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Conserved domains on  [gi|516412765|ref|WP_017802163|]
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Fe-S cluster assembly protein SufB [Erwinia toletana]

Protein Classification

Fe-S cluster assembly protein SufB( domain architecture ID 11485523)

Fe-S cluster assembly protein SufB is part of the SufBCD complex, which is an ATP-binding cassette (ABC) protein that functions in the biosynthesis of nascent Fe-S clusters

Gene Ontology:  GO:0016226

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK11814 PRK11814
cysteine desulfurase activator complex subunit SufB; Provisional
1-497 0e+00

cysteine desulfurase activator complex subunit SufB; Provisional


:

Pssm-ID: 236990 [Multi-domain]  Cd Length: 486  Bit Score: 1033.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765   1 MSRHTEASDDVQIWEgsHQNYKEGFFTNLETDELAHGLSEEVVRAISAKRNEPEWMLEFRLKAYEAWLKMEEPHWLKANY 80
Cdd:PRK11814   1 MSANTETTDDVKELV--NQEYKYGFVTDIETDELPKGLNEDVVRLISAKKNEPEWMLEWRLKAYRHWLTMEEPHWAKVHY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  81 KSLDYQDYSYYSAPSCgncddscASEPGATQAsgaepanyLTQEVEEAFKQLGVPVREG-----QEVAVDAIFDSVSVST 155
Cdd:PRK11814  79 PPIDYQDISYYSAPKC-------KSKPKSLDE--------VDPELLETFEKLGIPLREQkrlagREVAVDAVFDSVSVAT 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 156 TYRHKLAEQGIIFCSFSEAIHDHPELVQKYLGTVVPANDNFFAALNSAVASDGTFVYIPKGVRCPMELSTYFRINAAKTG 235
Cdd:PRK11814 144 TFKEKLAEAGVIFCSISEAIQEHPELVKKYLGSVVPVNDNFFAALNSAVFSDGSFVYIPKGVRCPMELSTYFRINAANTG 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 236 QFERTILVADEDSYVSYIEGCSAPVRDTYQLHAAVVEVIIHKNAEVKYSTVQNWFAGGE-AEGGILNFVTKRALCEGDGS 314
Cdd:PRK11814 224 QFERTLIIADEGSYVSYLEGCTAPMRDENQLHAAVVELVALDDAEIKYSTVQNWYPGDEnGKGGIYNFVTKRGLCRGENS 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 315 KMSWTQSETGSAITWKYPSVILRGDNSIGEFFSVALTAGHQQADTGTKMIHIGKNTKSTIISKGISAGKSENTYRGLVKI 394
Cdd:PRK11814 304 KISWTQVETGSAITWKYPSCILRGDNSVGEFYSVALTNGHQQADTGTKMIHIGKNTKSTIISKGISAGHSQNTYRGLVKI 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 395 MPTATNARNFTQCDSMLIGADCGAHTFPYVEVRNNTAQLEHEATTSRIGEDQLFYCVQRGISEDDAISMIVNGFCKDVFS 474
Cdd:PRK11814 384 MPKATNARNFTQCDSLLIGDQCGAHTFPYIEVKNNSAQVEHEATTSKISEDQLFYCRQRGISEEDAVSMIVNGFCKEVFQ 463
                        490       500
                 ....*....|....*....|...
gi 516412765 475 ELPLEFAVEAQKLLAISLEHSVG 497
Cdd:PRK11814 464 ELPMEFAVEAQKLLAISLEGSVG 486
 
