ID   W6L2I0_9TRYP            Unreviewed;      1053 AA.
AC   W6L2I0;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=GSEM1_T00002243001 {ECO:0000313|EMBL:CCW63736.1};
OS   Phytomonas sp. EM1.
OC   Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC   Trypanosomatida; Trypanosomatidae; Phytomonas.
OX   NCBI_TaxID=479712 {ECO:0000313|EMBL:CCW63736.1, ECO:0000313|Proteomes:UP000027080};
RN   [1] {ECO:0000313|EMBL:CCW63736.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=EM1 {ECO:0000313|EMBL:CCW63736.1};
RA   Genoscope - CEA;
RL   Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCW63736.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EM1 {ECO:0000313|EMBL:CCW63736.1};
RX   PubMed=24516393; DOI=10.1371/journal.pgen.1004007;
RA   Porcel B.M., Denoeud F., Opperdoes F., Noel B., Madoui M.A.,
RA   Hammarton T.C., Field M.C., Da Silva C., Couloux A., Poulain J.,
RA   Katinka M., Jabbari K., Aury J.M., Campbell D.A., Cintron R., Dickens N.J.,
RA   Docampo R., Sturm N.R., Koumandou V.L., Fabre S., Flegontov P., Lukes J.,
RA   Michaeli S., Mottram J.C., Szoor B., Zilberstein D., Bringaud F.,
RA   Wincker P., Dollet M.;
RT   "The Streamlined Genome of Phytomonas spp. Relative to Human Pathogenic
RT   Kinetoplastids Reveals a Parasite Tailored for Plants.";
RL   PLoS Genet. 10:e1004007-e1004007(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; HF955077; CCW63736.1; -; Genomic_DNA.
DR   AlphaFoldDB; W6L2I0; -.
DR   EnsemblProtists; CCW63736; CCW63736; GSEM1_T00002243001.
DR   OrthoDB; 5383069at2759; -.
DR   Proteomes; UP000027080; Unassembled WGS sequence.
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; IPR027370; Znf-RING_euk.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR25464; TRIPARTITE MOTIF-CONTAINING PROTEIN 2-LIKE PROTEIN; 1.
DR   PANTHER; PTHR25464:SF2; TRIPARTITE MOTIF-CONTAINING PROTEIN 2-LIKE PROTEIN; 1.
DR   Pfam; PF13445; zf-RING_UBOX; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027080};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          949..989
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          40..83
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..679
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          769..825
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        157..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1053 AA;  116859 MW;  4627493DFF0284AE CRC64;
     MLQAPVVSDI LQESGRNGNA SLAYVTRAVH ALELYPIRSK LPKNRSPPHG RSQLPSLDSK
     SDVAKSHENP FPTENESIQT EDTDSVDSLV TLPYASTSAQ LQARVKAELG KQLFGALKQR
     LQSRQRMLAR TAPVPTPVSA NLREAEPVTH STQASSLREA RKPDKAAALD QRQGGRRTGK
     VRRHASRSAA PSQFSMDYLA GAMPTATQCS WRPEMPAICV AQSVSSRTCS LLMTKGERLR
     RCDVNGLSMW QVDQTSEVDL LRVNRLKAIP NYNRGLFAGL DCFVTRSGLF IVGLTRGPDG
     RRIHPRAWHL LYGSVDAGEV SSGVSGRVGA DFITAEASGR KAMAHFSSRD DRGDLGSKHQ
     NLKRFSDVCR KDILRGILSD EERVEAVRLL RSLRKRALEM GTTPGERQGE EREEVRHRIY
     EGTPLSGDGF SCSSAAKDAS SLPAVQPRYS TEKREGESTA YGSDFLPVEA DEDEYLNSDL
     VTLSRTHTPR RSLRLAPDSL LRSASGSDIS NSLLDRTLFS PELEQFHLKG NKTRSFIVGQ
     KRKRKVRWSD SGNKVSCSSL SMSTGVISRK GNERDYPTSL FNEADVDSFF TPEEGSVALP
     NLISTLPNKV VTPDSTDRDH DRVSSALQSP YDEVTMLSPR NTDVSVSSEN PPNTPKMAPV
     KVRGRRGKGI KSKLSSDHMI SDDKKLDDES QADILNVNFP KAAEHVQLRK AANRILDDLD
     FDGGSFLGLA RFSDYSGDDL EYDQLPLENG KPNNITSDRS RDAHGLKEVQ ELEAHMGRLQ
     NQIDTEVEQD LADLIARRDQ LKAEVKEQQQ LIDAFQMDLH NLSKERKGAK GDAFAIQLTA
     EVNRYAMEHR LQLEEIYQEL LEDDDISMGG LTESMLKQFV RGKSEMCNVG TQVTDYDLGY
     IEDDLKETIE QMDEMFYHEK ALRDAIDLTH VALSKIISFH ASLELESTCK ECFFLFEQPR
     TLWPCGHTFC QLCLAEMYNK NGDLLCSECG SVCIVGYTPN LSIELIASYQ MLQDAKSKSP
     SGGKTIENTL QSLLSFLLST RDGFAAPSAA DTR
//