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Conserved domains on  [gi|2019726493|gb|KAG5381262|]
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hypothetical protein IGI04_029104 [Brassica rapa subsp. trilocularis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
531-688 5.51e-91

NADH-quinone oxidoreductase subunit NuoI;


:

Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 292.56  E-value: 5.51e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  531 FERSINTLFLTEMVRGLSLTLKYFFDPKVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAVCPAQAITIEAE 610
Cdd:PRK05888     1 IKQYLKSMLLKELLKGLGVTLKYFFKKKVTIQYPEEKLPLSPRFRGRHALRRDPNGEERCIACKLCAAICPADAITIEAA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  611 EREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKLLENGDRWETEIAENLKSESLY 688
Cdd:PRK05888    81 EREDGRRRTTRYDINFGRCIFCGFCEEACPTDAIVETPDFELATETREELIYDKEKLLANGDRVEREIAPGKAADANY 158
HAT_KAT11 super family cl02120
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 1802-2013 8.95e-41

Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11.


The actual alignment was detected with superfamily member pfam08214:

Pssm-ID: 413203  Cd Length: 348  Bit Score: 155.25  E-value: 8.95e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493 1802 PTAESLVIRVVSSVDKKLEVKPRFLDIFrEDSYPTEFAYKSKVVLLFQKIEGVEVCLFGMYVQEFGSECAFPNQRRVYLS 1881
Cdd:pfam08214   10 PKGVKVTIRHLSSPPKEVEALFGMPPRF-AESGKPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVCPDPNERRVFVS 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493 1882 YLDSVKYFRPEVrsyngealRTFVYHEILIGYLEYCKLRGFTSCYIWACPPLKGEDYILychPEIQKTPK----SDK--L 1955
Cdd:pfam08214   89 KADSTGFFHLRV--------RTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvlDGKglL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493 1956 REYLAMLKKA-------SKEGIVAETINLYD--HFFMQT-----------GECRAKVTAARLPYFDGDYWPGAAEDLI 2013
Cdd:pfam08214  158 KWWCKMLDKIlveykssAKAKLVIPGKDIFKtrKYLPATadplwlvghifHQICDDPARYEIPLFPDDPKPRFLEELI 235
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
 1670-1742 1.79e-38

PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar proteins; This family includes A. thaliana HACs (HAC1/2/4/5/12), which are histone acetyltransferases of the p300/CREB-binding protein (CBP) co-activator family. CBP-type HAT proteins are also found in animals, but absent in fungi. The domain architecture of CBP-type HAT proteins differs between plants and animals. Members in this family contain an N-terminal partially conserved KIX domain, a Zf-TAZ domain, a Cysteine rich CBP-type HAT domain that harbors a plant homeodomain (PHD) finger, a Zf-ZZ domain, and a Zf-TAZ domain. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


:

Pssm-ID: 277086  Cd Length: 73  Bit Score: 138.64  E-value: 1.79e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019726493 1670 FCIPCYNESRGDTIVAEGTPIPKARLEKKKNDEETEEWWVQCDKCEAWQHQICALFNGRRNDGGQAEYTCPYC 1742
Cdd:cd15614      1 WCSPCYNELKGENILIGGVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNGRRNADETAEYVCPLC 73
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1311-1389 1.10e-31

TAZ zinc finger, present in p300 and CBP;


:

Pssm-ID: 214717  Cd Length: 79  Bit Score: 119.39  E-value: 1.10e-31
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  1311 DPRFRNQQKWLLFLRHARNCKAPEGKCPDRNCVTVQKLWKHMDSCDAPQCSYPRCRPTKTLINHHRSCKESNCPVCIPV 1389
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCKAREAKCQYPNCKTMKKLLRHMDSCKVRKCKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
2260-2338 3.14e-26

TAZ zinc finger, present in p300 and CBP;


:

Pssm-ID: 214717  Cd Length: 79  Bit Score: 103.98  E-value: 3.14e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  2260 QLRVLQLRKMLDLLVHASQCRS--AQCQYPNCRKVKGLFRHGIQCKVR--ASGGCVLCKKMWYllqlHARACKESQCHVP 2335
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCKAreAKCQYPNCKTMKKLLRHMDSCKVRkcKYGYCASCKQLWQ----HSKHCKDSNCPVC 76


                    ...
gi 2019726493  2336 RCS 2338
Cdd:smart00551   77 KCV 79
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 2200-2245 2.44e-15

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


:

Pssm-ID: 239077  Cd Length: 41  Bit Score: 71.83  E-value: 2.44e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2019726493 2200 TTCNACHLDIETGqgWRCEVCPDYDVCDSCYRRdggVNHPHKLTNH 2245
Cdd:cd02337      1 YTCNECKHHVETR--WHCTVCEDYDLCITCYNT---KNHPHKMEKL 41
EPL1 super family cl38323
Enhancer of polycomb-like; This is a family of EPL1 (Enhancer of polycomb-like) proteins. The ...
 7-137 6.10e-10

Enhancer of polycomb-like; This is a family of EPL1 (Enhancer of polycomb-like) proteins. The EPL1 protein is a member of a histone acetyltransferase complex which is involved in transcriptional activation of selected genes.


The actual alignment was detected with superfamily member pfam10513:

Pssm-ID: 463128  Cd Length: 168  Bit Score: 60.19  E-value: 6.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493    7 RPRPLDIHKKLPILKSykdfEDDDTPTRNP---------------------------------------QLLRLASSVEL 47
Cdd:pfam10513    1 RHRRISIKQPLPIISE----DEVDGLDTSPdedepsecnsnkenslhavetgvdkeeedevhlkvinaaKKALSSSKKSQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493   48 DHEVSPVPSK-KLASEIPTPQFVVVDSYERDysptfgqPASYLRA-RGARSELGEFVEYDLDNEDDDWLYEFDKDNK--- 122
Cdd:pfam10513   77 NTSESSVPAPnKERLYLPTPDAGKFREFERP-------PASYIRFsETVEEELDEGVEYDMDEEDEAWLEELNEKRKseg 149

                          170
                   ....*....|....*..
gi 2019726493  123 --QLSPEMFESIIFKLE 137
Cdd:pfam10513  150 veKISEDEFEILMDRFE 166
ZZ super family cl00295
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 2076-2110 9.82e-04

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


The actual alignment was detected with superfamily member smart00291:

Pssm-ID: 412288 [Multi-domain]  Cd Length: 44  Bit Score: 38.96  E-value: 9.82e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2019726493  2076 VHLQPSCTHCCMLMVsGNRWRCSQCKHFQICDKCY 2110
Cdd:smart00291    1 VHHSYSCDTCGKPIV-GVRYHCLVCPDYDLCQSCF 34
 
Name Accession Description Interval E-value
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
531-688 5.51e-91

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 292.56  E-value: 5.51e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  531 FERSINTLFLTEMVRGLSLTLKYFFDPKVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAVCPAQAITIEAE 610
Cdd:PRK05888     1 IKQYLKSMLLKELLKGLGVTLKYFFKKKVTIQYPEEKLPLSPRFRGRHALRRDPNGEERCIACKLCAAICPADAITIEAA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  611 EREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKLLENGDRWETEIAENLKSESLY 688
Cdd:PRK05888    81 EREDGRRRTTRYDINFGRCIFCGFCEEACPTDAIVETPDFELATETREELIYDKEKLLANGDRVEREIAPGKAADANY 158
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 546-667 2.00e-63

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 211.89  E-value: 2.00e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  546 GLSLTLKYFFDPKVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAVCPAQAITIEAEEREDGSRRTTRYDID 625
Cdd:TIGR01971    1 GLGLTLKYFFSKPVTVQYPEEKLYLPPRFRGRIVLTRDPNGEEKCIGCTLCAAVCPADAIRVVPAEGEDGKRRLKFYEIN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2019726493  626 MTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKL 667
Cdd:TIGR01971   81 FGRCIFCGLCEEACPTDAIVLTPEFELATYTRSDLVYGKEDL 122
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 1802-2013 8.95e-41

Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11.


Pssm-ID: 400497  Cd Length: 348  Bit Score: 155.25  E-value: 8.95e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493 1802 PTAESLVIRVVSSVDKKLEVKPRFLDIFrEDSYPTEFAYKSKVVLLFQKIEGVEVCLFGMYVQEFGSECAFPNQRRVYLS 1881
Cdd:pfam08214   10 PKGVKVTIRHLSSPPKEVEALFGMPPRF-AESGKPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVCPDPNERRVFVS 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493 1882 YLDSVKYFRPEVrsyngealRTFVYHEILIGYLEYCKLRGFTSCYIWACPPLKGEDYILychPEIQKTPK----SDK--L 1955
Cdd:pfam08214   89 KADSTGFFHLRV--------RTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvlDGKglL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493 1956 REYLAMLKKA-------SKEGIVAETINLYD--HFFMQT-----------GECRAKVTAARLPYFDGDYWPGAAEDLI 2013
Cdd:pfam08214  158 KWWCKMLDKIlveykssAKAKLVIPGKDIFKtrKYLPATadplwlvghifHQICDDPARYEIPLFPDDPKPRFLEELI 235
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
 1670-1742 1.79e-38

PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar proteins; This family includes A. thaliana HACs (HAC1/2/4/5/12), which are histone acetyltransferases of the p300/CREB-binding protein (CBP) co-activator family. CBP-type HAT proteins are also found in animals, but absent in fungi. The domain architecture of CBP-type HAT proteins differs between plants and animals. Members in this family contain an N-terminal partially conserved KIX domain, a Zf-TAZ domain, a Cysteine rich CBP-type HAT domain that harbors a plant homeodomain (PHD) finger, a Zf-ZZ domain, and a Zf-TAZ domain. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 277086  Cd Length: 73  Bit Score: 138.64  E-value: 1.79e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019726493 1670 FCIPCYNESRGDTIVAEGTPIPKARLEKKKNDEETEEWWVQCDKCEAWQHQICALFNGRRNDGGQAEYTCPYC 1742
Cdd:cd15614      1 WCSPCYNELKGENILIGGVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNGRRNADETAEYVCPLC 73
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1311-1389 1.10e-31

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 119.39  E-value: 1.10e-31
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  1311 DPRFRNQQKWLLFLRHARNCKAPEGKCPDRNCVTVQKLWKHMDSCDAPQCSYPRCRPTKTLINHHRSCKESNCPVCIPV 1389
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCKAREAKCQYPNCKTMKKLLRHMDSCKVRKCKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 1317-1386 1.27e-28

TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.


