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Conserved domains on  [gi|1491342116|gb|RLJ01587|]
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MAG: CoA-binding protein, partial [Candidatus Aenigmatarchaeota archaeon]

Protein Classification

acetate--CoA ligase family protein( domain architecture ID 11437147)

acetate--CoA ligase family protein similar to ADP-forming acetate--CoA ligase that catalyzes the formation of acetate and ATP from acetyl-CoA by using ADP and phosphate

CATH:  3.30.1490.20
EC:  6.2.1.-
Gene Ontology:  GO:0043758|GO:0005524|GO:0046872
PubMed:  15491124|15316652
SCOP:  3000003

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
1-642 0e+00

Acyl-CoA synthetase (NDP forming) [Energy production and conversion];


:

Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 909.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116   1 YSSVLDVGEDVDLGVVAVPARIVPQVAEEAGEKGVKGLIVISAGFKEAGLEGAKRERELLDICRRYGVRLLGPNCLGLIN 80
Cdd:COG1042    60 YPSVADLPEPPDLAVIAVPAETVPDVVEECGEKGVKAAVVISAGFAETGEEGAALEQELLEIARRYGMRLLGPNCLGLIN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116  81 TSTPINASFAPRMPRKGGIAFASQSGALCTAILDWAAKEGVGFSNLISLGNMADMDETDFMEILAEDPATKVILIYVEGI 160
Cdd:COG1042   140 PATGLNATFAPVPPLPGNIALVSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGI 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 161 KDGKKFLKVSPRVSRVKPVVILKSGTSDAGAKAAASHTGSIAGSRVAYETAFKKCGVLQASTIEELFNLGIAFASQPLPQ 240
Cdd:COG1042   220 RDGRRFLSAARAAARGKPVVVLKSGRSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPR 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 241 GRNVSIVTNAGGPSIVATDACSRYGLNMAWLSPKTVEKLRSSLPEEASWTNPVDILGDATAERYRLALEAVFSDEFVDSV 320
Cdd:COG1042   300 GRRLAIVTNSGGPGVLAADALEDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAV 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 321 VVILTPQAMTQPLETAKHIVDLnSRFPRVPVFAVFMGGERVEEAVRLLKDAGIPVYSNPEDAASTIAGIVRYIDLLNRRV 400
Cdd:COG1042   380 LVILTPTAMTDPEEVAEALIEA-AKGSGKPVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLM 458

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 401 EE-DFPKFDVDRETVKSIIERAKRERRPSLLSVEARQVVQAYGIKVPESELAQNVRQAVNAARRIGYPVALKVVSPQILH 479
Cdd:COG1042   459 ETpASEDFDPDRERARAIIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILH 538

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 480 KTDVGGVKLNLKSDREVVIAFNEILRNVNVLMPEARVFGVEVQKMVPAGKEIIVGMNRDVQFGPLIMFGLGGIYVNILKD 559
Cdd:COG1042   539 KSDVGGVRLNLRDAEAVRAAFEEILARVRAARPDARIDGVLVQPMVPGGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKD 618

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 560 VSFRLAPLSRQEAYEMVAETKAYALLRGIRGEPPADIDSVVDTLLRVSQLALDFEEISEIDINPLFVYERGDGALALDVK 639
Cdd:COG1042   619 VALRLPPLNEALAREMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIR 698


                  ...
gi 1491342116 640 VTV 642
Cdd:COG1042   699 LAP 701
 
Name Accession Description Interval E-value
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
1-642 0e+00

Acyl-CoA synthetase (NDP forming) [Energy production and conversion];


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 909.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116   1 YSSVLDVGEDVDLGVVAVPARIVPQVAEEAGEKGVKGLIVISAGFKEAGLEGAKRERELLDICRRYGVRLLGPNCLGLIN 80
Cdd:COG1042    60 YPSVADLPEPPDLAVIAVPAETVPDVVEECGEKGVKAAVVISAGFAETGEEGAALEQELLEIARRYGMRLLGPNCLGLIN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116  81 TSTPINASFAPRMPRKGGIAFASQSGALCTAILDWAAKEGVGFSNLISLGNMADMDETDFMEILAEDPATKVILIYVEGI 160
Cdd:COG1042   140 PATGLNATFAPVPPLPGNIALVSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGI 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 161 KDGKKFLKVSPRVSRVKPVVILKSGTSDAGAKAAASHTGSIAGSRVAYETAFKKCGVLQASTIEELFNLGIAFASQPLPQ 240
Cdd:COG1042   220 RDGRRFLSAARAAARGKPVVVLKSGRSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPR 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 241 GRNVSIVTNAGGPSIVATDACSRYGLNMAWLSPKTVEKLRSSLPEEASWTNPVDILGDATAERYRLALEAVFSDEFVDSV 320
Cdd:COG1042   300 GRRLAIVTNSGGPGVLAADALEDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAV 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 321 VVILTPQAMTQPLETAKHIVDLnSRFPRVPVFAVFMGGERVEEAVRLLKDAGIPVYSNPEDAASTIAGIVRYIDLLNRRV 400
Cdd:COG1042   380 LVILTPTAMTDPEEVAEALIEA-AKGSGKPVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLM 458

