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Conserved domains on  [gi|489126057|ref|WP_003035854|]
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MULTISPECIES: YcbX family protein [Citrobacter]

Protein Classification

YcbX family protein( domain architecture ID 11461389)

YcbX family protein contains MOSC and Fe-S domains, similar to Escherichia coli 6-N-hydroxylaminopurine resistance protein YcbX

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
YcbX COG3217
N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and ...
 1-265 1.44e-104

N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and metabolism, Defense mechanisms];


:

Pssm-ID: 442450 [Multi-domain]  Cd Length: 240  Bit Score: 307.50  E-value: 1.44e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057   1 MVTLTRLFIHPVKSMRGIGLTHALADISGLAFDRIFMITEPDGTFITARQFPQMVRFTPSPFHDG-LHLTAPDGSSALVR 79
Cdd:COG3217    1 MGRVSRLYRYPVKSLAGEALESATLTAGGLPGDRRWALVDADGRFLTQRRHPRLALLRARLDEDGgLTLTAPGGESLTVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057  80 FvdfatqdaptevwgnhftARIAPVAINQWLSSFFSRDVQLRWVGPQLTRrvkrhvDVPLSFADGYPYLLANEASLRDVQ 159
Cdd:COG3217   81 L------------------DDDAGDAAAAWLSEYLGRPVRLVRLPPESRR------GPPVGFADGYPVLLISTASLADLN 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 160 QRSPASVKMEQFRPNLVVSGAGAWEEDTW--KVIRIGDVIFDVAKPCSRCIFTTVSPEKGQKHPsgEPLATLQTFRTAvd 237
Cdd:COG3217  137 ARLGAPVDMRRFRPNLVVDGLEPFAEDDWvgRRLRIGEVRLRVVKPCSRCVVTTVDPETGERDP--EPLRTLARYRGA-- 212

                        250       260
                 ....*....|....*....|....*...
gi 489126057 238 NGDVDFGQNLIARNSGVIRVGDEIEILA 265
Cdd:COG3217  213 DGHVDFGVNAIVLEGGTIRVGDEVEVLE 240
Fdx COG0633
Ferredoxin [Energy production and conversion];
288-367 1.66e-19

Ferredoxin [Energy production and conversion];


:

Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 82.20  E-value: 1.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 288 ATVLIDWQGQTFRGNNQQVLLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKSAIGD----DGTILCCSCVPKTA 363
Cdd:COG0633    2 PKVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDeeraAGSRLACQARPTSD 81


                 ....
gi 489126057 364 IRLE 367
Cdd:COG0633   82 LVVE 85
 
Name Accession Description Interval E-value
YcbX COG3217
N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and ...
 1-265 1.44e-104

N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and metabolism, Defense mechanisms];


Pssm-ID: 442450 [Multi-domain]  Cd Length: 240  Bit Score: 307.50  E-value: 1.44e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057   1 MVTLTRLFIHPVKSMRGIGLTHALADISGLAFDRIFMITEPDGTFITARQFPQMVRFTPSPFHDG-LHLTAPDGSSALVR 79
Cdd:COG3217    1 MGRVSRLYRYPVKSLAGEALESATLTAGGLPGDRRWALVDADGRFLTQRRHPRLALLRARLDEDGgLTLTAPGGESLTVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057  80 FvdfatqdaptevwgnhftARIAPVAINQWLSSFFSRDVQLRWVGPQLTRrvkrhvDVPLSFADGYPYLLANEASLRDVQ 159
Cdd:COG3217   81 L------------------DDDAGDAAAAWLSEYLGRPVRLVRLPPESRR------GPPVGFADGYPVLLISTASLADLN 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 160 QRSPASVKMEQFRPNLVVSGAGAWEEDTW--KVIRIGDVIFDVAKPCSRCIFTTVSPEKGQKHPsgEPLATLQTFRTAvd 237
Cdd:COG3217  137 ARLGAPVDMRRFRPNLVVDGLEPFAEDDWvgRRLRIGEVRLRVVKPCSRCVVTTVDPETGERDP--EPLRTLARYRGA-- 212

