|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08591 |
PRK08591 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-449 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 236307 [Multi-domain] Cd Length: 451 Bit Score: 889.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 1 MIKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIGPKASKDSYLNVTNIVSVAKLTGTDAIHP 80
Cdd:PRK08591 1 MFDKILIANRGEIALRIIRACKELGIKTVAVHSTADRDALHVQLADEAVCIGPAPSKKSYLNIPAIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 81 GYGFLAENADFAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGSQGIIENVEEAVSLANEIGYPVIIKAT 160
Cdd:PRK08591 81 GYGFLSENADFAEICEDSGFTFIGPSAETIRLMGDKVTAKATMKKAGVPVVPGSDGPVDDEEEALAIAKEIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 161 AGGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTIHLGERDCSIQRRLQKLLE 240
Cdd:PRK08591 161 AGGGGRGMRVVRTEAELEKAFSMARAEAKAAFGNPGVYMEKYLENPRHIEIQVLADGHGNAIHLGERDCSLQRRHQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 241 ESPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDYNEQrYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASGM 320
Cdd:PRK08591 241 EAPSPAITEELRRKIGEAAVKAAKAIGYRGAGTIEFLYEKNGE-FYFIEMNTRIQVEHPVTEMITGVDLVKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 321 ELSLKQEDVEFEGWAIECRINAENPSKNFMPSPGEIKMYLPPGGLGVRVDSAAYPGYSIPPYYDSMIAKVITYGKTRDET 400
Cdd:PRK08591 320 PLSIKQEDIVFRGHAIECRINAEDPAKNFMPSPGKITRYHPPGGPGVRVDSAVYTGYTIPPYYDSMIGKLIVHGETREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1242724987 401 IARMKRALSEFVIEGIETTIPFHLKLLEHETFVSGEFNTKFLETYDVMG 449
Cdd:PRK08591 400 IARMKRALSEFVIDGIKTTIPLHLRLLNDPNFQAGDYNIHYLEKKLALQ 448
|
|
| PccA |
COG4770 |
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism]; |
1-445 |
0e+00 |
|
Acetyl/propionyl-CoA carboxylase, alpha subunit [Lipid transport and metabolism];
Pssm-ID: 443802 [Multi-domain] Cd Length: 466 Bit Score: 828.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 1 MIKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIGPKASKDSYLNVTNIVSVAKLTGTDAIHP 80
Cdd:COG4770 1 MFKKVLIANRGEIAVRIIRTCRELGIRTVAVYSDADRDALHVRLADEAVCIGPAPAAESYLNIDAIIAAAKATGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 81 GYGFLAENADFAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGSQGIIENVEEAVSLANEIGYPVIIKAT 160
Cdd:COG4770 81 GYGFLSENADFAEACEDAGIVFIGPSPEAIRAMGDKIAAKKLMKAAGVPVVPGSDGPVQDAEEALAIAEEIGYPVLIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 161 AGGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTIHLGERDCSIQRRLQKLLE 240
Cdd:COG4770 161 AGGGGKGMRVVRSEEELEEAFESARREAKAAFGDDRVYLEKYIERPRHIEVQVLADKHGNVVHLGERDCSIQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 241 ESPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDyNEQRYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASGM 320
Cdd:COG4770 241 EAPSPALTEELRERMGEAAVRAAKAVGYVGAGTVEFLVD-ADGNFYFLEMNTRLQVEHPVTEMVTGIDLVEEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 321 ELSLKQEDVEFEGWAIECRINAENPSKNFMPSPGEIKMYLPPGGLGVRVDSAAYPGYSIPPYYDSMIAKVITYGKTRDET 400
Cdd:COG4770 320 PLPFTQEDIKLRGHAIECRINAEDPARGFLPSPGTITRLRPPGGPGVRVDSGVYEGYEIPPYYDSMIAKLIVWGPDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1242724987 401 IARMKRALSEFVIEGIETTIPFHLKLLEHETFVSGEFNTKFLETY 445
Cdd:COG4770 400 IARMRRALAEFVIEGVKTNIPFLRALLAHPDFRAGDVDTGFIERE 444
|
|
| accC |
TIGR00514 |
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin ... |
1-450 |
0e+00 |
|
acetyl-CoA carboxylase, biotin carboxylase subunit; This model represents the biotin carboxylase subunit found usually as a component of acetyl-CoA carboxylase. Acetyl-CoA carboxylase is designated EC 6.4.1.2 and this component, biotin carboxylase, has its own designation, EC 6.3.4.14. Homologous domains are found in eukaryotic forms of acetyl-CoA carboxylase and in a number of other carboxylases (e.g. pyruvate carboxylase), but seed members and trusted cutoff are selected so as to exclude these. In some systems, the biotin carboxyl carrier protein and this protein (biotin carboxylase) may be shared by different carboxyltransferases. However, this model is not intended to identify the biotin carboxylase domain of propionyl-coA carboxylase. The model should hit the full length of proteins, except for chloroplast transit peptides in plants. If it hits a domain only of a longer protein, there may be a problem with the identification. [Fatty acid and phospholipid metabolism, Biosynthesis]
Pssm-ID: 129605 [Multi-domain] Cd Length: 449 Bit Score: 803.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 1 MIKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIGPKASKDSYLNVTNIVSVAKLTGTDAIHP 80
Cdd:TIGR00514 1 MLDKILIANRGEIALRILRACKELGIKTVAVHSTADRDALHVLLADEAVCIGPAPSAKSYLNIPNIISAAEITGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 81 GYGFLAENADFAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGSQGIIENVEEAVSLANEIGYPVIIKAT 160
Cdd:TIGR00514 81 GYGFLSENANFAEQCERSGFTFIGPSAESIRLMGDKVSAIETMKKAGVPCVPGSDGLVEDEEENVRIAKRIGYPVIIKAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 161 AGGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTIHLGERDCSIQRRLQKLLE 240
Cdd:TIGR00514 161 AGGGGRGMRVVREPDELVKSISMTRAEAKAAFGNDGVYIEKYIENPRHVEIQVLADKYGNAIYLGERDCSIQRRHQKLLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 241 ESPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDYNEQrYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASGM 320
Cdd:TIGR00514 241 EAPSPALTPELRRKMGDAAVKAAVSIGYRGAGTVEFLLDKNGE-FYFMEMNTRIQVEHPVTEMITGVDLIKEQIRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 321 ELSLKQEDVEFEGWAIECRINAENPSKNFMPSPGEIKMYLPPGGLGVRVDSAAYPGYSIPPYYDSMIAKVITYGKTRDET 400
Cdd:TIGR00514 320 PLSLKQEDVVVRGHAIECRINAEDPIKTFLPSPGRITRYLPPGGPGVRWDSHVYSGYTVPPYYDSMIGKLITYGKTREVA 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1242724987 401 IARMKRALSEFVIEGIETTIPFHLKLLEHETFVSGEFNTKFLETYDVMGS 450
Cdd:TIGR00514 400 IARMKRALSEFIIDGIKTTIPFHQRILEDENFQHGGTNIHYLEKKLGMGE 449
|
|
| PRK08654 |
