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Database: UniProt
Entry: A0A0N4ZFY1_PARTI
LinkDB: A0A0N4ZFY1_PARTI
Original site: A0A0N4ZFY1_PARTI 
ID   A0A0N4ZFY1_PARTI        Unreviewed;       779 AA.
AC   A0A0N4ZFY1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DnaJ homolog subfamily C member 10 {ECO:0000256|ARBA:ARBA00020920};
DE   AltName: Full=DnaJ homolog subfamily C member 16 {ECO:0000256|ARBA:ARBA00020921};
DE   AltName: Full=Endoplasmic reticulum DNA J domain-containing protein 8 {ECO:0000256|ARBA:ARBA00035043};
OS   Parastrongyloides trichosuri (Possum-specific nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Parastrongyloides.
OX   NCBI_TaxID=131310 {ECO:0000313|Proteomes:UP000038045, ECO:0000313|WBParaSite:PTRK_0000665900.1};
RN   [1] {ECO:0000313|WBParaSite:PTRK_0000665900.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: Plays an important role in regulating the size of
CC       autophagosomes during the formation process.
CC       {ECO:0000256|ARBA:ARBA00035002}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein
CC       {ECO:0000256|ARBA:ARBA00004163}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein
CC       {ECO:0000256|ARBA:ARBA00004211}.
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DR   AlphaFoldDB; A0A0N4ZFY1; -.
DR   STRING; 131310.A0A0N4ZFY1; -.
DR   WBParaSite; PTRK_0000665900.1; PTRK_0000665900.1; PTRK_0000665900.
DR   Proteomes; UP000038045; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   CDD; cd06257; DnaJ; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 6.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   PANTHER; PTHR44340; DNAJ HOMOLOG SUBFAMILY C MEMBER 10; 1.
DR   PANTHER; PTHR44340:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 10; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF00085; Thioredoxin; 4.
DR   PRINTS; PR00625; JDOMAIN.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF52833; Thioredoxin-like; 4.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 3.
PE   4: Predicted;
KW   Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          21..86
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          94..220
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          507..643
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   DOMAIN          647..774
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
SQ   SEQUENCE   779 AA;  90332 MW;  4921689A1F811EE4 CRC64;
     MYIKYHLFVL YILFNFILAK DFYDLLGVSK DADDRTIRRA FKKLAIKLHP DKNPNDEDAH
     SNFVKINRAY EVLKDEELRK KYDQYGEEGL SDNFQGGNNY QSYSFYKDKF GIYDDDIEIV
     TLSHSDFQQS VIDSGEIWFI NFYSTFCSHC HDLAPTWREF AKEFENVIRV GAVNCAEGPN
     FCNSQNIRAF PSLVLYPYGI VYNGERTFKK LSDFIMSKLD TEVHKVTFKN YKSLSEEWDN
     YATKPWLIDF CDDNESCLSK DNRKKLSSIL KNMVNVGSVK CVEGDRDLLC KRVKESGVAY
     FPAGKINKES MKELDTFDPK EISNIILKFL PEIKVLSEDE YKELIENKEE SSPYLVYFLN
     GEDDNNNLLI EMKKLPFIFS EIEFRSVNCK NLPDKCDSLY LDDKKNRFIM FKSNGRYEIN
     FGKSNSIHDI SIFIRESLKS DLTVLTPETY QEAIDDEDNI WMIDYFAPWC GPCVRYIPVL
     RNLPNEIGGK SIKVGIINCD THKDICSNAG VQSYPASVIY YNGKDYRQVG YHDLHQVIEF
     FEDSINPVVI ELTSDNIDEI VENREEGNII FVDFFAPWCG PCQQLAPEFR KLARNMLKTY
     QEITFGTINC DEQKNLCQKY GVSSYPTLKL FPAKTSTRSI NYPPNWWRNA DSMMNFIIRY
     IPSEVISIGS EFYELVLRSS KPALVDFFAP WCSHCVQFAP TYDRIAKRLK DKINVFKVDC
     DNNPGVCQAA SIQAYPTLRF YSGTSNGNQQ HAFGVQLQTF DENAIVNWVE QQIPKHDEL
//
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