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Database: UniProt
Entry: F8MMJ3_NEUT8
LinkDB: F8MMJ3_NEUT8
Original site: F8MMJ3_NEUT8 
ID   F8MMJ3_NEUT8            Unreviewed;       700 AA.
AC   F8MMJ3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=J domain-containing protein {ECO:0000259|PROSITE:PS50076};
GN   ORFNames=NEUTE1DRAFT_63175 {ECO:0000313|EMBL:EGO57867.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO57867.1};
RN   [1] {ECO:0000313|EMBL:EGO57867.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO57867.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) 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; GL891304; EGO57867.1; -; Genomic_DNA.
DR   RefSeq; XP_009850949.1; XM_009852647.1.
DR   AlphaFoldDB; F8MMJ3; -.
DR   GeneID; 20828998; -.
DR   KEGG; nte:NEUTE1DRAFT63175; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_63175; -.
DR   HOGENOM; CLU_014210_0_0_1; -.
DR   OrthoDB; 1605at2759; -.
DR   Proteomes; UP000008065; 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; IPR018253; DnaJ_domain_CS.
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; PS00636; DNAJ_1; 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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..227
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          107..179
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   REGION          638..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..700
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   700 AA;  78049 MW;  37FA0E947F1EF133 CRC64;
     MSTDYAYDEE GHLWPFFVFT LTSIVTVPIT YSLIKSSRND PAAALKRIQT DYKHDQSAVV
     DTLRKSEKRK DGSKPWLIAL VIAGWAVMGY MIYLIKTTDA PVQHLWNPYD ILGIAESATE
     KQIKKTYKML SLKFHPDKAR PDASKNETID DLNRRYVEIS KAYQALTDED VRNNFIQFGN
     PDGKQGFSIN IALPKAIVSD GNGKYIVLIY FALFGVLLPY LVGSWWYGTL RRSKEGVLME
     SANRLFKEYQ DNIDEGGVVA ALSSGQEFED LFKGDKADAG LSKIESKVMA SDELPPKEKK
     KLEDVESGPR RKALALLWAY LGRIELGDAT LEKAKFQVAP VAHALNKSFN AIALAYMNTA
     PLLASYFASQ RLIQAIPPKA SPLYQLPHFN SAVVRAVEGD SRVHTTVQAF MDQPDAKRRS
     LVVGKGLLTD AQYKETIAYA KQLPYLRVAK AFFKVTGEKF IIPSSLVTLV VKGRFVPPGS
     EKVPDVTPID LEDIDPAEDD LDAILGRKKT KKVVGKDEKG KPIYEESAES EDVYPPLASS
     PYFARDHSPR WHVFLTDSKQ GRVAVPPFTF VSFDRPIYES DGKTPTFAMQ TMKAQFQAPP
     QAGHYTFVMH VVCDSYVGFD TKMEVTLVVE DASRAAEMKD EEEISEPEED SIAGIMNAAK
     GAPTKQRVVK DEEDSDEESG TDDDEDDDTS DTNTDTEPEN
//
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