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 401 EE-DFPKFDVDRETVKSIIERAKRERRPSLLSVEARQVVQAYGIKVPESELAQNVRQAVNAARRIGYPVALKVVSPQILH 479
Cdd:COG1042   459 ETpASEDFDPDRERARAIIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILH 538

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 480 KTDVGGVKLNLKSDREVVIAFNEILRNVNVLMPEARVFGVEVQKMVPAGKEIIVGMNRDVQFGPLIMFGLGGIYVNILKD 559
Cdd:COG1042   539 KSDVGGVRLNLRDAEAVRAAFEEILARVRAARPDARIDGVLVQPMVPGGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKD 618

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 560 VSFRLAPLSRQEAYEMVAETKAYALLRGIRGEPPADIDSVVDTLLRVSQLALDFEEISEIDINPLFVYERGDGALALDVK 639
Cdd:COG1042   619 VALRLPPLNEALAREMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIR 698


                  ...
gi 1491342116 640 VTV 642
Cdd:COG1042   699 LAP 701
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 1-392 0e+00

acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it is believed that this group of ADP-dependent acetyl-CoA synthetases (ACS) act in the direction of acetate and ATP production in the organisms in which it has been characterized. In most species this protein exists as a fused alpha-beta domain polypeptide. In Pyrococcus and related species, however the domains exist as separate polypeptides. This model represents the alpha (N-terminal) domain. In Pyrococcus and related species there appears to have been the development of a paralogous family such that four other proteins are close relatives. In reference, one of these (along with its beta-domain partner) was characterized as ACS-II showing specificity for phenylacetyl-CoA. This model has been constructed to exclude these non-ACS-I paralogs. This may result in new, authentic ACS-I sequences falling below the trusted cutoff.


Pssm-ID: 131764 [Multi-domain]  Cd Length: 447  Bit Score: 553.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116   1 YSSVLDVGEDVDLGVVAVPARIVPQVAEEAGEKGVKGLIVISAGFKEAGLEGAKRERELLDICRRYGVRLLGPNCLGLIN 80
Cdd:TIGR02717  55 YPSVLEIPDPVDLAVIVVPAKYVPQVVEECGEKGVKGAVVITAGFKEVGEEGAELEQELVEIARKYGMRLLGPNCLGIIN 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116  81 TSTPINASFAPRMPRKGGIAFASQSGALCTAILDWAAKEGVGFSNLISLGNMADMDETDFMEILAEDPATKVILIYVEGI 160
Cdd:TIGR02717 135 THIKLNATFAPTMPKKGGIAFISQSGALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGI 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 161 KDGKKFLKVSPRVSRVKPVVILKSGTSDAGAKAAASHTGSIAGSRVAYETAFKKCGVLQASTIEELFNLGIAFASQPLPQ 240
Cdd:TIGR02717 215 KDGRKFLKTAREISKKKPIVVLKSGTSEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPK 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 241 GRNVSIVTNAGGPSIVATDACSRYGLNMAWLSPKTVEKLRSSLPEEASWTNPVDILGDATAERYRLALEAVFSDEFVDSV 320
Cdd:TIGR02717 295 GNRVAIITNAGGPGVIATDACEENGLELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGV 374

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491342116 321 VVILTPQAMTQPLETAKHIVDLNSRFPRVPVFAVFMGGERVEEAVRLLKDAGIPVYSNPEDAASTIAGIVRY 392
Cdd:TIGR02717 375 VVVLTPTAMTDPEEVAKGIIEGAKKSNEKPVVAGFMGGKSVDPAKRILEENGIPNYTFPERAVKALSALYRY 446
ATP-grasp_5 pfam13549
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 420-642 2.53e-109

