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Database: UniProt
Entry: A0A0D2ABC4_9PEZI
LinkDB: A0A0D2ABC4_9PEZI
Original site: A0A0D2ABC4_9PEZI 
ID   A0A0D2ABC4_9PEZI        Unreviewed;       855 AA.
AC   A0A0D2ABC4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN   ORFNames=PV09_04910 {ECO:0000313|EMBL:KIW04093.1};
OS   Verruconis gallopava.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Venturiales; Sympoventuriaceae; Verruconis.
OX   NCBI_TaxID=253628 {ECO:0000313|EMBL:KIW04093.1, ECO:0000313|Proteomes:UP000053259};
RN   [1] {ECO:0000313|EMBL:KIW04093.1, ECO:0000313|Proteomes:UP000053259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 43764 {ECO:0000313|EMBL:KIW04093.1,
RC   ECO:0000313|Proteomes:UP000053259};
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 Ochroconis gallopava CBS43764.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN847542; KIW04093.1; -; Genomic_DNA.
DR   RefSeq; XP_016213962.1; XM_016358344.1.
DR   AlphaFoldDB; A0A0D2ABC4; -.
DR   STRING; 253628.A0A0D2ABC4; -.
DR   GeneID; 27312883; -.
DR   VEuPathDB; FungiDB:PV09_04910; -.
DR   HOGENOM; CLU_007230_0_0_1; -.
DR   InParanoid; A0A0D2ABC4; -.
DR   OrthoDB; 206729at2759; -.
DR   Proteomes; UP000053259; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd04813; PA_1; 1.
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; IPR011016; Znf_RING-CH.
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   SMART; SM00744; RINGv; 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:UP000053259};
KW   Signal {ECO:0000256|SAM:SignalP};
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   SIGNAL          1..31
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           32..855
FT                   /note="RING-type domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002238285"
FT   TRANSMEM        578..598
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          712..755
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          144..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..506
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          628..693
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..855
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..174
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        325..352
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..506
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..686
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        813..830
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   855 AA;  93316 MW;  EF7FB90999BEEEBE CRC64;
     MRPTRLLLTL TTSLVLLTIL LYLIPNRSSR ATPPPLTSSK RKSGLRALFS FHTPLFPPSA
     IISLTDDNST FFLARPAAFG PKLPSSGLSG QLWIGSGFGE DNLGSGGRAE GELGCSDVPG
     WDESMGKPSG RVINEGDEDV KYASHKGNVN KKTAKNTKRG EAEGEDTDVA IPKPEDDDGT
     DEHLFHAPDL SAIKDAANKG REKEHADIQS LQESAEIAGK VVLLSRGGCG FLEKVKWVQR
     RGGKALIVGD DIRGGPLVTM YARGDTSNIT VPALFTSYTT AHLLSSLIPS GGLFGASPVD
     GNKVGLGKIT AKLNEAKDKE AQSDDQPIFT TSTEVSKPTD EPLASQGKSS VSNIKHEEPK
     SQHGWLRRFI LWIVGMSDNH DVSRRPPGSG SIDWVMVQDF DEKPKKSSKE TKSPQGSQGS
     QDGHDGFVIG VHDWRDPDMV PARSSNDVGA RQTNDEKGPD SGANQLKGGI VTPGSGEYEK
     PKVVDSAQSK DKTKAKSDAN SKEHDSWLSH LPWTHGDEYF DEGAQKAAPC AGGKCKAKPH
     SASKADSKAL NDGLPKHEGL WVTLTPTNMS SSPFFDTLLV LVVSPLVTLT IVYALLLLRS
     RIRRRRWRAP KSVVDRLPVR TYHTIASEAS TTSLATPNAS SPTTPLLQPA PRRIPSRSSS
     RSRPRSRTTS EVPAQGTSSL LGDNSESPSA AEKREAGLAE WRRRYGGRQK ECVVCLEEYV
     DGVSRVMSLP CGHEFHAECI TPWLTTRRRT CPICKGDVVR SLQRGVLSRQ SSYEERTPSR
     ELSDIDDEDD DEVQAQVATS RNDSPSAALP MDTRDLERGE QQRQQRDAPW RDWMNDLMSR
     LTSQRRRTDG VDRDR
//
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