                        250       260
                 ....*....|....*....|....*...
gi 489126057 238 NGDVDFGQNLIARNSGVIRVGDEIEILA 265
Cdd:COG3217  213 DGHVDFGVNAIVLEGGTIRVGDEVEVLE 240
MOSC_N pfam03476
MOSC N-terminal beta barrel domain; This domain is found to the N-terminus of pfam03473. The ...
 1-117 5.27e-41

MOSC N-terminal beta barrel domain; This domain is found to the N-terminus of pfam03473. The function of this domain is unknown, however it is predicted to adopt a beta barrel fold.


Pssm-ID: 281474  Cd Length: 118  Bit Score: 140.19  E-value: 5.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057    1 MVTLTRLFIHPVKSMRGIGLTHALADISGLAFDRIFMITEPDGTFITARQFPQMVRFTPSPF-HDGLHLTAPDGSSALVR 79
Cdd:pfam03476   1 MARVSSLYVYPIKSCRGESLSRAELTAAGLAWDRRFMVVDSDGKFVTARREPRLVLIRTTLDeDGGLTLTAPGMPDLSVP 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 489126057   80 FVDFATQDAPTEVWGNHFTARIAPVAINQWLSSFFSRD 117
Cdd:pfam03476  81 LADNKFDLRGVLVWGLSFSGRDCGDAAADWFSDFLGKP 118
PLN02724 PLN02724
Molybdenum cofactor sulfurase
 4-261 3.67e-29

Molybdenum cofactor sulfurase


Pssm-ID: 215384 [Multi-domain]  Cd Length: 805  Bit Score: 118.82  E-value: 3.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057   4 LTRLFIHPVKSMRGIGLTHALADISGLAFDRIFMITEPDGTFITARQFPQMVRFTPS-PFHDG-LHLTAPDGSSAL-VRF 80
Cdd:PLN02724 520 LKSITVYPIKSCAGFSVERWPLSETGLLYDREWMIQSLTGEILTQKKVPEMCLITTFiDLESGkLVVRAPRCDHKLeIPL 599

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057  81 VD--FATQDAPTEVWGNHFTARIAPVAINQWLSSFFSRDVQL-----------RWVGPQLTRrvKRHVDVPLSFADGYPY 147
Cdd:PLN02724 600 ESdsQHEESGEVILCGNRAESMSYGTEINEWFTNALGRRCTLvrksssntrvcRNRNPSHSP--CGDDESRLSFANEGQF 677

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 148 LLANEASLRDVQQR-----SPASVKME--QFRPNLVVSGAGAWEEDTWKVIRIGDVIFDVAKPCSRCIFTTVSPEKGQKH 220
Cdd:PLN02724 678 LLISEASVEDLNRRlatgqEDAKIRLDptRFRPNLVVSGGEAYAEDEWQSLSIGDAEFTVLGGCNRCQMINIDQETGLVN 757

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 489126057 221 PSGEPLATLQTFRTAvdNGDVDFG----QNLIARNSGVIRVGDEI 261
Cdd:PLN02724 758 PSNEPLATLASYRRV--KGKILFGillrYEISDKRDQWIAVGSRV 800
Fdx COG0633
Ferredoxin [Energy production and conversion];
288-367 1.66e-19

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 82.20  E-value: 1.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 288 ATVLIDWQGQTFRGNNQQVLLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKSAIGD----DGTILCCSCVPKTA 363
Cdd:COG0633    2 PKVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDeeraAGSRLACQARPTSD 81


                 ....
gi 489126057 364 IRLE 367
Cdd:COG0633   82 LVVE 85
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 289-367 1.33e-17

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 76.66  E-value: 1.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 289 TVLIDWQGQTFRGNNQQVLLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKSAIGDD----GTILCCSCVPKTAI 364
Cdd:cd00207    2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEeaegGYVLACQTRVTDGL 81


