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Database: UniProt
Entry: A0A109FN40_9BASI
LinkDB: A0A109FN40_9BASI
Original site: A0A109FN40_9BASI 
ID   A0A109FN40_9BASI        Unreviewed;       665 AA.
AC   A0A109FN40;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=DnaJ-domain-containing protein {ECO:0000313|EMBL:KWU47394.1};
GN   ORFNames=RHOSPDRAFT_30816 {ECO:0000313|EMBL:KWU47394.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU47394.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU47394.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU47394.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KQ954464; KWU47394.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109FN40; -.
DR   STRING; 1305733.A0A109FN40; -.
DR   OrthoDB; 1605at2759; -.
DR   Proteomes; UP000062823; Unassembled WGS sequence.
DR   GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR004179; Sec63-dom.
DR   PANTHER; PTHR24075; SEC63 DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR24075:SF0; TRANSLOCATION PROTEIN SEC63 HOMOLOG; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF02889; Sec63; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00973; Sec63; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   4: Predicted;
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        68..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        196..218
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          100..170
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   REGION          476..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          591..665
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        604..618
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..665
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   665 AA;  72992 MW;  2FA9A17D10C4A77C CRC64;
     MAGSYTYDTS GQVYFFILTG LLVFLLPYTY ATLFGGAERA AARVKAPCAG WNRKSAEVKR
     TSNANRLFSV RHIVLAVGWL AFAVVVQRAR GIEGEGPQFD PFAILGVSSS STEKQIKKHY
     RKLSLKFHPD KVSYSDDAAK EEADSHFVEL TKAYKALTDE VSRRNYELYG HPDGKQEFSA
     GIALPAWIVE GKNSPLVIGA YALLLGVVLP VLVGRWWYGT RKLTKDGVLN STAAKYFHAL
     KEETTFPQML DILASSDEFA VDPALVKLRK SHSKAAIDEY ARLVSTVREG VDGKQGWEGY
     ATWSPAKKRA RVLIVAHLLR LPIQDVGLLK EKHLTASIAL PLCSGLSSIS LAHNWLSTYI
     AIVHLQQFLL QAVHPSSPQL LQLPHITPEL AVQIEEKTSV STVKQFGELK AGEVDKVLDG
     FPESEKRDAY EVAKHWPIIQ FVDAKFQVTG EKIVTPGAIV SFTLKLRLAP PGQAPQATAA
     ADSLHDAGNA EGEEKSVEEL IGRSKADEGV VPTPLAHAPH FPKNRKPAWY IFVGDHKLNR
     VFVAPHRFTD IGEGTTRTVR MTFQAPPGPG LYTFQVYVMC DSFVGADAQK DMRMQVEPPK
     EGDDGVSDVE DDISEPDEDS LAGQMALMKG QPVRRHGDSD EEGSDDESET ESESDSSSDS
     DSDSD
//
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