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: 328.28  E-value: 2.53e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 420 RAKRERRPSLLSVEARQVVQAYGIKVPESELAQNVRQAVNAARRIGYPVALKVVSPQILHKTDVGGVKLNLKSDREVVIA 499
Cdd:pfam13549   1 KALAEGRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 500 FNEILRNVNVLMPEARVFGVEVQKMVPAGKEIIVGMNRDVQFGPLIMFGLGGIYVNILKDVSFRLAPLSRQEAYEMVAET 579
Cdd:pfam13549  81 YEEILERVRRYRPDARIEGVLVQPMAPGGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMIRRT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491342116 580 KAYALLRGIRGEPPADIDSVVDTLLRVSQLALDFEEISEIDINPLFVYErgDGALALDVKVTV 642
Cdd:pfam13549 161 RAYKLLKGYRGEPPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADE--DGVVALDARIRL 221
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 1-45 1.04e-10

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 58.68  E-value: 1.04e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1491342116    1 YSSVLDVGE--DVDLGVVAVPARIVPQVAEEAGEKGVKGLIVISAGF 45
Cdd:smart00881  54 YDSVAEAPEetGVDVAVIFVPAEAAPDAIDEAIEAGIKGIVVITEGI 100
sucC PRK00696
ADP-forming succinate--CoA ligase subunit beta;
433-642 3.77e-07

ADP-forming succinate--CoA ligase subunit beta;


Pssm-ID: 234813 [Multi-domain]  Cd Length: 388  Bit Score: 52.78  E-value: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 433 EARQVVQAYGIKVPESELAQNVRQAVNAARRIGYPVAlkVVSPQIlH-----KtdVGGVKLnLKSDREVVIAFNEILRNV 507
Cdd:PRK00696    7 QAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVW--VVKAQV-HaggrgK--AGGVKL-AKSPEEAREFAKQILGMT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 508 NVLMPEA----RVFGVEVQKMVPAGKEIIVG--MNRDVQfGPLIMFGL-GGiyVNIlkdvsfrlaplsrqeayEMVAETK 580
Cdd:PRK00696   81 LVTHQTGpkgqPVNKVLVEEGADIAKEYYLSivLDRATR-RVVFMASTeGG--MDI-----------------EEVAEET 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 581 AYALLR-------GIR-----------GEPPADIDSVVDTLLRVSQLALDfEEISEIDINPLFVyeRGDGAL-ALDVKVT 641
Cdd:PRK00696  141 PEKIHKvaidpltGLQpfqareiafklGLPGEQVKQFAKILMGLYKAFVE-KDASLVEINPLVV--TKDGDLiALDAKIN 217


                  .
gi 1491342116 642 V 642
Cdd:PRK00696  218 F 218
 
Name Accession Description Interval E-value
PatZN COG1042
Acyl-CoA synthetase (NDP forming) [Energy production and conversion];
1-642 0e+00

Acyl-CoA synthetase (NDP forming) [Energy production and conversion];


Pssm-ID: 440664 [Multi-domain]  Cd Length: 708  Bit Score: 909.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116   1 YSSVLDVGEDVDLGVVAVPARIVPQVAEEAGEKGVKGLIVISAGFKEAGLEGAKRERELLDICRRYGVRLLGPNCLGLIN 80
Cdd:COG1042    60 YPSVADLPEPPDLAVIAVPAETVPDVVEECGEKGVKAAVVISAGFAETGEEGAALEQELLEIARRYGMRLLGPNCLGLIN 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116  81 TSTPINASFAPRMPRKGGIAFASQSGALCTAILDWAAKEGVGFSNLISLGNMADMDETDFMEILAEDPATKVILIYVEGI 160
Cdd:COG1042   140 PATGLNATFAPVPPLPGNIALVSQSGALGTAILDWAAARGIGFSHFVSLGNEADVDFADLLDYLADDPDTRVILLYLEGI 219

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 161 KDGKKFLKVSPRVSRVKPVVILKSGTSDAGAKAAASHTGSIAGSRVAYETAFKKCGVLQASTIEELFNLGIAFASQPLPQ 240
Cdd:COG1042   220 RDGRRFLSAARAAARGKPVVVLKSGRSEAGARAAASHTGALAGSDAVYDAAFRRAGVIRVDDLEELFDAAEALARQPPPR 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 241 GRNVSIVTNAGGPSIVATDACSRYGLNMAWLSPKTVEKLRSSLPEEASWTNPVDILGDATAERYRLALEAVFSDEFVDSV 320
Cdd:COG1042   300 GRRLAIVTNSGGPGVLAADALEDLGLELAELSEETQAALRAVLPPFASVGNPVDITGDADPERYAAALEALLADPNVDAV 379