                 ...
gi 489126057 365 RLE 367
Cdd:cd00207   82 VIE 84
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
307-367 1.81e-14

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 68.22  E-value: 1.81e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489126057 307 LLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKS-AIGDDGTILCCSCVPKTAIRLE 367
Cdd:PRK10713  22 LLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEPlAFIQPGEILPCCCRAKGDIEIE 83
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
290-361 3.08e-13

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 64.47  E-value: 3.08e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489126057  290 VLIDWQGQTFRGN-NQQVLLEQLENQGIRVPYSCRAGICGCCRIRLVDGEV----SPLKKSAIGDDGTILCCSCVPK 361
Cdd:pfam00111   1 VTINGKGVTIEVPdGETTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDqsdqSFLEDDELAAGYVVLACQTYPK 77
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 293-368 2.81e-08

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 50.92  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057  293 DWQGQTFRGNNQQVLLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKSAIGDD----GTILCCSCVPKTAIRLES 368
Cdd:TIGR02008  11 DGGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDqmeaGYVLTCVAYPTSDCTIET 90
 
Name Accession Description Interval E-value
YcbX COG3217
N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and ...
 1-265 1.44e-104

N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and metabolism, Defense mechanisms];


Pssm-ID: 442450 [Multi-domain]  Cd Length: 240  Bit Score: 307.50  E-value: 1.44e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057   1 MVTLTRLFIHPVKSMRGIGLTHALADISGLAFDRIFMITEPDGTFITARQFPQMVRFTPSPFHDG-LHLTAPDGSSALVR 79
Cdd:COG3217    1 MGRVSRLYRYPVKSLAGEALESATLTAGGLPGDRRWALVDADGRFLTQRRHPRLALLRARLDEDGgLTLTAPGGESLTVD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057  80 FvdfatqdaptevwgnhftARIAPVAINQWLSSFFSRDVQLRWVGPQLTRrvkrhvDVPLSFADGYPYLLANEASLRDVQ 159
Cdd:COG3217   81 L------------------DDDAGDAAAAWLSEYLGRPVRLVRLPPESRR------GPPVGFADGYPVLLISTASLADLN 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 160 QRSPASVKMEQFRPNLVVSGAGAWEEDTW--KVIRIGDVIFDVAKPCSRCIFTTVSPEKGQKHPsgEPLATLQTFRTAvd 237
Cdd:COG3217  137 ARLGAPVDMRRFRPNLVVDGLEPFAEDDWvgRRLRIGEVRLRVVKPCSRCVVTTVDPETGERDP--EPLRTLARYRGA-- 212

                        250       260
                 ....*....|....*....|....*...
gi 489126057 238 NGDVDFGQNLIARNSGVIRVGDEIEILA 265
Cdd:COG3217  213 DGHVDFGVNAIVLEGGTIRVGDEVEVLE 240
MOSC_N pfam03476
MOSC N-terminal beta barrel domain; This domain is found to the N-terminus of pfam03473. The ...
 1-117 5.27e-41

MOSC N-terminal beta barrel domain; This domain is found to the N-terminus of pfam03473. The function of this domain is unknown, however it is predicted to adopt a beta barrel fold.


Pssm-ID: 281474  Cd Length: 118  Bit Score: 140.19  E-value: 5.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057    1 MVTLTRLFIHPVKSMRGIGLTHALADISGLAFDRIFMITEPDGTFITARQFPQMVRFTPSPF-HDGLHLTAPDGSSALVR 79
Cdd:pfam03476   1 MARVSSLYVYPIKSCRGESLSRAELTAAGLAWDRRFMVVDSDGKFVTARREPRLVLIRTTLDeDGGLTLTAPGMPDLSVP 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 489126057   80 FVDFATQDAPTEVWGNHFTARIAPVAINQWLSSFFSRD 117
Cdd:pfam03476  81 LADNKFDLRGVLVWGLSFSGRDCGDAAADWFSDFLGKP 118
PLN02724 PLN02724
Molybdenum cofactor sulfurase
 4-261 3.67e-29