Pssm-ID: 460457  Cd Length: 72  Bit Score: 110.55  E-value: 1.27e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019726493 1317 QQKWLLFLRHARNCKAPE-GKCPDRNCVTVQKLWKHMDSCDA-PQCSYPRCRPTKTLINHHRSCKESNCPVC 1386
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpGPCSLPNCRKMKRLLRHMATCKRgGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
2260-2338 3.14e-26

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 103.98  E-value: 3.14e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  2260 QLRVLQLRKMLDLLVHASQCRS--AQCQYPNCRKVKGLFRHGIQCKVR--ASGGCVLCKKMWYllqlHARACKESQCHVP 2335
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCKAreAKCQYPNCKTMKKLLRHMDSCKVRkcKYGYCASCKQLWQ----HSKHCKDSNCPVC 76


                    ...
gi 2019726493  2336 RCS 2338
Cdd:smart00551   77 KCV 79
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 587-659 3.01e-24

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 97.89  E-value: 3.01e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEERedgsrrTTRYDIDMTKCIYCGFCQEACPVDAIVEGPnFEFATETHEE 659
Cdd:COG1143      1 EDKCIGCGLCVRVCPVDAITIEDGEP------GKVYVIDPDKCIGCGLCVEVCPTGAISMTP-FELAVEDREE 66
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 2266-2334 2.05e-19

TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.


Pssm-ID: 460457  Cd Length: 72  Bit Score: 84.36  E-value: 2.05e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019726493 2266 LRKMLDLLVHASQCRSA---QCQYPNCRKVKGLFRHGIQCKvrASGGC--VLCKKMWYLLQlHARACKESQCHV 2334
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPgpgPCSLPNCRKMKRLLRHMATCK--RGGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 587-645 4.02e-17

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 79.75  E-value: 4.02e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEeredgsrrtTRYDIDMTKCIYCGFCQEACPVDAIV 645
Cdd:cd10549     77 EEKCIGCGLCVKVCPVDAITLEDE---------LEIVIDKEKCIGCGICAEVCPVNAIK 126
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 2200-2245 2.44e-15

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 71.83  E-value: 2.44e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2019726493 2200 TTCNACHLDIETGqgWRCEVCPDYDVCDSCYRRdggVNHPHKLTNH 2245
Cdd:cd02337      1 YTCNECKHHVETR--WHCTVCEDYDLCITCYNT---KNHPHKMEKL 41
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 590-643 3.53e-14

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 68.71  E-value: 3.53e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2019726493  590 CIACKLCEAVCPAQAITIEAEEREDGsrrTTRYDIDMTKCIYCGFCQEACPVDA 643
Cdd:pfam12838    1 CIGCGACVAACPVGAITLDEVGEKKG---TKTVVIDPERCVGCGACVAVCPTGA 51
EPL1 pfam10513
Enhancer of polycomb-like; This is a family of EPL1 (Enhancer of polycomb-like) proteins. The ...
 7-137 6.10e-10

Enhancer of polycomb-like; This is a family of EPL1 (Enhancer of polycomb-like) proteins. The EPL1 protein is a member of a histone acetyltransferase complex which is involved in transcriptional activation of selected genes.


Pssm-ID: 463128  Cd Length: 168  Bit Score: 60.19  E-value: 6.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493    7 RPRPLDIHKKLPILKSykdfEDDDTPTRNP---------------------------------------QLLRLASSVEL 47
Cdd:pfam10513    1 RHRRISIKQPLPIISE----DEVDGLDTSPdedepsecnsnkenslhavetgvdkeeedevhlkvinaaKKALSSSKKSQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493   48 DHEVSPVPSK-KLASEIPTPQFVVVDSYERDysptfgqPASYLRA-RGARSELGEFVEYDLDNEDDDWLYEFDKDNK--- 122
Cdd:pfam10513   77 NTSESSVPAPnKERLYLPTPDAGKFREFERP-------PASYIRFsETVEEELDEGVEYDMDEEDEAWLEELNEKRKseg 149

                          170
                   ....*....|....*..
gi 2019726493  123 --QLSPEMFESIIFKLE 137
Cdd:pfam10513  150 veKISEDEFEILMDRFE 166
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 2198-2241 9.00e-08

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 50.13  E-value: 9.00e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 2019726493  2198 FVTTCNACHLDIeTGQGWRCEVCPDYDVCDSCYrRDGGVNHPHK 2241
Cdd:smart00291    3 HSYSCDTCGKPI-VGVRYHCLVCPDYDLCQSCF-AKGSAGGEHS 44
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 552-644 5.80e-07

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 52.94  E-value: 5.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  552 KYFFDPKVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAVCPAQAITIEAEEREDGSrrttrydidmtKCIY 631
Cdd:NF038196   149 KKGPEKKKGFIPRLLSKLVNPLFYKFKVKDKKFHVTDKCIGCGICAKVCPVNNIEMEDGKPVWGH-----------NCTH 217

                           90
                   ....*....|...
gi 2019726493  632 CGFCQEACPVDAI 644
Cdd:NF038196   218 CLACIHRCPKEAI 230
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 2198-2241 2.97e-05

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 43.24  E-value: 2.97e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2019726493 2198 FVTTCNACHLDIETGQGWRCEVCPDYDVCDSCYRRDggVNHPHK 2241
Cdd:pfam00569    3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTH--KGGNHQ 44
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1700-1742 6.27e-05

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 42.20  E-value: 6.27e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2019726493  1700 NDEETEEWWVQCDKCEAWQHQICALFNGRRNDGGqAEYTCPYC 1742
Cdd:smart00249    6 GKPDDGGELLQCDGCDRWYHQTCLGPPLLEEEPD-GKWYCPKC 47
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 1700-1745 7.84e-05

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 42.09  E-value: 7.84e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2019726493 1700 NDEETEEWWVQCDKCEAWQHQICALFNGRRNDGGQAEYTCPYCYIA 1745
Cdd:pfam00628    6 GKSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSGEWLCPECKPK 51
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 2076-2110 9.82e-04

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 38.96  E-value: 9.82e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2019726493  2076 VHLQPSCTHCCMLMVsGNRWRCSQCKHFQICDKCY 2110
Cdd:smart00291    1 VHHSYSCDTCGKPIV-GVRYHCLVCPDYDLCQSCF 34
 
Name Accession Description Interval E-value
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
531-688 5.51e-91

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 292.56  E-value: 5.51e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  531 FERSINTLFLTEMVRGLSLTLKYFFDPKVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAVCPAQAITIEAE 610
Cdd:PRK05888     1 IKQYLKSMLLKELLKGLGVTLKYFFKKKVTIQYPEEKLPLSPRFRGRHALRRDPNGEERCIACKLCAAICPADAITIEAA 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  611 EREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKLLENGDRWETEIAENLKSESLY 688
Cdd:PRK05888    81 EREDGRRRTTRYDINFGRCIFCGFCEEACPTDAIVETPDFELATETREELIYDKEKLLANGDRVEREIAPGKAADANY 158
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 546-667 2.00e-63

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 211.89  E-value: 2.00e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  546 GLSLTLKYFFDPKVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAVCPAQAITIEAEEREDGSRRTTRYDID 625
Cdd:TIGR01971    1 GLGLTLKYFFSKPVTVQYPEEKLYLPPRFRGRIVLTRDPNGEEKCIGCTLCAAVCPADAIRVVPAEGEDGKRRLKFYEIN 80

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 2019726493  626 MTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEKL 667
Cdd:TIGR01971   81 FGRCIFCGLCEEACPTDAIVLTPEFELATYTRSDLVYGKEDL 122
HAT_KAT11 pfam08214
Histone acetylation protein; Histone acetylation is required in many cellular processes ...
 1802-2013 8.95e-41

Histone acetylation protein; Histone acetylation is required in many cellular processes including transcription, DNA repair, and chromatin assembly. This family contains the fungal KAT11 protein (previously known as RTT109) which is required for H3K56 acetylation. Loss of KAT11 results in the loss of H3K56 acetylation, both on bulk histone and on chromatin. KAT11 and H3K56 acetylation appear to correlate with actively transcribed genes and associate with the elongating form of Pol II in yeast. This family also incorporates the p300/CBP histone acetyltransferase domain which has different catalytic properties and cofactor regulation to KAT11.


Pssm-ID: 400497  Cd Length: 348  Bit Score: 155.25  E-value: 8.95e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493 1802 PTAESLVIRVVSSVDKKLEVKPRFLDIFrEDSYPTEFAYKSKVVLLFQKIEGVEVCLFGMYVQEFGSECAFPNQRRVYLS 1881
Cdd:pfam08214   10 PKGVKVTIRHLSSPPKEVEALFGMPPRF-AESGKPEFTYKEKHFFALSEIDGVEVIFFGLEVQVYGTVCPDPNERRVFVS 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493 1882 YLDSVKYFRPEVrsyngealRTFVYHEILIGYLEYCKLRGFTSCYIWACPPLKGEDYILychPEIQKTPK----SDK--L 1955
Cdd:pfam08214   89 KADSTGFFHLRV--------RTAVIHEILLSYLLYIKQRGYLRAVIWALFTRAQDQYLF---PNSSKNPKkhvlDGKglL 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493 1956 REYLAMLKKA-------SKEGIVAETINLYD--HFFMQT-----------GECRAKVTAARLPYFDGDYWPGAAEDLI 2013
Cdd:pfam08214  158 KWWCKMLDKIlveykssAKAKLVIPGKDIFKtrKYLPATadplwlvghifHQICDDPARYEIPLFPDDPKPRFLEELI 235
PHD_HAC_like cd15614
PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar ...
 1670-1742 1.79e-38

PHD finger found in Arabidopsis thaliana histone acetyltransferases (HATs) HAC and similar proteins; This family includes A. thaliana HACs (HAC1/2/4/5/12), which are histone acetyltransferases of the p300/CREB-binding protein (CBP) co-activator family. CBP-type HAT proteins are also found in animals, but absent in fungi. The domain architecture of CBP-type HAT proteins differs between plants and animals. Members in this family contain an N-terminal partially conserved KIX domain, a Zf-TAZ domain, a Cysteine rich CBP-type HAT domain that harbors a plant homeodomain (PHD) finger, a Zf-ZZ domain, and a Zf-TAZ domain. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 277086  Cd Length: 73  Bit Score: 138.64  E-value: 1.79e-38
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019726493 1670 FCIPCYNESRGDTIVAEGTPIPKARLEKKKNDEETEEWWVQCDKCEAWQHQICALFNGRRNDGGQAEYTCPYC 1742
Cdd:cd15614      1 WCSPCYNELKGENILIGGVPVKKSDLVKKKNDEEFEEAWVQCDKCERWQHQICGLYNGRRNADETAEYVCPLC 73
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
1311-1389 1.10e-31

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 119.39  E-value: 1.10e-31
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  1311 DPRFRNQQKWLLFLRHARNCKAPEGKCPDRNCVTVQKLWKHMDSCDAPQCSYPRCRPTKTLINHHRSCKESNCPVCIPV 1389
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCKAREAKCQYPNCKTMKKLLRHMDSCKVRKCKYGYCASCKQLWQHSKHCKDSNCPVCKCV 79
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 1317-1386 1.27e-28

TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.


