ID C1G4U6_PARBD Unreviewed; 827 AA.
AC C1G4U6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 2.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=PADG_01962 {ECO:0000313|EMBL:EEH45812.2};
OS Paracoccidioides brasiliensis (strain Pb18).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH45812.2, ECO:0000313|Proteomes:UP000001628};
RN [1] {ECO:0000313|EMBL:EEH45812.2, ECO:0000313|Proteomes:UP000001628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pb18 {ECO:0000313|EMBL:EEH45812.2,
RC ECO:0000313|Proteomes:UP000001628};
RX PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT "Comparative genomic analysis of human fungal pathogens causing
RT paracoccidioidomycosis.";
RL PLoS Genet. 7:E1002345-E1002345(2011).
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DR EMBL; KN275958; EEH45812.2; -; Genomic_DNA.
DR RefSeq; XP_010757140.1; XM_010758838.1.
DR AlphaFoldDB; C1G4U6; -.
DR STRING; 502780.C1G4U6; -.
DR GeneID; 22581531; -.
DR KEGG; pbn:PADG_01962; -.
DR VEuPathDB; FungiDB:PADG_01962; -.
DR eggNOG; KOG0828; Eukaryota.
DR HOGENOM; CLU_010475_0_0_1; -.
DR InParanoid; C1G4U6; -.
DR OMA; LEGWMRF; -.
DR OrthoDB; 51730at2759; -.
DR Proteomes; UP000001628; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR22763; RING ZINC FINGER PROTEIN; 1.
DR PANTHER; PTHR22763:SF165; TRANSMEMBRANE E3 UBIQUITIN-PROTEIN LIGASE 1; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000001628};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..827
FT /note="RING-type domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002909728"
FT TRANSMEM 390..409
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 448..469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 558..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 611..633
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 645..663
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 753..821
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 484..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 720..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 533..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 827 AA; 92106 MW; 3522E8F8336024F2 CRC64;
METRRALLFF VLLFFLLSAP ESRPPTIGFE REHRQQKTEE RTLSLLNSSR YGDLDNASDR
WLPLGGLTKG DGYAWGLLPV VKERTRDQLY SILQRSGLLD QQPIGWRTRP LRSDLNSSEL
HIPVYHNVTG KIRGDWVRWR GAETEKRPQL NTTAIMLRHD YFTREFAHNI TADHGTLLID
LQEEDGKGMA LADARAREIR ADMTLYTDES LGDSHFIRLF GVHFPSSGGI ILSTTSEKFA
GLLALPQFAL TNDTFELSRQ LLNMSLTETL AEKKTGSVDY LPWSSLPHGP STVTFAAPRC
EYIVYLQQHP VVIDGQIAQQ PVLKLIEDEL RFPAGAPVPS PPLMTMSLTL FSPDCGFVLE
NKGSPSYSPS DGLYLSGPKQ EQYRKHAGRL VVIMAAVLCS QISLLIRQMK EASTPSTRSR
VSFYTIAMMS MGDALFGSFI LMQLYEEAPF LLLTATTFLA LFSVSFLAMK FQIEVWAVQA
PERRDADRSS STRGGAAGPQ QSLPVSATTS RPVDTGATPI IILPPDQDES PEATADPPTT
QTTSDSAAND TGAMYSRFYF LLFVLLFFSS WALFWPTRLS RMYGQLISFL YLSFWIPQIH
RNVMRNCRKA LTYEFVVGQS VIRLFPFLYF YAIPGNVLFI KPDPLFILSI TAWVWLQTIT
LAAQDLLGPR FFVPHGWAPP AYDYHPILRD TSSSGSSEDI EAGGTLPIGY LRGDEGNAAV
PSSVTRDDGK QGSANDSSGK DKDKDRKNRL FDCAICMQDI SVPVLTAPSG VGAGVAPSSV
AEGAANLLSR RAYMVTPCRH IFHSTCLESW MRLRLQCPIC RENLPPI
//