Molybdenum cofactor sulfurase


Pssm-ID: 215384 [Multi-domain]  Cd Length: 805  Bit Score: 118.82  E-value: 3.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057   4 LTRLFIHPVKSMRGIGLTHALADISGLAFDRIFMITEPDGTFITARQFPQMVRFTPS-PFHDG-LHLTAPDGSSAL-VRF 80
Cdd:PLN02724 520 LKSITVYPIKSCAGFSVERWPLSETGLLYDREWMIQSLTGEILTQKKVPEMCLITTFiDLESGkLVVRAPRCDHKLeIPL 599

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057  81 VD--FATQDAPTEVWGNHFTARIAPVAINQWLSSFFSRDVQL-----------RWVGPQLTRrvKRHVDVPLSFADGYPY 147
Cdd:PLN02724 600 ESdsQHEESGEVILCGNRAESMSYGTEINEWFTNALGRRCTLvrksssntrvcRNRNPSHSP--CGDDESRLSFANEGQF 677

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 148 LLANEASLRDVQQR-----SPASVKME--QFRPNLVVSGAGAWEEDTWKVIRIGDVIFDVAKPCSRCIFTTVSPEKGQKH 220
Cdd:PLN02724 678 LLISEASVEDLNRRlatgqEDAKIRLDptRFRPNLVVSGGEAYAEDEWQSLSIGDAEFTVLGGCNRCQMINIDQETGLVN 757

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 489126057 221 PSGEPLATLQTFRTAvdNGDVDFG----QNLIARNSGVIRVGDEI 261
Cdd:PLN02724 758 PSNEPLATLASYRRV--KGKILFGillrYEISDKRDQWIAVGSRV 800
Fdx COG0633
Ferredoxin [Energy production and conversion];
288-367 1.66e-19

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 82.20  E-value: 1.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 288 ATVLIDWQGQTFRGNNQQVLLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKSAIGD----DGTILCCSCVPKTA 363
Cdd:COG0633    2 PKVTFIPEGHTVEVPAGESLLEAALRAGIDLPYSCRSGACGTCHVRVLEGEVDHREEDALSDeeraAGSRLACQARPTSD 81


                 ....
gi 489126057 364 IRLE 367
Cdd:COG0633   82 LVVE 85
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 289-367 1.33e-17

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 76.66  E-value: 1.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 289 TVLIDWQGQTFRGNNQQVLLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKSAIGDD----GTILCCSCVPKTAI 364
Cdd:cd00207    2 TINVPGSGVEVEVPEGETLLDAAREAGIDIPYSCRAGACGTCKVEVVEGEVDQSDPSLLDEEeaegGYVLACQTRVTDGL 81


                 ...
gi 489126057 365 RLE 367
Cdd:cd00207   82 VIE 84
MOSC pfam03473
MOSC domain; The MOSC (MOCO sulfurase C-terminal) domain is a superfamily of beta-strand-rich ...
 136-262 3.17e-16

MOSC domain; The MOSC (MOCO sulfurase C-terminal) domain is a superfamily of beta-strand-rich domains identified in the molybdenum cofactor sulfurase and several other proteins from both prokaryotes and eukaryotes. These MOSC domains contain an absolutely conserved cysteine and occur either as stand-alone forms such as Swiss:P32157, or fused to other domains such as NifS-like catalytic domain in Molybdenum cofactor sulfurase. The MOSC domain is predicted to be a sulfur-carrier domain that receives sulfur abstracted by the pyridoxal phosphate-dependent NifS-like enzymes, on its conserved cysteine, and delivers it for the formation of diverse sulfur-metal clusters.


