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Conserved domains on  [gi|517996658|ref|WP_019166866|]
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MULTISPECIES: Fe-S cluster assembly protein SufB [Staphylococcus intermedius group]

Protein Classification

Fe-S cluster assembly protein SufB( domain architecture ID 11493419)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
sufB TIGR01980
FeS assembly protein SufB; This protein, SufB, forms a cytosolic complex SufBCD. This complex ...
9-456 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: 832.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658    9 GDYKYGFHDEDVSIFRSERGLTENIVREISRMKNEPEWMLDFRLKSLKQFYKMPMPQWGGDLSELDFDDITYYVKPSERS 88
Cdd:TIGR01980   1 TEYKYGFHDEDKYAYETEKGLTEEVVEEISEKKGEPDWMLDFRLRALELFEKMPMPTWGPDLSGIDYEDIVYYSKPDKKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658   89 ERSWDEVPEEIKRTFDKLGIPEAEQKYLAGVSAQYESEVVYHNMEKELEEKGIIFKDTDTALKENEELFKEYFASVIPAA 168
Cdd:TIGR01980  81 ATSWDEVPDEIKDTFEKLGIPEAERKALAGVGAQYDSEVIYHNIKEDLEEKGVIFCDMDTALKEYPDLVKEYFMSVVPPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  169 DNKFAALNSAVWSGGSFIYVPKNVKLDTPLQAYFRINSENMGQFERTLIIADEGASVNYVEGCTAPVYTTNSLHSAVVEI 248
Cdd:TIGR01980 161 DNKFAALNGAVWSGGSFVYVPKGVRVDMPLQTYFRINSENTGQFEHTLIIADEGASVHYIEGCSAPIYSTNSLHAAVVEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  249 IVHKDAHVRYTTIQNWANNVYNLVTKRTFVHENGNMEWVDGNLGSKLTMKYPACVLLGEGAKGSTLSIAFAGKGQVQDAG 328
Cdd:TIGR01980 241 IVKEDARVRYSTVQNWSKNVYNLVTKRALVEENGTMEWVSGSIGSKITMKYPSSILKGEGAKTEFLSIAFAGKGQHLDTG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  329 AKMIHKAPNTSSTIVSKSISKDGGKVVYRGIVHFGRKAKGARSNIECDTLILDNQSTSDTIPYNEIFNDHISLEHEAKVS 408
Cdd:TIGR01980 321 AKMIHLAPNTSSTIISKSISKGGGKSTYRGLVKIGPGAKGAKSHVQCDSLLIDDESASDTIPYIEIFNDTVDVEHEATVS 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 517996658  409 KVSEEQLFYLMSRGISEEEATEMIVMGFIEPFTKELPMEYAVEMNRLI 456
Cdd:TIGR01980 401 KISEEQLFYLMSRGLSEEDARAMIVRGFVEPITKELPMEYAVELNRLI 448
 
