ID K1VHV7_TRIAC Unreviewed; 748 AA.
AC K1VHV7;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
GN ORFNames=A1Q2_06933 {ECO:0000313|EMBL:EKC98701.1};
OS Trichosporon asahii var. asahii (strain CBS 8904) (Yeast).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Trichosporonales; Trichosporonaceae; Trichosporon.
OX NCBI_TaxID=1220162 {ECO:0000313|EMBL:EKC98701.1, ECO:0000313|Proteomes:UP000006757};
RN [1] {ECO:0000313|EMBL:EKC98701.1, ECO:0000313|Proteomes:UP000006757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 8904 {ECO:0000313|EMBL:EKC98701.1,
RC ECO:0000313|Proteomes:UP000006757};
RX PubMed=23193141; DOI=10.1128/EC.00264-12;
RA Yang R.Y., Li H.T., Zhu H., Zhou G.P., Wang M., Wang L.;
RT "Genome sequence of the Trichosporon asahii environmental strain CBS
RT 8904.";
RL Eukaryot. Cell 11:1586-1587(2012).
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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:EKC98701.1}.
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DR EMBL; AMBO01000382; EKC98701.1; -; Genomic_DNA.
DR AlphaFoldDB; K1VHV7; -.
DR STRING; 1220162.K1VHV7; -.
DR eggNOG; ENOG502T6IS; Eukaryota.
DR HOGENOM; CLU_371801_0_0_1; -.
DR InParanoid; K1VHV7; -.
DR OrthoDB; 208457at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000006757; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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 InterPro; IPR024766; Znf_RING_H2.
DR PANTHER; PTHR46539; E3 UBIQUITIN-PROTEIN LIGASE ATL42; 1.
DR PANTHER; PTHR46539:SF2; RING FINGER PROTEIN 150 ISOFORM X1; 1.
DR Pfam; PF12678; zf-rbx1; 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:UP000006757};
KW 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 TRANSMEM 23..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 328..347
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 474..527
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 132..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 712..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..265
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..565
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..635
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 81054 MW; 955A09A5AA1B8E8C CRC64;
METSLWKLGN PLLAVSPWHS KTWFLALAPL GHGAQVASMI GLLIASTQLE TLDERGRVQK
QIAVAPSYVR YCAINIVRLS IHVLLESWLV YRHSRRYRPQ PWLLANAEEE GVQPEVGDGV
DMALEYLRPR EEVGRVPTPH PDPSPSYTVP PRTGETESTS GGDGREKVDE VAVKSMEGQF
EKLDQLEVRI DQLEEMLGKM EKKPKSREEA KEEEKVEDDK SSSSAPASSS STNAVPVLNT
SSADSASLPR ATTSSSTSSS PLSRSRRARC LAARSDSPKD SDAATAEQIL ADPPAQIAAF
IPSAAAEAAK RRAERLQRYD SAASNADLWV CCWGFIMWVV GMIVAFPPEP ARSRAPLVFA
ATMVSMASNW FTALGFTACF LLWSLGYIIV LVAWLLWHLG IIRGAQPVLF PRASAMKLPK
EELDKCPLVI YCADPEEETP EWEDLPGRPL ALGEIDREKL PHPLRVLGVN KATCGICHTE
FLPPCIVEEQ EAYEVEVLRE LPCLHTFHRE CVDEWLLNHA DTCPYCTQSV PAMLKDPGKA
KAAEQAEARG EESGELAELR RTMSRRRSQR SIRTIRSDRS AVSIASARSN TSTSAKGAVR
SIEASSDPAD ASASGSSSSS SSSSGSSSSS GSLRPGQGVA ERKEKTDTAS ISSEDSASTQ
QFHDSREAST PTPVPASPAS HSMSRNASLS TAYETAASSL ALASMRTATP STPIDVAWSD
TPARVDTPGT PGTPGMLEAK KNENVERE
//
