ID S3CHH7_OPHP1 Unreviewed; 1062 AA.
AC S3CHH7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Ring finger ubiquitin ligase {ECO:0000313|EMBL:EPE05783.1};
GN ORFNames=F503_08314 {ECO:0000313|EMBL:EPE05783.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE05783.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE05783.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE05783.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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DR EMBL; KE148155; EPE05783.1; -; Genomic_DNA.
DR AlphaFoldDB; S3CHH7; -.
DR STRING; 1262450.S3CHH7; -.
DR VEuPathDB; FungiDB:F503_08314; -.
DR eggNOG; KOG0828; Eukaryota.
DR HOGENOM; CLU_010475_0_0_1; -.
DR OMA; PIPRCEY; -.
DR OrthoDB; 51730at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000016923; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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 Ligase {ECO:0000313|EMBL:EPE05783.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923};
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..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..1062
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012813647"
FT TRANSMEM 631..651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 663..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 693..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 816..838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 844..862
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 874..894
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 906..925
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 995..1056
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 32..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 118194 MW; C68D628F9383E875 CRC64;
MNGFVGLTQL PSLLATLHLC IDTCIQRHPD QIDSLNDNSH PPNPPKYTRD SPHLNRDGHR
SPSTHQQHPY ATPRNRAPPS DGYRDSPPNR GWDQRVVDTM PQPQDNARFV LLVMFILWLN
TSNEVTSGIL SAPSLILEKV QRQRMSYYTM QNSHWGDFAP AQYTDTERTP DGADEPTPDS
DGKYLNITGF RKEDGLVWGD LDRFRQRCLE WSRNAYPFVD GVSLWDKGLT MLTWQNATGS
VSGFWERNQA SFPRYATSYN LTSLMSLDTA GLGGGRGHGT NTSDATAAAQ RRSADNTQED
APESNDKKAD GEKGQKKTSE KDAEGEKENQ DTQSSLFSPM HMMDWGRNVT GPSGKMIIRI
TDEDDELAFP EERLMSSGPP TGGLVRSATA TVTIEDVEGT GSSYDMKLHG VHWPRQGTLL
LTTTSDKFSG IFGLPHLTPD PEYFVSSQRL LKVTLDKALK ERENARSFGP PDPALSTPLW
SSTVDAIPDG LTPIPRCEYL MYLQIHPLDT SQFLPHKAPQ KVSPARAAAG VAARDVYDNS
TRLGARALPE DFDYSQDDMT QLMLGIENEL RFPTGAPIFH NGVPEIQVSA VLFSPDCGYF
IETKGPPKFG RSEFQHLRGR KVEEFIYEAR MWMIALAAVL FCQIQLFLSQ ARETSTPSTL
GRISFLTMAA MVLADGLVLA IASTWSLTAS ASFLPSLTVT FAGFASTIAG GYFLSEIYGS
HEPERRRRER EQQQQVQQQQ QNVRDRLREH FANTRAETAP IIVPSDQDID AEIAENELTT
AAIAAPLLPA PATARRPPAA AAVAATTSHS LPFSTVVARM SLIGVVLLFL SLAATTWWAS
VRAYYTNTIG FIYLSLWIPQ ILRNIERNSR RAFSWRFMIG QSVLRLMPLA YFYLRPDNIL
FAETDWVSFS FLAAWVWIQL FVLAFQDALG PRYGIRKSWV SEAWDYHRVL REDDLEAGGL
PIGLVPAVTE DMPKSPAGTL PLGATSTTNI WTMDCPICCE TLDVPLVRAG VVDPTEGGVA
GVFARRQYMA TPCRHIFHTK CLVGWLNKRL QCPICREEVP PL
//
