ID A0A0D2E417_9EURO Unreviewed; 891 AA.
AC A0A0D2E417;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=PV05_11823 {ECO:0000313|EMBL:KIW50213.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW50213.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW50213.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW50213.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN847323; KIW50213.1; -; Genomic_DNA.
DR RefSeq; XP_013310797.1; XM_013455343.1.
DR AlphaFoldDB; A0A0D2E417; -.
DR STRING; 348802.A0A0D2E417; -.
DR GeneID; 25333731; -.
DR HOGENOM; CLU_007230_0_0_1; -.
DR OrthoDB; 206729at2759; -.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16454; RING-H2_PA-TM-RING; 1.
DR Gene3D; 3.50.30.30; -; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR046450; PA_dom_sf.
DR InterPro; IPR003137; PA_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22765; RING FINGER AND PROTEASE ASSOCIATED DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR22765:SF483; RING FINGER PROTEIN MUG145; 1.
DR Pfam; PF02225; PA; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52025; PA domain; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT TRANSMEM 602..622
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 730..773
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 133..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..869
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..543
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..578
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 648..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..801
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 802..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 842..856
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 96538 MW; 55A625CF4FC021AD CRC64;
MRPLRFLLLL TCFVAVPIAL LFSLFTFSDN AADSFQAGYN RPSRLRALFS FSTPSSLFPP
SAIISLTNDN STFFLARPAA FGPSLPSKGL SGQLWVGKGF GDDALLKEEN IHIVGWELGC
SDVPGWADGA SKRVQNLPQV EQPPRRTRRP RDLSQDGSVG EQNPDGPDAL ADDITDDGTD
DHLHHPLPDS NPATPGQLGE PANVDPSDKK NPTHADIESL QESADVAGKI VMLSRGGCGF
LEKVKWAQRR GGIALIVGDN ERGAQLTIMY AKGDTSNVTI PALFTSYTSA HLLASLVPPE
SGEDEASDKT SKGSDKHANQ KQQDSKPVFT STNTQAREPT IVPAMQGSEG KTKKTWVNNV
LDAIVMNENS PFSHVEDSRR PPSSGNIDWV LLEDWDEEAP AKSSKKAKTA ANVPTMSTST
LKAKSTSTKR LGGDDFVIGV QDWRDTDLVA PKPTTSSTFV PADAKNGKDV QAETASTVKS
SSSPQDTLKG GSITPGSGEY AHERSEQVNR YNRGKGQSKQ QAKQASSPQG QESKGSWFDL
FKSSQPSKDA PKPAASKQEK NEKASTARNH HPLGQQEDEE HPGLWVTLTP TSVSTSPFFD
TLLVLVVSPL VTLTVVYALL LLRSRIRRRR WRAPKSVVER LPVRTYHTMS TASSTTSSQV
ASPNASSPSS PLLISTSQNV SQRSRPRSQT TNAVFSGSTE TVSKARTPPS EKSPAKFTRR
KRYTGRQVEC VVCLEEYVDG ESQVMSLPCG HEFHAECITP WLVTRRRTCP ICKGDVVRSL
ARATSRGGDD ETQEGEQTSD EVQDRVAQST NEEASAAIPI PSLLRGDDGD VEQGQNVDVD
VDAPLLEEED DDDVQGQGVG EASSVWRNIS ASVSRLSGDT LWRQTPADRN R
//