Pssm-ID: 460936  Cd Length: 116  Bit Score: 73.77  E-value: 3.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057  136 DVPLSFADGYPYLLANEASLRDVQQR-SPASVKMEQFRPNLVVSGAgaweedTWKVIRIGDViFDVAKPCSRcifTTVSP 214
Cdd:pfam03473   1 DRKHHGGDDKAVLLYSRESYDAWNAElGRGPLDPGRFRENLVVSGG------TWKEVCIGDR-FRIGGACLR---LEVTQ 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 489126057  215 ekgqkhpSGEPLATLQTfRTAVDNGD------VDFGQNLIARNSGVIRVGDEIE 262
Cdd:pfam03473  71 -------PREPCKTLAK-RFGERRVDkrfkgsGRFGWYLRVLEEGTVRVGDEVE 116
PRK10713 PRK10713
2Fe-2S ferredoxin-like protein;
307-367 1.81e-14

2Fe-2S ferredoxin-like protein;


Pssm-ID: 182668 [Multi-domain]  Cd Length: 84  Bit Score: 68.22  E-value: 1.81e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489126057 307 LLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKS-AIGDDGTILCCSCVPKTAIRLE 367
Cdd:PRK10713  22 LLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEPlAFIQPGEILPCCCRAKGDIEIE 83
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
290-361 3.08e-13

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 64.47  E-value: 3.08e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489126057  290 VLIDWQGQTFRGN-NQQVLLEQLENQGIRVPYSCRAGICGCCRIRLVDGEV----SPLKKSAIGDDGTILCCSCVPK 361
Cdd:pfam00111   1 VTINGKGVTIEVPdGETTLLDAAEEAGIDIPYSCRGGGCGTCAVKVLEGEDqsdqSFLEDDELAAGYVVLACQTYPK 77
petF CHL00134
ferredoxin; Validated
 297-362 1.71e-10

ferredoxin; Validated


Pssm-ID: 177056 [Multi-domain]  Cd Length: 99  Bit Score: 57.42  E-value: 1.71e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 297 QTFRGNNQQVLLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKSAIGDD----GTILCCSCVPKT 362
Cdd:CHL00134  17 VTIDCPDDVYILDAAEEQGIDLPYSCRAGACSTCAGKVTEGTVDQSDQSFLDDDqleaGFVLTCVAYPTS 86
PTZ00038 PTZ00038
ferredoxin; Provisional
 307-368 4.66e-10

ferredoxin; Provisional


Pssm-ID: 240237 [Multi-domain]  Cd Length: 191  Bit Score: 58.31  E-value: 4.66e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489126057 307 LLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKSAIGDD----GTILCCSCVPKTAIRLES 368
Cdd:PTZ00038 117 ILDAAERQGVELPYSCRGGSCSTCAAKLLEGEVDNEDQSYLDDEqlkkGYCLLCTCYPKSDCTIET 182
fdx_plant TIGR02008
ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ...
 293-368 2.81e-08

ferredoxin [2Fe-2S]; This model represents single domain 2Fe-2S (also called plant type) ferredoxins. In general, these occur as a single domain proteins or with a chloroplast transit peptide. Species tend to be photosynthetic, but several forms may occur in one species and individually may not be associated with photocynthesis. Halobacterial forms differ somewhat in architecture; they score between trusted and noise cutoffs. Sequences scoring below the noise cutoff tend to be ferredoxin-related domains of larger proteins.


Pssm-ID: 273926 [Multi-domain]  Cd Length: 97  Bit Score: 50.92  E-value: 2.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057  293 DWQGQTFRGNNQQVLLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKSAIGDD----GTILCCSCVPKTAIRLES 368
Cdd:TIGR02008  11 DGGEETIECPDDQYILDAAEEAGIDLPYSCRAGACSTCAGKVEEGTVDQSDQSFLDDDqmeaGYVLTCVAYPTSDCTIET 90
PRK10684 PRK10684
HCP oxidoreductase, NADH-dependent; Provisional
 297-367 1.95e-07