PRK08654 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236325 [Multi-domain] Cd Length: 499 Bit Score: 705.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 1 MIKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIGPKASKDSYLNVTNIVSVAKLTGTDAIHP 80
Cdd:PRK08654 1 MFKKILIANRGEIAIRVMRACRELGIKTVAVYSEADKNALFVKYADEAYPIGPAPPSKSYLNIERIIDVAKKAGADAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 81 GYGFLAENADFAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGSQGIIENVEEAVSLANEIGYPVIIKAT 160
Cdd:PRK08654 81 GYGFLAENPEFAKACEKAGIVFIGPSSDVIEAMGSKINAKKLMKKAGVPVLPGTEEGIEDIEEAKEIAEEIGYPVIIKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 161 AGGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTIHLGERDCSIQRRLQKLLE 240
Cdd:PRK08654 161 AGGGGIGMRVVYSEEELEDAIESTQSIAQSAFGDSTVFIEKYLEKPRHIEIQILADKHGNVIHLGDRECSIQRRHQKLIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 241 ESPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDYNEqrYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASGM 320
Cdd:PRK08654 241 EAPSPIMTPELRERMGEAAVKAAKAINYENAGTVEFLYSNGN--FYFLEMNTRLQVEHPITEMVTGIDIVKEQIKIAAGE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 321 ELSLKQEDVEFEGWAIECRINAENPSKNFMPSPGEIKMYLPPGGLGVRVDSAAYPGYSIPPYYDSMIAKVITYGKTRDET 400
Cdd:PRK08654 319 ELSFKQEDITIRGHAIECRINAEDPLNDFAPSPGKIKRYRSPGGPGVRVDSGVHMGYEIPPYYDSMISKLIVWGRTREEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1242724987 401 IARMKRALSEFVIEGIETTIPFHLKLLEHETFVSGEFNTKFLETY 445
Cdd:PRK08654 399 IARMRRALYEYVIVGVKTNIPFHKAVMENENFVRGNLHTHFIEEE 443
|
|
| PRK05586 |
PRK05586 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-443 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180150 [Multi-domain] Cd Length: 447 Bit Score: 696.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 1 MIKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIGPKASKDSYLNVTNIVSVAKLTGTDAIHP 80
Cdd:PRK05586 1 MFKKILIANRGEIAVRIIRACREMGIETVAVYSEADKDALHVQLADEAVCIGPASSKDSYLNIQNIISATVLTGAQAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 81 GYGFLAENADFAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGSQGIIENVEEAVSLANEIGYPVIIKAT 160
Cdd:PRK05586 81 GFGFLSENSKFAKMCKECNIVFIGPDSETIELMGNKSNAREIMIKAGVPVVPGSEGEIENEEEALEIAKEIGYPVMVKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 161 AGGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTIHLGERDCSIQRRLQKLLE 240
Cdd:PRK05586 161 AGGGGRGIRIVRSEEELIKAFNTAKSEAKAAFGDDSMYIEKFIENPKHIEFQILGDNYGNVVHLGERDCSLQRRNQKVLE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 241 ESPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDYNEQrYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASGM 320
Cdd:PRK05586 241 EAPSPVMTEELRKKMGEIAVKAAKAVNYKNAGTIEFLLDKDGN-FYFMEMNTRIQVEHPITEMITGVDLVKEQIKIAYGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 321 ELSLKQEDVEFEGWAIECRINAENPSKNFMPSPGEIKMYLPPGGLGVRVDSAAYPGYSIPPYYDSMIAKVITYGKTRDET 400
Cdd:PRK05586 320 KLSIKQEDIKINGHSIECRINAEDPKNGFMPCPGKIEELYIPGGLGVRVDSAVYSGYTIPPYYDSMIGKLIVYGKDREEA 399
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1242724987 401 IARMKRALSEFVIEGIETTIPFHLKLLEHETFVSGEFNTKFLE 443
Cdd:PRK05586 400 IQKMKRALGEFIIEGVNTNIDFQFIILEDEEFIKGTYDTSFIE 442
|
|
| PRK06111 |
PRK06111 |
acetyl-CoA carboxylase biotin carboxylase subunit; Validated |
1-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Validated
Pssm-ID: 180406 [Multi-domain] Cd Length: 450 Bit Score: 664.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 1 MIKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIGPKASKDSYLNVTNIVSVAKLTGTDAIHP 80
Cdd:PRK06111 1 MFQKVLIANRGEIAVRIIRTCQKLGIRTVAIYSEADRDALHVKMADEAYLIGGPRVQESYLNLEKIIEIAKKTGAEAIHP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 81 GYGFLAENADFAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGSQGIIENVEEAVSLANEIGYPVIIKAT 160
Cdd:PRK06111 81 GYGLLSENASFAERCKEEGIVFIGPSADIIAKMGSKIEARRAMQAAGVPVVPGITTNLEDAEEAIAIARQIGYPVMLKAS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 161 AGGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTIHLGERDCSIQRRLQKLLE 240
Cdd:PRK06111 161 AGGGGIGMQLVETEQELTKAFESNKKRAANFFGNGEMYIEKYIEDPRHIEIQLLADTHGNTVYLWERECSVQRRHQKVIE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 241 ESPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDyNEQRYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASGM 320
Cdd:PRK06111 241 EAPSPFLDEETRKAMGERAVQAAKAIGYTNAGTIEFLVD-EQKNFYFLEMNTRLQVEHPVTEEITGIDLVEQQLRIAAGE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 321 ELSLKQEDVEFEGWAIECRINAENPsKNFMPSPGEIKMYLPPGGLGVRVDSAAYPGYSIPPYYDSMIAKVITYGKTRDET 400
Cdd:PRK06111 320 KLSFTQDDIKRSGHAIEVRIYAEDP-KTFFPSPGKITDLTLPGGEGVRHDHAVENGVTVTPFYDPMIAKLIAHGETREEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1242724987 401 IARMKRALSEFVIEGIETTIPFHLKLLEHETFVSGEFNTKFLETY 445
Cdd:PRK06111 399 ISRLHDALEELKVEGIKTNIPLLLQVLEDPVFKAGGYTTGFLTKQ 443
|
|
| PRK12999 |
PRK12999 |
pyruvate carboxylase; Reviewed |
1-444 |
0e+00 |
|
pyruvate carboxylase; Reviewed
Pssm-ID: 237263 [Multi-domain] Cd Length: 1146 Bit Score: 614.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 1 MIKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIG-PKASKDSYLNVTNIVSVAKLTGTDAIH 79
Cdd:PRK12999 4 KIKKVLVANRGEIAIRIFRAATELGIRTVAIYSEEDKLSLHRFKADEAYLIGeGKHPVRAYLDIDEIIRVAKQAGVDAIH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 80 PGYGFLAENADFAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGSQGIIENVEEAVSLANEIGYPVIIKA 159
Cdd:PRK12999 84 PGYGFLSENPEFARACAEAGITFIGPTAEVLRLLGDKVAARNAAIKAGVPVIPGSEGPIDDIEEALEFAEEIGYPIMLKA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 160 TAGGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTIHLGERDCSIQRRLQKLL 239
Cdd:PRK12999 164 SAGGGGRGMRIVRSEEELEEAFERAKREAKAAFGNDEVYLEKYVENPRHIEVQILGDKHGNVVHLYERDCSVQRRHQKVV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 240 EESPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDyNEQRYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASG 319
