698
Cdd:pfam19326 470 SHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVW 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207133710 699 KLSTCDTCEIARNSVLQSGLSHQEKKYFLGEKYLDDGPEGNDIRKTNVAQIRMAYRHETLCNELSFLVEAVKS 771
Cdd:pfam19326 550 KLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELALISDAVKS 622
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
157-765 |
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: 975.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 157 EDYEQAAKSLLTALFIREKYSRLAYHRFPRTAAKFLRSANNEKWSEDEEVLPDICPSPSEGEDPYSMEDL--PQNLNYSL 234
Cdd:TIGR01429 1 EDLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQGYPESVPLEEGLPDFHPPPDPQEDPYCLDDDapPIELGYLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 235 KMKDGIIYVYDNEDALKQDLPRSLPYPDLETFAIDLSHVLAMIADGPTKTYCHRRLNFLTSKFQLHEMLNEMAELKELKC 314
Cdd:TIGR01429 81 RMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEMSELKEQKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 315 VPHRDFYNVRKVDTHIHAAACMNQKHLLKFIQDSYQTEADRVVLEKGGKKFTLKQVFENLKMDPYDLTVDSLDVHAGRQT 394
Cdd:TIGR01429 161 VPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTLDVHADRNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 395 FHRFDKFNSKYNPVGANELREIYLKTDNYINGEYFARLIKEVAHDLEESKYQHAEPRLSIYGRAPEEWESLSKWFIMQKL 474
Cdd:TIGR01429 241 FHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLARWIIDHDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 475 HSPNMRWMIQVPRIYDIFRSKKIIANFAKMLENIFLPLFQATVNPQKHKEMHVFLKHVTGFDSVDDESKHSDHIFNYKSP 554
Cdd:TIGR01429 321 FSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHEDHMFSRKFP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 555 KPEEWTSEENPPYTYYLFHMYANIMVLNNLRKERGLNTFLFRPHCGEAGSITHLVSAFLTADNISHGLNLKKSPVLQYLY 634
Cdd:TIGR01429 401 SPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRKVPVLQYLY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 635 YLAQVPIAMSPLSNNSLFLEYSKNPLREFLQKGLCVSLSTDDPLQFHYTKEALMEEYAIAAQLWKLSTCDTCEIARNSVL 714
Cdd:TIGR01429 481 YLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMCELARNSVL 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1207133710 715 QSGLSHQEKKYFLGEKYLDDGPEGNDIRKTNVAQIRMAYRHETLCNELSFL 765
Cdd:TIGR01429 561 QSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
266-762 |
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: 969.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 266 FAIDLSHVLAMIADGPTKTYCHRRLNFLTSKFQLHEMLNEMAELKELKCVPHRDFYNVRKVDTHIHAAACMNQKHLLKFI 345
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 346 QDSYQTEADRVVLEKGGKKFTLKQVFENLKMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGANELREIYLKTDNYIN 425
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 426 GEYFARLIKEVAHDLEESKYQHAEPRLSIYGRAPEEWESLSKWFIMQKLHSPNMRWMIQVPRIYDIFRSKKIIANFAKML 505
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 506 ENIFLPLFQATVNPQKHKEMHVFLKHVTGFDSVDDESKhSDHIFNYKSPKPEEWTSEENPPYTYYLFHMYANIMVLNNLR 585
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESK-SERRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 586 KERGLNTFLFRPHCGEAGSITHLVSAFLTADNISHGLNLKKSPVLQYLYYLAQVPIAMSPLSNNSLFLEYSKNPLREFLQ 665
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 666 KGLCVSLSTDDPLQFHYTKEALMEEYAIAAQLWKLSTCDTCEIARNSVLQSGLSHQEKKYFLGEKYLDDGPEGNDIRKTN 745
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 1207133710 746 VAQIRMAYRHETLCNEL 762
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| PLN02768 |
PLN02768 |
AMP deaminase |