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 321 VVILTPQAMTQPLETAKHIVDLnSRFPRVPVFAVFMGGERVEEAVRLLKDAGIPVYSNPEDAASTIAGIVRYIDLLNRRV 400
Cdd:COG1042   380 LVILTPTAMTDPEEVAEALIEA-AKGSGKPVLASWMGGDSVAEARRLLREAGIPTFRTPERAVRALAALVRYRRNQERLM 458

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 401 EE-DFPKFDVDRETVKSIIERAKRERRPSLLSVEARQVVQAYGIKVPESELAQNVRQAVNAARRIGYPVALKVVSPQILH 479
Cdd:COG1042   459 ETpASEDFDPDRERARAIIEAALAEGRGVLTEAEAKALLAAYGIPVVPTRLARSAEEAVAAAEEIGYPVVLKIVSPDILH 538

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 480 KTDVGGVKLNLKSDREVVIAFNEILRNVNVLMPEARVFGVEVQKMVPAGKEIIVGMNRDVQFGPLIMFGLGGIYVNILKD 559
Cdd:COG1042   539 KSDVGGVRLNLRDAEAVRAAFEEILARVRAARPDARIDGVLVQPMVPGGVELIVGVKRDPVFGPVIMFGLGGIFVEVLKD 618

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 560 VSFRLAPLSRQEAYEMVAETKAYALLRGIRGEPPADIDSVVDTLLRVSQLALDFEEISEIDINPLFVYERGDGALALDVK 639
Cdd:COG1042   619 VALRLPPLNEALAREMIRELRAAKLLRGYRGRPPADLDALADVLVRLSQLAADLPEILELDINPLLVVPEGVVAVDARIR 698


                  ...
gi 1491342116 640 VTV 642
Cdd:COG1042   699 LAP 701
AcCoA-syn-alpha TIGR02717
acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it ...
 1-392 0e+00

acetyl coenzyme A synthetase (ADP forming), alpha domain; Although technically reversible, it is believed that this group of ADP-dependent acetyl-CoA synthetases (ACS) act in the direction of acetate and ATP production in the organisms in which it has been characterized. In most species this protein exists as a fused alpha-beta domain polypeptide. In Pyrococcus and related species, however the domains exist as separate polypeptides. This model represents the alpha (N-terminal) domain. In Pyrococcus and related species there appears to have been the development of a paralogous family such that four other proteins are close relatives. In reference, one of these (along with its beta-domain partner) was characterized as ACS-II showing specificity for phenylacetyl-CoA. This model has been constructed to exclude these non-ACS-I paralogs. This may result in new, authentic ACS-I sequences falling below the trusted cutoff.


Pssm-ID: 131764 [Multi-domain]  Cd Length: 447  Bit Score: 553.07  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116   1 YSSVLDVGEDVDLGVVAVPARIVPQVAEEAGEKGVKGLIVISAGFKEAGLEGAKRERELLDICRRYGVRLLGPNCLGLIN 80
Cdd:TIGR02717  55 YPSVLEIPDPVDLAVIVVPAKYVPQVVEECGEKGVKGAVVITAGFKEVGEEGAELEQELVEIARKYGMRLLGPNCLGIIN 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116  81 TSTPINASFAPRMPRKGGIAFASQSGALCTAILDWAAKEGVGFSNLISLGNMADMDETDFMEILAEDPATKVILIYVEGI 160
Cdd:TIGR02717 135 THIKLNATFAPTMPKKGGIAFISQSGALLTALLDWAEKNGVGFSYFVSLGNKADIDESDLLEYLADDPDTKVILLYLEGI 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 161 KDGKKFLKVSPRVSRVKPVVILKSGTSDAGAKAAASHTGSIAGSRVAYETAFKKCGVLQASTIEELFNLGIAFASQPLPQ 240
Cdd:TIGR02717 215 KDGRKFLKTAREISKKKPIVVLKSGTSEAGAKAASSHTGALAGSDEAYDAAFKQAGVIRADSIEELFDLARLLSNQPLPK 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 241 GRNVSIVTNAGGPSIVATDACSRYGLNMAWLSPKTVEKLRSSLPEEASWTNPVDILGDATAERYRLALEAVFSDEFVDSV 320
Cdd:TIGR02717 295 GNRVAIITNAGGPGVIATDACEENGLELAELSEATKNKLRNILPPEASIKNPVDVLGDATPERYAKALKTVAEDENVDGV 374

