ID T2NG95_PORGN Unreviewed; 272 AA.
AC T2NG95;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Putative iron-sulfur cluster-binding protein {ECO:0000313|EMBL:EOA11921.1};
GN ORFNames=A343_0139 {ECO:0000313|EMBL:EOA11921.1};
OS Porphyromonas gingivalis JCVI SC001.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1195243 {ECO:0000313|EMBL:EOA11921.1};
RN [1] {ECO:0000313|EMBL:EOA11921.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCVI SC001 {ECO:0000313|EMBL:EOA11921.1};
RX PubMed=23564253; DOI=10.1101/gr.150433.112;
RA McLean J.S., Lombardo M.J., Ziegler M.G., Novotny M., Yee-Greenbaum J.,
RA Badger J.H., Tesler G., Nurk S., Lesin V., Brami D., Hall A.P., Edlund A.,
RA Allen L.Z., Durkin S., Reed S., Torriani F., Nealson K.H., Pevzner P.A.,
RA Friedman R., Venter J.C., Lasken R.S.;
RT "Genome of the pathogen Porphyromonas gingivalis recovered from a biofilm
RT in a hospital sink using a high-throughput single-cell genomics platform.";
RL Genome Res. 23:867-877(2013).
RN [2] {ECO:0000313|EMBL:EOA11921.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCVI SC001 {ECO:0000313|EMBL:EOA11921.1};
RA McLean J., Yee-Greenbaum J., Durkin A.S., Lasken R.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOA11921.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; APMB01000002; EOA11921.1; -; Genomic_DNA.
DR AlphaFoldDB; T2NG95; -.
DR PATRIC; fig|1195243.10.peg.1714; -.
DR HOGENOM; CLU_030790_0_0_10; -.
DR Proteomes; UP000016542; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.20; -; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR004453; QueG.
DR InterPro; IPR013542; QueG_DUF1730.
DR NCBIfam; TIGR00276; tRNA epoxyqueuosine(34) reductase QueG; 1.
DR PANTHER; PTHR30002; EPOXYQUEUOSINE REDUCTASE; 1.
DR PANTHER; PTHR30002:SF4; EPOXYQUEUOSINE REDUCTASE; 1.
DR Pfam; PF13484; Fer4_16; 1.
DR Pfam; PF08331; QueG_DUF1730; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 1.
PE 4: Predicted;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Queuosine biosynthesis {ECO:0000256|ARBA:ARBA00022785};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT DOMAIN 127..157
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT REGION 248..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 272 AA; 30623 MW; 5F1FE452E39F6FFA CRC64;
MDYLERNREL RYSPAELLPG TRTVISVALN YYPKIKQPAS APQIAYYAYG KDYHKVVKRL
LDKLLDYIRR EVCPSVSGRS FSDSAPIAER YWACRAGIGW VGRSGMLILP RGGTFFFLGE
LLVDIDLPPD APMPSRCGAC RNCIESCPTG AISEEGMDSR LCVSYLTIEH EGEIPPELVG
KLGNRFYGCD SCQLCCPWNR YAHPSEVEAF VPREALFTFD RDDLVSLDEE KYLHFFAGSP
MKRAGLDGLR RNARALEQGD KKEDEQPTDE DG
//