Pssm-ID: 460457  Cd Length: 72  Bit Score: 110.55  E-value: 1.27e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019726493 1317 QQKWLLFLRHARNCKAPE-GKCPDRNCVTVQKLWKHMDSCDA-PQCSYPRCRPTKTLINHHRSCKESNCPVC 1386
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPGpGPCSLPNCRKMKRLLRHMATCKRgGGCPYPHCKRSRQLLRHAKNCKDEDCPVC 72
RING_CBP-p300 cd15802
atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP ...
 1638-1706 4.41e-28

atypical RING domain found in CREB-binding protein and p300 histone acetyltransferases; CBP and p300 (also known as CREBBP or KAT3A and EP300 or KAT3B, respectively) are two histone acetyltransferases (HATs) that associate with and acetylate transcriptional regulators and chromatin. The catalytic core of animal CBP-p300 contains a bromodomain, a CH2 region containing a discontinuous PHD domain interrupted by this RING domain, and a HAT domain. Bromodomain-RING-PHD forms a compact module in which the RING domain is juxtaposed with the HAT substrate-binding site. This ring domain contains only a single zinc ion-binding cluster instead of two; instead of a second zinc atom, a network of hydrophobic interactions stabilizes the domain. The RING domain has an inhibitory role. Disease mutations that disrupt RING attachment lead to upregulation of HAT activity. HAT regulation may require repositioning of the RING domain to facilitate access to an otherwise partially occluded HAT active site. Plant CBP-p300 type HATs lack a bromodomain whose role in the animal animal CBP-p300's is to bind acetylated histones; it has been suggested that these plant proteins may utilize a different domain or another bromodomain protein to perform this function. This RING domain has also been referred to as DUF902.


Pssm-ID: 276805  Cd Length: 73  Bit Score: 108.92  E-value: 4.41e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019726493 1638 FEPPPIYC-TPCGARIKRNAMYYTVGAGDTRHYFCIPCYNESRGDTIVAE---GTPIPKARLEKKKNDEETEE 1706
Cdd:cd15802      1 FEPQVLYCsGKCTIPRKRNAVYYSYQNLDNRYHFCEKCFNEIRGDEITLGddqGTSISKSQFEKKKNDELDEE 73
ZnF_TAZ smart00551
TAZ zinc finger, present in p300 and CBP;
2260-2338 3.14e-26

TAZ zinc finger, present in p300 and CBP;


Pssm-ID: 214717  Cd Length: 79  Bit Score: 103.98  E-value: 3.14e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  2260 QLRVLQLRKMLDLLVHASQCRS--AQCQYPNCRKVKGLFRHGIQCKVR--ASGGCVLCKKMWYllqlHARACKESQCHVP 2335
Cdd:smart00551    1 QTRYKQLQRWLELLVHARRCKAreAKCQYPNCKTMKKLLRHMDSCKVRkcKYGYCASCKQLWQ----HSKHCKDSNCPVC 76


                    ...
gi 2019726493  2336 RCS 2338
Cdd:smart00551   77 KCV 79
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 587-659 3.01e-24

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 97.89  E-value: 3.01e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEERedgsrrTTRYDIDMTKCIYCGFCQEACPVDAIVEGPnFEFATETHEE 659
Cdd:COG1143      1 EDKCIGCGLCVRVCPVDAITIEDGEP------GKVYVIDPDKCIGCGLCVEVCPTGAISMTP-FELAVEDREE 66
zf-TAZ pfam02135
TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 ...
 2266-2334 2.05e-19

TAZ zinc finger; The TAZ2 domain of CBP binds to other transcription factors such as the p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1. The zinc coordinating motif that is necessary for binding to target DNA sequences consists of HCCC.


Pssm-ID: 460457  Cd Length: 72  Bit Score: 84.36  E-value: 2.05e-19
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019726493 2266 LRKMLDLLVHASQCRSA---QCQYPNCRKVKGLFRHGIQCKvrASGGC--VLCKKMWYLLQlHARACKESQCHV 2334
Cdd:pfam02135    1 LQRWLLLLLHASKCSAPgpgPCSLPNCRKMKRLLRHMATCK--RGGGCpyPHCKRSRQLLR-HAKNCKDEDCPV 71
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 543-672 2.35e-19

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 87.78  E-value: 2.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  543 MVRGLSLTLKYffdPKVTINYPFEKGPLSPRFRG--EHALrryptgeERCIACKLCEAVCPAQAITIEAEEredgSRRTT 620
Cdd:PRK12387     1 MFKLIKKVIKT---GTATSSYPLEPIAVDKNFRGkpEYNP-------QQCIGCAACVNACPSNALTVETDL----ATGEL 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2019726493  621 RYDIDMTKCIYCGFCQEACPVDAIVEGPNFEFAtetheelLYDKEKLLENGD 672
Cdd:PRK12387    67 AWEFNLGRCIFCGRCEEVCPTAAIKLSQEFELA-------VWKKEDLLQQSE 111
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 587-645 4.02e-17

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 79.75  E-value: 4.02e-17
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEeredgsrrtTRYDIDMTKCIYCGFCQEACPVDAIV 645
Cdd:cd10549     77 EEKCIGCGLCVKVCPVDAITLEDE---------LEIVIDKEKCIGCGICAEVCPVNAIK 126
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
578-651 7.17e-16

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 74.38  E-value: 7.17e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019726493  578 HALRRYPTGEERCIACKLCEAVCPAQAITIEAEeredgsrrttRYDIDMTKCIYCGFCQEACPVDAIVEGPNFE 651
Cdd:COG2768      1 HSLGKPYVDEEKCIGCGACVKVCPVGAISIEDG----------KAVIDPEKCIGCGACIEVCPVGAIKIEWEED 64
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 587-666 9.39e-16

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 75.90  E-value: 9.39e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEaeerEDGSRRTTRyDIDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDKEK 666
Cdd:cd10549      5 PEKCIGCGICVKACPTDAIELG----PNGAIARGP-EIDEDKCVFCGACVEVCPTGAIELTPEGKEYVPKEKEAEIDEEK 79
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 587-652 2.38e-15

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 72.39  E-value: 2.38e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEeredgsrrttRYDIDMTKCIYCGFCQEACPVDAIVEGPNFEF 652
Cdd:COG2221     14 EEKCIGCGLCVAVCPTGAISLDDG----------KLVIDEEKCIGCGACIRVCPTGAIKGEKPKKF 69
ZZ_CBP cd02337
Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif ...
 2200-2245 2.44e-15

Zinc finger, ZZ type. Zinc finger present in CBP/p300 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. CREB-binding protein (CBP) is a large multidomain protein that provides binding sites for transcriptional coactivators, the role of the ZZ domain in CBP/p300 is unclear.


Pssm-ID: 239077  Cd Length: 41  Bit Score: 71.83  E-value: 2.44e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2019726493 2200 TTCNACHLDIETGqgWRCEVCPDYDVCDSCYRRdggVNHPHKLTNH 2245
Cdd:cd02337      1 YTCNECKHHVETR--WHCTVCEDYDLCITCYNT---KNHPHKMEKL 41
PRK08222 PRK08222
hydrogenase 4 subunit H; Validated
 559-664 2.98e-15

hydrogenase 4 subunit H; Validated


Pssm-ID: 181301 [Multi-domain]  Cd Length: 181  Bit Score: 75.94  E-value: 2.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  559 VTINYPFEKGPLSPRFRGEHALrryptGEERCIACKLCEAVCPAQAITIEAEErEDGSRRttrYDIDMTKCIYCGFCQEA 638
Cdd:PRK08222    14 ATVKYPFAPLEVSPGFRGKPDL-----MPSQCIACGACTCACPANALTIQTDD-QQNSRT---WQLYLGRCIYCGRCEEV 84

                           90       100
                   ....*....|....*....|....*.
gi 2019726493  639 CPVDAIVEGPNFEFATeTHEELLYDK 664
Cdd:PRK08222    85 CPTRAIQLTNNFELTV-TNKADLYTR 109
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 587-644 1.29e-14

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 72.43  E-value: 1.29e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEaEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:cd10549     39 EDKCVFCGACVEVCPTGAIELT-PEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAI 95
ndhI CHL00014
NADH dehydrogenase subunit I
 545-664 1.59e-14

NADH dehydrogenase subunit I


Pssm-ID: 214334 [Multi-domain]  Cd Length: 167  Bit Score: 73.64  E-value: 1.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  545 RGLSLTLKYFFDPKVTINYPFEKGPLSPRFRGehalrRYPTGEERCIACKLCEAVCPAQAITIEAE-EREDGSRRTTRYD 623
Cdd:CHL00014    21 QGFMITLSHANRLPVTIQYPYEKLITSERFRG-----RIHFEFDKCIACEVCVRVCPIDLPVVDWKlETDIRKKRLLNYS 95

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 2019726493  624 IDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEELLYDK 664
Cdd:CHL00014    96 IDFGVCIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQ 136
NapF COG1145
Ferredoxin [Energy production and conversion];
587-644 2.12e-14

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 75.14  E-value: 2.12e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEREdgsrrttrYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:COG1145    181 AEKCIGCGLCVKVCPTGAIRLKDGKPQ--------IVVDPDKCIGCGACVKVCPVGAI 230
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 590-643 3.53e-14

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 68.71  E-value: 3.53e-14
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2019726493  590 CIACKLCEAVCPAQAITIEAEEREDGsrrTTRYDIDMTKCIYCGFCQEACPVDA 643
Cdd:pfam12838    1 CIGCGACVAACPVGAITLDEVGEKKG---TKTVVIDPERCVGCGACVAVCPTGA 51
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 587-645 2.30e-13

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 66.99  E-value: 2.30e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEaeereDGSRRttrydIDMTKCIYCGFCQEACPVDAIV 645
Cdd:COG4231     21 EDKCTGCGACVKVCPADAIEEG-----DGKAV-----IDPDLCIGCGSCVQVCPVDAIK 69
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 587-648 5.19e-13

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 65.90  E-value: 5.19e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEredgsrrttRYDIDMTKCIYCGFCQEACPVDAIVEGP 648
Cdd:COG1149     10 EEKCIGCGLCVEVCPEGAIKLDDGG---------APVVDPDLCTGCGACVGVCPTGAITLEE 62
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 587-645 5.47e-13

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 66.23  E-value: 5.47e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEeredgsrrtTRYDIDMTKCIYCGFCQEACPVDAIV 645
Cdd:COG1144     29 EDKCIGCGLCWIVCPDGAIRVDDG---------KYYGIDYDYCKGCGICAEVCPVKAIE 78
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 587-644 2.93e-12

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 63.57  E-value: 2.93e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEeredgSRRTTRYDIDmtKCIYCGFCQEACPVDAI 644
Cdd:COG1146      7 TDKCIGCGACVEVCPVDVLELDEE-----GKKALVINPE--ECIGCGACELVCPVGAI 57
PHD_TCF19_like cd15517
PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and ...
 1701-1742 1.89e-11

PHD finger found in Transcription factor 19 (TCF-19), Lysine-specific demethylase KDM5A and KDM5B, and other similar proteins; TCF-19 was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. KDM5A was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interaction with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK, and BMAL1. KDM5B has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. Both KDM5A and KDM5B function as trimethylated histone H3 lysine 4 (H3K4me3) demethylases. This family also includes Caenorhabditis elegans Lysine-specific demethylase 7 homolog (ceKDM7A). ceKDM7A (also termed JmjC domain-containing protein 1.2, PHD finger protein 8 homolog, or PHF8 homolog) is a plant homeodomain (PHD)- and JmjC domain-containing protein that functions as a histone demethylase specific for H3K9me2 and H3K27me2. The binding of the PHD finger to H3K4me3 guides H3K9me2- and H3K27me2-specific demethylation by its catalytic JmjC domain in a trans-histone regulation mechanism. In addition, this family includes plant protein OBERON 1 and OBERON 2, Alfin1-like (AL) proteins, histone acetyltransferases (HATs) HAC, and AT-rich interactive domain-containing protein 4 (ARID4).


