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Database: UniProt
Entry: E8QX76_ISOPI
LinkDB: E8QX76_ISOPI
Original site: E8QX76_ISOPI 
ID   E8QX76_ISOPI            Unreviewed;       711 AA.
AC   E8QX76;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=Redoxin domain protein {ECO:0000313|EMBL:ADV60909.1};
GN   OrderedLocusNames=Isop_0314 {ECO:0000313|EMBL:ADV60909.1};
OS   Isosphaera pallida (strain ATCC 43644 / DSM 9630 / IS1B).
OC   Bacteria; Planctomycetota; Planctomycetia; Isosphaerales; Isosphaeraceae;
OC   Isosphaera.
OX   NCBI_TaxID=575540 {ECO:0000313|EMBL:ADV60909.1, ECO:0000313|Proteomes:UP000008631};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 43644;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Eisen J.A.;
RT   "The complete sequence of chromosome of Isophaera pallida ATCC 43644.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADV60909.1, ECO:0000313|Proteomes:UP000008631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43644 / DSM 9630 / IS1B
RC   {ECO:0000313|Proteomes:UP000008631};
RX   PubMed=21475588; DOI=10.4056/sigs.1533840;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Goker M., Cleland D., Saunders E., Lapidus A., Nolan M., Lucas S.,
RA   Hammon N., Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L.,
RA   Pitluck S., Liolios K., Pagani I., Ivanova N., Mavromatis K., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Detter J.C., Beck B., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Isosphaera pallida type strain (IS1B).";
RL   Stand. Genomic Sci. 4:63-71(2011).
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DR   EMBL; CP002353; ADV60909.1; -; Genomic_DNA.
DR   AlphaFoldDB; E8QX76; -.
DR   STRING; 575540.Isop_0314; -.
DR   KEGG; ipa:Isop_0314; -.
DR   eggNOG; COG0526; Bacteria.
DR   HOGENOM; CLU_020308_0_0_0; -.
DR   InParanoid; E8QX76; -.
DR   OMA; EMPRTHI; -.
DR   Proteomes; UP000008631; Chromosome.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0016715; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen; IEA:InterPro.
DR   Gene3D; 2.60.120.230; -; 1.
DR   Gene3D; 2.60.120.310; Copper type II, ascorbate-dependent monooxygenase, N-terminal domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   InterPro; IPR014784; Cu2_ascorb_mOase-like_C.
DR   InterPro; IPR036939; Cu2_ascorb_mOase_N_sf.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR008977; PHM/PNGase_F_dom_sf.
DR   InterPro; IPR047262; PRX-like1.
DR   InterPro; IPR013740; Redoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR43640; OS07G0260300 PROTEIN; 1.
DR   PANTHER; PTHR43640:SF1; THIOREDOXIN-DEPENDENT PEROXIREDOXIN; 1.
DR   Pfam; PF08534; Redoxin; 1.
DR   SUPFAM; SSF49742; PHM/PNGase F; 2.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS51007; CYTC; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Heme {ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PROSITE-ProRule:PRU00433};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00433}; Reference proteome {ECO:0000313|Proteomes:UP000008631};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           40..711
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003229845"
FT   DOMAIN          58..187
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          271..362
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   REGION          659..678
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..711
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        694..711
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   711 AA;  78912 MW;  C1B5EEC2F7128365 CRC64;
     MIGRICRCRV TPRWSRSLPV SAGRIGLALA LATSAFLQAA EPPAQDAHAN LLTALDRGVG
     QPLSMNFKLI GLDDKPISFR QFIGKKAVVI VFIGTDCPIG NLYMPTLVEL AKEYEPRGIQ
     FVLVNSNQSE TLDDMRKHAE EYGLNGVPGL LVAKDPGNEL ADLALAERTN EAILIDATLD
     FLNKLARIRY RGMIDDQYHY NARRDQPKRT PLKDALEDFL AGREVRVAGT EVQGCLIERG
     APKVLVDRQG AMVRTMPEEI RAEFAKARAM EPIAVGPVTY HKDVAPIVQA KCQTCHRPNQ
     VAPFSLLTYE QAKRWKGMIR EVVDDGRMPP WHANPNYGAF ANDRSLTPLE RAILLAWVDQ
     DAPEGNPADS PAPRTFAEGW TIGKPDLIIE MPRTHIVPAG GVVDYVRYPV DFEVKEDLWI
     QAIEARPGDP AVVHHIILYY VLPGDPAPRY LVGYAPGDLS ETFPEGTAKR LPKGSRFFFE
     MHYTPIGKVR QDKSSVGIVL AKTPPTRETI TRPIASRELE QRLISIPPGH PNYPITSAIE
     FKTDVELIGM MPHMHLRGKD FRYILTDPQG KETILLDVPA YDFAWQNFYW TKQPIPIPAG
     SRIDCVAHFD NSEDNPYNPD PSASVTWGDQ TYEEMMIGFI EYTVPLDIQG SWTQHAKRVT
     PKLVPGQDPL PEARPSTGAA GLLNRLLGGL NPATTPKTAP TTTPTRSDPG Q
//
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