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1491342116 321 VVILTPQAMTQPLETAKHIVDLNSRFPRVPVFAVFMGGERVEEAVRLLKDAGIPVYSNPEDAASTIAGIVRY 392
Cdd:TIGR02717 375 VVVLTPTAMTDPEEVAKGIIEGAKKSNEKPVVAGFMGGKSVDPAKRILEENGIPNYTFPERAVKALSALYRY 446
ATP-grasp_5 pfam13549
ATP-grasp domain; This family includes a diverse set of enzymes that possess ATP-dependent ...
 420-642 2.53e-109

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: 328.28  E-value: 2.53e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 420 RAKRERRPSLLSVEARQVVQAYGIKVPESELAQNVRQAVNAARRIGYPVALKVVSPQILHKTDVGGVKLNLKSDREVVIA 499
Cdd:pfam13549   1 KALAEGRTVLTEPEAKALLAAYGIPVVPTRLARSPEEAVAAAEEIGYPVVLKIVSPDILHKSDVGGVRLNLRSAEAVRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 500 FNEILRNVNVLMPEARVFGVEVQKMVPAGKEIIVGMNRDVQFGPLIMFGLGGIYVNILKDVSFRLAPLSRQEAYEMVAET 579
Cdd:pfam13549  81 YEEILERVRRYRPDARIEGVLVQPMAPGGRELIVGVTRDPQFGPVIMFGLGGIAVEVLKDVAFRLPPLNMTLAREMIRRT 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1491342116 580 KAYALLRGIRGEPPADIDSVVDTLLRVSQLALDFEEISEIDINPLFVYErgDGALALDVKVTV 642
Cdd:pfam13549 161 RAYKLLKGYRGEPPADLDALEDVLVRVSQLVIDFPEIRELDINPLLADE--DGVVALDARIRL 221
Succ_CoA_lig pfam13607
Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from ...
 96-233 1.94e-64

Succinyl-CoA ligase like flavodoxin domain; This domain contains the catalytic domain from Succinyl-CoA ligase alpha subunit and other related enzymes. A conserved histidine is involved in phosphoryl transfer.


Pssm-ID: 433345 [Multi-domain]  Cd Length: 138  Bit Score: 208.47  E-value: 1.94e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116  96 KGGIAFASQSGALCTAILDWAAKEGVGFSNLISLGNMADMDETDFMEILAEDPATKVILIYVEGIKDGKKFLKVSPRVSR 175
Cdd:pfam13607   1 PGNIALVSQSGALGAALLDWARSRGIGFSKFVSLGNEADVDFADLLEYLADDPETRVILLYLEGIRDGRRFLRAARRAAR 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1491342116 176 VKPVVILKSGTSDAGAKAAASHTGSIAGSRVAYETAFKKCGVLQASTIEELFNLGIAF 233
Cdd:pfam13607  81 RKPVVVLKAGRSEAGARAAASHTGALAGSDAVYDAAFRQAGVIRVDDLEELFDAAEAL 138
SucD COG0074
Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA ...
 10-226 1.16e-13

Succinyl-CoA synthetase, alpha subunit [Energy production and conversion]; Succinyl-CoA synthetase, alpha subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 439844 [Multi-domain]  Cd Length: 288  Bit Score: 72.02  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116  10 DVDLGVVAVPARIVPQVAEEAGEKGVKGLIVISagfkeaglEG--AKRERELLDICRRYGVRLLGPNCLGLIntsTPiNA 87
Cdd:COG0074    64 GADASVIFVPPPFAADAILEAIDAGIKLIVCIT--------EGipVLDMVRVKRYAKAKGTRLIGPNCPGII---TP-GE 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116  88 SFAPRMP----RKGGIAFASQSGALCTAILDWAAKEGVGFSNLISLGN--MADMDETDFMEILAEDPATKVILIYVE-G- 159
Cdd:COG0074   132 CKLGIMPghifKPGRVGIVSRSGTLTYEAVWQLTQAGLGQSTCVGIGGdpIIGTSFIDVLELFEEDPETEAIVMIGEiGg 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 160 ---------IKDGKKflkvsprvsrvKPVVILKSGTS--------DAGAKaAASHTGSiAGSRVAyetAFKKCGVLQAST 222
Cdd:COG0074   212 saeeeaaeyIKENMT-----------KPVVAYIAGRTappgkrmgHAGAI-ISGGKGT-AESKIE---ALEAAGVPVAES 275


                  ....
gi 1491342116 223 IEEL 226
Cdd:COG0074   276 PSEI 279
Ligase_CoA_2 pfam19045
Ligase-CoA domain; This domain is related to pfam00549 and adopts a flavodoxin fold.
 244-376 9.73e-11

Ligase-CoA domain; This domain is related to pfam00549 and adopts a flavodoxin fold.