Pssm-ID: 276992 [Multi-domain]  Cd Length: 49  Bit Score: 61.03  E-value: 1.89e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2019726493 1701 DEETEEWWVQCDKCEAWQHQICALFNGRRNDGGqAEYTCPYC 1742
Cdd:cd15517      9 TAAVDELWVQCDGCDKWFHQFCLGLSNERYADE-DKFKCPNC 49
Fer4_9 pfam13187
4Fe-4S dicluster domain;
589-644 3.29e-10

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 57.56  E-value: 3.29e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2019726493  589 RCIACKLCEAVCPAQAItieaeeREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:pfam13187    1 KCTGCGACVAACPAGAI------VPDLVGQTIRGDIAGLACIGCGACVDACPRGAI 50
EPL1 pfam10513
Enhancer of polycomb-like; This is a family of EPL1 (Enhancer of polycomb-like) proteins. The ...
 7-137 6.10e-10

Enhancer of polycomb-like; This is a family of EPL1 (Enhancer of polycomb-like) proteins. The EPL1 protein is a member of a histone acetyltransferase complex which is involved in transcriptional activation of selected genes.


Pssm-ID: 463128  Cd Length: 168  Bit Score: 60.19  E-value: 6.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493    7 RPRPLDIHKKLPILKSykdfEDDDTPTRNP---------------------------------------QLLRLASSVEL 47
Cdd:pfam10513    1 RHRRISIKQPLPIISE----DEVDGLDTSPdedepsecnsnkenslhavetgvdkeeedevhlkvinaaKKALSSSKKSQ 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493   48 DHEVSPVPSK-KLASEIPTPQFVVVDSYERDysptfgqPASYLRA-RGARSELGEFVEYDLDNEDDDWLYEFDKDNK--- 122
Cdd:pfam10513   77 NTSESSVPAPnKERLYLPTPDAGKFREFERP-------PASYIRFsETVEEELDEGVEYDMDEEDEAWLEELNEKRKseg 149

                          170
                   ....*....|....*..
gi 2019726493  123 --QLSPEMFESIIFKLE 137
Cdd:pfam10513  150 veKISEDEFEILMDRFE 166
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
587-666 8.18e-10

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 63.89  E-value: 8.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEREdgsrrttrydIDMTKCIYCGFCQEACPVDAIVEgpnfefATETHE--ELLYDK 664
Cdd:COG4624     90 KEKCKNCYPCVRACPVKAIKVDDGKAE----------IDEEKCISCGQCVAVCPFGAITE------KSDIEKvkKALKDP 153


                   ..
gi 2019726493  665 EK 666
Cdd:COG4624    154 EK 155
PRK13984 PRK13984
putative oxidoreductase; Provisional
 552-639 8.49e-10

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 64.02  E-value: 8.49e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  552 KYFFDPKVTINYPFEKGPLSPRFRGEHAlrrypTGEERCIACKLCEAVCPAQAIT-IEAEE--REDGSrRTTRYDIDMTK 628
Cdd:PRK13984    14 KFLFRKPVTIKVPNVKREAAERYRGFHI-----NDWEKCIGCGTCSKICPTDAITmVEVPDlpQEYGK-KPQRPVIDYGR 87

                           90
                   ....*....|.
gi 2019726493  629 CIYCGFCQEAC 639
Cdd:PRK13984    88 CSFCALCVDIC 98
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 547-655 8.52e-10

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 58.69  E-value: 8.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  547 LSLTLKYFFDPKVTINYP-FEKGPLSPRFRGEHALRRyptgeERCIACKLCEAVCPAQAITIEAEERedgsrrttRYDID 625
Cdd:PRK08348     5 LPTVLRNLFKKPATNLFPaTEPVPVPEDFRGKILYDV-----DKCVGCRMCVTVCPAGVFVYLPEIR--------KVALW 71

                           90       100       110
                   ....*....|....*....|....*....|
gi 2019726493  626 MTKCIYCGFCQEACPVDAIVEGPNFEFATE 655
Cdd:PRK08348    72 TGRCVFCGQCVDVCPTGALQMSDDFLLASY 101
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
590-646 1.49e-09

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 61.49  E-value: 1.49e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  590 CIACKLCEAVCPAQAITIE---AEeredgsrrttrydIDMTKCIYCGFCQEACPVDAIVE 646
Cdd:PRK07118   215 CIGCGKCVKACPAGAITMEnnlAV-------------IDQEKCTSCGKCVEKCPTKAIRI 261
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 577-645 1.56e-08

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 55.47  E-value: 1.56e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  577 EHALRRYPTG-----EERCIACKLCEAVCPAQAITIEAEEREdgsrrttrydidMTKCIYCGF---------CQEACPVD 642
Cdd:cd04410     64 TGAIYKDEDGivlidEDKCIGCGSCVEACPYGAIVFDPEPGK------------AVKCDLCGDrldeglepaCVKACPTG 131


                   ...
gi 2019726493  643 AIV 645
Cdd:cd04410    132 ALT 134
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 578-645 2.90e-08

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 55.72  E-value: 2.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  578 HALRRYPTG-----EERCIACKLCEAVCPAQAITIeaeEREDGSrrttrydidMTKCIYCGF---------CQEACPVDA 643
Cdd:COG0437     75 GATYKREDGivlvdYDKCIGCRYCVAACPYGAPRF---NPETGV---------VEKCTFCADrldegllpaCVEACPTGA 142


                   ..
gi 2019726493  644 IV 645
Cdd:COG0437    143 LV 144
PRK06273 PRK06273
ferredoxin; Provisional
 587-669 7.31e-08

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 54.33  E-value: 7.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  587 EERCIACKLCEAVCPAQAIT---IEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIvegpnFEFATETH-----E 658
Cdd:PRK06273    48 EELCIGCGGCANVCPTKAIEmipVEPVKITEGYVKTKIPKIDYEKCVYCLYCHDFCPVFAL-----FNEISPIHprdvgE 122

                           90
                   ....*....|.
gi 2019726493  659 ELLYDKEKLLE 669
Cdd:PRK06273   123 DIEVDVSKLLE 133
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
587-644 8.99e-08

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 57.56  E-value: 8.99e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEeredgsrrtTRYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:COG1148    495 PEKCTGCGRCVEVCPYGAISIDEK---------GVAEVNPALCKGCGTCAAACPSGAI 543
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 2198-2241 9.00e-08

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 50.13  E-value: 9.00e-08
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|....
gi 2019726493  2198 FVTTCNACHLDIeTGQGWRCEVCPDYDVCDSCYrRDGGVNHPHK 2241
Cdd:smart00291    3 HSYSCDTCGKPI-VGVRYHCLVCPDYDLCQSCF-AKGSAGGEHS 44
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 587-644 1.21e-07

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 53.03  E-value: 1.21e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEREDGSRRTTRYDIdMTKCIYCGF------CQEACPVDAI 644
Cdd:cd10554     84 EERCIGCKLCVLACPFGAIEMAPTTVPGVDWERGPRAV-AVKCDLCAGreggpaCVEACPTKAL 146
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
590-644 1.22e-07

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 52.74  E-value: 1.22e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2019726493  590 CIACKL--CEAVCPAQAITieaeeREDGsrrttRYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:COG1142     52 CRHCEDapCAEVCPVGAIT-----RDDG-----AVVVDEEKCIGCGLCVLACPFGAI 98
FeFe_hydrog_B1 TIGR04105
[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.
 588-646 1.97e-07

[FeFe] hydrogenase, group B1/B3; See for descriptions of different groups.


Pssm-ID: 274983 [Multi-domain]  Cd Length: 462  Bit Score: 56.06  E-value: 1.97e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019726493  588 ERCIACKLCEAVCPAQAIT------IEA------EEREDGsrrttRYDIDMTKCIYCGFCQEACPVDAIVE 646
Cdd:TIGR04105  142 EKCIECGKCKKACPYNAIVeierpcEKAcpvgaiSSDEDG-----RAVIDYDKCISCGACMVACPFGAISD 207
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
587-644 2.54e-07

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 54.30  E-value: 2.54e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  587 EERCIACKLCEAVCPAQaITIEAEEredgsrrttrydIDMTKCIYCGFCQEACPVDAI 644
Cdd:COG0348    209 RGDCIDCGLCVKVCPMG-IDIRKGE------------INQSECINCGRCIDACPKDAI 253
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 587-640 2.54e-07

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 49.56  E-value: 2.54e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEREDGSRRTtryDIDMTKCIYCGFCQEACP 640
Cdd:pfam13237    6 PDKCIGCGRCTAACPAGLTRVGAIVERLEGEAV---RIGVWKCIGCGACVEACP 56
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 587-645 2.62e-07

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 52.26  E-value: 2.62e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  587 EERCIA------CKLCEAVCPAQAITIEAEereDGSRRTTrydIDMTKCIYCGFCQEACPVD---AIV 645
Cdd:cd16373     90 KDRCLAwqggtdCGVCVEACPTEAIAIVLE---DDVLRPV---VDEDKCVGCGLCEYVCPVEppkAIV 151
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 581-645 2.71e-07

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 51.81  E-value: 2.71e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  581 RRYPTGEERCIACKLCE-----AVCPAQAITIEAEeredgsrrTTRYDIDMTKCIYCGFCQEACPVDAIV 645
Cdd:cd10550     37 RFEPEGLDVPVVCRQCEdapcvEACPVGAISRDEE--------TGAVVVDEDKCIGCGMCVEACPFGAIR 98
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 588-645 4.21e-07

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 52.53  E-value: 4.21e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  588 ERCIACKLCEAVCPAQAITI---EAEEREDGSRRTTRYdidMTKCIYC------G---FCQEACPVDAIV 645
Cdd:cd10551     83 DKCIGCRYCMAACPYGARYFnpeEPHEFGEVPVRPKGV---VEKCTFCyhrldeGllpACVEACPTGARI 149
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
590-640 4.47e-07

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 49.03  E-value: 4.47e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019726493  590 CIACKLCEAVCPAQAITIEAEEREdgSRRTTRYDIDMTK--------------CIYCGFCQEACP 640
Cdd:pfam13484    1 CGSCGKCIDACPTGAIVGPEGVLD--ARRCISYLTIEKKglipdelrcllgnrCYGCDICQDVCP 63
ZZ cd02249
Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ...
 2201-2245 4.92e-07

Zinc finger, ZZ type. Zinc finger present in dystrophin, CBP/p300 and many other proteins. The ZZ motif coordinates one or two zinc ions and most likely participates in ligand binding or molecular scaffolding. Many proteins containing ZZ motifs have other zinc-binding motifs as well, and the majority serve as scaffolds in pathways involving acetyltransferase, protein kinase, or ubiqitin-related activity. ZZ proteins can be grouped into the following functional classes: chromatin modifying, cytoskeletal scaffolding, ubiquitin binding or conjugating, and membrane receptor or ion-channel modifying proteins.