Name Accession Description Interval E-value
PRK11814 PRK11814
cysteine desulfurase activator complex subunit SufB; Provisional
1-497 0e+00

cysteine desulfurase activator complex subunit SufB; Provisional


Pssm-ID: 236990 [Multi-domain]  Cd Length: 486  Bit Score: 1033.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765   1 MSRHTEASDDVQIWEgsHQNYKEGFFTNLETDELAHGLSEEVVRAISAKRNEPEWMLEFRLKAYEAWLKMEEPHWLKANY 80
Cdd:PRK11814   1 MSANTETTDDVKELV--NQEYKYGFVTDIETDELPKGLNEDVVRLISAKKNEPEWMLEWRLKAYRHWLTMEEPHWAKVHY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  81 KSLDYQDYSYYSAPSCgncddscASEPGATQAsgaepanyLTQEVEEAFKQLGVPVREG-----QEVAVDAIFDSVSVST 155
Cdd:PRK11814  79 PPIDYQDISYYSAPKC-------KSKPKSLDE--------VDPELLETFEKLGIPLREQkrlagREVAVDAVFDSVSVAT 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 156 TYRHKLAEQGIIFCSFSEAIHDHPELVQKYLGTVVPANDNFFAALNSAVASDGTFVYIPKGVRCPMELSTYFRINAAKTG 235
Cdd:PRK11814 144 TFKEKLAEAGVIFCSISEAIQEHPELVKKYLGSVVPVNDNFFAALNSAVFSDGSFVYIPKGVRCPMELSTYFRINAANTG 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 236 QFERTILVADEDSYVSYIEGCSAPVRDTYQLHAAVVEVIIHKNAEVKYSTVQNWFAGGE-AEGGILNFVTKRALCEGDGS 314
Cdd:PRK11814 224 QFERTLIIADEGSYVSYLEGCTAPMRDENQLHAAVVELVALDDAEIKYSTVQNWYPGDEnGKGGIYNFVTKRGLCRGENS 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 315 KMSWTQSETGSAITWKYPSVILRGDNSIGEFFSVALTAGHQQADTGTKMIHIGKNTKSTIISKGISAGKSENTYRGLVKI 394
Cdd:PRK11814 304 KISWTQVETGSAITWKYPSCILRGDNSVGEFYSVALTNGHQQADTGTKMIHIGKNTKSTIISKGISAGHSQNTYRGLVKI 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 395 MPTATNARNFTQCDSMLIGADCGAHTFPYVEVRNNTAQLEHEATTSRIGEDQLFYCVQRGISEDDAISMIVNGFCKDVFS 474
Cdd:PRK11814 384 MPKATNARNFTQCDSLLIGDQCGAHTFPYIEVKNNSAQVEHEATTSKISEDQLFYCRQRGISEEDAVSMIVNGFCKEVFQ 463
                        490       500
                 ....*....|....*....|...
gi 516412765 475 ELPLEFAVEAQKLLAISLEHSVG 497
Cdd:PRK11814 464 ELPMEFAVEAQKLLAISLEGSVG 486
sufB TIGR01980
FeS assembly protein SufB; This protein, SufB, forms a cytosolic complex SufBCD. This complex ...
19-488 0e+00