Pssm-ID: 408815  Cd Length: 162  Bit Score: 60.74  E-value: 9.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 244 VSIVTNAGGPSIVATDACSRYGLNMAWLSPKTVEKLRSSLPEEASWTNPVDILGDATAERYRLALEAVFSDEFVDSVVV- 322
Cdd:pfam19045   1 VVIITGAGGSGVLLSDACVDNGLTLMAIPPDLDAAFRKFIPPFGAAGNPVDITGGEPPSTYEATIRLGLEDPRIHALILg 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1491342116 323 ----ILTPQAMTQPLeTAKHIVDLNSRFPRVPVFAVFMGGERVEEAVRLLKDAGIPVY 376
Cdd:pfam19045  81 ywhtIVTPPMVFAEL-MVRVVEEMRAKGIDKPVVASLAGDVEVEEAAEYLFQHGIVAY 137
CoA_binding smart00881
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 1-45 1.04e-10

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 214881 [Multi-domain]  Cd Length: 100  Bit Score: 58.68  E-value: 1.04e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1491342116    1 YSSVLDVGE--DVDLGVVAVPARIVPQVAEEAGEKGVKGLIVISAGF 45
Cdd:smart00881  54 YDSVAEAPEetGVDVAVIFVPAEAAPDAIDEAIEAGIKGIVVITEGI 100
CoA_binding_2 pfam13380
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 1-81 1.18e-10

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 433162 [Multi-domain]  Cd Length: 116  Bit Score: 59.09  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116   1 YSSVLDVGEDVDLGVVAVPARIVPQVAEEAGEKGVKGLIVISAGfkeaglegakRERELLDICRRYGVRLLGPNCLGLIN 80
Cdd:pfam13380  46 YPSLADPPEPVDLVDVFRPPEAVPEIVEEALALGAKAVWLQPGI----------ENEEAAAIARAAGIRVVGDRCLGVEH 115


                  .
gi 1491342116  81 T 81
Cdd:pfam13380 116 P 116
SucC COG0045
Succinyl-CoA synthetase, beta subunit [Energy production and conversion]; Succinyl-CoA ...
 433-642 5.85e-08

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: 55.44  E-value: 5.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 433 EARQVVQAYGIKVPESELAQNVRQAVNAARRIGYPVAlkVVSPQILH----KtdVGGVKLnLKSDREVVIAFNEILRNV- 507
Cdd:COG0045     7 QAKELLAKYGVPVPRGIVATTPEEAVAAAEELGGPPV--VVKAQVHAggrgK--AGGVKL-AKSPEEAREAAEEILGMTl 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 508 --NVLMPEAR-VFGVEVQKMVPAGKEIIVGM--NRDVQfGPLIMF-GLGGiyVNIlkdvsfrlaplsrqeayEMVAETKA 581
Cdd:COG0045    82 vtHQTGPKGKpVNKVLVEEGVDIAKELYLSIllDRATR-RPVIMAsTEGG--MDI-----------------EEVAEETP 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1491342116 582 YALLR-------GIR-----------GEPPADIDSVVDTLLRVSQLALDfEEISEIDINPLFVYERGDgALALDVKVTV 642
Cdd:COG0045   142 EKIIKvpidplvGLQpyqarelafalGLPGKQVKQFAKILKKLYRAFVE-KDASLVEINPLVVTKDGR-LVALDAKVNF 218
sucC PRK00696
ADP-forming succinate--CoA ligase subunit beta;
433-642 3.77e-07

ADP-forming succinate--CoA ligase subunit beta;