Name Accession Description Interval E-value
sufB TIGR01980
FeS assembly protein SufB; This protein, SufB, forms a cytosolic complex SufBCD. This complex ...
9-456 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: 832.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658    9 GDYKYGFHDEDVSIFRSERGLTENIVREISRMKNEPEWMLDFRLKSLKQFYKMPMPQWGGDLSELDFDDITYYVKPSERS 88
Cdd:TIGR01980   1 TEYKYGFHDEDKYAYETEKGLTEEVVEEISEKKGEPDWMLDFRLRALELFEKMPMPTWGPDLSGIDYEDIVYYSKPDKKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658   89 ERSWDEVPEEIKRTFDKLGIPEAEQKYLAGVSAQYESEVVYHNMEKELEEKGIIFKDTDTALKENEELFKEYFASVIPAA 168
Cdd:TIGR01980  81 ATSWDEVPDEIKDTFEKLGIPEAERKALAGVGAQYDSEVIYHNIKEDLEEKGVIFCDMDTALKEYPDLVKEYFMSVVPPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  169 DNKFAALNSAVWSGGSFIYVPKNVKLDTPLQAYFRINSENMGQFERTLIIADEGASVNYVEGCTAPVYTTNSLHSAVVEI 248
Cdd:TIGR01980 161 DNKFAALNGAVWSGGSFVYVPKGVRVDMPLQTYFRINSENTGQFEHTLIIADEGASVHYIEGCSAPIYSTNSLHAAVVEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  249 IVHKDAHVRYTTIQNWANNVYNLVTKRTFVHENGNMEWVDGNLGSKLTMKYPACVLLGEGAKGSTLSIAFAGKGQVQDAG 328
Cdd:TIGR01980 241 IVKEDARVRYSTVQNWSKNVYNLVTKRALVEENGTMEWVSGSIGSKITMKYPSSILKGEGAKTEFLSIAFAGKGQHLDTG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  329 AKMIHKAPNTSSTIVSKSISKDGGKVVYRGIVHFGRKAKGARSNIECDTLILDNQSTSDTIPYNEIFNDHISLEHEAKVS 408
Cdd:TIGR01980 321 AKMIHLAPNTSSTIISKSISKGGGKSTYRGLVKIGPGAKGAKSHVQCDSLLIDDESASDTIPYIEIFNDTVDVEHEATVS 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 517996658  409 KVSEEQLFYLMSRGISEEEATEMIVMGFIEPFTKELPMEYAVEMNRLI 456
Cdd:TIGR01980 401 KISEEQLFYLMSRGLSEEDARAMIVRGFVEPITKELPMEYAVELNRLI 448
SufB COG0719
Fe-S cluster assembly scaffold protein SufB [Posttranslational modification, protein turnover, ...
60-464 0e+00

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


Pssm-ID: 440483 [Multi-domain]  Cd Length: 393  Bit Score: 537.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  60 KMPMPQ-----WGG-DLSELDFDDITYyvKPSErserswDEVPEEIKRTFdklgiPEAEqkylAGVsAQYESEVVYHNME 133
Cdd:COG0719    1 KLGLPTrrdeeWKYtDLSPLDLDDFAY--APKA------VEVPEEIKATL-----PEAE----AGR-LVFVDGVFVAELS 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 134 KELEEKGIIFKDTDTALKENEELFKEYFASVIPAADNKFAALNSAVWSGGSFIYVPKNVKLDTPLQAYFRINSENMGQFE 213
Cdd:COG0719   63 DELAPKGVIFTSLSEALREHPELVKKYLGKVVPPDDDKFAALNTALWSDGVFIYVPKGVKVEKPLQLYFRINAEGTGQFE 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 214 RTLIIADEGASVNYVEGCTAPVyTTNSLHSAVVEIIVHKDAHVRYTTIQNWANNVYNLVTKRTFVHENGNMEWVDGNLGS 293
Cdd:COG0719  143 RTLIVAEEGAEVTYIEGCTAPG-DEASLHNAVVEIVVGDNARLRYSTVQNWSGNAYHFVTKRARVGRDARYEWTTGSLGS 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 294 KLTMKYPACVLLGEGAKGSTLSIAFAGKGQVQDAGAKMIHKAPNTSSTIVSKSISKDGGKVVYRGIVHFGRKAKGARSNI 373
Cdd:COG0719  222 KLTRNYPSVILNGEGAEAELNGVALAGGGQHADTGTKVIHAAPNTTSRILSKGILDDRARGVFRGKIKVAKGAQKTDAYQ 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 374 ECDTLILDNQSTSDTIPYNEIFNDHISLEHEAKVSKVSEEQLFYLMSRGISEEEATEMIVMGFIEPFTKELP-MEYAVEM 452
Cdd:COG0719  302 SNRNLLLSDKARADTKPELEIYADDVKCSHGATVGQIDEEQLFYLRSRGISEEEARALLVNGFAAEVIEELPdEELREEL 381
                        410
                 ....*....|..
gi 517996658 453 NRLIKFEMEGSI 464
Cdd:COG0719  382 NRLIELKLEGSV 393
PRK11814 PRK11814
cysteine desulfurase activator complex subunit SufB; Provisional
7-465 0e+00

