ID A0A421JF04_9ASCO Unreviewed; 982 AA.
AC A0A421JF04;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Peroxisome biogenesis factor 10 {ECO:0000313|EMBL:RLV87896.1};
GN ORFNames=JA9_002378 {ECO:0000313|EMBL:RLV87896.1};
OS Meyerozyma sp. JA9.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=2028340 {ECO:0000313|EMBL:RLV87896.1, ECO:0000313|Proteomes:UP000286412};
RN [1] {ECO:0000313|EMBL:RLV87896.1, ECO:0000313|Proteomes:UP000286412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA9 {ECO:0000313|EMBL:RLV87896.1,
RC ECO:0000313|Proteomes:UP000286412};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Component of the PEX2-PEX10-PEX12 retrotranslocation channel,
CC composed of PEX2, PEX10 and PEX12. {ECO:0000256|ARBA:ARBA00034505}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}. Peroxisome membrane
CC {ECO:0000256|ARBA:ARBA00004585}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004585}.
CC -!- SIMILARITY: Belongs to the pex2/pex10/pex12 family.
CC {ECO:0000256|ARBA:ARBA00008704}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLV87896.1}.
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; NSDU01000007; RLV87896.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A421JF04; -.
DR STRING; 2028340.A0A421JF04; -.
DR Proteomes; UP000286412; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070987; P:error-free translesion synthesis; IEA:UniProt.
DR GO; GO:0016562; P:protein import into peroxisome matrix, receptor recycling; IEA:UniProt.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProt.
DR CDD; cd16527; RING-HC_PEX10; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.1170.60; -; 1.
DR Gene3D; 3.30.1490.100; DNA polymerase, Y-family, little finger domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR006845; Pex_N.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45873; DNA POLYMERASE ETA; 1.
DR PANTHER; PTHR45873:SF1; DNA POLYMERASE ETA; 1.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF04757; Pex2_Pex12; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF100879; Lesion bypass DNA polymerase (Y-family), little finger domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50173; UMUC; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000286412};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 758..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 788..814
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 846..865
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 44..314
FT /note="UmuC"
FT /evidence="ECO:0000259|PROSITE:PS50173"
FT DOMAIN 932..970
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 982 AA; 111112 MW; DC9A4E1C06E12F4E CRC64;
MSILKDVHKS TDLRTVPQPT KFSVSDLQSL SNPSIAYKSP LAVIALVDMN AFFAQVEQIR
LNLSIDDPVV CVQWSTLIAV SYAARKYGIN RMDNVKSARE KCPDVVLAHA AVFKKGNPYW
SYVEGLPNQA EHKVSLDPYR RESRKIIKII KQHCDVVEKA SVDECYLDLG REVHKRLLLE
FPQLRRLGSE LPDIPSQLPE SLYWQGEAVR TESENAELQL RENVSSSQKS PESPPTITDW
DDICVLIGAQ VLYKIRKLIY DELSYTTSGG IARNKFLAKL AAGFNKPDNQ TIIRSASIAN
FLTNFQFNDV SGMGGKAGDN VLARFDTPPG VNLFTHLREN YTLQDIQKEY PQDQQFAQKI
YDIVRGDDKQ PLRLRTDVKS MMSRKNFIPQ RPVKTLYDIF SWLRVYAGDL HNRFIDLDDE
NMNLSMSSVS HKEKGVLVRP KTMSLQVGFL SGARISKQVT LPVFRSLDKL HQVVESTSLK
LMKEMLESSG KIEDTGGTDI KSIKLDDDDK LKLVKVNPIL NCALIVSNFT VTSDSSLIDR
YVGESGAQDA EETIKRMFDA VKEEQASMPP SPKKPKTAKV AKVDNEYITK LFSDYRRKSE
NAPKREKKPS PKPDIFARLN SQAKKSTLSI EDGYCTQCGC QVEDETEHRD YHYALAYVHA
APKIHSQPRF PSITNTVRAH QKDAYFESSF RTKIQDVIHV LKGQRFVHTH PEEITVAAKS
LYLALTTLLG ARTLGEEYVD LMYVNRSGKR LPHMLPKIGF IVSYALLPYV VSRLVQRWRA
GKAGDERWYF SAFLSSYTKI LDVVMNLHIA VFYFSGEYYS LSKRIFGMRY VFGHNKDPKK
LKQATGSYGL LGAVILLQFA VKALLNVRTH LTPKNKPENE SNAQSDTHIT NIGQLEKIGT
AVNNNDAVYK ATNIDLSDPT HLAYIPDNAR ACMLCLSPMT NPAAANCGHF FCWVCIVDWI
RDHPECPLCR QHCDEQNLLP LR
//