203-762 |
0e+00 |
|
AMP deaminase
Pssm-ID: 215411 Cd Length: 835 Bit Score: 718.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 203 DEEVLPDICpSPSEGEDPYSMEDLPQNLNYsLKMKDGIIYVYDNEDAlKQDLprsLPYPDLETFAIDLSHVLAMIADGPT 282
Cdd:PLN02768 267 EKEIISDPS-TPKPNPNPFSYTPEGKSDHY-FEMQDGVVHVYANKDS-KEEL---FPVADATTFFTDLHHILRVIAAGNI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 283 KTYCHRRLNFLTSKFQLHEMLNEMAELKELKCVPHRDFYNVRKVDTHIHAAACMNQKHLLKFIQDSYQTEADRVVLEKGG 362
Cdd:PLN02768 341 RTLCHHRLNLLEQKFNLHLMLNADREFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDG 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 363 KKFTLKQVFENLKMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGANELREIYLKTDNYINGEYFARLIKEVAHDLEE 442
Cdd:PLN02768 421 TYLTLKEVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKQVFSDLEA 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 443 SKYQHAEPRLSIYGRAPEEWESLSKWFIMQKLHSPNMRWMIQVPRIYDIFRSKKIIANFAKMLENIFLPLFQATVNPQKH 522
Cdd:PLN02768 501 SKYQMAEYRISIYGRKQSEWDQLASWIVNNELYSENVVWLIQLPRLYNVYKEMGIVTSFQNILDNIFIPLFEVTVDPDSH 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 523 KEMHVFLKHVTGFDSVDDESK----HSDHIfnyksPKPEEWTSEENPPYTYYLFHMYANIMVLNNLRKERGLNTFLFRPH 598
Cdd:PLN02768 581 PQLHVFLKQVVGLDLVDDESKperrPTKHM-----PTPAQWTNVFNPAFSYYVYYCYANLYTLNKLRESKGMTTIKFRPH 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 599 CGEAGSITHLVSAFLTADNISHGLNLKKSPVLQYLYYLAQVPIAMSPLSNNSLFLEYSKNPLREFLQKGLCVSLSTDDPL 678
Cdd:PLN02768 656 SGEAGDIDHLAATFLTCHNIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFLRGLNVSLSTDDPL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 679 QFHYTKEALMEEYAIAAQLWKLSTCDTCEIARNSVLQSGLSHQEKKYFLGEKYLDDGPEGNDIRKTNVAQIRMAYRHETL 758
Cdd:PLN02768 736 QIHLTKEPLVEEYSIAASVWKLSSCDLCEIARNSVYQSGFSHALKSHWIGKEYYKRGPDGNDIHKTNVPHIRVEFRDTIW 815
|
....
gi 1207133710 759 CNEL 762
Cdd:PLN02768 816 KEEM 819
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
597-729 |
2.32e-18 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 87.06 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 597 PHCGEAGSITHLVSA--FLTADNISHGLNLKKSPVLqyLYYLA--QVPIAMSPLSNNSL--FLEYSKNPLREFLQKGLCV 670
Cdd:COG1816 186 AHAGEAGGPESIWEAldLLGAERIGHGVRAIEDPAL--VARLAdrGIPLEVCPTSNVQLgvVPSLAEHPLRRLLDAGVRV 263
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207133710 671 SLSTDDPLQFHYTkeaLMEEYAIAAQLWKLSTCDTCEIARNSVLQSGLSHQEKKYFLGE 729
Cdd:COG1816 264 TLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAALLAE 319
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| AMP_deaminase |
pfam19326 |
AMP deaminase; |
139-771 |
0e+00 |
|
AMP deaminase;
Pssm-ID: 437158 [Multi-domain] Cd Length: 622 Bit Score: 1069.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 139 PEFQRVTISGDYCAGITVEDYEQAAKSLLTALFIREKYSrlayhrFPRTAAKFLRSANNEKWSEDEEVLPDICPSPSEGE 218
Cdd:pfam19326 1 PEVQRVTISGDYKLGVPTEDLEEAYKSLAECLEIREKYM------FPETTAPYLKSVQGEDSTPKENDEPVFHPPPKKGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 219 DPYSMEDLPQNLNYSLKMKDGIIYVYDNEDALKQdlprSLPYPDLETFAIDLSHVLAMIADGPTKTYCHRRLNFLTSKFQ 298
Cdd:pfam19326 75 DPYELFNFPPDLGYHLRMQDGVVHVYANKDALED----SLPYPDLRDFYTDLEHLLALIADGPIKTFCHRRLQYLESKFN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 299 LHEMLNEMAELKELKCVPHRDFYNVRKVDTHIHAAACMNQKHLLKFIQDSYQTEADRVVLEKGGKKFTLKQVFENLKMDP 378
Cdd:pfam19326 151 LHLMLNEMKELKAQKSNPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLKLTG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 379 YDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGANELREIYLKTDNYINGEYFARLIKEVAHDLEESKYQHAEPRLSIYGRA 458