FeS assembly protein SufB; This protein, SufB, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 131035 [Multi-domain]  Cd Length: 448  Bit Score: 681.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765   19 QNYKEGFFTNLE-TDELAHGLSEEVVRAISAKRNEPEWMLEFRLKAYEAWLKMEEPHWLKAnYKSLDYQDYSYYSAPScg 97
Cdd:TIGR01980   1 TEYKYGFHDEDKyAYETEKGLTEEVVEEISEKKGEPDWMLDFRLRALELFEKMPMPTWGPD-LSGIDYEDIVYYSKPD-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765   98 ncddscasepgatqASGAEPANYLTQEVEEAFKQLGVPVREGQEVA-VDAIFDSVSVSTTYRHKLAEQGIIFCSFSEAIH 176
Cdd:TIGR01980  78 --------------KKKATSWDEVPDEIKDTFEKLGIPEAERKALAgVGAQYDSEVIYHNIKEDLEEKGVIFCDMDTALK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  177 DHPELVQKYLGTVVPANDNFFAALNSAVASDGTFVYIPKGVRCPMELSTYFRINAAKTGQFERTILVADEDSYVSYIEGC 256
Cdd:TIGR01980 144 EYPDLVKEYFMSVVPPSDNKFAALNGAVWSGGSFVYVPKGVRVDMPLQTYFRINSENTGQFEHTLIIADEGASVHYIEGC 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  257 SAPVRDTYQLHAAVVEVIIHKNAEVKYSTVQNWFAGgeaeggILNFVTKRALCEGDGsKMSWTQSETGSAITWKYPSVIL 336
Cdd:TIGR01980 224 SAPIYSTNSLHAAVVELIVKEDARVRYSTVQNWSKN------VYNLVTKRALVEENG-TMEWVSGSIGSKITMKYPSSIL 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  337 RGDNSIGEFFSVALTAGHQQADTGTKMIHIGKNTKSTIISKGISAGKSENTYRGLVKIMPTATNARNFTQCDSMLIGADC 416
Cdd:TIGR01980 297 KGEGAKTEFLSIAFAGKGQHLDTGAKMIHLAPNTSSTIISKSISKGGGKSTYRGLVKIGPGAKGAKSHVQCDSLLIDDES 376
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516412765  417 GAHTFPYVEVRNNTAQLEHEATTSRIGEDQLFYCVQRGISEDDAISMIVNGFCKDVFSELPLEFAVEAQKLL 488
Cdd:TIGR01980 377 ASDTIPYIEIFNDTVDVEHEATVSKISEEQLFYLMSRGLSEEDARAMIVRGFVEPITKELPMEYAVELNRLI 448
SufB COG0719
Fe-S cluster assembly scaffold protein SufB [Posttranslational modification, protein turnover, ...
69-496 1.32e-175

Fe-S cluster assembly scaffold protein SufB [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440483 [Multi-domain]  Cd Length: 393  Bit Score: 498.90  E-value: 1.32e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  69 KMEEPH-----WLKANYKSLDYQDYSYysapscgncddscasepgatqasgAEPANYLTQEVEEAFKQLGvpvregqevA 143
Cdd:COG0719    1 KLGLPTrrdeeWKYTDLSPLDLDDFAY------------------------APKAVEVPEEIKATLPEAE---------A 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 144 VDAIF-DSVSVsTTYRHKLAEQGIIFCSFSEAIHDHPELVQKYLGTVVPANDNFFAALNSAVASDGTFVYIPKGVRCPME 222
Cdd:COG0719   48 GRLVFvDGVFV-AELSDELAPKGVIFTSLSEALREHPELVKKYLGKVVPPDDDKFAALNTALWSDGVFIYVPKGVKVEKP 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 223 LSTYFRINAAKTGQFERTILVADEDSYVSYIEGCSAPVrDTYQLHAAVVEVIIHKNAEVKYSTVQNWfaggeaEGGILNF 302
Cdd:COG0719  127 LQLYFRINAEGTGQFERTLIVAEEGAEVTYIEGCTAPG-DEASLHNAVVEIVVGDNARLRYSTVQNW------SGNAYHF 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 303 VTKRALCEGDgSKMSWTQSETGSAITWKYPSVILRGDNSIGEFFSVALTAGHQQADTGTKMIHIGKNTKSTIISKGISAG 382
Cdd:COG0719  200 VTKRARVGRD-ARYEWTTGSLGSKLTRNYPSVILNGEGAEAELNGVALAGGGQHADTGTKVIHAAPNTTSRILSKGILDD 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 383 KSENTYRGLVKIMPTATNARNFTQCDSMLIGADCGAHTFPYVEVRNNTAQLEHEATTSRIGEDQLFYCVQRGISEDDAIS 462
Cdd:COG0719  279 RARGVFRGKIKVAKGAQKTDAYQSNRNLLLSDKARADTKPELEIYADDVKCSHGATVGQIDEEQLFYLRSRGISEEEARA 358
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 516412765 463 MIVNGFCKDVFSELPL-EFAVEAQKLLAISLEHSV 496
Cdd:COG0719  359 LLVNGFAAEVIEELPDeELREELNRLIELKLEGSV 393
SUFBD pfam01458
SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors ...
235-468 1.86e-88

SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S] and [4Fe-4S]. FeS cluster assembly is a complex process involving the mobilization of Fe and S atoms from storage sources, their assembly into [Fe-S] form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S] clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems. The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA, acting as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets. This entry represents SufB and SufD proteins, which are homologous, and form part of the SufBCD complex in the SUF system. SufB accepts sulfur transferred from SufE, whereas SufD may play a role in iron acquisition.