Cdd:PRK12999 244 EIAPAPGLSEELRERICEAAVKLARAVGYVNAGTVEFLVD-ADGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 320 MELS------LKQEDVEFEGWAIECRINAENPSKNFMPSPGEIKMYLPPGGLGVRVDS-AAYPGYSIPPYYDSMIAKVIT 392
Cdd:PRK12999 323 ATLHdleigiPSQEDIRLRGYAIQCRITTEDPANNFMPDTGRITAYRSPGGFGVRLDGgNAFAGAEITPYYDSLLVKLTA 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1242724987 393 YGKTRDETIARMKRALSEFVIEGIETTIPFHLKLLEHETFVSGEFNTKFLET 444
Cdd:PRK12999 403 WGRTFEQAVARMRRALREFRIRGVKTNIPFLENVLKHPDFRAGDYTTSFIDE 454
|
|
| PRK07178 |
PRK07178 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
1-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 180865 [Multi-domain] Cd Length: 472 Bit Score: 602.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 1 MIKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIGPKaSKDSYLNVTNIVSVAKLTGTDAIHP 80
Cdd:PRK07178 1 MIKKILIANRGEIAVRIVRACAEMGIRSVAIYSEADRHALHVKRADEAYSIGAD-PLAGYLNPRRLVNLAVETGCDALHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 81 GYGFLAENADFAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGSQGIIENVEEAVSLANEIGYPVIIKAT 160
Cdd:PRK07178 80 GYGFLSENAELAEICAERGIKFIGPSAEVIRRMGDKTEARRAMIKAGVPVTPGSEGNLADLDEALAEAERIGYPVMLKAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 161 AGGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTIHLGERDCSIQRRLQKLLE 240
Cdd:PRK07178 160 SGGGGRGIRRCNSREELEQNFPRVISEATKAFGSAEVFLEKCIVNPKHIEVQILADSHGNVVHLFERDCSIQRRNQKLIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 241 ESPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDyNEQRYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASGM 320
Cdd:PRK07178 240 IAPSPQLTPEQRAYIGDLAVRAAKAVGYENAGTVEFLLD-ADGEVYFMEMNTRVQVEHTITEEITGIDIVREQIRIASGL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 321 ELSLKQEDVEFEGWAIECRINAENPSKNFMPSPGEIKMYLPPGGLGVRVDSAAYPGYSIPPYYDSMIAKVITYGKTRDET 400
Cdd:PRK07178 319 PLSYKQEDIQHRGFALQFRINAEDPKNDFLPSFGKITRYYAPGGPGVRTDTAIYTGYTIPPYYDSMCAKLIVWALTWEEA 398
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1242724987 401 IARMKRALSEFVIEGIETTIPFHLKLLEHETFVSGEFNTKFLETY 445
Cdd:PRK07178 399 LDRGRRALDDMRVQGVKTTIPYYQEILRNPEFRSGQFNTSFVESH 443
|
|
| PycA |
COG1038 |
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the ... |
1-444 |
0e+00 |
|
Pyruvate carboxylase [Energy production and conversion]; Pyruvate carboxylase is part of the Pathway/BioSystem: Urea cycle
Pssm-ID: 440660 [Multi-domain] Cd Length: 1144 Bit Score: 600.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 1 MIKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIG-PKASKDSYLNVTNIVSVAKLTGTDAIH 79
Cdd:COG1038 3 KIKKVLVANRGEIAIRVFRAATELGIRTVAIYSEEDRYSLHRFKADEAYLIGeGKGPVDAYLDIEEIIRVAKEKGVDAIH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 80 PGYGFLAENADFAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGSQGIIENVEEAVSLANEIGYPVIIKA 159
Cdd:COG1038 83 PGYGFLSENPEFARACEEAGITFIGPSPEVLEMLGDKVAARAAAIEAGVPVIPGTEGPVDDLEEALAFAEEIGYPVMLKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 160 TAGGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTIHLGERDCSIQRRLQKLL 239
Cdd:COG1038 163 AAGGGGRGMRVVRSEEELEEAFESARREAKAAFGDDEVFLEKYIERPKHIEVQILGDKHGNIVHLFERDCSVQRRHQKVV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 240 EESPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDyNEQRYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASG 319
Cdd:COG1038 243 EIAPAPNLDEELREAICEAAVKLAKAVGYVNAGTVEFLVD-DDGNFYFIEVNPRIQVEHTVTEEVTGIDIVQSQILIAEG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 320 MELS------LKQEDVEFEGWAIECRINAENPSKNFMPSPGEIKMYLPPGGLGVRVDSA-AYPGYSIPPYYDSMIAKVIT 392
Cdd:COG1038 322 YSLDdpeigiPSQEDIRLNGYAIQCRITTEDPANNFMPDTGRITAYRSAGGFGIRLDGGnAYTGAVITPYYDSLLVKVTA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1242724987 393 YGKTRDETIARMKRALSEFVIEGIETTIPFHLKLLEHETFVSGEFNTKFLET 444
Cdd:COG1038 402 WGRTFEEAIRKMRRALREFRIRGVKTNIPFLENVLNHPDFLAGECTTSFIDE 453
|
|
| PRK12833 |
PRK12833 |
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional |
2-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit; Provisional
Pssm-ID: 183781 [Multi-domain] Cd Length: 467 Bit Score: 581.71 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 2 IKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIGPKASKDSYLNVTNIVSVAKLTGTDAIHPG 81
Cdd:PRK12833 5 IRKVLVANRGEIAVRIIRAARELGMRTVAACSDADRDSLAARMADEAVHIGPSHAAKSYLNPAAILAAARQCGADAIHPG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 82 YGFLAENADFAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGSQGIIENVEEAVSLANEIGYPVIIKATA 161
Cdd:PRK12833 85 YGFLSENAAFAEAVEAAGLIFVGPDAQTIRTMGDKARARRTARRAGVPTVPGSDGVVASLDAALEVAARIGYPLMIKAAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 162 GGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYgNTIHLGERDCSIQRRLQKLLEE 241
Cdd:PRK12833 165 GGGGRGIRVAHDAAQLAAELPLAQREAQAAFGDGGVYLERFIARARHIEVQILGDGE-RVVHLFERECSLQRRRQKILEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 242 SPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDYNEQRYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASGME 321
Cdd:PRK12833 244 APSPSLTPAQRDALCASAVRLARQVGYRGAGTLEYLFDDARGEFYFIEMNTRIQVEHPVTEAITGIDLVQEMLRIADGEP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 322 LSLKQEDVEFEGWAIECRINAENPSKNFMPSPGEIKMYLPPGGLGVRVDSAAYPGYSIPPYYDSMIAKVITYGKTRDETI 401
Cdd:PRK12833 324 LRFAQGDIALRGAALECRINAEDPLRDFFPNPGRIDALVWPQGPGVRVDSLLYPGYRVPPFYDSLLAKLIVHGEDRAAAL 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1242724987 402 ARMKRALSEFVIEGIETTIPFHLKLLEHETFVSGEFNTKFLETY 445
Cdd:PRK12833 404 ARAARALRELRIDGMKTTAPLHRALLADADVRAGRFHTNFLEAW 447
|
|
| PRK08462 |
PRK08462 |
acetyl-CoA carboxylase biotin carboxylase subunit; |
2-445 |
0e+00 |
|
acetyl-CoA carboxylase biotin carboxylase subunit;
Pssm-ID: 236269 [Multi-domain] Cd Length: 445 Bit Score: 570.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 2 IKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIGPKASKDSYLNVTNIVSVAKLTGTDAIHPG 81
Cdd:PRK08462 4 IKRILIANRGEIALRAIRTIQEMGKEAIAIYSTADKDALYLKYADAKICIGGAKSSESYLNIPAIISAAEIFEADAIFPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 82 YGFLAENADFAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGSQGIIENVEEAVSLANEIGYPVIIKATA 161