cysteine desulfurase activator complex subunit SufB; Provisional


Pssm-ID: 236990 [Multi-domain]  Cd Length: 486  Bit Score: 530.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658   7 DVGDYKYGFhdedVSIFRSE---RGLTENIVREISRMKNEPEWMLDFRLKSLKQFYKMPMPQWG-GDLSELDFDDITYYV 82
Cdd:PRK11814  15 VNQEYKYGF----VTDIETDelpKGLNEDVVRLISAKKNEPEWMLEWRLKAYRHWLTMEEPHWAkVHYPPIDYQDISYYS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  83 KPSERSE-RSWDEVPEEIKRTFDKLGIPEAEQKYLAG----VSAQYESEVVYHNMEKELEEKGIIFKDTDTALKENEELF 157
Cdd:PRK11814  91 APKCKSKpKSLDEVDPELLETFEKLGIPLREQKRLAGrevaVDAVFDSVSVATTFKEKLAEAGVIFCSISEAIQEHPELV 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 158 KEYFASVIPAADNKFAALNSAVWSGGSFIYVPKNVKLDTPLQAYFRINSENMGQFERTLIIADEGASVNYVEGCTAPVYT 237
Cdd:PRK11814 171 KKYLGSVVPVNDNFFAALNSAVFSDGSFVYIPKGVRCPMELSTYFRINAANTGQFERTLIIADEGSYVSYLEGCTAPMRD 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 238 TNSLHSAVVEIIVHKDAHVRYTTIQNW----ANN---VYNLVTKRTFVH-ENGNMEWVDGNLGSKLTMKYPACVLLGEGA 309
Cdd:PRK11814 251 ENQLHAAVVELVALDDAEIKYSTVQNWypgdENGkggIYNFVTKRGLCRgENSKISWTQVETGSAITWKYPSCILRGDNS 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 310 KGSTLSIAFAGKGQVQDAGAKMIHKAPNTSSTIVSKSISKDGGKVVYRGIVHFGRKAKGARSNIECDTLILDNQSTSDTI 389
Cdd:PRK11814 331 VGEFYSVALTNGHQQADTGTKMIHIGKNTKSTIISKGISAGHSQNTYRGLVKIMPKATNARNFTQCDSLLIGDQCGAHTF 410
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517996658 390 PYNEIFNDHISLEHEAKVSKVSEEQLFYLMSRGISEEEATEMIVMGFIEPFTKELPMEYAVEMNRLIKFEMEGSIG 465
Cdd:PRK11814 411 PYIEVKNNSAQVEHEATTSKISEDQLFYCRQRGISEEDAVSMIVNGFCKEVFQELPMEFAVEAQKLLAISLEGSVG 486
SUFBD pfam01458
SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors ...
210-436 1.36e-104

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: 310.15  E-value: 1.36e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  210 GQFERTLIIADEGASVNYVEgctapvyttNSLHSAVVEIIVHKDAHVRYTTIQNWANNVYNLVTKRTFVHENGNMEWVDG 289
Cdd:pfam01458   1 GQFPRNLIVAEEGAEVTIIE---------EYEGCGVVEIYVGKGAKLRYVTVQNWGENAYNFVTTRAELGADARVEWVQV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  290 NLGSKLTMKYPACVLLGEGAKGSTLSIAFAGKGQVQDAGAKMIHKAPNTSSTIVSKSISKDGGKVVYRGIVHFGRKAKGA 369
Cdd:pfam01458  72 SLGGKLTRNYPSVQLKGEGAEAELNGVYLADGGQHADTGTKVIHNGPNTSSNILSKGVLKDRSRGVFRGLIKVRKGAQKT 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517996658  370 RSNIECDTLILDNQSTSDTIPYNEIFNDHISLEHEAKVSKVSEEQLFYLMSRGISEEEATEMIVMGF 436
Cdd:pfam01458 152 DGHQECRNLLLSDKARADTIPELEIYADDVKCSHGATVGKIDEEQLFYLMSRGLSEEEARRLIVRGF 218
 