Cdd:pfam19326 231 YDLSVDTLDVHADRDTFHRFDKFNLKYNPIGESRLREIFLKTDNYINGRYLAEITKEVFSDLEESKYQMAEYRISIYGRS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 459 PEEWESLSKWFIMQKLHSPNMRWMIQVPRIYDIFRSKKIIANFAKMLENIFLPLFQATVNPQKHKEMHVFLKHVTGFDSV 538
Cdd:pfam19326 311 PDEWDKLASWIVDNKVYSPNVRWLIQVPRLYDIYKKKGIVPSFQKMLENIFLPLFEATVNPQSHPELHVFLKRVIGFDSV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 539 DDESKHSDHIFNyKSPKPEEWTSEENPPYTYYLFHMYANIMVLNNLRKERGLNTFLFRPHCGEAGSITHLVSAFLTADNI 618
Cdd:pfam19326 391 DDESKPERRMFR-KSPKPALWTNEQNPPYSYYLYYMYANIAVLNSLRKERGFNTFVLRPHCGEAGDIDHLVSAFLLAHGI 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 619 SHGLNLKKSPVLQYLYYLAQVPIAMSPLSNNSLFLEYSKNPLREFLQKGLCVSLSTDDPLQFHYTKEALMEEYAIAAQLW 698
Cdd:pfam19326 470 SHGILLRKSPVLQYLYYLAQIGIAMSPLSNNSLFLEYHKNPFPEFFKRGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVW 549
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207133710 699 KLSTCDTCEIARNSVLQSGLSHQEKKYFLGEKYLDDGPEGNDIRKTNVAQIRMAYRHETLCNELSFLVEAVKS 771
Cdd:pfam19326 550 KLSACDMCELARNSVLQSGFSHQLKSHWLGKDYYKEGPEGNDIRRTNVPDIRVAYRYETLCQELALISDAVKS 622
|
|
| AMP_deaminase |
TIGR01429 |
AMP deaminase; This model describes AMP deaminase, a large, well-conserved eukaryotic protein ... |
157-765 |
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: 975.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 157 EDYEQAAKSLLTALFIREKYSRLAYHRFPRTAAKFLRSANNEKWSEDEEVLPDICPSPSEGEDPYSMEDL--PQNLNYSL 234
Cdd:TIGR01429 1 EDLAEAAKSLAKALMLREKYARLAYHRFPDTTAQYLSHQGYPESVPLEEGLPDFHPPPDPQEDPYCLDDDapPIELGYLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 235 KMKDGIIYVYDNEDALKQDLPRSLPYPDLETFAIDLSHVLAMIADGPTKTYCHRRLNFLTSKFQLHEMLNEMAELKELKC 314
Cdd:TIGR01429 81 RMHGGVLFVYDNDTMLERQEPHFLVPPTLETYYVDMEHLLALISDGPTKSFCFRRLQYLESKFNLHELLNEMSELKEQKS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 315 VPHRDFYNVRKVDTHIHAAACMNQKHLLKFIQDSYQTEADRVVLEKGGKKFTLKQVFENLKMDPYDLTVDSLDVHAGRQT 394
Cdd:TIGR01429 161 VPHRDFYNVRKVDTHIHAAASMNQKHLLRFIKHKLKTEPDETVIERDGKKLTLREVFDSLHLDPYDLSVDTLDVHADRNT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 395 FHRFDKFNSKYNPVGANELREIYLKTDNYINGEYFARLIKEVAHDLEESKYQHAEPRLSIYGRAPEEWESLSKWFIMQKL 474
Cdd:TIGR01429 241 FHRFDKFNLKYNPVGESRLREIFLKTDNYIGGKYFAELVKEVFTDLEDSKYQYAEPRLSIYGRSPKEWDSLARWIIDHDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 475 HSPNMRWMIQVPRIYDIFRSKKIIANFAKMLENIFLPLFQATVNPQKHKEMHVFLKHVTGFDSVDDESKHSDHIFNYKSP 554
Cdd:TIGR01429 321 FSPNVRWLIQVPRLYDVYRSKKLVPNFGDMLENVFLPLFEVTKDPSSHPELHLFLQQVTGFDSVDDESKHEDHMFSRKFP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 555 KPEEWTSEENPPYTYYLFHMYANIMVLNNLRKERGLNTFLFRPHCGEAGSITHLVSAFLTADNISHGLNLKKSPVLQYLY 634
Cdd:TIGR01429 401 SPDEWTSEQNPPYSYYLYYMYANIMVLNNFRRERGLNTFLLRPHCGEAGSVDHLVSAFLTSHGINHGILLRKVPVLQYLY 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 635 YLAQVPIAMSPLSNNSLFLEYSKNPLREFLQKGLCVSLSTDDPLQFHYTKEALMEEYAIAAQLWKLSTCDTCEIARNSVL 714
Cdd:TIGR01429 481 YLTQIPIAMSPLSNNSLFLEYSKNPLPEYLHKGLNVSLSTDDPLQFHYTKEALMEEYAIAAQVWKLSTCDMCELARNSVL 560
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1207133710 715 QSGLSHQEKKYFLGEKYLDDGPEGNDIRKTNVAQIRMAYRHETLCNELSFL 765
Cdd:TIGR01429 561 QSGFEHQVKQHWLGPNYYKEGPEGNDIRRTNVPDIRVAFRYETLCNELSLL 611
|
|
| AMPD |
cd01319 |
AMP deaminase (AMPD) catalyzes the hydrolytic deamination of adensosine monophosphate (AMP) at ... |
266-762 |