Cdd:PRK08462 84 YGFLSENQNFVEICSHHNIKFIGPSVEVMALMSDKSKAKEVMKRAGVPVIPGSDGALKSYEEAKKIAKEIGYPVILKAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 162 GGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTIHLGERDCSIQRRLQKLLEE 241
Cdd:PRK08462 164 GGGGRGMRVVEDESDLENLYLAAESEALSAFGDGTMYMEKFINNPRHIEVQILGDKHGNVIHVGERDCSLQRRHQKLIEE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 242 SPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDYNeQRYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASGME 321
Cdd:PRK08462 244 SPAVVLDEKTRERLHETAIKAAKAIGYEGAGTFEFLLDSN-LDFYFMEMNTRLQVEHTVSEMVSGLDLIEWMIKIAEGEE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 322 LsLKQEDVEFEGWAIECRINAENPSKnFMPSPGEIKMYLPPGGLGVRVDSAAYPGYSIPPYYDSMIAKVITYGKTRDETI 401
Cdd:PRK08462 323 L-PSQESIKLKGHAIECRITAEDPKK-FYPSPGKITKWIAPGGRNVRMDSHAYAGYVVPPYYDSMIGKLIVWGEDRNRAI 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1242724987 402 ARMKRALSEFVIEGIETTIPFHLKLLEHETFVSGEFNTKFLETY 445
Cdd:PRK08462 401 AKMKRALKEFKVEGIKTTIPFHLEMMENADFINNKYDTKYLEEH 444
|
|
| PRK08463 |
PRK08463 |
acetyl-CoA carboxylase subunit A; Validated |
1-444 |
0e+00 |
|
acetyl-CoA carboxylase subunit A; Validated
Pssm-ID: 169452 [Multi-domain] Cd Length: 478 Bit Score: 522.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 1 MIKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIGPKASKdSYLNVTNIVSVAKLTGTDAIHP 80
Cdd:PRK08463 1 MIHKILIANRGEIAVRVIRACRDLHIKSVAIYTEPDRECLHVKIADEAYRIGTDPIK-GYLDVKRIVEIAKACGADAIHP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 81 GYGFLAENADFAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGSQGI-IENVEEAVSLANEIGYPVIIKA 159
Cdd:PRK08463 80 GYGFLSENYEFAKAVEDAGIIFIGPKSEVIRKMGNKNIARYLMKKNGIPIVPGTEKLnSESMEEIKIFARKIGYPVILKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 160 TAGGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTIHLGERDCSIQRRLQKLL 239
Cdd:PRK08463 160 SGGGGGRGIRVVHKEEDLENAFESCKREALAYFNNDEVFMEKYVVNPRHIEFQILGDNYGNIIHLCERDCSIQRRHQKVI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 240 EESPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYD-YNeqRYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVAS 318
Cdd:PRK08463 240 EIAPCPSISDNLRKTMGVTAVAAAKAVGYTNAGTIEFLLDdYN--RFYFMEMNTRIQVEHGVTEEITGIDLIVRQIRIAA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 319 GMELSLKQEDVEFEGWAIECRINAENPSKNFMPSPGEIKMYLPPGGLGVRVDSAAYPGYSIPPYYDSMIAKVITYGKTRD 398
Cdd:PRK08463 318 GEILDLEQSDIKPRGFAIEARITAENVWKNFIPSPGKITEYYPALGPSVRVDSHIYKDYTIPPYYDSMLAKLIVKATSYD 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1242724987 399 ETIARMKRALSEFVIEGIETTIPFHLKLLEHETFVSGEFNTKFLET 444
Cdd:PRK08463 398 LAVNKLERALKEFVIDGIRTTIPFLIAITKTREFRRGYFDTSYIET 443
|
|
| CPSase_L_D2 |
pfam02786 |
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ... |
116-323 |
1.98e-86 |
|
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
Pssm-ID: 397079 [Multi-domain] Cd Length: 209 Bit Score: 263.01 E-value: 1.98e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 116 KDVARETMKQAGVPIVPGSQGIIENVEEAVSLANEIGYPVIIKATAGGGGKGIRVARTEEELINGIKITQQEAATAFGNP 195
Cdd:pfam02786 2 KVLFKAAMKEAGVPTVPGTAGPVETEEEALAAAKEIGYPVIIKAAFGGGGLGMGIARNEEELAELFALALAEAPAAFGNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 196 GVYIEKYIEDFRHVEIQVLADNYGNTIHLGERDCSIQRRLQKLLEESPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVE 275
Cdd:pfam02786 82 QVLVEKSLKGPKHIEYQVLRDAHGNCITVCNRECSDQRRTQKSIEVAPSQTLTDEERQMLREAAVKIARHLGYVGAGTVE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1242724987 276 FIYDYNEQRYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASGMELS 323
Cdd:pfam02786 162 FALDPFSGEYYFIEMNTRLQVEHALAEKATGYDLAKEAAKIALGYPLP 209
|
|
| Biotin_carb_N |
pfam00289 |
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp ... |
2-109 |
2.55e-67 |
|
Biotin carboxylase, N-terminal domain; This domain is structurally related to the PreATP-grasp domain. The family contains the N-terminus of biotin carboxylase enzymes, and propionyl-CoA carboxylase A chain.
Pssm-ID: 425585 [Multi-domain] Cd Length: 108 Bit Score: 210.04 E-value: 2.55e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 2 IKKLLIANRGEIAVRIIRACRELGIETVAVYSEADKDALHVQMADEAFCIGPKASKDSYLNVTNIVSVAKLTGTDAIHPG 81
Cdd:pfam00289 1 IKKVLIANRGEIAVRIIRACRELGIRTVAVYSEADANSLHVRLADEAVCLGPGPASESYLNIDAIIDAAKETGADAIHPG 80
|
90 100
....*....|....*....|....*...
gi 1242724987 82 YGFLAENADFAELCEEVNVTFVGPSADA 109
Cdd:pfam00289 81 YGFLSENAEFARACEEAGIIFIGPSPEA 108
|
|
| Biotin_carb_C |
smart00878 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
337-443 |
2.41e-64 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyses the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 214878 [Multi-domain] Cd Length: 107 Bit Score: 202.26 E-value: 2.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 337 ECRINAENPSKNFMPSPGEIKMYLPPGGLGVRVDSAAYPGYSIPPYYDSMIAKVITYGKTRDETIARMKRALSEFVIEGI 416
Cdd:smart00878 1 ECRINAEDPANGFLPSPGRITRYRFPGGPGVRVDSGVYEGYEVPPYYDSMIAKLIVWGEDREEAIARLRRALDEFRIRGV 80
|
90 100
....*....|....*....|....*..
gi 1242724987 417 ETTIPFHLKLLEHETFVSGEFNTKFLE 443
Cdd:smart00878 81 KTNIPFLRALLRHPDFRAGDVDTGFLE 107
|
|
| Biotin_carb_C |
pfam02785 |
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA ... |
337-444 |
2.32e-61 |
|
Biotin carboxylase C-terminal domain; Biotin carboxylase is a component of the acetyl-CoA carboxylase multi-component enzyme which catalyzes the first committed step in fatty acid synthesis in animals, plants and bacteria. Most of the active site residues reported in reference are in this C-terminal domain.
Pssm-ID: 426981 [Multi-domain] Cd Length: 108 Bit Score: 194.63 E-value: 2.32e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 337 ECRINAENPSKNFMPSPGEIKMYLPPGGLGVRVDSAAYPGYSIPPYYDSMIAKVITYGKTRDETIARMKRALSEFVIEGI 416
Cdd:pfam02785 1 EARIYAEDPDNNFLPSPGKVTRYRFPGGPGVRVDSGVYAGYTVSPYYDSMIAKLIVHGPTREEAIARLRRALAEFRIEGV 80
|
90 100
....*....|....*....|....*...
