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Database: UniProt
Entry: A0A1R2CTP8_9CILI
LinkDB: A0A1R2CTP8_9CILI
Original site: A0A1R2CTP8_9CILI 
ID   A0A1R2CTP8_9CILI        Unreviewed;       555 AA.
AC   A0A1R2CTP8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=RanBP-type and C3HC4-type zinc finger-containing protein 1 {ECO:0000256|ARBA:ARBA00017887};
DE            EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN   ORFNames=SteCoe_4846 {ECO:0000313|EMBL:OMJ92399.1};
OS   Stentor coeruleus.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Postciliodesmatophora;
OC   Heterotrichea; Heterotrichida; Stentoridae; Stentor.
OX   NCBI_TaxID=5963 {ECO:0000313|EMBL:OMJ92399.1, ECO:0000313|Proteomes:UP000187209};
RN   [1] {ECO:0000313|EMBL:OMJ92399.1, ECO:0000313|Proteomes:UP000187209}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WM001 {ECO:0000313|EMBL:OMJ92399.1};
RA   Slabodnick M., Ruby J.G., Reiff S.B., Swart E.C., Gosai S., Prabakaran S.,
RA   Witkowska E., Larue G.E., Fisher S., Freeman R.M., Gunawardena J., Chu W.,
RA   Stover N.A., Gregory B.D., Nowacki M., Derisi J., Roy S.W., Marshall W.F.,
RA   Sood P.;
RT   "The macronuclear genome of Stentor coeruleus: a giant cell with tiny
RT   introns.";
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.;
CC         EC=2.3.2.31; Evidence={ECO:0000256|ARBA:ARBA00001798};
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:OMJ92399.1}.
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DR   EMBL; MPUH01000062; OMJ92399.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R2CTP8; -.
DR   OrthoDB; 178077at2759; -.
DR   Proteomes; UP000187209; Unassembled WGS sequence.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd20343; BRcat_RBR_HHARI-like; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001876; Znf_RanBP2.
DR   InterPro; IPR036443; Znf_RanBP2_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SMART; SM00647; IBR; 2.
DR   SMART; SM00547; ZnF_RBZ; 1.
DR   SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS01358; ZF_RANBP2_1; 1.
DR   PROSITE; PS50199; ZF_RANBP2_2; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000187209};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00322}.
FT   DOMAIN          121..330
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          125..171
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          522..551
FT                   /note="RanBP2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50199"
SQ   SEQUENCE   555 AA;  64383 MW;  41257109F28EB015 CRC64;
     MSIKDDFSSG SEFSDCEDYS HEIIEDDYNH EIIEDDYPSI SLTGIVKHNR KDSYEIIDSN
     DIYLKEEDAI SNIIEDLGLN RADAVMLLVE NSWDPKIVIE KINSGRIEIP WHMKKMLDPT
     NNFTCLLCFE VLTFSGMTFL DCAHEICTKC YKTYLEESIN AGRECLKRKC PAKDCPIVIP
     KELFQQLLSS ELYEKYQILM INSFVDLNPY AKWCPEPGCN LAAVYKKNYC RDIKCICGHV
     WCFNCQNDAH KPLTCELLKM WNEKIALEDK TSFIDIDAKA CPKCGTPIQK SLGCLHMTCI
     CQYEFCWMCL GAWSYHVSIT PVNYKCNKFS LANSPITYNP ARYIMSVESE KKRFEHYFTR
     YMNHKASIEI AKTKHALALS QIAEVYDVTN ETNILEFFSN ATYLLFKAKQ SLAYSYAIGY
     FLASKRKLDF FEFIQGELEQ AALKLDDFTN IDVRKFIIKD QVFPFHQKDF QEYRNSVVKL
     TEVIKNFFEK SYIELESGLP EIADEEYKDD IQEAQMLIEE VNSGKWICQN CTFANLSNIF
     LCEMCNNPKD SYNSS
//
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