Pssm-ID: 239069 [Multi-domain]  Cd Length: 46  Bit Score: 48.20  E-value: 4.92e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2019726493 2201 TCNACHLDIeTGQGWRCEVCPDYDVCDSCYRRDGGVNHP-HKLTNH 2245
Cdd:cd02249      2 SCDGCLKPI-VGVRYHCLVCEDFDLCSSCYAKGKKGHPPdHSFTEI 46
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
587-645 4.98e-07

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 51.20  E-value: 4.98e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEREDGSrrttrydidmTKCIYCGF------CQEACPVDAIV 645
Cdd:COG1142     80 EEKCIGCGLCVLACPFGAITMVGEKSRAVA----------VKCDLCGGreggpaCVEACPTGALR 134
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 552-644 5.80e-07

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 52.94  E-value: 5.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  552 KYFFDPKVTINYPFEKGPLSPRFRGEHALRRYPTGEERCIACKLCEAVCPAQAITIEAEEREDGSrrttrydidmtKCIY 631
Cdd:NF038196   149 KKGPEKKKGFIPRLLSKLVNPLFYKFKVKDKKFHVTDKCIGCGICAKVCPVNNIEMEDGKPVWGH-----------NCTH 217

                           90
                   ....*....|...
gi 2019726493  632 CGFCQEACPVDAI 644
Cdd:NF038196   218 CLACIHRCPKEAI 230
HybA COG0437
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ...
 596-644 1.10e-06

Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];


Pssm-ID: 440206 [Multi-domain]  Cd Length: 184  Bit Score: 51.10  E-value: 1.10e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2019726493  596 CEAVCPAQAITIeaeeREDGSRRttrydIDMTKCIYCGFCQEACPVDAI 644
Cdd:COG0437     68 CVKVCPTGATYK----REDGIVL-----VDYDKCIGCRYCVAACPYGAP 107
NapF COG1145
Ferredoxin [Energy production and conversion];
586-649 2.25e-06

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 51.26  E-value: 2.25e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019726493  586 GEERCIACKLCEAVCPAQAITIEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPN 649
Cdd:COG1145    141 EAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGAIRLKDG 204
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 589-644 2.32e-06

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 49.56  E-value: 2.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  589 RCIACKLCEAVCPAQAITIEAeeREDGSR--RTTRYDIDMTKCIYCG-FCQEACPVDAI 644
Cdd:cd16373     15 LCIRCGLCVEACPTGVIQPAG--LEDGLEggRTPYLDPREGPCDLCCdACVEVCPTGAL 71
PRK13795 PRK13795
hypothetical protein; Provisional
 589-641 3.25e-06

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 52.69  E-value: 3.25e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2019726493  589 RCIACKLCEAVCPAQAITIEAEERedgsrrttRYDIDMTKCIYCGFCQEACPV 641
Cdd:PRK13795   582 ECVGCGVCVGACPTGAIRIEEGKR--------KISVDEEKCIHCGKCTEVCPV 626
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 587-644 4.20e-06

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 48.34  E-value: 4.20e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEREdgsrrttrydidMTKCIYCG---FCQEACPVDAI 644
Cdd:cd10550     79 EDKCIGCGMCVEACPFGAIRVDPETGK------------AIKCDLCGgdpACVKVCPTGAL 127
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 591-644 4.29e-06

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 48.39  E-value: 4.29e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2019726493  591 IACKLCEAVCPAQAITIEAeeREDGSRRTTrydIDMTKCIYCGFCQEACPVDAI 644
Cdd:cd10564     86 VECRSCQDACPTQAIRFRP--RLGGIALPE---LDADACTGCGACVSVCPVGAI 134
PFLE_PFLC TIGR02494
glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) ...
 587-644 4.48e-06

glycyl-radical enzyme activating protein; This subset of the radical-SAM family (pfam04055) includes a number of probable activating proteins acting on different enzymes all requiring an amino-acid-centered radical. The closest relatives to this family are the pyruvate-formate lyase activating enzyme (PflA, 1.97.1.4, TIGR02493) and the anaerobic ribonucleotide reductase activating enzyme (TIGR02491). Included within this subfamily are activators of hydroxyphenyl acetate decarboxylase (HdpA), benzylsuccinate synthase (BssD), gycerol dehydratase (DhaB2) as well as enzymes annotated in E. coli as activators of different isozymes of pyruvate-formate lyase (PFLC and PFLE) however, these appear to lack characterization and may activate enzymes with distinctive functions. Most of the sequence-level variability between these forms is concentrated within an N-terminal domain which follows a conserved group of three cysteines and contains a variable pattern of 0 to 8 additional cysteines.


Pssm-ID: 274163 [Multi-domain]  Cd Length: 295  Bit Score: 50.80  E-value: 4.48e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  587 EERCIACKLCEAVCPAQaiTIEAEEREDGSrrtTRYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:TIGR02494   47 ENRCLGCGKCVEVCPAG--TARLSELADGR---NRIIIRREKCTHCGKCTEACPSGAL 99
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 622-644 4.80e-06

4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 44.93  E-value: 4.80e-06
                           10        20
                   ....*....|....*....|...
gi 2019726493  622 YDIDMTKCIYCGFCQEACPVDAI 644
Cdd:pfam00037    1 VVIDEEKCIGCGACVEVCPVGAI 23
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 591-645 6.55e-06

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 47.94  E-value: 6.55e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  591 IACKLCE-----AVCPAQAITIeaeeREDGsrrTTRYDIDmtKCIYCGFCQEACPVDAIV 645
Cdd:cd16371     52 MSCNHCEnpacvKVCPTGAITK----REDG---IVVVDQD--KCIGCGYCVWACPYGAPQ 102
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 590-648 6.83e-06

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 51.41  E-value: 6.83e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  590 CIACKLCEAVCPAQAITIEAEERedgsrrttRYDIDMTKCIYCGFCQEACPVDAIVEGP 648
Cdd:PRK12771   512 CFECDNCYGACPQDAIIKLGPGR--------RYHFDYDKCTGCHICADVCPCGAIEMGP 562
PRK14028 PRK14028
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
 589-644 7.27e-06

pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional


Pssm-ID: 172522 [Multi-domain]  Cd Length: 312  Bit Score: 50.38  E-value: 7.27e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  589 RCIACKLCEAVCPAQAItIEAEEREDGSR----RTTRYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:PRK14028   248 KCIMCRKCWLYCPDDAI-IEAWREAEGPRgrkfRMKMIDFDYQYCKGCGVCAEVCPTGAI 306
PsrB cd10551
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ...
 596-644 7.67e-06

polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.


Pssm-ID: 319873 [Multi-domain]  Cd Length: 185  Bit Score: 48.68  E-value: 7.67e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2019726493  596 CEAVCPAQAITIeaeeREDGsrrttRYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:cd10551     61 CVKVCPTGATYK----REDG-----IVLVDYDKCIGCRYCMAACPYGAR 100
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
587-644 8.46e-06

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 46.86  E-value: 8.46e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  587 EERCIACKLCEAVCPAQAITIeaeeREDGSrrttrYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:PRK09623    50 ESKCVKCYICWKFCPEPAIYI----KEDGY-----VAIDYDYCKGCGICANECPTKAI 98
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 576-615 9.21e-06

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 45.47  E-value: 9.21e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2019726493  576 GEHALRRYPtgeERCIACKLCEAVCPAQAITIEAEEREDG 615
Cdd:COG1146     31 GKKALVINP---EECIGCGACELVCPVGAITVEDDEPEEQ 67
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 590-644 1.11e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 46.88  E-value: 1.11e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2019726493  590 CIACKL--CEAVCPAQAItieaEEREDGSrrtTRYDIDmtKCIYCGFCQEACPVDAI 644
Cdd:cd16370     53 CRACEDppCAEACPTGAL----EPRKGGG---VVLDKE--KCIGCGNCVKACIVGAI 100
ZZ_PCMF_like cd02338
Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and ...
 2201-2246 1.30e-05

Zinc finger, ZZ type. Zinc finger present in potassium channel modulatory factor (PCMF) 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Human potassium channel modulatory factor 1 or FIGC has been shown to possess intrinsic E3 ubiquitin ligase activity and to promote ubiquitination.