gi 1242724987 417 ETTIPFHLKLLEHETFVSGEFNTKFLET 444
Cdd:pfam02785 81 KTNIPFLRAILEHPDFRAGEVDTGFLEE 108
|
|
| AccC |
COG0439 |
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ... |
69-321 |
6.59e-58 |
|
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440208 [Multi-domain] Cd Length: 263 Bit Score: 191.24 E-value: 6.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 69 VAKLTGTDAIhpgygfLAENAD----FAELCEEVNvtFVGPSADAISKMGTKDVARETMKQAGVPiVPGSQgIIENVEEA 144
Cdd:COG0439 12 LARETGIDAV------LSESEFavetAAELAEELG--LPGPSPEAIRAMRDKVLMREALAAAGVP-VPGFA-LVDSPEEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 145 VSLANEIGYPVIIKATAGGGGKGIRVARTEEELINGIKITQQEAATAFGNPGVYIEKYIEDfRHVEIQVLADNyGNTIHl 224
Cdd:COG0439 82 LAFAEEIGYPVVVKPADGAGSRGVRVVRDEEELEAALAEARAEAKAGSPNGEVLVEEFLEG-REYSVEGLVRD-GEVVV- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 225 gerdCSIQRRLQK------LLEESPSPaLDSEIREQMGDAAVKAAKAVGY-TGAGTVEFIYDyNEQRYYFMEMNTRIQVE 297
Cdd:COG0439 159 ----CSITRKHQKppyfveLGHEAPSP-LPEELRAEIGELVARALRALGYrRGAFHTEFLLT-PDGEPYLIEINARLGGE 232
|
250 260
....*....|....*....|....*.
gi 1242724987 298 H--PVTEMVTGTDLIKEQIKVASGME 321
Cdd:COG0439 233 HipPLTELATGVDLVREQIRLALGEP 258
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
18-322 |
7.04e-16 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 80.43 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 18 IRACRELGIETVAVYSEADKDALHVQMADEAFcIGPkaskdsyLNVTNIVSVAKLTGTDAIHPGYG-----FLAENADFA 92
Cdd:TIGR01369 33 CKALKEEGYRVILVNSNPATIMTDPEMADKVY-IEP-------LTPEAVEKIIEKERPDAILPTFGgqtalNLAVELEES 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 93 ELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPiVPGSQgIIENVEEAVSLANEIGYPVIIKATAGGGGKGIRVAR 172
Cdd:TIGR01369 105 GVLEKYGVEVLGTPVEAIKKAEDRELFREAMKEIGEP-VPESE-IAHSVEEALAAAKEIGYPVIVRPAFTLGGTGGGIAY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 173 TEEELingIKITQQeAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTI-------------HLGErdcSIQrrlqkll 239
Cdd:TIGR01369 183 NREEL---KEIAER-ALSASPINQVLVEKSLAGWKEIEYEVMRDSNDNCItvcnmenfdpmgvHTGD---SIV------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 240 eESPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDYNEQRYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASG 319
Cdd:TIGR01369 249 -VAPSQTLTDKEYQMLRDASIKIIRELGIEGGCNVQFALNPDSGRYYVIEVNPRVSRSSALASKATGYPIAKVAAKLAVG 327
|
...
gi 1242724987 320 MEL 322
Cdd:TIGR01369 328 YTL 330
|
|
| CPSaseII_lrg |
TIGR01369 |
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes ... |
14-322 |
2.52e-15 |
|
carbamoyl-phosphate synthase, large subunit; Carbamoyl-phosphate synthase (CPSase) catalyzes the first committed step in pyrimidine, arginine, and urea biosynthesis. In general, it is a glutamine-dependent enzyme, EC 6.3.5.5, termed CPSase II in eukaryotes. An exception is the mammalian mitochondrial urea-cycle form, CPSase I, in which the glutamine amidotransferase domain active site Cys on the small subunit has been lost, and the enzyme is ammonia-dependent. In both CPSase I and the closely related, glutamine-dependent CPSase III (allosterically activated by acetyl-glutamate) demonstrated in some other vertebrates, the small and large chain regions are fused in a single polypeptide chain. This model represents the large chain of glutamine-hydrolysing carbamoyl-phosphate synthases, or the corresponding regions of larger, multifunctional proteins, as found in all domains of life, and CPSase I forms are considered exceptions within the family. In several thermophilic species (Methanobacterium thermoautotrophicum, Methanococcus jannaschii, Aquifex aeolicus), the large subunit appears split, at different points, into two separate genes. [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis]
Pssm-ID: 273581 [Multi-domain] Cd Length: 1050 Bit Score: 78.50 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 14 AVRIIRACRELGIETVAV----------YSEADK---DALHVQmadeafcigpkaskdsylNVTNIVSVAKLTGTdAIHP 80
Cdd:TIGR01369 577 CVHAVLALRELGYETIMInynpetvstdYDTSDRlyfEPLTFE------------------DVMNIIELEKPEGV-IVQF 637
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 81 GyGFLAENAdfAELCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGsqGIIENVEEAVSLANEIGYPVIIKAT 160
Cdd:TIGR01369 638 G-GQTPLNL--AKALEEAGVPILGTSPESIDRAEDREKFSELLDELGIPQPKW--KTATSVEEAVEFASEIGYPVLVRPS 712
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 161 AGGGGKGIRVARTEEELINGIKitqqEAATAFGNPGVYIEKYIEDFRHVEIQVLADN-----YGNT-------IHLGERD 228
Cdd:TIGR01369 713 YVLGGRAMEIVYNEEELRRYLE----EAVAVSPEHPVLIDKYLEDAVEVDVDAVSDGeevliPGIMehieeagVHSGDST 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 229 CSIqrrlqklleesPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDYNEqrYYFMEMNTRIQVEHPVTEMVTGTD 308
Cdd:TIGR01369 789 CVL-----------PPQTLSAEIVDRIKDIVRKIAKELNVKGLMNIQFAVKDGE--VYVIEVNPRASRTVPFVSKATGVP 855
|
330
....*....|....
gi 1242724987 309 LIKEQIKVASGMEL 322
Cdd:TIGR01369 856 LAKLAVRVMLGKKL 869
|
|
| COG3919 |
COG3919 |
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only]; |
17-294 |
1.44e-12 |
|
Predicted ATP-dependent carboligase, ATP-grasp superfamily [General function prediction only];
Pssm-ID: 443124 [Multi-domain] Cd Length: 382 Bit Score: 68.80 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 17 IIRACRELGIETVAVYSEADKDALHVQMADEAF-CIGPKASKDSYLNvtNIVSVAKLTGTDAIHPGY----GFLAENADf 91