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: 969.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 266 FAIDLSHVLAMIADGPTKTYCHRRLNFLTSKFQLHEMLNEMAELKELKCVPHRDFYNVRKVDTHIHAAACMNQKHLLKFI 345
Cdd:cd01319 1 FYLDLEFLLALISDGPAKSFCYRRLQYLESKFQLHVLLNEDRELKEQKTVPHRDFYNVRKVDTHVHHSACMNQKHLLRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 346 QDSYQTEADRVVLEKGGKKFTLKQVFENLKMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGANELREIYLKTDNYIN 425
Cdd:cd01319 81 KKKLRTEPDEVVIFRDGKKLTLKEVFDSLKLTAYDLSVDTLDVHADRNTFHRFDKFNLKYNPIGESRLREIFLKTDNYIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 426 GEYFARLIKEVAHDLEESKYQHAEPRLSIYGRAPEEWESLSKWFIMQKLHSPNMRWMIQVPRIYDIFRSKKIIANFAKML 505
Cdd:cd01319 161 GRYLAEITKEVFSDLEESKYQHAEYRLSIYGRSKDEWDKLASWVVDNDLFSPNVRWLIQIPRLYDVYKKSGIVNSFQEML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 506 ENIFLPLFQATVNPQKHKEMHVFLKHVTGFDSVDDESKhSDHIFNYKSPKPEEWTSEENPPYTYYLFHMYANIMVLNNLR 585
Cdd:cd01319 241 ENIFEPLFEATKDPSSHPELHVFLQQVIGFDSVDDESK-SERRFTRKFPKPEEWTSEENPPYSYYLYYMYANITTLNSFR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 586 KERGLNTFLFRPHCGEAGSITHLVSAFLTADNISHGLNLKKSPVLQYLYYLAQVPIAMSPLSNNSLFLEYSKNPLREFLQ 665
Cdd:cd01319 320 KARGFNTFVLRPHCGEAGDIDHLASAFLLAHGISHGINLRKVPVLQYLYYLTQIGIAMSPLSNNSLFLSYEKNPFPEFFK 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 666 KGLCVSLSTDDPLQFHYTKEALMEEYAIAAQLWKLSTCDTCEIARNSVLQSGLSHQEKKYFLGEKYLDDGPEGNDIRKTN 745
Cdd:cd01319 400 RGLNVSLSTDDPLQFHFTKEPLMEEYSIAAQVWKLSTCDMCELARNSVLQSGFEHSIKRHWLGPNYLKRGVAGNDIRRTN 479
|
490
....*....|....*..
gi 1207133710 746 VAQIRMAYRHETLCNEL 762
Cdd:cd01319 480 VPQIRMAYRYETLCEEL 496
|
|
| PLN02768 |
PLN02768 |
AMP deaminase |
203-762 |
0e+00 |
|
AMP deaminase
Pssm-ID: 215411 Cd Length: 835 Bit Score: 718.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 203 DEEVLPDICpSPSEGEDPYSMEDLPQNLNYsLKMKDGIIYVYDNEDAlKQDLprsLPYPDLETFAIDLSHVLAMIADGPT 282
Cdd:PLN02768 267 EKEIISDPS-TPKPNPNPFSYTPEGKSDHY-FEMQDGVVHVYANKDS-KEEL---FPVADATTFFTDLHHILRVIAAGNI 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 283 KTYCHRRLNFLTSKFQLHEMLNEMAELKELKCVPHRDFYNVRKVDTHIHAAACMNQKHLLKFIQDSYQTEADRVVLEKGG 362
Cdd:PLN02768 341 RTLCHHRLNLLEQKFNLHLMLNADREFLAQKSAPHRDFYNVRKVDTHVHHSACMNQKHLLRFIKSKLRKEPDEVVIFRDG 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 363 KKFTLKQVFENLKMDPYDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGANELREIYLKTDNYINGEYFARLIKEVAHDLEE 442
Cdd:PLN02768 421 TYLTLKEVFESLDLTGYDLNVDLLDVHADKSTFHRFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKQVFSDLEA 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 443 SKYQHAEPRLSIYGRAPEEWESLSKWFIMQKLHSPNMRWMIQVPRIYDIFRSKKIIANFAKMLENIFLPLFQATVNPQKH 522
Cdd:PLN02768 501 SKYQMAEYRISIYGRKQSEWDQLASWIVNNELYSENVVWLIQLPRLYNVYKEMGIVTSFQNILDNIFIPLFEVTVDPDSH 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 523 KEMHVFLKHVTGFDSVDDESK----HSDHIfnyksPKPEEWTSEENPPYTYYLFHMYANIMVLNNLRKERGLNTFLFRPH 598
Cdd:PLN02768 581 PQLHVFLKQVVGLDLVDDESKperrPTKHM-----PTPAQWTNVFNPAFSYYVYYCYANLYTLNKLRESKGMTTIKFRPH 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 599 CGEAGSITHLVSAFLTADNISHGLNLKKSPVLQYLYYLAQVPIAMSPLSNNSLFLEYSKNPLREFLQKGLCVSLSTDDPL 678
Cdd:PLN02768 656 SGEAGDIDHLAATFLTCHNIAHGINLRKSPVLQYLYYLAQIGLAMSPLSNNSLFLDYHRNPFPMFFLRGLNVSLSTDDPL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 679 QFHYTKEALMEEYAIAAQLWKLSTCDTCEIARNSVLQSGLSHQEKKYFLGEKYLDDGPEGNDIRKTNVAQIRMAYRHETL 758
Cdd:PLN02768 736 QIHLTKEPLVEEYSIAASVWKLSSCDLCEIARNSVYQSGFSHALKSHWIGKEYYKRGPDGNDIHKTNVPHIRVEFRDTIW 815
|
....