Name Accession Description Interval E-value
sufB TIGR01980
FeS assembly protein SufB; This protein, SufB, forms a cytosolic complex SufBCD. This complex ...
9-456 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: 832.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658    9 GDYKYGFHDEDVSIFRSERGLTENIVREISRMKNEPEWMLDFRLKSLKQFYKMPMPQWGGDLSELDFDDITYYVKPSERS 88
Cdd:TIGR01980   1 TEYKYGFHDEDKYAYETEKGLTEEVVEEISEKKGEPDWMLDFRLRALELFEKMPMPTWGPDLSGIDYEDIVYYSKPDKKK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658   89 ERSWDEVPEEIKRTFDKLGIPEAEQKYLAGVSAQYESEVVYHNMEKELEEKGIIFKDTDTALKENEELFKEYFASVIPAA 168
Cdd:TIGR01980  81 ATSWDEVPDEIKDTFEKLGIPEAERKALAGVGAQYDSEVIYHNIKEDLEEKGVIFCDMDTALKEYPDLVKEYFMSVVPPS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  169 DNKFAALNSAVWSGGSFIYVPKNVKLDTPLQAYFRINSENMGQFERTLIIADEGASVNYVEGCTAPVYTTNSLHSAVVEI 248
Cdd:TIGR01980 161 DNKFAALNGAVWSGGSFVYVPKGVRVDMPLQTYFRINSENTGQFEHTLIIADEGASVHYIEGCSAPIYSTNSLHAAVVEL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  249 IVHKDAHVRYTTIQNWANNVYNLVTKRTFVHENGNMEWVDGNLGSKLTMKYPACVLLGEGAKGSTLSIAFAGKGQVQDAG 328
Cdd:TIGR01980 241 IVKEDARVRYSTVQNWSKNVYNLVTKRALVEENGTMEWVSGSIGSKITMKYPSSILKGEGAKTEFLSIAFAGKGQHLDTG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  329 AKMIHKAPNTSSTIVSKSISKDGGKVVYRGIVHFGRKAKGARSNIECDTLILDNQSTSDTIPYNEIFNDHISLEHEAKVS 408
Cdd:TIGR01980 321 AKMIHLAPNTSSTIISKSISKGGGKSTYRGLVKIGPGAKGAKSHVQCDSLLIDDESASDTIPYIEIFNDTVDVEHEATVS 400
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 517996658  409 KVSEEQLFYLMSRGISEEEATEMIVMGFIEPFTKELPMEYAVEMNRLI 456
Cdd:TIGR01980 401 KISEEQLFYLMSRGLSEEDARAMIVRGFVEPITKELPMEYAVELNRLI 448
SufB COG0719
Fe-S cluster assembly scaffold protein SufB [Posttranslational modification, protein turnover, ...
60-464 0e+00