Cdd:COG3919 20 VARSLGEAGVRVIVVDRDPLGPAARSRYVDEVVvVPDPGDDPEAFVD--ALLELAERHGPDVLIPTGdeyvELLSRHRD- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 92 aELCEevNVTFVGPSADAISKMGTKDVARETMKQAGVPiVPGSQgIIENVEEAVSLANEIGYPVIIKAT--------AGG 163
Cdd:COG3919 97 -ELEE--HYRLPYPDADLLDRLLDKERFYELAEELGVP-VPKTV-VLDSADDLDALAEDLGFPVVVKPAdsvgydelSFP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 164 GGKGIRVARTEEELINGIkitqqEAATAFGNPGVyIEKYIEDFRHVE--IQVLADNYGNTIHLgerdCSIQRRLQKLLEE 241
Cdd:COG3919 172 GKKKVFYVDDREELLALL-----RRIAAAGYELI-VQEYIPGDDGEMrgLTAYVDRDGEVVAT----FTGRKLRHYPPAG 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1242724987 242 SPSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDYNEQRYYFMEMNTRI 294
Cdd:COG3919 242 GNSAARESVDDPELEEAARRLLEALGYHGFANVEFKRDPRDGEYKLIEINPRF 294
|
|
| CarB |
COG0458 |
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ... |
15-222 |
1.55e-12 |
|
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase large subunit is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 440226 [Multi-domain] Cd Length: 536 Bit Score: 69.14 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 15 VRIIRACRELGIETVAV----------YSEADKdalhvqmadeaFCIGPkaskdsyLNVTNIVSVAKLTGTDAIHPGYG- 83
Cdd:COG0458 19 VQACKALREEGYEVILVnsnpetvstdYDTADR-----------LYFEP-------LTVEDVLDIIEKEKPDGVIVQFGg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 84 ----FLAEnaDFAELCEEVNVTFVGPSADAIskmgtkDVA------RETMKQAGVPIVPGsqGIIENVEEAVSLANEIGY 153
Cdd:COG0458 81 qtalNLAV--ELEEAGILEGVKILGTSPDAI------DLAedrelfKELLDKLGIPQPKS--GTATSVEEALAIAEEIGY 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1242724987 154 PVIIKATAGGGGKGIRVARTEEELINGIKitqqEAATAFGNPGVYIEKYIEDFRHVEIQVLADNYGNTI 222
Cdd:COG0458 151 PVIVRPSYVLGGRGMGIVYNEEELEEYLE----RALKVSPDHPVLIDESLLGAKEIEVDVVRDGEDNVI 215
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
96-222 |
1.47e-10 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 63.58 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 96 EEVNVTFVGPSADAISKMGTKDVARETMKQAGVPiVPGSqGIIENVEEAVSLANEIGYPVIikataggggkgIR------ 169
Cdd:PRK05294 109 EKYGVELIGAKLEAIDKAEDRELFKEAMKKIGLP-VPRS-GIAHSMEEALEVAEEIGYPVI-----------IRpsftlg 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1242724987 170 -----VARTEEELI----NGIK---ITQqeaatafgnpgVYIEKYIEDFRHVEIQVLADNYGNTI 222
Cdd:PRK05294 176 gtgggIAYNEEELEeiveRGLDlspVTE-----------VLIEESLLGWKEYEYEVMRDKNDNCI 229
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
96-294 |
1.63e-10 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 63.45 E-value: 1.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 96 EEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIvpGSQGIIENVEEAVSLANEIGYPVIIKATAGGGGKGIRVARTEE 175
Cdd:PRK12815 109 EQYGVELLGTNIEAIQKGEDRERFRALMKELGEPV--PESEIVTSVEEALAFAEKIGFPIIVRPAYTLGGTGGGIAENLE 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 176 ELINGIKitQQEAATAFGNpgVYIEKYIEDFRHVEIQVLADNYGNT-------------IHLGErdcSIQrrlqklleES 242
Cdd:PRK12815 187 ELEQLFK--QGLQASPIHQ--CLLEESIAGWKEIEYEVMRDRNGNCitvcnmenidpvgIHTGD---SIV--------VA 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1242724987 243 PSPAL-DSEIREqMGDAAVKAAKAVGYTGAGTVEFIYDYNEQRYYFMEMNTRI 294
Cdd:PRK12815 252 PSQTLtDDEYQM-LRSASLKIISALGVVGGCNIQFALDPKSKQYYLIEVNPRV 303
|
|
| carB |
PRK12815 |
carbamoyl phosphate synthase large subunit; Reviewed |
96-323 |
1.10e-07 |
|
carbamoyl phosphate synthase large subunit; Reviewed
Pssm-ID: 237215 [Multi-domain] Cd Length: 1068 Bit Score: 54.20 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 96 EEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGsqGIIENVEEAVSLANEIGYPVIIKATAGGGGKGIRVARTEE 175
Cdd:PRK12815 651 EEAGLTILGTSPDTIDRLEDRDRFYQLLDELGLPHVPG--LTATDEEEAFAFAKRIGYPVLIRPSYVIGGQGMAVVYDEP 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 176 ELingikitQQEAATAFGNP-GVYIEKYIEDfRHVEIQVLADNYGNTI------------HLGERDCSIqrrlqkllees 242
Cdd:PRK12815 729 AL-------EAYLAENASQLyPILIDQFIDG-KEYEVDAISDGEDVTIpgiiehieqagvHSGDSIAVL----------- 789
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 243 PSPALDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDYNEqrYYFMEMNTRIQVEHPVTEMVTGTDLIKEQIKVASGMEL 322
Cdd:PRK12815 790 PPQSLSEEQQEKIRDYAIKIAKKLGFRGIMNIQFVLANDE--IYVLEVNPRASRTVPFVSKATGVPLAKLATKVLLGKSL 867
|
.
gi 1242724987 323 S 323
Cdd:PRK12815 868 A 868
|
|
| PRK12767 |
PRK12767 |
carbamoyl phosphate synthase-like protein; Provisional |
43-293 |
3.32e-06 |
|
carbamoyl phosphate synthase-like protein; Provisional
Pssm-ID: 237195 [Multi-domain] Cd Length: 326 Bit Score: 48.73 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 43 QMADEAFcIGPKASKDSYLNVtnIVSVAKLTGTDAIHPGY----GFLAENAD-FaelcEEVNVTFVGPSADAISKMGTKD 117
Cdd:PRK12767 41 YFADKFY-VVPKVTDPNYIDR--LLDICKKEKIDLLIPLIdpelPLLAQNRDrF----EEIGVKVLVSSKEVIEICNDKW 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 118 VARETMKQAGVPIV----PGSqgiIENVEEAvSLANEIGYPVIIKATAGGGGKGIRVARTEEELINGIKitqqeaatafG 193
Cdd:PRK12767 114 LTYEFLKENGIPTPksylPES---LEDFKAA-LAKGELQFPLFVKPRDGSASIGVFKVNDKEELEFLLE----------Y 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 194 NPGVYIEKYIEDfRHVEIQVLADNYGNTIHlgerdcSIQRRLQKLLEESPSPAL---DSEIREQMGDaavkAAKAVGYTG 270
Cdd:PRK12767 180 VPNLIIQEFIEG-QEYTVDVLCDLNGEVIS------IVPRKRIEVRAGETSKGVtvkDPELFKLAER----LAEALGARG 248
|
250 260
....*....|....*....|...
