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
//