gi 1207133710 759 CNEL 762
Cdd:PLN02768 816 KEEM 819
|
|
| PLN03055 |
PLN03055 |
AMP deaminase; Provisional |
157-765 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 178613 Cd Length: 602 Bit Score: 703.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 157 EDYEQAAKSLLTALFIREKYSrlayhrfprtaakFLRSANNEKWSEDEEVLPDICPspsegeDPYSMEDLPQNlNYSLKM 236
Cdd:PLN03055 6 DEEEEVCAMMQECLELRDKYL-------------FREKLPPWRKGIFESSTSKPNP------DPFRYEPEPPS-QHVFRM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 237 KDGIIYVYDNEDAlKQDLprsLPYPDLETFAIDLSHVLAMIADGPTKTYCHRRLNFLTSKFQLHEMLNEMAELKELKCVP 316
Cdd:PLN03055 66 VDGVMHVYAPDDA-KEEL---FPVPDATTFFTDMHRILRIVSLGNVRTFCHHRLKLLEQKFSLHLMLNADREFLAQKSAP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 317 HRDFYNVRKVDTHIHAAACMNQKHLLKFIQDSYQTEADRVVLEKGGKKFTLKQVFENLKMDPYDLTVDSLDVHAGRQTFH 396
Cdd:PLN03055 142 HRDFYNVRKVDTHVHHSSCMNQKHLLRFIKSKLRKEPDEVVIFRDGKYLTLREVFESLDLTGYDLNVDLLDVHADKNTFH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 397 RFDKFNSKYNPVGANELREIYLKTDNYINGEYFARLIKEVAHDLEESKYQHAEPRLSIYGRAPEEWESLSKWFIMQKLHS 476
Cdd:PLN03055 222 RFDKFNLKYNPCGQSRLREIFLKQDNLIQGRFLAELTKEVFSDLEASKYQMAEYRISIYGRKQSEWDQLASWIVNNRLYS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 477 PNMRWMIQVPRIYDIFRSKKIIANFAKMLENIFLPLFQATVNPQKHKEMHVFLKHVTGFDSVDDESKHSDHIFNYKSPkP 556
Cdd:PLN03055 302 ENVVWLIQLPRLYNVYKEMGIVQSFQQILDNIFKPLFEVTVDPSSHPQLHVFLKMVVGFDMVDDESKPERRPTKHMQT-P 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 557 EEWTSEENPPYTYYLFHMYANIMVLNNLRKERGLNTFLFRPHCGEAGSITHLVSAFLTADNISHGLNLKKSPVLQYLYYL 636
Cdd:PLN03055 381 EQWDIPFNPAYSYWAYYVYANLYTLNKLRESKGLNTIKFRPHAGEAGDIDHLAAAFLLAHNIAHGNNLRKSPGLQYLYYL 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 637 AQVPIAMSPLSNNSLFLEYSKNPLREFLQKGLCVSLSTDDPLQFHYTKEALMEEYAIAAQLWKLSTCDTCEIARNSVLQS 716
Cdd:PLN03055 461 AQIGLAMSPLSNNSLFLDYHRNPFPMFFARGLNVSLSTDDPLQIHLTKEPLVEEYSIAAQVWKLSSCDLCEIARNSVLQS 540
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1207133710 717 GLSHQEKKYFLGEKYLDDGPEGNDIRKTNVAQIRMAYRHETLCNELSFL 765
Cdd:PLN03055 541 GFPHASKKHWVGDNYWLRGPAGNDIHKTNVPHMRVEFRHEVWKEELQYV 589
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
255-768 |
0e+00 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 595.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 255 PRSLPypDLETFAIDLSHVLAMIADGPTKTYCHRRLNFLTSKFQLHEMLNEMAEL--KELKCVPHRDFYNVRKVDTHIHA 332
Cdd:PTZ00310 776 PRFLP--TLTEFIRDLSELRDICSSVEVKRLATKRLENLEHKFRLHLALNHSNEAgtTEERESSNRDFYQAYKVDTHIHM 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 333 AACMNQKHLLKFIQDSYQTEADRVVLEKGGKKFTLKQVFENLKMDPyDLTVDSLDVHAGRQTFHRFDKFNSKYNPVGANE 412
Cdd:PTZ00310 854 AAGMTARQLLEFVVDKLLESGDDIAFKRGDHIVTLGQLFSKYGITP-NLTVDQLNVQADHTLFERFDNFNSKYNPMENPD 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 413 LREIYLKTDNYINGEYFARLIKEVAHDLEESKYQHAEPRLSIYGRAPEEWESLSKWFIMQKLHSPNMRWMIQVPRIYDIF 492
Cdd:PTZ00310 933 LRSLLLKTDNFMKGRYFAELIKDVFEQYSRDRFTYAENRLSIYGINVKEWDDLAHWFDTHGMASKHNKWMIQVPRVYKVF 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 493 RSKKIIANFAKMLENIFLPLFQATVNPQKHKEMHVFLKHVTGFDSVDDESKhSDHIFNYKSPkpEEWTSEENPPYTYYLF 572