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


Pssm-ID: 440483 [Multi-domain]  Cd Length: 393  Bit Score: 537.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  60 KMPMPQ-----WGG-DLSELDFDDITYyvKPSErserswDEVPEEIKRTFdklgiPEAEqkylAGVsAQYESEVVYHNME 133
Cdd:COG0719    1 KLGLPTrrdeeWKYtDLSPLDLDDFAY--APKA------VEVPEEIKATL-----PEAE----AGR-LVFVDGVFVAELS 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 134 KELEEKGIIFKDTDTALKENEELFKEYFASVIPAADNKFAALNSAVWSGGSFIYVPKNVKLDTPLQAYFRINSENMGQFE 213
Cdd:COG0719   63 DELAPKGVIFTSLSEALREHPELVKKYLGKVVPPDDDKFAALNTALWSDGVFIYVPKGVKVEKPLQLYFRINAEGTGQFE 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 214 RTLIIADEGASVNYVEGCTAPVyTTNSLHSAVVEIIVHKDAHVRYTTIQNWANNVYNLVTKRTFVHENGNMEWVDGNLGS 293
Cdd:COG0719  143 RTLIVAEEGAEVTYIEGCTAPG-DEASLHNAVVEIVVGDNARLRYSTVQNWSGNAYHFVTKRARVGRDARYEWTTGSLGS 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 294 KLTMKYPACVLLGEGAKGSTLSIAFAGKGQVQDAGAKMIHKAPNTSSTIVSKSISKDGGKVVYRGIVHFGRKAKGARSNI 373
Cdd:COG0719  222 KLTRNYPSVILNGEGAEAELNGVALAGGGQHADTGTKVIHAAPNTTSRILSKGILDDRARGVFRGKIKVAKGAQKTDAYQ 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 374 ECDTLILDNQSTSDTIPYNEIFNDHISLEHEAKVSKVSEEQLFYLMSRGISEEEATEMIVMGFIEPFTKELP-MEYAVEM 452
Cdd:COG0719  302 SNRNLLLSDKARADTKPELEIYADDVKCSHGATVGQIDEEQLFYLRSRGISEEEARALLVNGFAAEVIEELPdEELREEL 381
                        410
                 ....*....|..
gi 517996658 453 NRLIKFEMEGSI 464
Cdd:COG0719  382 NRLIELKLEGSV 393
PRK11814 PRK11814
cysteine desulfurase activator complex subunit SufB; Provisional
7-465 0e+00

cysteine desulfurase activator complex subunit SufB; Provisional


Pssm-ID: 236990 [Multi-domain]  Cd Length: 486  Bit Score: 530.19  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658   7 DVGDYKYGFhdedVSIFRSE---RGLTENIVREISRMKNEPEWMLDFRLKSLKQFYKMPMPQWG-GDLSELDFDDITYYV 82
Cdd:PRK11814  15 VNQEYKYGF----VTDIETDelpKGLNEDVVRLISAKKNEPEWMLEWRLKAYRHWLTMEEPHWAkVHYPPIDYQDISYYS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  83 KPSERSE-RSWDEVPEEIKRTFDKLGIPEAEQKYLAG----VSAQYESEVVYHNMEKELEEKGIIFKDTDTALKENEELF 157
Cdd:PRK11814  91 APKCKSKpKSLDEVDPELLETFEKLGIPLREQKRLAGrevaVDAVFDSVSVATTFKEKLAEAGVIFCSISEAIQEHPELV 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 158 KEYFASVIPAADNKFAALNSAVWSGGSFIYVPKNVKLDTPLQAYFRINSENMGQFERTLIIADEGASVNYVEGCTAPVYT 237
Cdd:PRK11814 171 KKYLGSVVPVNDNFFAALNSAVFSDGSFVYIPKGVRCPMELSTYFRINAANTGQFERTLIIADEGSYVSYLEGCTAPMRD 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 238 TNSLHSAVVEIIVHKDAHVRYTTIQNW----ANN---VYNLVTKRTFVH-ENGNMEWVDGNLGSKLTMKYPACVLLGEGA 309
Cdd:PRK11814 251 ENQLHAAVVELVALDDAEIKYSTVQNWypgdENGkggIYNFVTKRGLCRgENSKISWTQVETGSAITWKYPSCILRGDNS 330
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 310 KGSTLSIAFAGKGQVQDAGAKMIHKAPNTSSTIVSKSISKDGGKVVYRGIVHFGRKAKGARSNIECDTLILDNQSTSDTI 389
Cdd:PRK11814 331 VGEFYSVALTNGHQQADTGTKMIHIGKNTKSTIISKGISAGHSQNTYRGLVKIMPKATNARNFTQCDSLLIGDQCGAHTF 410
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517996658 390 PYNEIFNDHISLEHEAKVSKVSEEQLFYLMSRGISEEEATEMIVMGFIEPFTKELPMEYAVEMNRLIKFEMEGSIG 465
Cdd:PRK11814 411 PYIEVKNNSAQVEHEATTSKISEDQLFYCRQRGISEEDAVSMIVNGFCKEVFQELPMEFAVEAQKLLAISLEGSVG 486
ycf24 CHL00085
putative ABC transporter
11-465 2.60e-175