HCP oxidoreductase, NADH-dependent; Provisional


Pssm-ID: 236735 [Multi-domain]  Cd Length: 332  Bit Score: 52.02  E-value: 1.95e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489126057 297 QTFRGNNQQVLLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKSAIGD----DGTILCCSCVPKTAIRLE 367
Cdd:PRK10684 258 REFYAPVGTTLLEALESNKVPVVAACRAGVCGCCKTKVVSGEYTVSSTMTLTPaeiaQGYVLACSCHPQGDLVLA 332
PRK07609 PRK07609
CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated
 296-368 2.44e-07

CDP-6-deoxy-delta-3,4-glucoseen reductase; Validated


Pssm-ID: 181058 [Multi-domain]  Cd Length: 339  Bit Score: 51.80  E-value: 2.44e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489126057 296 GQTFRGNNQQVLLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVS--PLKKSAIGDD----GTILCCSCVPKTAIRLES 368
Cdd:PRK07609  11 GRQFTAEPDETILDAALRQGIHLPYGCKNGACGSCKGRLLEGEVEqgPHQASALSGEeraaGEALTCCAKPLSDLVLEA 89
PLN03136 PLN03136
Ferredoxin; Provisional
 307-368 1.05e-06

Ferredoxin; Provisional


Pssm-ID: 178681 [Multi-domain]  Cd Length: 148  Bit Score: 47.82  E-value: 1.05e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489126057 307 LLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKSAIGD----DGTILCCSCVPKTAIRLES 368
Cdd:PLN03136  76 VLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSIDQSDQSFLDDeqisEGYVLTCVAYPTSDVVIET 141
PRK05713 PRK05713
iron-sulfur-binding ferredoxin reductase;
307-358 1.82e-06

iron-sulfur-binding ferredoxin reductase;


Pssm-ID: 235575 [Multi-domain]  Cd Length: 312  Bit Score: 48.95  E-value: 1.82e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489126057 307 LLEQLENQGIRVPYSCRAGICGCCRIRLVDGEVSPLKKSAIGDD----GTILCCSC 358
Cdd:PRK05713  19 LLDALNAAGVAVPYSCRAGSCHACLVRCLQGEPEDALPEALAAEkreqGWRLACQC 74
YiiM COG2258
N-hydroxylaminopurine reductase YiiM, contains MOSC domain [Nucleotide transport and ...
 147-270 6.44e-04

N-hydroxylaminopurine reductase YiiM, contains MOSC domain [Nucleotide transport and metabolism, Defense mechanisms];


Pssm-ID: 441859  Cd Length: 162  Bit Score: 39.77  E-value: 6.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 147 YLLANEaSLRDVQQRSPASVKMEQFRPNLVVSGagaWEEDTWKV---IRIGDVIFDVAKPCSRC-----IFttvspekGQ 218
Cdd:COG2258   50 TLYAAE-HYDAWAAELGRDLPPGAFGENLTTEG---LDLSDLPIgdrLRIGEALLEVTQPRKPChkleaRL-------GG 118

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 489126057 219 KhpsGEPLATLQTFRTavdngdvdfGQNLIARNSGVIRVGDEIEILATGPAR 270
Cdd:COG2258  119 P---GLAKAMCQMGRG---------GIYARVLEGGEVRAGDEVELLERPEPG 158
COG3894 COG3894
Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain ...
 286-360 7.11e-04

Uncharacterized 2Fe-2S and 4Fe-4S clusters-containing protein, contains DUF4445 domain [Function unknown];


Pssm-ID: 443101 [Multi-domain]  Cd Length: 621  Bit Score: 41.71  E-value: 7.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489126057 286 PDATVLIDWQGQTFRGNNQQVLLEQLENQGIRVPYSCR-AGICGCCRIRLVDGEVSPLKKSAIG-------DDGTILCCS 357
Cdd:COG3894    2 PKVKVTFLPSGKRVEVEAGTTLLDAAREAGVDIDAPCGgRGTCGKCKVKVEEGEFSPVTEEERRllspeelAEGYRLACQ 81


                 ...
gi 489126057 358 CVP 360
Cdd:COG3894   82 ARV 84
 
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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