Pssm-ID: 460219 [Multi-domain]  Cd Length: 218  Bit Score: 270.09  E-value: 1.86e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  235 GQFERTILVADEDSYVSYIEgcsapvrdtYQLHAAVVEVIIHKNAEVKYSTVQNWfaggeaEGGILNFVTKRALCEGDgS 314
Cdd:pfam01458   1 GQFPRNLIVAEEGAEVTIIE---------EYEGCGVVEIYVGKGAKLRYVTVQNW------GENAYNFVTTRAELGAD-A 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  315 KMSWTQSETGSAITWKYPSVILRGDNSIGEFFSVALTAGHQQADTGTKMIHIGKNTKSTIISKGISAGKSENTYRGLVKI 394
Cdd:pfam01458  65 RVEWVQVSLGGKLTRNYPSVQLKGEGAEAELNGVYLADGGQHADTGTKVIHNGPNTSSNILSKGVLKDRSRGVFRGLIKV 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516412765  395 MPTATNARNFTQCDSMLIGADCGAHTFPYVEVRNNTAQLEHEATTSRIGEDQLFYCVQRGISEDDAISMIVNGF 468
Cdd:pfam01458 145 RKGAQKTDGHQECRNLLLSDKARADTIPELEIYADDVKCSHGATVGKIDEEQLFYLMSRGLSEEEARRLIVRGF 218
 
Name Accession Description Interval E-value
PRK11814 PRK11814
cysteine desulfurase activator complex subunit SufB; Provisional
1-497 0e+00

cysteine desulfurase activator complex subunit SufB; Provisional


Pssm-ID: 236990 [Multi-domain]  Cd Length: 486  Bit Score: 1033.65  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765   1 MSRHTEASDDVQIWEgsHQNYKEGFFTNLETDELAHGLSEEVVRAISAKRNEPEWMLEFRLKAYEAWLKMEEPHWLKANY 80
Cdd:PRK11814   1 MSANTETTDDVKELV--NQEYKYGFVTDIETDELPKGLNEDVVRLISAKKNEPEWMLEWRLKAYRHWLTMEEPHWAKVHY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  81 KSLDYQDYSYYSAPSCgncddscASEPGATQAsgaepanyLTQEVEEAFKQLGVPVREG-----QEVAVDAIFDSVSVST 155
Cdd:PRK11814  79 PPIDYQDISYYSAPKC-------KSKPKSLDE--------VDPELLETFEKLGIPLREQkrlagREVAVDAVFDSVSVAT 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 156 TYRHKLAEQGIIFCSFSEAIHDHPELVQKYLGTVVPANDNFFAALNSAVASDGTFVYIPKGVRCPMELSTYFRINAAKTG 235
Cdd:PRK11814 144 TFKEKLAEAGVIFCSISEAIQEHPELVKKYLGSVVPVNDNFFAALNSAVFSDGSFVYIPKGVRCPMELSTYFRINAANTG 223
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 236 QFERTILVADEDSYVSYIEGCSAPVRDTYQLHAAVVEVIIHKNAEVKYSTVQNWFAGGE-AEGGILNFVTKRALCEGDGS 314
Cdd:PRK11814 224 QFERTLIIADEGSYVSYLEGCTAPMRDENQLHAAVVELVALDDAEIKYSTVQNWYPGDEnGKGGIYNFVTKRGLCRGENS 303
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 315 KMSWTQSETGSAITWKYPSVILRGDNSIGEFFSVALTAGHQQADTGTKMIHIGKNTKSTIISKGISAGKSENTYRGLVKI 394
Cdd:PRK11814 304 KISWTQVETGSAITWKYPSCILRGDNSVGEFYSVALTNGHQQADTGTKMIHIGKNTKSTIISKGISAGHSQNTYRGLVKI 383
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 395 MPTATNARNFTQCDSMLIGADCGAHTFPYVEVRNNTAQLEHEATTSRIGEDQLFYCVQRGISEDDAISMIVNGFCKDVFS 474
Cdd:PRK11814 384 MPKATNARNFTQCDSLLIGDQCGAHTFPYIEVKNNSAQVEHEATTSKISEDQLFYCRQRGISEEDAVSMIVNGFCKEVFQ 463
                        490       500
                 ....*....|....*....|...
gi 516412765 475 ELPLEFAVEAQKLLAISLEHSVG 497
Cdd:PRK11814 464 ELPMEFAVEAQKLLAISLEGSVG 486
ycf24 CHL00085
putative ABC transporter
18-497 0e+00