putative ABC transporter


Pssm-ID: 214359 [Multi-domain]  Cd Length: 485  Bit Score: 500.31  E-value: 2.60e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  11 YKYGFHDeDVSIFRSERGLTENIVREISRMKNEPEWMLDFRLKSLKQFYKMPMPQWGG-DLSELDFDDITYYVKPSERSE 89
Cdd:CHL00085  20 YKYGFST-LIETERLPKGLNEDIVRLISKKKNEPIFLLIFRLKAYKKWKKMKEPDWAFlKYPEIDYQDISYYSAPKLKKK 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  90 -RSWDEVPEEIKRTFDKLGIPEAEQKYLAGVS--AQYESEVVYHNMEKELEEKGIIFKDTDTALKENEELFKEYFASVIP 166
Cdd:CHL00085  99 lNSLDEVDPELLDTFEKLGISLNEQKRLANVAvdAVFDSVSIGTTFKEELAKAGVIFCSISEAIQKYPELIKKYLGSVVP 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 167 AADNKFAALNSAVWSGGSFIYVPKNVKLDTPLQAYFRINSENMGQFERTLIIADEGASVNYVEGCTAPVYTTNSLHSAVV 246
Cdd:CHL00085 179 IGDNYFAALNSAVFSDGSFCYIPKDTKCPLELSTYFRINNEESGQFERTLIIAEENSYVSYLEGCTAPQYDTNQLHAAVV 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 247 EIIVHKDAHVRYTTIQNW-ANN------VYNLVTKRTF-VHENGNMEWVDGNLGSKLTMKYPACVLLGEGAKGSTLSIAF 318
Cdd:CHL00085 259 ELIALENAEIKYSTVQNWyAGDengeggIYNFVTKRGLcAGKNSKISWTQVETGSAITWKYPSCILIGDNSQGEFYSVAL 338
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 319 AGKGQVQDAGAKMIHKAPNTSSTIVSKSISKDGGKVVYRGIVHFGRKAKGARSNIECDTLILDNQSTSDTIPYNEIFNDH 398
Cdd:CHL00085 339 TNNYQQADTGTKMIHIGKNTKSRIISKGISAGKSKNSYRGLVKIGPKALNSRNYSQCDSLLIGNKSQANTFPYIQVQNST 418
                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517996658 399 ISLEHEAKVSKVSEEQLFYLMSRGISEEEATEMIVMGFIEPFTKELPMEYAVEMNRLIKFEMEGSIG 465
Cdd:CHL00085 419 AKIEHEASTSKIGEEQLFYFLQRGINLEEAISLLISGFCKDVFNKLPMEFALEADRLLSLKLEGSVG 485
SUFBD pfam01458
SUF system FeS cluster assembly, SufBD; Iron-sulphur (FeS) clusters are important cofactors ...
210-436 1.36e-104