Pssm-ID: 234813 [Multi-domain]  Cd Length: 388  Bit Score: 52.78  E-value: 3.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 433 EARQVVQAYGIKVPESELAQNVRQAVNAARRIGYPVAlkVVSPQIlH-----KtdVGGVKLnLKSDREVVIAFNEILRNV 507
Cdd:PRK00696    7 QAKELFAKYGVPVPRGIVATTPEEAVEAAEELGGGVW--VVKAQV-HaggrgK--AGGVKL-AKSPEEAREFAKQILGMT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 508 NVLMPEA----RVFGVEVQKMVPAGKEIIVG--MNRDVQfGPLIMFGL-GGiyVNIlkdvsfrlaplsrqeayEMVAETK 580
Cdd:PRK00696   81 LVTHQTGpkgqPVNKVLVEEGADIAKEYYLSivLDRATR-RVVFMASTeGG--MDI-----------------EEVAEET 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 581 AYALLR-------GIR-----------GEPPADIDSVVDTLLRVSQLALDfEEISEIDINPLFVyeRGDGAL-ALDVKVT 641
Cdd:PRK00696  141 PEKIHKvaidpltGLQpfqareiafklGLPGEQVKQFAKILMGLYKAFVE-KDASLVEINPLVV--TKDGDLiALDAKIN 217


                  .
gi 1491342116 642 V 642
Cdd:PRK00696  218 F 218
ATP-grasp_2 pfam08442
ATP-grasp domain;
433-624 4.93e-07

ATP-grasp domain;


Pssm-ID: 400651 [Multi-domain]  Cd Length: 202  Bit Score: 50.72  E-value: 4.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 433 EARQVVQAYGIKVPESELAQNVRQAVNAARRIGYPVAlkVVSPQIL--HKTDVGGVKlnLKSDREVVIAFNEILRNVNVL 510
Cdd:pfam08442   6 QAKEIFAKYGIPVPRGEVATSPEEAEEIAKKLGGKVY--VVKAQVLagGRGKAGGVK--LAKSPEEAKEVAKEMLGKNLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 511 MPEARVFGVEVQK-MVPAGKEI-------IVgMNRDVQfGPLIMFGL-GGiyVNIlkdvsfrlaplsrqeayEMVAETKA 581
Cdd:pfam08442  82 TKQTGPDGQPVNKvLVEEALDIkkeyylsIV-LDRASK-GPVIIASTeGG--VDI-----------------EEVAAKNP 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1491342116 582 YALLR-------GIR-----------GEPPADIDSVVDTLLRVSQLALDfEEISEIDINPL 624
Cdd:pfam08442 141 EKIHKfpidplkGLTpyqareiafklGLPGELIKQAADIIKKLYKLFVE-YDATLVEINPL 200
CoA_binding pfam02629
CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins ...
 1-44 2.39e-06

CoA binding domain; This domain has a Rossmann fold and is found in a number of proteins including succinyl CoA synthetases, malate and ATP-citrate ligases.


Pssm-ID: 396961 [Multi-domain]  Cd Length: 97  Bit Score: 46.05  E-value: 2.39e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1491342116   1 YSSVLDVGE--DVDLGVVAVPARIVPQVAEEAGEKGVKGLIVISAG 44
Cdd:pfam02629  52 YNSVDELEEktGVDVAVITVPAPFAQEAIDELVDAGIKGIVNITPG 97
PRK14016 PRK14016
cyanophycin synthetase; Provisional
 439-530 4.46e-06

cyanophycin synthetase; Provisional


Pssm-ID: 237586 [Multi-domain]  Cd Length: 727  Bit Score: 49.77  E-value: 4.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 439 QAYGIKVPESELAQNVRQAVNAARRIGYPVALKvvsPQIlhktdvG----GVKLNLKSDREVVIAFneilrnvNVLMPEA 514
Cdd:PRK14016  223 AAAGVPVPEGRVVTSAEDAWEAAEEIGYPVVVK---PLD------GnhgrGVTVNITTREEIEAAY-------AVASKES 286

                          90
                  ....*....|....*.
gi 1491342116 515 RvfGVEVQKMVPaGKE 530
Cdd:PRK14016  287 S--DVIVERYIP-GKD 299
PTZ00187 PTZ00187
succinyl-CoA synthetase alpha subunit; Provisional
 12-217 5.05e-05

succinyl-CoA synthetase alpha subunit; Provisional


Pssm-ID: 240307 [Multi-domain]  Cd Length: 317  Bit Score: 45.86  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116  12 DLGVVAVPARIVPQVAEEAGEKGVKGLIVISAGFKEAGLegAKRERELLDICRrygVRLLGPNCLGLINtstPINASFAP 91
Cdd:PTZ00187   90 DASVIYVPPPHAASAIIEAIEAEIPLVVCITEGIPQHDM--VKVKHALLSQNK---TRLIGPNCPGIIK---PGECKIGI 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116  92 rMP----RKGGIAFASQSGALCTAILDWAAKEGVGFSNLISLG----NMADMdeTDFMEILAEDPATKVILIYVE----G 159
Cdd:PTZ00187  162 -MPghihKKGKIGIVSRSGTLTYEAVAQTTAVGLGQSTCVGIGgdpfNGTNF--IDCLKLFLNDPETEGIILIGEiggtA 238

