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
//