Pssm-ID: 239078  Cd Length: 49  Bit Score: 44.26  E-value: 1.30e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2019726493 2201 TCNACHLDIETGQGWRCEVCPDYDVCDSCYrrDGGVNHPHKLTNHP 2246
Cdd:cd02338      2 SCDGCGKSNFTGRRYKCLICYDYDLCADCY--DSGVTTERHLFDHP 45
PHD3_KDM5A_like cd15610
PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins; ...
 1708-1742 1.55e-05

PHD finger 3 found in Lysine-specific demethylase 5A (KDM5A), 5B (KDM5B), and similar proteins; The family includes KDM5A and KDM5B, both of which belong to the JARID subfamily within the JmjC proteins. KDM5A, also termed Histone demethylase JARID1A, or Jumonji/ARID domain-containing protein 1A, or Retinoblastoma-binding protein 2 (RBBP-2 or RBP2), was originally identified as a retinoblastoma protein (Rb)-binding partner and its inactivation may be important for Rb to promote differentiation. It is involved in transcription through interacting with TBP, p107, nuclear receptors, Myc, Sin3/HDAC, Mad1, RBP-J, CLOCK and BMAL1. KDM5A functions as the trimethylated histone H3 lysine 4 (H3K4me3) demethylase. It also displays DNA-binding activities that can recognize the specific DNA sequence CCGCCC. KDM5B, also termed Cancer/testis antigen 31 (CT31), or Histone demethylase JARID1B, or Jumonji/ARID domain-containing protein 1B (JARID1B), or PLU-1, or retinoblastoma-binding protein 2 homolog 1 (RBP2-H1 or RBBP2H1A), has a restricted expression pattern in the testis, ovary, and transiently in the mammary gland of the pregnant female and has been shown to be upregulated in breast cancer, prostate cancer, and lung cancer, suggesting a potential role in tumorigenesis. KDM5B acts as a histone demethylase that catalyzes the removal of trimethylation of lysine 4 on histone H3 (H3K4me3), induced by polychlorinated biphenyls (PCBs). It also mediates demethylation of H3K4me2 and H3K4me1. Moreover, KDM5B functions as a negative regulator of hematopoietic stem cell (HSC) self-renewal and progenitor cell activity. KDM5B has also been shown to interact with the DNA binding transcription factors BF-1 and PAX9, as well asTIEG1/KLF10 (transforming growth factor-beta inducible early gene-1/Kruppel-like transcription factor 10), and possibly function as a transcriptional corepressor. The family also includes the Drosophila melanogaster protein little imaginal discs (Lid) that functions as a JmjC-dependent trimethyl histone H3K4 (H3K4me3) demethylase, which is required for dMyc-induced cell growth. It positively regulates Hox gene expression in S2 cells. Members in this family contain the catalytic JmjC domain, JmjN, the BRIGHT domain, which is an AT-rich interacting domain (ARID), and a Cys5HisCys2 zinc finger, as well as three plant homeodomain (PHD) fingers. This model corresponds to the third PHD finger.


Pssm-ID: 277083 [Multi-domain]  Cd Length: 50  Bit Score: 44.24  E-value: 1.55e-05
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 2019726493 1708 WVQCDKCEAWQHQICALFNgRRNDGGQAEYTCPYC 1742
Cdd:cd15610     17 WVQCDGCEEWFHLLCVGLS-PEEVAEDEDYICPSC 50
ZZ_NBR1_like cd02340
Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 ...
 2201-2239 1.77e-05

Zinc finger, ZZ type. Zinc finger present in Drosophila ref(2)P, NBR1, Human sequestosome 1 and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Drosophila ref(2)P appears to control the multiplication of sigma rhabdovirus. NBR1 (Next to BRCA1 gene 1 protein) interacts with fasciculation and elongation protein zeta-1 (FEZ1) and calcium and integrin binding protein (CIB), and may function in cell signalling pathways. Sequestosome 1 is a phosphotyrosine independent ligand for the Lck SH2 domain and binds noncovalently to ubiquitin via its UBA domain.


Pssm-ID: 239080  Cd Length: 43  Bit Score: 43.79  E-value: 1.77e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2019726493 2201 TCNACHLDIeTGQGWRCEVCPDYDVCDSCYRRDGGVNHP 2239
Cdd:cd02340      2 ICDGCQGPI-VGVRYKCLVCPDYDLCESCEAKGVHPEHA 39
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 624-659 2.12e-05

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 44.31  E-value: 2.12e-05
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2019726493  624 IDMTKCIYCGFCQEACPVDAIVEGPNFEFATETHEE 659
Cdd:COG1146      5 IDTDKCIGCGACVEVCPVDVLELDEEGKKALVINPE 40
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
589-644 2.54e-05

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 49.25  E-value: 2.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2019726493  589 RCIACKLCEAVCPAQAITIEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:COG4624     53 RCCLCCCCCCRCCVAISCIQVRGIIIIDKRGPSIIRDKEKCKNCYPCVRACPVKAI 108
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 589-644 2.81e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 46.11  E-value: 2.81e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  589 RCIACK--LCEAVCPAQAITIEaeerEDGSRRttrydIDMTKCIYCGFCQEACPVDAI 644
Cdd:cd16374     42 RCRHCEdaPCMEVCPTGAIYRD----EDGAVL-----VDPDKCIGCGMCAMACPFGVP 90
ZZ pfam00569
Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds ...
 2198-2241 2.97e-05

Zinc finger, ZZ type; Zinc finger present in dystrophin, CBP/p300. ZZ in dystrophin binds calmodulin. Putative zinc finger; binding not yet shown. Four to six cysteine residues in its sequence are responsible for coordinating zinc ions, to reinforce the structure.


Pssm-ID: 395451  Cd Length: 45  Bit Score: 43.24  E-value: 2.97e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2019726493 2198 FVTTCNACHLDIETGQGWRCEVCPDYDVCDSCYRRDggVNHPHK 2241
Cdd:pfam00569    3 KVYTCNGCSNDPSIGVRYHCLRCSDYDLCQSCFQTH--KGGNHQ 44
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 587-644 3.52e-05

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 47.68  E-value: 3.52e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEaeerEDGSRRttrydIDMTKCIYCGFCQEACPVDAI 644
Cdd:COG2878    136 EYGCIGCGDCIKACPFDAIVGA----AKGMHT-----VDEDKCTGCGLCVEACPVDCI 184
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 618-649 3.56e-05

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 43.88  E-value: 3.56e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2019726493  618 RTT--RYDIDMTKCIYCGFCQEACPVDAIVEGPN 649
Cdd:COG4231     11 RTTamRYVIDEDKCTGCGACVKVCPADAIEEGDG 44
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 587-648 4.39e-05

Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 45.46  E-value: 4.39e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  587 EERCIACKLCEAVCPaQAITIEAEEREDGSRRTTRYDIDM----TKCIYCGF--CQEACPVDAIVEGP 648
Cdd:cd04410      5 LDRCIGCGTCEVACK-QEHGLRPGPDWSRIKVIEGGGLERaflpVSCMHCEDppCVKACPTGAIYKDE 71
DMSOR_beta_like cd16370
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 579-644 5.42e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319892 [Multi-domain]  Cd Length: 131  Bit Score: 44.96  E-value: 5.42e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2019726493  579 ALRRYPTG-----EERCIACKLCEAVCPAQAITIEAEeredgsrrtTRYDIdmtKCIYCGFCQEACPVDAI 644
Cdd:cd16370     69 ALEPRKGGgvvldKEKCIGCGNCVKACIVGAIFWDEE---------TNKPI---ICIHCGYCARYCPHDVL 127
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 609-655 5.62e-05

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 43.50  E-value: 5.62e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2019726493  609 AEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAI--VEGPNFEFATE 655
Cdd:COG1144     12 TAAYKTGGWRVERPVVDEDKCIGCGLCWIVCPDGAIrvDDGKYYGIDYD 60
Fer4_8 pfam13183
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 589-642 5.90e-05

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 433017 [Multi-domain]  Cd Length: 64  Bit Score: 43.07  E-value: 5.90e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019726493  589 RCIACKLCEAVCPA---------QAITIEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVD 642
Cdd:pfam13183    1 RCIRCGACLAACPVylvtggrfpGDPRGGAAALLGRLEALEGLAEGLWLCTLCGACTEVCPVG 63
PHD smart00249
PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in ...
 1700-1742 6.27e-05

PHD zinc finger; The plant homeodomain (PHD) finger is a C4HC3 zinc-finger-like motif found in nuclear proteins thought to be involved in epigenetics and chromatin-mediated transcriptional regulation. The PHD finger binds two zinc ions using the so-called 'cross-brace' motif and is thus structurally related to the RING finger and the FYVE finger. It is not yet known if PHD fingers have a common molecular function. Several reports suggest that it can function as a protein-protein interacton domain and it was recently demonstrated that the PHD finger of p300 can cooperate with the adjacent BROMO domain in nucleosome binding in vitro. Other reports suggesting that the PHD finger is a ubiquitin ligase have been refuted as these domains were RING fingers misidentified as PHD fingers.


Pssm-ID: 214584 [Multi-domain]  Cd Length: 47  Bit Score: 42.20  E-value: 6.27e-05
                            10        20        30        40
                    ....*....|....*....|....*....|....*....|...
gi 2019726493  1700 NDEETEEWWVQCDKCEAWQHQICALFNGRRNDGGqAEYTCPYC 1742
Cdd:smart00249    6 GKPDDGGELLQCDGCDRWYHQTCLGPPLLEEEPD-GKWYCPKC 47
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 588-644 6.42e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 44.88  E-value: 6.42e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  588 ERCIACKLCEAVC---------PAQA-ITIEAEEREDgsrrttrYDIDMTkCIYCG--FCQEACPVDAI 644
Cdd:cd10550      6 EKCTGCRTCELACslkhegvfnPSLSrIRVVRFEPEG-------LDVPVV-CRQCEdaPCVEACPVGAI 66
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 579-655 6.80e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 44.96  E-value: 6.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  579 ALRRYPTG-----EERCIACKLCEAVCPAQAITIEAEEREdgsrrttrydidMTKCIYCG---------FCQEACPVDAI 644
Cdd:cd16374     59 AIYRDEDGavlvdPDKCIGCGMCAMACPFGVPRFDPSLKV------------AVKCDLCIdrrregklpACVEACPTGAL 126

                           90
                   ....*....|.
gi 2019726493  645 VEGPNFEFATE 655
Cdd:cd16374    127 KFGDIEELLKE 137
PHD pfam00628
PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar ...
 1700-1745 7.84e-05

PHD-finger; PHD folds into an interleaved type of Zn-finger chelating 2 Zn ions in a similar manner to that of the RING and FYVE domains. Several PHD fingers have been identified as binding modules of methylated histone H3.