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: 310.15  E-value: 1.36e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  210 GQFERTLIIADEGASVNYVEgctapvyttNSLHSAVVEIIVHKDAHVRYTTIQNWANNVYNLVTKRTFVHENGNMEWVDG 289
Cdd:pfam01458   1 GQFPRNLIVAEEGAEVTIIE---------EYEGCGVVEIYVGKGAKLRYVTVQNWGENAYNFVTTRAELGADARVEWVQV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  290 NLGSKLTMKYPACVLLGEGAKGSTLSIAFAGKGQVQDAGAKMIHKAPNTSSTIVSKSISKDGGKVVYRGIVHFGRKAKGA 369
Cdd:pfam01458  72 SLGGKLTRNYPSVQLKGEGAEAELNGVYLADGGQHADTGTKVIHNGPNTSSNILSKGVLKDRSRGVFRGLIKVRKGAQKT 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517996658  370 RSNIECDTLILDNQSTSDTIPYNEIFNDHISLEHEAKVSKVSEEQLFYLMSRGISEEEATEMIVMGF 436
Cdd:pfam01458 152 DGHQECRNLLLSDKARADTIPELEIYADDVKCSHGATVGKIDEEQLFYLMSRGLSEEEARRLIVRGF 218
sufD TIGR01981
FeS assembly protein SufD; This protein, SufD, forms a cytosolic complex SufBCD. This complex ...
178-447 6.24e-66

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: 212.86  E-value: 6.24e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  178 AVWSGGSFIYVPKNVKLDTPLQAYFRINSENMGQFERTLIIADEGASVNYVEGCTAPvyTTNSLHSAVVEIIVHKDAHVR 257
Cdd:TIGR01981   2 ALFNSGLVLYIPKGVEAEEPIELRFIMGSENRVLAPRLLIVVEEGAKATVLERHDSG--EGDAFLNGLVEINVGENASVE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  258 YTTIQNWANNVYNLVTKRTFVHENGNMEWVDGNLGSKLTMKYPACVLLGEGAKGSTLSIAFAGKGQVQDAGAKMIHKAPN 337
Cdd:TIGR01981  80 FIKVQFLSATSFHFSTVRITLERDARVRLSDVNLGGKLSRHDTDVDLNGEGSKAEIKGLYFGDGSQHIDVHTNVIHNGPH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658  338 TSSTIVSKSISKDGGKVVYRGIVHFGRKAKGARSNIECDTLILDNQSTSDTIPYNEIFNDHISLEHEAKVSKVSEEQLFY 417
Cdd:TIGR01981 160 TVSNILHRGVLDDRAHGVFNGNIDIPKGAQGTDARQSNRTLLLSDKARADTKPELEIDADDVKASHGATVGQLDEEQLFY 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 517996658  418 LMSRGISEEEATEMIVMGFIEPFTKELPME 447
Cdd:TIGR01981 240 LRSRGIDEAEAKRLLIEGFFGEVIEEIPDE 269
PRK10948 PRK10948
Fe-S cluster assembly protein SufD;
291-436 4.07e-16

Fe-S cluster assembly protein SufD;


Pssm-ID: 236804 [Multi-domain]  Cd Length: 424  Bit Score: 80.08  E-value: 4.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517996658 291 LGSKLTMKYPACVLLGEGAKGSTLSIAFAGKGQVQDAGAKMIHKAPNTSSTIVSKSISKDGGKVVYRGIVHFGR---KAK 367
Cdd:PRK10948 249 LGAAVLRHNTSTQLNGENSTLRLNSLAMPVKNEVCDTRTWLEHNKGYCNSRQLHKTIVSDKGRAVFNGLIKVAQhaiKTD 328
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517996658 368 GARSNiecDTLILDNQSTSDTIPYNEIFNDHISLEHEAKVSKVSEEQLFYLMSRGISEEEATEMIVMGF 436
Cdd:PRK10948 329 GQMTN---NNLLLGKLAEVDTKPQLEIYADDVKCSHGATVGRIDDEQLFYLRSRGINQQDAQQMIIYAF 394
SufBD_N pfam19295
SufBD protein N-terminal region; This entry represents the N-terminal part of the SufB and ...
149-199 1.35e-06

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: 48.28  E-value: 1.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 517996658  149 ALKENEELFKEYFASVIPAADNKFAALNSAVWSGGSFIYVPKNVKLDTPLQ 199
Cdd:pfam19295 121 AAEKYPELVEKYYGKLAKTDEDGLTALNTMLAQDGLFVYVPKGVVVERPIQ 171
 
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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