Cdd:PTZ00310 1013 RAQNVIGSFGQYLDNIFQPLWEASLHPSKHPKFHYFLNHVSGFDSVDNEAT-IDLPFTDVSP--WAWTSVENPPYNYYLY 1089
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 573 HMYANIMVLNNLRKERGLNTFLFRPHCGEAGSITHLVSAFLTADNISHGLNLKKSPVLQYLYYLAQVPIAMSPLSNNSLF 652
Cdd:PTZ00310 1090 YLYANIRTLNEFRASRGFSTFALRPHCGESGSMDHLYGAFLCANSICHGINLRNDPPMQYLYYLAQIGLHVSPLSNNALF 1169
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 653 LEYSKNPLREFLQKGLCVSLSTDDPLQFHYTKEALMEEYAIAAQLWKLSTCDTCEIARNSVLQSGLSHQEKKYFLGEKYL 732
Cdd:PTZ00310 1170 LAFLENPFPVFFHRGLNVSLSTDDPLMFHQTQEPLIEEYSIAARVWGLSLNDLCEIARNSVLQSGFDAAFKRNAIGDRWY 1249
|
490 500 510
....*....|....*....|....*....|....*.
gi 1207133710 733 DDGPEGNDIRKTNVAQIRMAYRHETLCNELSFLVEA 768
Cdd:PTZ00310 1250 LSSSLGNDSLRTHLSDIRVAFRFETYHTELNFLELC 1285
|
|
| PTZ00310 |
PTZ00310 |
AMP deaminase; Provisional |
129-765 |
3.49e-90 |
|
AMP deaminase; Provisional
Pssm-ID: 240354 [Multi-domain] Cd Length: 1453 Bit Score: 310.20 E-value: 3.49e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 129 APEGQMPVNIPEFQRVTISGDYcAGItveDYEQAAKSLLTALFIREKYSRLAYHRFPRtaakflrsannekwseDEEVLP 208
Cdd:PTZ00310 53 APEVSLAAVASTMFRVVIDGDD-GGV---DMRKVHGRIAAAIRVRQLYKPTDTKVPEG----------------EREQPS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 209 DICPSPSEgedpysmedlpqnlnYSLKMKDGIiYVYDNEDAlkqdlpRSLPYPDLETFAIDLSHVLAMIADGPTKTYCHR 288
Cdd:PTZ00310 113 DSTPMPSL---------------VTIVQRDGV-YRFSGMDT------SVVLPPPWEQYVRDVQAVYLTVGNGPCLSACRH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 289 RLNFLTSKFQLHEMLNemAELKElKCVPHRD---FYNVRKVDTHIHAAACMNQKHLLKFIQDSYQTEADRVVLEKGGKKF 365
Cdd:PTZ00310 171 RLTIIQERSRMFFLLN--AEIEE-RADLYKAggvFSPCTKVDNAVLLSTSVDAQELLEFVVTTYREQPRAPLRLRDGSNS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 366 TLKQVFENLKM-DPYDLTVDSLDVHA--GRQTFHRFDKFNSKyNPVGA--NELREIYLKTDNYINGeyfaRLIKEVAHDL 440
Cdd:PTZ00310 248 TLREYLEAHGVrDPRELTVEGLGWQPtkYRNKYGQYDLFDAK-NPMGAlgAELRQSFLSLHGNLCG----KLLRRELERR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 441 EESKY--QHAEPRLSIYGRAPEEWESLSKWFIMQKLHS-PNMRWMIQVpriydifRSKKIIAN--------FAKMLENIF 509
Cdd:PTZ00310 323 EYQKQqpQATEYSLPLYGHHPEELTDLAEWVRRQGFGPfSRNRWILAI-------SFKELGPFqvpsscttVQDQLDNIF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 510 LPLFQATVNPQKHKEMHV--FLKHVTGFdSVDDESKHSDHIFNYKSPKPEEWTSEENPPYTYYLFHMYANIMVLNNLRKE 587
Cdd:PTZ00310 396 LPLFKATLCPSDPQWSDVawLLCQVGGL-QILTHAVVRSEDFDETAPDPDQVPYTAKCSDLYYFYYVYANLAVLNSLRKR 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 588 RGLNTFLFRPHCGEAGSITHLVSAFLTADNISHGLNLKKSPVLQYLYYLAQVPIAMSPLSNNSL-FLEYSKNPLREFLQK 666
Cdd:PTZ00310 475 KGLNTLQLRPSGEKAPAYDQLISSYLLGDVITRATSIADYPVLQYLCGLHRVGLTVSPLRDHALsITAYFDHPLPKFLHR 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 667 GLCVSLSTDDPLQFHYTKEALMEEYAIAAQLWKLSTCDTCEIARNSVLQSGLSHQEKKYFLGEKYlDDGPEGNDIRKTNV 746
Cdd:PTZ00310 555 CLRVSISTSDPLYFHHHSQPLIEEYATAMKLFSLSPLDTTELARNSVLNSSFPPEVKQQWLGERF-QLGVEGNDFERSGV 633
|
650
....*....|....*....