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1491342116 160 IKDGKKFLKVSPrvsRVKPVVILKSGTSdAGAKAAASHTGSI-------AGSRVAyetAFKKCGV 217
Cdd:PTZ00187  239 EEEAAEWIKNNP---IKKPVVSFIAGIT-APPGRRMGHAGAIisggkgtAPGKIE---ALEAAGV 296
PRK05678 PRK05678
succinyl-CoA synthetase subunit alpha; Validated
 1-154 7.17e-05

succinyl-CoA synthetase subunit alpha; Validated


Pssm-ID: 180194 [Multi-domain]  Cd Length: 291  Bit Score: 45.16  E-value: 7.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116   1 YSSVLDVGE--DVDLGVVAVPARIVPQVAEEAGEKGVKGLIVISAGFKEAGLEGAKRErelldiCRRYGVRLLGPNCLGL 78
Cdd:PRK05678   54 FNTVAEAVEatGANASVIYVPPPFAADAILEAIDAGIDLIVCITEGIPVLDMLEVKAY------LERKKTRLIGPNCPGI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116  79 IntsTPiNASFAPRMP----RKGGIAFASQSGALCTAILDWAAKEGVGFSNLISLGNmadmDE---TDFMEILA---EDP 148
Cdd:PRK05678  128 I---TP-GECKIGIMPghihKKGRVGVVSRSGTLTYEAVAQLTDLGFGQSTCVGIGG----DPingTNFIDVLEafeEDP 199


                  ....*.
gi 1491342116 149 ATKVIL 154
Cdd:PRK05678  200 ETEAIV 205
AccC COG0439
Biotin carboxylase [Lipid transport and metabolism]; Biotin carboxylase is part of the Pathway ...
 432-545 1.55e-04

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: 43.71  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116 432 VEARQVVQAYGIKVPESELAQNVRQAVNAARRIGYPVALKVVSpqilhktDVG--GVKLnLKSDREVVIAFNEILRNVNV 509
Cdd:COG0439    56 VLMREALAAAGVPVPGFALVDSPEEALAFAEEIGYPVVVKPAD-------GAGsrGVRV-VRDEEELEAALAEARAEAKA 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1491342116 510 LMPEARVF--------GVEVQKMVPAGKEIIVGMNRDVQFGPLI 545
Cdd:COG0439   128 GSPNGEVLveeflegrEYSVEGLVRDGEVVVCSITRKHQKPPYF 171
PRK06091 PRK06091
membrane protein FdrA; Validated
 10-153 4.59e-03

membrane protein FdrA; Validated


Pssm-ID: 180395 [Multi-domain]  Cd Length: 555  Bit Score: 40.03  E-value: 4.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1491342116  10 DVDLGVVAVPARIVPQVAEEAGEKGvKGLIVISAGF---KEAGLEGAKRERELLdicrrygvrLLGPNCLGLINTSTPIn 86
Cdd:PRK06091  117 DANLALISVAGEYAAELAEQALDRN-LNVMMFSDNVtleDEIRLKTRAREKGLL---------VMGPDCGTAMIAGTPL- 185

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1491342116  87 aSFAPRMPrKGGIAFASQSGA----LCTAIldwaAKEGVGFSNLISLGNMaDMDET-------DFMEILAEDPATKVI 153
Cdd:PRK06091  186 -AFANVMP-EGNIGVIGASGTgiqeLCSQI----ALAGEGITHAIGLGGR-DLSAEvggisalTALEMLSADEKSEVI 256
CarB COG0458
Carbamoylphosphate synthase large subunit [Amino acid transport and metabolism, Nucleotide ...
 435-468 4.71e-03

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: 39.86  E-value: 4.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1491342116 435 RQVVQAYGIKVPESELAQNVRQAVNAARRIGYPV 468
Cdd:COG0458   119 KELLDKLGIPQPKSGTATSVEEALAIAEEIGYPV 152
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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