ID A0A0J6YF31_COCIT Unreviewed; 723 AA.
AC A0A0J6YF31;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Disulfide-isomerase A6 {ECO:0000313|EMBL:KMP06295.1};
GN ORFNames=CIRG_05976 {ECO:0000313|EMBL:KMP06295.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP06295.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004389}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004389}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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; DS028096; KMP06295.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6YF31; -.
DR STRING; 404692.A0A0J6YF31; -.
DR Proteomes; UP000054565; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR CDD; cd02961; PDI_a_family; 2.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR46426; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR PANTHER; PTHR46426:SF1; PROTEIN DISULFIDE-ISOMERASE TMX3; 1.
DR Pfam; PF00085; Thioredoxin; 3.
DR SUPFAM; SSF52833; Thioredoxin-like; 3.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 2.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:KMP06295.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..723
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005284920"
FT TRANSMEM 658..679
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 10..180
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT DOMAIN 237..465
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 185..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 723 AA; 81695 MW; E2A6D4019F0241B1 CRC64;
MKASFLAFSL LAAVFQPVFA ASHGQEKRAD AKLENDASDR TTIFNDVRVP PMKEVNAAGF
DETIKDGYWF VKFYSPYCHF CKAVRPAWQT LYEFYYTSNP LKSSTSKQVP NPESSLNSFQ
GYYDFHFAEM DCVVNGDKCQ ELEVKEWPTF ALYHDGKLVE KYDGGRNMEG LSRFVEKWLE
SIKPGSRPRG EMKLPEPGAK IAPEQPKDQE GAIIGEPDIN AGSSTPAASQ KSDDSVKPAA
PALPERKQPA PNPQGMSVPL TAESFQKLVT TTRDPWFVKF YAPWCVHCQA LAPIWSQMAK
DLKGKLNIGE VNCEVEKRLC KDARVNVYPT MYFFRGGERV EYEGLRGLGD LVNYARKAVD
VVGSGVQYVD ATAFKKMEET EEVIFLYFFD HATTSEDFAA LDRLTLSLVG RARLVKTNST
ILAERFKIST WPRLLVSRDG RPSYYTALAP KDMRDFRQVL AWMQKVWLPI VPEMTASNAK
EIMERKYVVL GILNRQRSDE FIQDKRELKN AALEWMEKQT KLFQLERQEL RDAKELRIEE
ADDRDDQRAL RAAKNTRITI KEDDKKQVAF AWVDGIFWDR WIRTTYGIDV RNGERVIIND
EENRRYWDTT PNGGFIVPSR TSILETITHV VSNPSKLKSK STVGTFEGLF FSIRTFTFAH
PIITFLLFVA VLFVSSFIAR GKLRRGRSAG GLLGSVGGSS GGFFHLDGKE GLLGGGSGGG
KVD
//