putative ABC transporter


Pssm-ID: 214359 [Multi-domain]  Cd Length: 485  Bit Score: 761.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  18 HQNYKEGFFTNLETDELAHGLSEEVVRAISAKRNEPEWMLEFRLKAYEAWLKMEEPHWLKANYKSLDYQDYSYYSAPScg 97
Cdd:CHL00085  17 NQPYKYGFSTLIETERLPKGLNEDIVRLISKKKNEPIFLLIFRLKAYKKWKKMKEPDWAFLKYPEIDYQDISYYSAPK-- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  98 ncddscasepgatQASGAEPANYLTQEVEEAFKQLGVPVREGQE---VAVDAIFDSVSVSTTYRHKLAEQGIIFCSFSEA 174
Cdd:CHL00085  95 -------------LKKKLNSLDEVDPELLDTFEKLGISLNEQKRlanVAVDAVFDSVSIGTTFKEELAKAGVIFCSISEA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 175 IHDHPELVQKYLGTVVPANDNFFAALNSAVASDGTFVYIPKGVRCPMELSTYFRINAAKTGQFERTILVADEDSYVSYIE 254
Cdd:CHL00085 162 IQKYPELIKKYLGSVVPIGDNYFAALNSAVFSDGSFCYIPKDTKCPLELSTYFRINNEESGQFERTLIIAEENSYVSYLE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 255 GCSAPVRDTYQLHAAVVEVIIHKNAEVKYSTVQNWFAGGE-AEGGILNFVTKRALCEGDGSKMSWTQSETGSAITWKYPS 333
Cdd:CHL00085 242 GCTAPQYDTNQLHAAVVELIALENAEIKYSTVQNWYAGDEnGEGGIYNFVTKRGLCAGKNSKISWTQVETGSAITWKYPS 321
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 334 VILRGDNSIGEFFSVALTAGHQQADTGTKMIHIGKNTKSTIISKGISAGKSENTYRGLVKIMPTATNARNFTQCDSMLIG 413
Cdd:CHL00085 322 CILIGDNSQGEFYSVALTNNYQQADTGTKMIHIGKNTKSRIISKGISAGKSKNSYRGLVKIGPKALNSRNYSQCDSLLIG 401
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 414 ADCGAHTFPYVEVRNNTAQLEHEATTSRIGEDQLFYCVQRGISEDDAISMIVNGFCKDVFSELPLEFAVEAQKLLAISLE 493
Cdd:CHL00085 402 NKSQANTFPYIQVQNSTAKIEHEASTSKIGEEQLFYFLQRGINLEEAISLLISGFCKDVFNKLPMEFALEADRLLSLKLE 481

                 ....
gi 516412765 494 HSVG 497
Cdd:CHL00085 482 GSVG 485
sufB TIGR01980
FeS assembly protein SufB; This protein, SufB, forms a cytosolic complex SufBCD. This complex ...
19-488 0e+00