gi 1207133710 747 AQIRMAYRHETLCNELSFL 765
Cdd:PTZ00310 634 TNYRLAFREEAWALEEALL 652
|
|
| ADA_AMPD |
cd00443 |
Adenosine/AMP deaminase. Adenosine deaminases (ADAs) are present in pro- and eukaryotic ... |
324-729 |
1.45e-57 |
|
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: 198.73 E-value: 1.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 324 RKVDTHIHAAACMNQKHLLKFIqdsyqteadrvvlekggkkftlkqvfenlkmdpydltvdsldvhagrqtfhrfdkfns 403
Cdd:cd00443 2 PKVELHAHLSGSISPETLLELI---------------------------------------------------------- 23
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 404 kynpvgANELREIYLKTDNY-INGEYFARLIKEVAHDLEESKYQHAEPRLSIYGRAPEEWES-LSKWFIMQKLHSPNMRW 481
Cdd:cd00443 24 ------KKEFFEKFLLVHNLlQKGEALARALKEVIEEFAEDNVQYLELRTTPRLLETEKGLTkEQYWLLVIEGISEAKQW 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 482 --MIQVPRIYDIFRSKkiianfakmleniflPLFQATVNPQKHKEMHVFLK-HVTGFDSVDDESKHsdhifnykspkpee 558
Cdd:cd00443 98 fpPIKVRLILSVDRRG---------------PYVQNYLVASEILELAKFLSnYVVGIDLVGDESKG-------------- 148
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 559 wtseENPPYTYYLFHMYANImvlnnlrkergLNTFLFRPHCGEAGSITHLVSAF-LTADNISHGLNLKKSPVLQYLYYLA 637
Cdd:cd00443 149 ----ENPLRDFYSYYEYARR-----------LGLLGLTLHCGETGNREELLQALlLLPDRIGHGIFLLKHPELIYLVKLR 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 638 QVPIAMSPLSNNSLFL--EYSKNPLREFLQKGLCVSLSTDDPLQFHYTkeaLMEEYAIAAQLWKLSTCDTCEIARNSVLQ 715
Cdd:cd00443 214 NIPIEVCPTSNVVLGTvqSYEKHPFMRFFKAGLPVSLSTDDPGIFGTS---LSEEYSLAAKTFGLTFEDLCELNRNSVLS 290
|
410
....*....|....