Pssm-ID: 425785 [Multi-domain]  Cd Length: 51  Bit Score: 42.09  E-value: 7.84e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2019726493 1700 NDEETEEWWVQCDKCEAWQHQICALFNGRRNDGGQAEYTCPYCYIA 1745
Cdd:pfam00628    6 GKSDDGGELVQCDGCDDWFHLACLGPPLDPAEIPSGEWLCPECKPK 51
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 587-644 8.09e-05

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 44.86  E-value: 8.09e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEREdgsrrttrydidMTKCIYC------G---FCQEACPVDAI 644
Cdd:cd16371     83 QDKCIGCGYCVWACPYGAPQYNPETGK------------MDKCDMCvdrldeGekpACVAACPTRAL 137
PRK09898 PRK09898
ferredoxin-like protein;
587-644 8.27e-05

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 45.98  E-value: 8.27e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEREDgsrrttrydidmTKCIYCGFCQEACPVDAI 644
Cdd:PRK09898   153 HKRCIGCSACTTACPWMMATVNTESKKS------------SKCVLCGECANACPTGAL 198
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 587-615 9.01e-05

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 42.41  E-value: 9.01e-05
                           10        20
                   ....*....|....*....|....*....
gi 2019726493  587 EERCIACKLCEAVCPAQAITIeaEEREDG 615
Cdd:COG1149     40 PDLCTGCGACVGVCPTGAITL--EEREAG 66
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 587-645 1.01e-04

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 45.17  E-value: 1.01e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  587 EERCIACKLCEAVCPAQAITieaeeredGSRRTTRYDIdMTKCIYCGFCQEACPVDAIV 645
Cdd:TIGR01944  112 EDNCIGCTKCIQACPVDAIV--------GAAKAMHTVI-ADECTGCDLCVEPCPTDCIE 161
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 581-644 1.22e-04

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 44.16  E-value: 1.22e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  581 RRYPTGEE-----RCIACKLCEAVCPAQAITIeaeeredGSRRTTRYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:cd10564      1 RPPWAVDEalfldLCTRCGDCVEACPEGIIVR-------GDGGFPELDFSRGECTFCGACAEACPEGAL 62
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 585-649 1.37e-04

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 43.86  E-value: 1.37e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019726493  585 TGEERCIACKLCEAVCpAQAITIEaEEREDGSRRTTRYD--IDMTKCIYCGFCQEACPVDAIVEGPN 649
Cdd:cd16372      5 TDPEKCIGCLQCEEAC-SKTFFKE-EDREKSCIRITETEggYAINVCNQCGECIDVCPTGAITRDAN 69
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 624-645 1.49e-04

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 42.02  E-value: 1.49e-04
                           10        20
                   ....*....|....*....|..
gi 2019726493  624 IDMTKCIYCGFCQEACPVDAIV 645
Cdd:COG1149      8 IDEEKCIGCGLCVEVCPEGAIK 29
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 590-644 2.80e-04

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 42.71  E-value: 2.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2019726493  590 CIACKLCEAVCPAQAItIEAEEREDGSrrttrydidmtKCIYCGFCQEACPVDAI 644
Cdd:cd16372     79 CVGCLMCVGFCPEGAM-FKHEDYPEPF-----------KCIACGICVKACPTGAL 121
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 587-645 2.81e-04

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 42.32  E-value: 2.81e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEredgsrrttrYDI-DMTKCIYCGFCQEACPVDAIV 645
Cdd:PRK09624    50 RDKCVRCYLCYIYCPEPAIYLDEEG----------YPVfDYDYCKGCGICANECPTKAIE 99
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
587-622 2.89e-04

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 41.25  E-value: 2.89e-04
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEREDGSRRTTRY 622
Cdd:COG2768     39 PEKCIGCGACIEVCPVGAIKIEWEEDEEFQEKMAEY 74
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 590-645 3.14e-04

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 42.71  E-value: 3.14e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  590 CIACKLCEAVCPAQAITieaeeredgsrRTTR--YDIDMTKCIYCGFCQEACPVDAIV 645
Cdd:cd16372     49 CNQCGECIDVCPTGAIT-----------RDANgvVMINKKLCVGCLMCVGFCPEGAMF 95
CooF_like cd10563
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ...
 579-645 3.25e-04

CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.


Pssm-ID: 319885 [Multi-domain]  Cd Length: 140  Bit Score: 43.01  E-value: 3.25e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2019726493  579 ALRRYP-TG-----EERCIACKLCEAVCPAQAITIEAEEREdgsrrttrydidMTKCIYCGF-----CQEACPVDAIV 645
Cdd:cd10563     73 AMHKDPeTGivihdEEKCVGCWMCVMVCPYGAIRPDKERKV------------ALKCDLCPDretpaCVEACPTGALV 138
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 587-613 4.34e-04

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 40.80  E-value: 4.34e-04
                           10        20
                   ....*....|....*....|....*..
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEERE 613
Cdd:COG4231     50 PDLCIGCGSCVQVCPVDAIKLEKRVPE 76
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 587-606 4.57e-04

4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 39.15  E-value: 4.57e-04
                           10        20
                   ....*....|....*....|
gi 2019726493  587 EERCIACKLCEAVCPAQAIT 606
Cdd:pfam00037    5 EEKCIGCGACVEVCPVGAIT 24
NapF COG1145
Ferredoxin [Energy production and conversion];
587-613 5.01e-04

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 44.33  E-value: 5.01e-04
                           10        20
                   ....*....|....*....|....*..
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEERE 613
Cdd:COG1145    212 PDKCIGCGACVKVCPVGAISLEPKEIE 238
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 591-644 5.33e-04

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 42.63  E-value: 5.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  591 IACKLCE-----AVCPAQAITieaeeREDGSRRttrydIDMTKCIYCGFCQEACPVDAI 644
Cdd:cd10554     54 VQCRQCEdapcaNVCPVGAIS-----QEDGVVQ-----VDEERCIGCKLCVLACPFGAI 102
ZZ_Mind_bomb cd02339
Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. ...
 2200-2233 5.56e-04

Zinc finger, ZZ type. Zinc finger present in Drosophila Mind bomb (D-mib) and related proteins. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Mind bomb is an E3 ubiqitin ligase that has been shown to regulate signaling by the Notch ligand Delta in Drosophila melanogaster.


Pssm-ID: 239079  Cd Length: 45  Bit Score: 39.75  E-value: 5.56e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 2019726493 2200 TTCNACHLDIETGQGWRCEVCPDYDVCDSCYRRD 2233
Cdd:cd02339      1 IICDTCRKQGIIGIRWKCAECPNYDLCTTCYHGD 34
PHD_ARID4_like cd15615
PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 ...
 1696-1742 8.60e-04

PHD finger found in Arabidopsis thaliana AT-rich interactive domain-containing protein 4 (ARID4) and similar proteins; This family includes A. thaliana ARID4 (ARID domain-containing protein 4) and similar proteins. Their biological roles remain unclear, but they all contain an AT-rich interactive domain (ARID) and a plant homeodomain (PHD) finger at the C-terminus. ARID is a helix-turn-helix motif-based DNA-binding domain conserved in all eukaryotes. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins.


Pssm-ID: 277087  Cd Length: 57  Bit Score: 39.39  E-value: 8.60e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2019726493 1696 EKKKNDEETEEWWVQCDKCEAWQHQIC------ALFNGRRNDGgqAEYTCPYC 1742
Cdd:cd15615      7 QVYEENEGDEKEWVQCDSCSEWVHFECdgrtglGAFKYAKSDG--LQYVCPRC 57
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
587-646 8.84e-04

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 44.16  E-value: 8.84e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2019726493  587 EERCIACKLCEAVC---PAQAITIEaeerEDGSRRttrYDIDMTKCIYCGFCQEACPVDAIVE 646
Cdd:PRK08318   341 QDKCIGCGRCYIACedtSHQAIEWD----EDGTRT---PEVIEEECVGCNLCAHVCPVEGCIT 396
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 587-644 9.52e-04

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 39.19  E-value: 9.52e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2019726493  587 EERCIACKLCEAVCPA---QAITIEAEeredgsrrtTRYDIDMTKCIYCGFCQEACPV-DAI 644
Cdd:pfam14697    5 EDTCIGCGKCYIACPDtshQAIVGDGK---------RHHTVIEDECTGCNLCVSVCPVdDCI 57
ZnF_ZZ smart00291
Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain ...
 2076-2110 9.82e-04

Zinc-binding domain, present in Dystrophin, CREB-binding protein; Putative zinc-binding domain present in dystrophin-like proteins, and CREB-binding protein/p300 homologues. The ZZ in dystrophin appears to bind calmodulin. A missense mutation of one of the conserved cysteines in dystrophin results in a patient with Duchenne muscular dystrophy.


Pssm-ID: 197633 [Multi-domain]  Cd Length: 44  Bit Score: 38.96  E-value: 9.82e-04
                            10        20        30
                    ....*....|....*....|....*....|....*
gi 2019726493  2076 VHLQPSCTHCCMLMVsGNRWRCSQCKHFQICDKCY 2110
Cdd:smart00291    1 VHHSYSCDTCGKPIV-GVRYHCLVCPDYDLCQSCF 34
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 623-664 1.34e-03

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 40.84  E-value: 1.34e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2019726493  623 DIDMTKCIYCGFCQEACPVDAIVEGPNfeFATETHEELLYDK 664
Cdd:cd10549      2 KYDPEKCIGCGICVKACPTDAIELGPN--GAIARGPEIDEDK 41
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 590-640 1.50e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 41.60  E-value: 1.50e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2019726493  590 CIACKL--CEAVCPAQAITIEaeerEDGSRRTTrydiDMTKCIYCGFCQEACP 640
Cdd:cd16369     51 CMHCEDptCAEVCPADAIKVT----EDGVVQSA----LKPRCIGCSNCVNACP 95
PRK06991 PRK06991
electron transport complex subunit RsxB;
575-648 1.63e-03

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 42.86  E-value: 1.63e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2019726493  575 RGEHALRRYPTGEERCIAcKLCEAV-CPAqaITIEAEEREDGSRRTTRydIDMTKCIYCGFCQEACPVDAIVEGP 648
Cdd:PRK06991    37 AGEANYNRCPPGGAEGIA-RLAALLgKPV--IPLDPANGVERPRAVAV--IDEQLCIGCTLCMQACPVDAIVGAP 106
oorD PRK09626
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
 587-658 1.70e-03

2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed


Pssm-ID: 236597 [Multi-domain]  Cd Length: 103  Bit Score: 40.09  E-value: 1.70e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEeredgSRRTTRYDIDMT---KCIYCGFCQEACPVDAI--VEGPNFEFATETHE 658
Cdd:PRK09626    15 ESRCKACDICVSVCPAGVLAMRID-----PHAVLGKMIKVVhpeSCIGCRECELHCPDFAIyvADRKEFKFAKLSKE 86
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 587-608 1.72e-03

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 40.84  E-value: 1.72e-03
                           10        20
                   ....*....|....*....|..
gi 2019726493  587 EERCIACKLCEAVCPAQAITIE 608
Cdd:cd10549    107 KEKCIGCGICAEVCPVNAIKLV 128
FDH_b_like cd10562
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ...
 596-644 1.73e-03

uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.


Pssm-ID: 319884 [Multi-domain]  Cd Length: 161  Bit Score: 41.52  E-value: 1.73e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2019726493  596 CEAVCPAQAITIEaeerEDGSrrttrYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:cd10562     78 CVKVCPTGALYKT----ENGA-----VVVDEDKCIGCGYCVAACPFDVP 117
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 624-650 1.81e-03

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 41.32  E-value: 1.81e-03
                           10        20
                   ....*....|....*....|....*..
gi 2019726493  624 IDMTKCIYCGFCQEACPVDAIVEGPNF 650
Cdd:TIGR01944  110 IDEDNCIGCTKCIQACPVDAIVGAAKA 136
PHD_SF cd15489
PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) ...
 1699-1742 2.09e-03

PHD finger superfamily; The PHD finger superfamily includes a canonical plant homeodomain (PHD) finger typically characterized as Cys4HisCys3, and a non-canonical extended PHD finger, characterized as Cys2HisCys5HisCys2His. Variations include the RAG2 PHD finger characterized by Cys3His2Cys2His and the PHD finger 5 found in nuclear receptor-binding SET domain-containing proteins characterized by Cys4HisCys2His. The PHD finger is also termed LAP (leukemia-associated protein) motif or TTC (trithorax consensus) domain. Single or multiple copies of PHD fingers have been found in a variety of eukaryotic proteins involved in the control of gene transcription and chromatin dynamics. PHD fingers can recognize the unmodified and modified histone H3 tail, and some have been found to interact with non-histone proteins. They also function as epigenome readers controlling gene expression through molecular recruitment of multi-protein complexes of chromatin regulators and transcription factors. The PHD finger domain SF is structurally similar to the RING and FYVE_like superfamilies.