FeS assembly protein SufB; This protein, SufB, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 131035 [Multi-domain]  Cd Length: 448  Bit Score: 681.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765   19 QNYKEGFFTNLE-TDELAHGLSEEVVRAISAKRNEPEWMLEFRLKAYEAWLKMEEPHWLKAnYKSLDYQDYSYYSAPScg 97
Cdd:TIGR01980   1 TEYKYGFHDEDKyAYETEKGLTEEVVEEISEKKGEPDWMLDFRLRALELFEKMPMPTWGPD-LSGIDYEDIVYYSKPD-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765   98 ncddscasepgatqASGAEPANYLTQEVEEAFKQLGVPVREGQEVA-VDAIFDSVSVSTTYRHKLAEQGIIFCSFSEAIH 176
Cdd:TIGR01980  78 --------------KKKATSWDEVPDEIKDTFEKLGIPEAERKALAgVGAQYDSEVIYHNIKEDLEEKGVIFCDMDTALK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  177 DHPELVQKYLGTVVPANDNFFAALNSAVASDGTFVYIPKGVRCPMELSTYFRINAAKTGQFERTILVADEDSYVSYIEGC 256
Cdd:TIGR01980 144 EYPDLVKEYFMSVVPPSDNKFAALNGAVWSGGSFVYVPKGVRVDMPLQTYFRINSENTGQFEHTLIIADEGASVHYIEGC 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  257 SAPVRDTYQLHAAVVEVIIHKNAEVKYSTVQNWFAGgeaeggILNFVTKRALCEGDGsKMSWTQSETGSAITWKYPSVIL 336
Cdd:TIGR01980 224 SAPIYSTNSLHAAVVELIVKEDARVRYSTVQNWSKN------VYNLVTKRALVEENG-TMEWVSGSIGSKITMKYPSSIL 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  337 RGDNSIGEFFSVALTAGHQQADTGTKMIHIGKNTKSTIISKGISAGKSENTYRGLVKIMPTATNARNFTQCDSMLIGADC 416
Cdd:TIGR01980 297 KGEGAKTEFLSIAFAGKGQHLDTGAKMIHLAPNTSSTIISKSISKGGGKSTYRGLVKIGPGAKGAKSHVQCDSLLIDDES 376
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516412765  417 GAHTFPYVEVRNNTAQLEHEATTSRIGEDQLFYCVQRGISEDDAISMIVNGFCKDVFSELPLEFAVEAQKLL 488
Cdd:TIGR01980 377 ASDTIPYIEIFNDTVDVEHEATVSKISEEQLFYLMSRGLSEEDARAMIVRGFVEPITKELPMEYAVELNRLI 448
SufB COG0719
Fe-S cluster assembly scaffold protein SufB [Posttranslational modification, protein turnover, ...
69-496 1.32e-175

Fe-S cluster assembly scaffold protein SufB [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440483 [Multi-domain]  Cd Length: 393  Bit Score: 498.90  E-value: 1.32e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  69 KMEEPH-----WLKANYKSLDYQDYSYysapscgncddscasepgatqasgAEPANYLTQEVEEAFKQLGvpvregqevA 143
Cdd:COG0719    1 KLGLPTrrdeeWKYTDLSPLDLDDFAY------------------------APKAVEVPEEIKATLPEAE---------A 47
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 144 VDAIF-DSVSVsTTYRHKLAEQGIIFCSFSEAIHDHPELVQKYLGTVVPANDNFFAALNSAVASDGTFVYIPKGVRCPME 222
Cdd:COG0719   48 GRLVFvDGVFV-AELSDELAPKGVIFTSLSEALREHPELVKKYLGKVVPPDDDKFAALNTALWSDGVFIYVPKGVKVEKP 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 223 LSTYFRINAAKTGQFERTILVADEDSYVSYIEGCSAPVrDTYQLHAAVVEVIIHKNAEVKYSTVQNWfaggeaEGGILNF 302
Cdd:COG0719  127 LQLYFRINAEGTGQFERTLIVAEEGAEVTYIEGCTAPG-DEASLHNAVVEIVVGDNARLRYSTVQNW------SGNAYHF 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 303 VTKRALCEGDgSKMSWTQSETGSAITWKYPSVILRGDNSIGEFFSVALTAGHQQADTGTKMIHIGKNTKSTIISKGISAG 382
Cdd:COG0719  200 VTKRARVGRD-ARYEWTTGSLGSKLTRNYPSVILNGEGAEAELNGVALAGGGQHADTGTKVIHAAPNTTSRILSKGILDD 278
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 383 KSENTYRGLVKIMPTATNARNFTQCDSMLIGADCGAHTFPYVEVRNNTAQLEHEATTSRIGEDQLFYCVQRGISEDDAIS 462
Cdd:COG0719  279 RARGVFRGKIKVAKGAQKTDAYQSNRNLLLSDKARADTKPELEIYADDVKCSHGATVGQIDEEQLFYLRSRGISEEEARA 358
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 516412765 463 MIVNGFCKDVFSELPL-EFAVEAQKLLAISLEHSV 496
Cdd:COG0719  359 LLVNGFAAEVIEELPDeELREELNRLIELKLEGSV 393
SUFBD pfam01458
SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors ...
235-468 1.86e-88

SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors for numerous proteins involved in electron transfer, in redox and non-redox catalysis, in gene regulation, and as sensors of oxygen and iron. These functions depend on the various FeS cluster prosthetic groups, the most common being [2Fe-2S] and [4Fe-4S]. FeS cluster assembly is a complex process involving the mobilization of Fe and S atoms from storage sources, their assembly into [Fe-S] form, their transport to specific cellular locations, and their transfer to recipient apoproteins. So far, three FeS assembly machineries have been identified, which are capable of synthesising all types of [Fe-S] clusters: ISC (iron-sulphur cluster), SUF (sulphur assimilation), and NIF (nitrogen fixation) systems. The SUF system is an alternative pathway to the ISC system that operates under iron starvation and oxidative stress. It is found in eubacteria, archaea and eukaryotes (plastids). The SUF system is encoded by the suf operon (sufABCDSE), and the six encoded proteins are arranged into two complexes (SufSE and SufBCD) and one protein (SufA). SufS is a pyridoxal-phosphate (PLP) protein displaying cysteine desulphurase activity. SufE acts as a scaffold protein that accepts S from SufS and donates it to SufA. SufC is an ATPase with an unorthodox ATP-binding cassette (ABC)-like component. SufA is homologous to IscA, acting as a scaffold protein in which Fe and S atoms are assembled into [FeS] cluster forms, which can then easily be transferred to apoproteins targets. This entry represents SufB and SufD proteins, which are homologous, and form part of the SufBCD complex in the SUF system. SufB accepts sulfur transferred from SufE, whereas SufD may play a role in iron acquisition.


Pssm-ID: 460219 [Multi-domain]  Cd Length: 218  Bit Score: 270.09  E-value: 1.86e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  235 GQFERTILVADEDSYVSYIEgcsapvrdtYQLHAAVVEVIIHKNAEVKYSTVQNWfaggeaEGGILNFVTKRALCEGDgS 314
Cdd:pfam01458   1 GQFPRNLIVAEEGAEVTIIE---------EYEGCGVVEIYVGKGAKLRYVTVQNW------GENAYNFVTTRAELGAD-A 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  315 KMSWTQSETGSAITWKYPSVILRGDNSIGEFFSVALTAGHQQADTGTKMIHIGKNTKSTIISKGISAGKSENTYRGLVKI 394
Cdd:pfam01458  65 RVEWVQVSLGGKLTRNYPSVQLKGEGAEAELNGVYLADGGQHADTGTKVIHNGPNTSSNILSKGVLKDRSRGVFRGLIKV 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 516412765  395 MPTATNARNFTQCDSMLIGADCGAHTFPYVEVRNNTAQLEHEATTSRIGEDQLFYCVQRGISEDDAISMIVNGF 468
Cdd:pfam01458 145 RKGAQKTDGHQECRNLLLSDKARADTIPELEIYADDVKCSHGATVGKIDEEQLFYLMSRGLSEEEARRLIVRGF 218
sufD TIGR01981
FeS assembly protein SufD; This protein, SufD, forms a cytosolic complex SufBCD. This complex ...
203-484 9.09e-50