gi 1242724987 271 AGTVEFIYDynEQRYYFMEMNTR 293
Cdd:PRK12767 249 PLNIQCFVT--DGEPYLFEINPR 269
|
|
| carB |
PRK05294 |
carbamoyl-phosphate synthase large subunit; |
96-225 |
1.07e-05 |
|
carbamoyl-phosphate synthase large subunit;
Pssm-ID: 235393 [Multi-domain] Cd Length: 1066 Bit Score: 48.17 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 96 EEVNVTFVGPSADAIskmgtkDVA--RE----TMKQAGVPIVPGsqGIIENVEEAVSLANEIGYPVII--------KAta 161
Cdd:PRK05294 650 EAAGVPILGTSPDAI------DLAedRErfskLLEKLGIPQPPN--GTATSVEEALEVAEEIGYPVLVrpsyvlggRA-- 719
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1242724987 162 ggggkgIRVARTEEELINGIKitqqEAATAFGNPGVYIEKYIEDFRHVEIQVLADnyGNTIHLG 225
Cdd:PRK05294 720 ------MEIVYDEEELERYMR----EAVKVSPDHPVLIDKFLEGAIEVDVDAICD--GEDVLIG 771
|
|
| PRK14016 |
PRK14016 |
cyanophycin synthetase; Provisional |
116-207 |
2.18e-05 |
|
cyanophycin synthetase; Provisional
Pssm-ID: 237586 [Multi-domain] Cd Length: 727 Bit Score: 47.07 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 116 KDVARETMKQAGVPiVPgSQGIIENVEEAVSLANEIGYPVIIKATAGGGGKGIRV-ARTEEELINGIKITQQEAAtafgn 194
Cdd:PRK14016 215 KELTKRLLAAAGVP-VP-EGRVVTSAEDAWEAAEEIGYPVVVKPLDGNHGRGVTVnITTREEIEAAYAVASKESS----- 287
|
90
....*....|....*
gi 1242724987 195 pGVYIEKYIE--DFR 207
Cdd:PRK14016 288 -DVIVERYIPgkDHR 301
|
|
| DdlA |
COG1181 |
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, ... |
60-204 |
4.29e-05 |
|
D-alanine-D-alanine ligase or related ATP-grasp enzyme [Cell wall/membrane/envelope biogenesis, General function prediction only]; D-alanine-D-alanine ligase or related ATP-grasp enzyme is part of the Pathway/BioSystem: Mureine biosynthesis
Pssm-ID: 440794 [Multi-domain] Cd Length: 303 Bit Score: 45.10 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 60 YLNVTNIVSVAKLTGTD----AIHPGYGflaENADFAELCEEVNVTFVGPSADAiSKMGT-KDVARETMKQAGVPIVPG- 133
Cdd:COG1181 39 GIDVEDLPAALKELKPDvvfpALHGRGG---EDGTIQGLLELLGIPYTGSGVLA-SALAMdKALTKRVLAAAGLPTPPYv 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1242724987 134 --SQGIIENVEEAVSlanEIGYPVIIKATAGGGGKGIRVARTEEELINGIkitqqEAATAFGNPgVYIEKYIE 204
Cdd:COG1181 115 vlRRGELADLEAIEE---ELGLPLFVKPAREGSSVGVSKVKNAEELAAAL-----EEAFKYDDK-VLVEEFID 178
|
|
| ddl |
PRK01372 |
D-alanine--D-alanine ligase; Reviewed |
106-292 |
4.78e-05 |
|
D-alanine--D-alanine ligase; Reviewed
Pssm-ID: 234948 [Multi-domain] Cd Length: 304 Bit Score: 45.10 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 106 SADAISKMGTKDVaretMKQAGVPIVPGSqgIIENVEEAVSLANEIGYPVIIKATAGGGGKGIRVARTEEELINGIkitq 185
Cdd:PRK01372 93 SALAMDKLRTKLV----WQAAGLPTPPWI--VLTREEDLLAAIDKLGLPLVVKPAREGSSVGVSKVKEEDELQAAL---- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 186 qEAATAFGNPgVYIEKYI------------EDFRHVEIQVLADNY--------GNTIHLgerdCsiqrrlqklleesPSP 245
Cdd:PRK01372 163 -ELAFKYDDE-VLVEKYIkgreltvavlggKALPVIEIVPAGEFYdyeakylaGGTQYI----C-------------PAG 223
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1242724987 246 aLDSEIREQMGDAAVKAAKAVGYTGAGTVEFIYDyNEQRYYFMEMNT 292
Cdd:PRK01372 224 -LPAEIEAELQELALKAYRALGCRGWGRVDFMLD-EDGKPYLLEVNT 268
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
2-217 |
5.09e-05 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 45.92 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 2 IKKLLIANRGEIAV-----------RIIRACRELGIETVAVYSEADKDALHVQMADEAFcIGPKASKdsylNVTNIVSVA 70
Cdd:PLN02735 23 LKKIMILGAGPIVIgqacefdysgtQACKALKEEGYEVVLINSNPATIMTDPETADRTY-IAPMTPE----LVEQVIAKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 71 KltgTDAIHPGYG---------FLAENAdfaeLCEEVNVTFVGPSADAISKMGTKDVARETMKQAGVPIVPgsQGIIENV 141
Cdd:PLN02735 98 R---PDALLPTMGgqtalnlavALAESG----ILEKYGVELIGAKLDAIKKAEDRELFKQAMEKIGLKTPP--SGIATTL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 142 EEAVSLANEIG-YPVIIKATAGGGGKGIRVARTEEELINGIKITQQEAATAfgnpGVYIEKYIEDFRHVEIQV---LADN 217
Cdd:PLN02735 169 DECFEIAEDIGeFPLIIRPAFTLGGTGGGIAYNKEEFETICKAGLAASITS----QVLVEKSLLGWKEYELEVmrdLADN 244
|
|
| PRK06019 |
PRK06019 |
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed |
20-215 |
1.08e-04 |
|
phosphoribosylaminoimidazole carboxylase ATPase subunit; Reviewed
Pssm-ID: 235674 [Multi-domain] Cd Length: 372 Bit Score: 44.37 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 20 ACRELGIEtVAVYSEaDKDALHVQMADEAFCigpkaskDSYLNVTNIVSVAKltGTDAIhpGYGFlaEN--ADFAE-LCE 96
Cdd:PRK06019 20 AAAPLGYK-VIVLDP-DPDSPAAQVADEVIV-------ADYDDVAALRELAE--QCDVI--TYEF--ENvpAEALDaLAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 97 EVNVTfvgPSADAISKmgTKDvaRETMKQ----AGVPIVPGSqgIIENVEEAVSLANEIGYPVIIKATaggggkgiR--- 169
Cdd:PRK06019 85 RVPVP---PGPDALAI--AQD--RLTEKQfldkLGIPVAPFA--VVDSAEDLEAALADLGLPAVLKTR--------Rggy 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1242724987 170 ------VARTEEELingikitqQEAATAFGNPGVYIEKYIeDFRHvEIQVLA 215
Cdd:PRK06019 148 dgkgqwVIRSAEDL--------EAAWALLGSVPCILEEFV-PFER-EVSVIV 189
|
|
| PatZN |
COG1042 |
Acyl-CoA synthetase (NDP forming) [Energy production and conversion]; |
119-159 |
3.47e-04 |
|
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
Pssm-ID: 440664 [Multi-domain] Cd Length: 708 Bit Score: 43.19 E-value: 3.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1242724987 119 ARETMKQAGVPIVPGsqGIIENVEEAVSLANEIGYPVIIKA 159
Cdd:COG1042 493 AKALLAAYGIPVVPT--RLARSAEEAVAAAEEIGYPVVLKI 531
|
|
| PLN02735 |
PLN02735 |
carbamoyl-phosphate synthase |
99-231 |
8.00e-04 |
|
carbamoyl-phosphate synthase
Pssm-ID: 215391 [Multi-domain] Cd Length: 1102 Bit Score: 42.07 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 99 NVTFVGPSADAISKMGTKDVARETMKQAGVPIVPGsqGIIENVEEAVSLANEIGYPVIIKATAGGGGKGIRVARTEEELI 178
Cdd:PLN02735 686 NVKIWGTSPDSIDAAEDRERFNAILNELKIEQPKG--GIARSEADALAIAKRIGYPVVVRPSYVLGGRAMEIVYSDDKLK 763
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1242724987 179 NGIKITQQEaatafgNPG--VYIEKYIEDFRHVEIQVLADNYGNT-------------IHLGERDCSI 231
Cdd:PLN02735 764 TYLETAVEV------DPErpVLVDKYLSDATEIDVDALADSEGNVviggimehieqagVHSGDSACSL 825
|
|
| PurK |
COG0026 |
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and ... |
22-215 |
1.00e-03 |
|
Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) [Nucleotide transport and metabolism]; Phosphoribosylaminoimidazole carboxylase (NCAIR synthetase) is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439797 [Multi-domain] Cd Length: 353 Bit Score: 41.21 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 22 RELGIEtVAVYSEaDKDALHVQMADEAFCigpkaskDSYLNVTNIVSVAKltGTDAIhpGYGFlaENADF---AELCEEV 98
Cdd:COG0026 11 KRLGYR-VHVLDP-DPDSPAAQVADEHIV-------ADYDDEEALREFAE--RCDVV--TFEF--ENVPAealEALEAEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 99 NVTfvgPSADAISKmgTKDvaRETMKQ----AGVPIVPGSqgIIENVEEAVSLANEIGYPVIIKATaggggkgiR----- 169
Cdd:COG0026 76 PVR---PGPEALEI--AQD--RLLEKAflaeLGIPVAPFA--AVDSLEDLEAAIAELGLPAVLKTR--------Rggydg 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1242724987 170 ----VARTEEELingikitqQEAATAFGNPGVYIEKYIeDFRHvEIQVLA 215
Cdd:COG0026 139 kgqvVIKSAADL--------EAAWAALGGGPCILEEFV-PFER-ELSVIV 178
|
|
| GARS_A |
pfam01071 |
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide ... |
114-218 |
1.12e-03 |
|
Phosphoribosylglycinamide synthetase, ATP-grasp (A) domain; Phosphoribosylglycinamide synthetase catalyzes the second step in the de novo biosynthesis of purine. The reaction catalyzed by Phosphoribosylglycinamide synthetase is the ATP- dependent addition of 5-phosphoribosylamine to glycine to form 5'phosphoribosylglycinamide. This domain is related to the ATP-grasp domain of biotin carboxylase/carbamoyl phosphate synthetase (see pfam02786).