gi 1207133710 716 SGLSHQEKKYFLGE 729
Cdd:cd00443 291 SFAKDEEKKSLLEV 304
|
|
| Add |
COG1816 |
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the ... |
597-729 |
2.32e-18 |
|
Adenosine deaminase [Nucleotide transport and metabolism]; Adenosine deaminase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441421 Cd Length: 326 Bit Score: 87.06 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 597 PHCGEAGSITHLVSA--FLTADNISHGLNLKKSPVLqyLYYLA--QVPIAMSPLSNNSL--FLEYSKNPLREFLQKGLCV 670
Cdd:COG1816 186 AHAGEAGGPESIWEAldLLGAERIGHGVRAIEDPAL--VARLAdrGIPLEVCPTSNVQLgvVPSLAEHPLRRLLDAGVRV 263
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207133710 671 SLSTDDPLQFHYTkeaLMEEYAIAAQLWKLSTCDTCEIARNSVLQSGLSHQEKKYFLGE 729
Cdd:COG1816 264 TLNTDDPLYFGTT---LTDEYELAAEAFGLSDADLAQLARNAIEASFLPEEEKAALLAE 319
|
|
| PRK09358 |
PRK09358 |
adenosine deaminase; Provisional |
586-729 |
1.23e-16 |
|
adenosine deaminase; Provisional
Pssm-ID: 236480 Cd Length: 340 Bit Score: 82.15 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 586 KERGLntfLFRPHCGEAG---SITHLVsAFLTADNISHGLNLKKSPVLqyLYYLA--QVPIAMSPLSNNSL--FLEYSKN 658
Cdd:PRK09358 192 RDAGL---RLTAHAGEAGgpeSIWEAL-DELGAERIGHGVRAIEDPAL--MARLAdrRIPLEVCPTSNVQTgaVPSLAEH 265
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207133710 659 PLREFLQKGLCVSLSTDDPLQFHYTkeaLMEEYAIAAQLWKLSTCDTCEIARNSVLQSGLSHQEKKYFLGE 729
Cdd:PRK09358 266 PLKTLLDAGVRVTINTDDPLVFGTT---LTEEYEALAEAFGLSDEDLAQLARNALEAAFLSEEEKAALLAE 333
|
|
| ADA |
cd01320 |
Adenosine deaminase (ADA) is a monomeric zinc dependent enzyme which catalyzes the ... |
586-724 |
1.45e-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: 78.40 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 586 KERGLNtflFRPHCGEAGSITHLVSAF--LTADNISHGLNLKKSPVLqyLYYLA--QVPIAMSPLSNnsLFL----EYSK 657
Cdd:cd01320 183 REAGLR---LTAHAGEAGGPESVRDALdlLGAERIGHGIRAIEDPEL--VKRLAerNIPLEVCPTSN--VQTgavkSLAE 255
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207133710 658 NPLREFLQKGLCVSLSTDDPLQFHYTkeaLMEEYAIAAQLWKLSTCDTCEIARNSVLQSGLSHQEKK 724
Cdd:cd01320 256 HPLRELLDAGVKVTINTDDPTVFGTY---LTDEYELLAEAFGLTEEELKKLARNAVEASFLSEEEKA 319
|
|
| A_deaminase |
pfam00962 |
Adenosine deaminase; |
594-729 |
3.78e-11 |
|
Adenosine deaminase;
Pssm-ID: 425964 Cd Length: 330 Bit Score: 65.14 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 594 LFRPHCGEAGSITHLVSA--FLTADNISHGLNLKKSPVLqyLYYLA--QVPIAMSPLSN--NSLFLEYSKNPLREFLQKG 667
Cdd:pfam00962 190 HLTVHAGEAGGPQSVWEAldDLGAERIGHGVRSAEDPRL--LDRLAdrQIPLEICPTSNvqTGAVASLAEHPLKTFLRAG 267
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207133710 668 LCVSLSTDDPLQFhytKEALMEEYAIAAQLWKLSTCDTCEIARNSVLQSGLSHQEKKYFLGE 729
Cdd:pfam00962 268 VPVSLNTDDPLMF---GSDLLDEYQVAKRAPGFDEEELARLAKNAVKGSFLPADEKRALLDE 326
|
|
| metallo-dependent_hydrolases |
cd01292 |
Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a ... |
563-700 |
5.23e-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: 58.11 E-value: 5.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 563 ENPPYTYYLFHMYaniMVLNNLRKERGLNTfLFRPHCGEAGSITHLVSAFLTAD------NISHGLNLkkSPVLQYLYYL 636
Cdd:cd01292 121 LAGPYTATGLSDE---SLRRVLEEARKLGL-PVVIHAGELPDPTRALEDLVALLrlggrvVIGHVSHL--DPELLELLKE 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207133710 637 AQVPIAMSPLSNNSLFLEYSK-NPLREFLQKGLCVSLSTDDPlqFHYTKEALMEEYAIAAQLWKL 700
Cdd:cd01292 195 AGVSLEVCPLSNYLLGRDGEGaEALRRLLELGIRVTLGTDGP--PHPLGTDLLALLRLLLKVLRL 257
|
|
| ADGF |
cd01321 |
Adenosine deaminase-related growth factors (ADGF), a novel family of secreted growth-factors ... |
593-724 |
6.35e-06 |
|
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: 49.19 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207133710 593 FLFrpHCGE-AGSIT----HLVSA-FLTADNISHGLNLKKSPVLQYLYYLAQVPIAMSPLSN--NSLFLEYSKNPLREFL 664
Cdd:cd01321 197 FFF--HAGEtNGDGTetdeNLVDAlLLNTKRIGHGFALPKHPLLMDLVKKKNIAIEVCPISNqvLGLVSDLRNHPAAALL 274
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207133710 665 QKGLCVSLSTDDPLQFHYTK------EALMeeyAIAAQLWKLSTCDTceIARNSVLQSGLSHQEKK 724
Cdd:cd01321 275 ARGVPVVISSDDPGFWGAKGlshdfyQAFM---GLAPADAGLRGLKQ--LAENSIRYSALSDQEKD 335
|
|
| |