FeS assembly protein SufD; This protein, SufD, forms a cytosolic complex SufBCD. This complex enhances the cysteine desulfurase of SufSE. The system, together with SufA, is believed to act in iron-sulfur cluster formation during oxidative stress. SufB and SufD are homologous. Note that SufC belongs to the family of ABC transporter ATP binding proteins, so this protein, encoded by an adjacent gene, has often been annotated as a transporter component. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273908  Cd Length: 275  Bit Score: 171.65  E-value: 9.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  203 AVASDGTFVYIPKGVRCPMELSTYFRINAAKTGQFERTILVADEDSYVSYIEGCSAPVRDTYqlHAAVVEVIIHKNAEVK 282
Cdd:TIGR01981   2 ALFNSGLVLYIPKGVEAEEPIELRFIMGSENRVLAPRLLIVVEEGAKATVLERHDSGEGDAF--LNGLVEINVGENASVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  283 YSTVQNWfaGGEAeggiLNFVTKRAlCEGDGSKMSWTQSETGSAITWKYPSVILRGDNSIGEFFSVALTAGHQQADTGTK 362
Cdd:TIGR01981  80 FIKVQFL--SATS----FHFSTVRI-TLERDARVRLSDVNLGGKLSRHDTDVDLNGEGSKAEIKGLYFGDGSQHIDVHTN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765  363 MIHIGKNTKSTIISKGISAGKSENTYRGLVKIMPTATNARNFTQCDSMLIGADCGAHTFPYVEVRNNTAQLEHEATTSRI 442
Cdd:TIGR01981 153 VIHNGPHTVSNILHRGVLDDRAHGVFNGNIDIPKGAQGTDARQSNRTLLLSDKARADTKPELEIDADDVKASHGATVGQL 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 516412765  443 GEDQLFYCVQRGISEDDAISMIVNGFCKDVFSELPLEFAVEA 484
Cdd:TIGR01981 233 DEEQLFYLRSRGIDEAEAKRLLIEGFFGEVIEEIPDESLKEE 274
SufBD_N pfam19295
SufBD protein N-terminal region; This entry represents the N-terminal part of the SufB and ...
164-218 8.05e-14

SufBD protein N-terminal region; This entry represents the N-terminal part of the SufB and SufD proteins. It has a right handed beta helix structure. This family is associated with the C-terminal region pfam01458


Pssm-ID: 437127  Cd Length: 172  Bit Score: 69.47  E-value: 8.05e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 516412765  164 QGIIFCSFSEAIHDHPELVQKYLGTVVPANDNFFAALNSAVASDGTFVYIPKGVR 218
Cdd:pfam19295 111 EGVIVGSLAEAAEKYPELVEKYYGKLAKTDEDGLTALNTMLAQDGLFVYVPKGVV 165
PRK10948 PRK10948
Fe-S cluster assembly protein SufD;
324-468 4.70e-12

Fe-S cluster assembly protein SufD;


Pssm-ID: 236804 [Multi-domain]  Cd Length: 424  Bit Score: 67.75  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516412765 324 GSAITWKYPSVILRGDNSIGEFFSVALTAGHQQADTGTKMIHIGKNTKSTIISKGISAGKSENTYRGLVKIMPTA----- 398
Cdd:PRK10948 250 GAAVLRHNTSTQLNGENSTLRLNSLAMPVKNEVCDTRTWLEHNKGYCNSRQLHKTIVSDKGRAVFNGLIKVAQHAiktdg 329
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516412765 399 --TNarnftqcDSMLIGADCGAHTFPYVEVRNNTAQLEHEATTSRIGEDQLFYCVQRGISEDDAISMIVNGF 468
Cdd:PRK10948 330 qmTN-------NNLLLGKLAEVDTKPQLEIYADDVKCSHGATVGRIDDEQLFYLRSRGINQQDAQQMIIYAF 394
 
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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