Pssm-ID: 395851 [Multi-domain] Cd Length: 194 Bit Score: 39.96 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 114 GTKDVARETMKQAGVPIvpGSQGIIENVEEAVSLANEIGYPVI-IKATAGGGGKGIRVARTEEELINGIK-ITQQEAATA 191
Cdd:pfam01071 1 ASKSFAKDFMKRYGIPT--AEYETFTDPEEAKSYIQEAGFPAIvVKADGLAAGKGVIVASSNEEAIKAVDeILEQKKFGE 78
|
90 100
....*....|....*....|....*..
gi 1242724987 192 FGNPgVYIEKYIEDFrHVEIQVLADNY 218
Cdd:pfam01071 79 AGET-VVIEEFLEGE-EVSVLAFVDGK 103
|
|
| LysX |
COG0189 |
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ... |
1-204 |
1.15e-03 |
|
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 40.69 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 1 MIKKLLIAN--RGEIAVRIIRACRELGIETVavyseadkdalHVQMADEAFCIGPKASkdsylnvtnIVSVAKLTGTDAI 78
Cdd:COG0189 1 MMKIAILTDppDKDSTKALIEAAQRRGHEVE-----------VIDPDDLTLDLGRAPE---------LYRGEDLSEFDAV 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 79 -----HPGYGFlaenaDFAELCEEVNVTFVgPSADAISKMGTKDVARETMKQAGVPIVPgsQGIIENVEEAVSLANEIGY 153
Cdd:COG0189 61 lpridPPFYGL-----ALLRQLEAAGVPVV-NDPEAIRRARDKLFTLQLLARAGIPVPP--TLVTRDPDDLRAFLEELGG 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1242724987 154 PVIIKATAGGGGKGIRVARTEEELINGIkitqqEAATAFGNPGVYIEKYIE 204
Cdd:COG0189 133 PVVLKPLDGSGGRGVFLVEDEDALESIL-----EALTELGSEPVLVQEFIP 178
|
|
| ATP-grasp |
pfam02222 |
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family ... |
124-215 |
1.72e-03 |
|
ATP-grasp domain; This family does not contain all known ATP-grasp domain members. This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 396689 [Multi-domain] Cd Length: 169 Bit Score: 39.16 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 124 KQAGVPiVPGSQgIIENVEEAVSLANEIGYPVIIKA-TAGGGGKGIRVARTEEELingikitqQEAATAFGNPGVYIEKY 202
Cdd:pfam02222 1 QKLGLP-TPRFM-AAESLEELIEAGQELGYPCVVKArRGGYDGKGQYVVRSEADL--------PQAWEELGDGPVIVEEF 70
|
90
....*....|...
gi 1242724987 203 IeDFRhVEIQVLA 215
Cdd:pfam02222 71 V-PFD-RELSVLV 81
|
|
| Dala_Dala_lig_C |
pfam07478 |
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the ... |
123-292 |
1.86e-03 |
|
D-ala D-ala ligase C-terminus; This family represents the C-terminal, catalytic domain of the D-alanine--D-alanine ligase enzyme EC:6.3.2.4. D-Alanine is one of the central molecules of the cross-linking step of peptidoglycan assembly. There are three enzymes involved in the D-alanine branch of peptidoglycan biosynthesis: the pyridoxal phosphate-dependent D-alanine racemase (Alr), the ATP-dependent D-alanine:D-alanine ligase (Ddl), and the ATP-dependent D-alanine:D-alanine-adding enzyme (MurF).
Pssm-ID: 429483 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 123 MKQAGVPIVP-----------GSQGIIENVEEAVslaneiGYPVIIKATAGGGGKGIRVARTEEELINGIkitqqEAATA 191
Cdd:pfam07478 2 LKAAGLPVVPfvtftradwklNPKEWCAQVEEAL------GYPVFVKPARLGSSVGVSKVESREELQAAI-----EEAFQ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 192 FgNPGVYIEKYIEDfRHVEIQVLADNYGNTIHLGER--DCSIQRRLQKLLEESPS---PA-LDSEIREQMGDAAVKAAKA 265
Cdd:pfam07478 71 Y-DEKVLVEEGIEG-REIECAVLGNEDPEVSPVGEIvpSGGFYDYEAKYIDDSAQivvPAdLEEEQEEQIQELALKAYKA 148
|
170 180
....*....|....*....|....*..
gi 1242724987 266 VGYTGAGTVEFIYDyNEQRYYFMEMNT 292
Cdd:pfam07478 149 LGCRGLARVDFFLT-EDGEIVLNEVNT 174
|
|
| SucC |
COG0045 |
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ... |
119-159 |
2.99e-03 |
|
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA synthetase, beta subunit is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439815 [Multi-domain] Cd Length: 388 Bit Score: 39.65 E-value: 2.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1242724987 119 ARETMKQAGVPIVPGsqGIIENVEEAVSLANEIGY-PVIIKA 159
Cdd:COG0045 8 AKELLAKYGVPVPRG--IVATTPEEAVAAAEELGGpPVVVKA 47
|
|
| ATP-grasp_5 |
pfam13549 |
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ... |
127-158 |
4.72e-03 |
|
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent carboxylate-amine ligase activity.
Pssm-ID: 463918 [Multi-domain] Cd Length: 221 Bit Score: 38.23 E-value: 4.72e-03
10 20 30
....*....|....*....|....*....|..
gi 1242724987 127 GVPIVPgsQGIIENVEEAVSLANEIGYPVIIK 158
Cdd:pfam13549 23 GIPVVP--TRLARSPEEAVAAAEEIGYPVVLK 52
|
|
| rimK_fam |
TIGR00768 |
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione ... |
106-214 |
8.67e-03 |
|
alpha-L-glutamate ligase, RimK family; This family, related to bacterial glutathione synthetases, contains at least three different alpha-L-glutamate ligases. One is RimK, as in E. coli, which adds additional Glu residues to the native Glu-Glu C-terminus of ribosomal protein S6, but not to Lys-Glu mutants. Most species with a member of this subfamily lack an S6 homolog ending in Glu-Glu, however. Members in Methanococcus jannaschii act instead as a tetrahydromethanopterin:alpha-l-glutamate ligase (MJ0620) and a gamma-F420-2:alpha-l-glutamate ligase (MJ1001).
Pssm-ID: 273261 [Multi-domain] Cd Length: 276 Bit Score: 38.10 E-value: 8.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1242724987 106 SADAISKMGTKDVARETMKQAGVPiVPGSqGIIENVEEAVSLANEIGYPVIIKATAGGGGKGIRVARTEEELINGIKITQ 185
Cdd:TIGR00768 79 SSDAILNAGDKFLSHQLLAKAGIP-LPRT-GLAGSPEEALKLIEEIGFPVVLKPVFGSWGRGVSLARDRQAAESLLEHFE 156
|
90 100
....*....|....*....|....*....
gi 1242724987 186 QEAATAfgnPGVYIEKYIEDFRHVEIQVL 214
Cdd:TIGR00768 157 QLNGPQ---NLFLVQEYIKKPGGRDIRVF 182
|
|
| |