Pssm-ID: 276966 [Multi-domain]  Cd Length: 48  Bit Score: 38.07  E-value: 2.09e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2019726493 1699 KNDEETEEWWVQCDKCEAWQHQICALFNGRRNDGGQaEYTCPYC 1742
Cdd:cd15489      6 GKGGDLGGELLQCDGCGKWFHADCLGPPLSSFVPNG-KWICPVC 48
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 593-652 2.68e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 40.70  E-value: 2.68e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  593 CKLCEAVCPAQAITIEAEERED---GsrrTTRYDIDmtKCI-Y-----CGFCQEACPVDAIVEGPNFEF 652
Cdd:cd16373     59 CDACVEVCPTGALRPLDLEEQKvkmG---VAVIDKD--RCLaWqggtdCGVCVEACPTEAIAIVLEDDV 122
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 574-649 2.81e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 40.37  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  574 FRGEHALRRyptGEERCIACKLCEAVCpaqaitieaEEREDGS----RRTTRYD-IDM-TKCIYC--GFCQEACPVDAIV 645
Cdd:cd16367      8 IQGTNLLVI---DLDRCIRCDNCEKAC---------ADTHDGHsrldRNGLRFGnLLVpTACRHCvdPVCMIGCPTGAIH 75


                   ....
gi 2019726493  646 EGPN 649
Cdd:cd16367     76 RDDG 79
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 619-644 2.83e-03

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 38.49  E-value: 2.83e-03
                           10        20
                   ....*....|....*....|....*.
gi 2019726493  619 TTRYDIDMTKCIYCGFCQEACPVDAI 644
Cdd:COG2221      7 TWPPKIDEEKCIGCGLCVAVCPTGAI 32
PHD_MLL5 cd15550
PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that ...
 1701-1722 3.16e-03

PHD finger found in mixed lineage leukemia 5 (MLL5); MLL5 is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. It contains a single plant homeodomain (PHD) finger followed by a catalytic SET domain. MLL5 can be recruited to E2F1-responsive promoters to stimulate H3K4 trimethylation and transcriptional activation by binding to the cell cycle regulator host cell factor (HCF-1), thereby facilitating the cell cycle G1 to S phase transition. It is also involved in mitotic fidelity and genomic integrity by modulating the stability of the chromosomal passenger complex (CPC) via the interaction with Borealin. Moreover, MLL5 is a component of a complex associated with retinoic acid receptor that requires GlcN Acylation of its SET domain in order to activate its histone lysine methyltransferase activity. It also participates in the camptothecin (CPT)-induced p53 activation. Furthermore, MLL5 indirectly regulates H3K4 methylation, represses cyclin A2 (CycA) expression, and promotes myogenic differentiation.


Pssm-ID: 277025 [Multi-domain]  Cd Length: 44  Bit Score: 37.30  E-value: 3.16e-03
                           10        20
                   ....*....|....*....|..
gi 2019726493 1701 DEETEEWWVQCDKCEAWQHQIC 1722
Cdd:cd15550      6 FEHDDGFMICCDKCSVWQHGDC 27
PRK00783 PRK00783
DNA-directed RNA polymerase subunit D; Provisional
 575-656 3.82e-03

DNA-directed RNA polymerase subunit D; Provisional


Pssm-ID: 234837 [Multi-domain]  Cd Length: 263  Bit Score: 41.41  E-value: 3.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  575 RG-EHA---------LRRYP--TGEERCIACKLCEAVCPAQAITIEAEEREDGsrrttrydiDMTKCIYCGFCQEACPVD 642
Cdd:PRK00783   144 RGkEHAkwqpgsacgYKYYPriEVSEDCDECEKCVEACPRGVLELKEGKLVVT---------DLLNCSLCKLCERACPGK 214

                           90
                   ....*....|....*..
gi 2019726493  643 AIVEG--PN-FEFATET 656
Cdd:PRK00783   215 AIRVSddENkFIFTVES 231
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 590-681 4.07e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 42.30  E-value: 4.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  590 CIACKLCEAVCPAQAIT-------------IEAEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVDAIVEGPnfefATET 656
Cdd:PRK06259   135 CIECLSCVSTCPARKVSdypgptfmrqlarFAFDPRDEGDREKEAFDEGLYNCTTCGKCVEVCPKEIDIPGK----AIEK 210

                           90       100
                   ....*....|....*....|....*
gi 2019726493  657 HEELLYDKEKLLENgdrwETEIAEN 681
Cdd:PRK06259   211 LRALAFKKGLGLPA----HLEVREN 231
PRK09898 PRK09898
ferredoxin-like protein;
588-640 4.35e-03

ferredoxin-like protein;


Pssm-ID: 182135 [Multi-domain]  Cd Length: 208  Bit Score: 40.97  E-value: 4.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2019726493  588 ERCIACK--LCEAVCPAQAITIEAEEredGSrrttrYDIDMTKCIYCGFCQEACP 640
Cdd:PRK09898   121 DTCRQCKepQCMNVCPIGAITWQQKE---GC-----ITVDHKRCIGCSACTTACP 167
ZZ_dystrophin cd02334
Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif ...
 2202-2246 5.06e-03

Zinc finger, ZZ type. Zinc finger present in dystrophin and dystrobrevin. The ZZ motif coordinates two zinc ions and most likely participates in ligand binding or molecular scaffolding. Dystrophin attaches actin filaments to an integral membrane glycoprotein complex in muscle cells. The ZZ domain in dystrophin has been shown to be essential for binding to the membrane protein beta-dystroglycan.


Pssm-ID: 239074  Cd Length: 49  Bit Score: 36.95  E-value: 5.06e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2019726493 2202 CNACHLDIETGQGWRCEVCPDYDVCDSCYRRdGGVNHPHKLtNHP 2246
Cdd:cd02334      3 CNICKEFPITGFRYRCLKCFNYDLCQSCFFS-GRTSKSHKN-SHP 45
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 588-611 5.38e-03

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 38.11  E-value: 5.38e-03
                           10        20
                   ....*....|....*....|....
gi 2019726493  588 ERCIACKLCEAVCPAQAITIEAEE 611
Cdd:COG1144     60 DYCKGCGICAEVCPVKAIEMVPEE 83
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 587-651 5.55e-03

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 41.13  E-value: 5.55e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEREDgSRRTTRYDIDMTKCIYC-GFCQEACPVDAIVEGPNFE 651
Cdd:COG2878    166 EDKCTGCGLCVEACPVDCIEMVPVSPTV-VVSSWDKGKAVRKVVGCiGLCCKKCCPAAAITVNNLA 230
FDH_beta_like cd16366
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ...
 579-647 5.63e-03

beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.


Pssm-ID: 319888 [Multi-domain]  Cd Length: 156  Bit Score: 39.69  E-value: 5.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  579 ALRRYPTG-----EERCIACKLCEAVCPAQAITIEAEeredgsrrttryDIDMTKCIYC------GF---CQEACPVDAI 644
Cdd:cd16366     86 AIIRTETGtvvvdPETCIGCGYCVNACPFDIPRFDEE------------TGRVAKCTLCydrisnGLqpaCVKTCPTGAL 153


                   ...
gi 2019726493  645 VEG 647
Cdd:cd16366    154 TFG 156
HybA_like cd10561
the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 ...
 578-674 5.68e-03

the FeS subunit of hydrogenase 2; This subfamily includes the beta-subunit of hydrogenase 2 (Hyd-2), an enzyme that catalyzes the reversible oxidation of H2 to protons and electrons. Hyd-2 is membrane-associated and forms an unusual heterotetrameric [NiFe]-hydrogenase in that it lacks the typical cytochrome b membrane anchor subunit that transfers electrons to the quinone pool. The electron transfer subunit of Hyd-2 (HybA) which is predicted to contain four iron-sulfur clusters, is essential for electron transfer from Hyd-2 to menaquinone/demethylmenaquinone (MQ/DMQ) to couple hydrogen oxidation to fumarate reduction.


Pssm-ID: 319883 [Multi-domain]  Cd Length: 196  Bit Score: 40.27  E-value: 5.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  578 HALRRYPTG-----EERCIACKLCEAVCPAQAITIEaeeredgsrrttrYDI---DMTKCIYCgF----------CQEAC 639
Cdd:cd10561     84 GALRKTPEGpvtydEDKCIGCRYCMVACPFNIPKYE-------------WDSanpKIRKCTMC-YdrlkegkqpaCVEAC 149

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2019726493  640 PVDAIVEGPnfefatetHEELLYD-KEKLLENGDRW 674
Cdd:cd10561    150 PTGALLFGK--------REELLAEaKRRIAANPGRY 177
QueG COG1600
Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and ...
 587-669 6.78e-03

Epoxyqueuosine reductase QueG (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; Epoxyqueuosine reductase QueG (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 441208 [Multi-domain]  Cd Length: 345  Bit Score: 41.34  E-value: 6.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2019726493  587 EERCIACKLCEAVCPAQAI---------------TIE------AEEREdgsrrttrydiDMTKCIY-CGFCQEACPVdai 644
Cdd:COG1600    183 EDHCGSCTRCLDACPTGAIvapyvldarrcisylTIElkgpipEELRP-----------KMGNRIYgCDDCQDVCPW--- 248

                           90       100
                   ....*....|....*....|....*
gi 2019726493  645 vegpNfEFATETHEELLYDKEKLLE 669
Cdd:COG1600    249 ----N-RFAQPTREPDFQPRPELAA 268
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 587-644 7.06e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 41.66  E-value: 7.06e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2019726493  587 EERCIACKLCEAVCPAQAITIEAEEREDGSRRTTRYdidmtKCIYCG------FCQEACPVDAI 644
Cdd:PRK12769    84 QQKCIGCKSCVVACPFGTMQIVLTPVAAGKVKATAH-----KCDLCAgrengpACVENCPADAL 142
Fer4_17 pfam13534
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 589-642 9.68e-03

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 433287 [Multi-domain]  Cd Length: 61  Bit Score: 36.67  E-value: 9.68e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2019726493  589 RCIACKLCEAVCP-AQAITIE----AEEREDGSRRTTRYDIDMTKCIYCGFCQEACPVD 642
Cdd:pfam13534    1 RCIQCGCCVDECPrYLLNGDEpkklMRAAYLGDLEELQANKVANLCSECGLCEYACPMG 59
 
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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