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Database: UniProt
Entry: A0A2K5YUW4_MANLE
LinkDB: A0A2K5YUW4_MANLE
Original site: A0A2K5YUW4_MANLE 
ID   A0A2K5YUW4_MANLE        Unreviewed;       484 AA.
AC   A0A2K5YUW4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=RC3H2 {ECO:0000313|Ensembl:ENSMLEP00000019320.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000019320.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000019320.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC       {ECO:0000256|ARBA:ARBA00004201}.
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DR   AlphaFoldDB; A0A2K5YUW4; -.
DR   Ensembl; ENSMLET00000042809.1; ENSMLEP00000019320.1; ENSMLEG00000033809.1.
DR   GeneTree; ENSGT00940000157685; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1790; -; 1.
DR   Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR041523; ROQ_II.
DR   InterPro; IPR048575; Roquin_1_2-like_ROQ.
DR   InterPro; IPR000571; Znf_CCCH.
DR   InterPro; IPR036855; Znf_CCCH_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR13139; RING FINGER AND CCCH-TYPE ZINC FINGER DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR13139:SF2; ROQUIN-2; 1.
DR   Pfam; PF18386; ROQ_II; 1.
DR   Pfam; PF21206; Roquin_1_2-like_ROQ; 1.
DR   Pfam; PF00642; zf-CCCH; 1.
DR   Pfam; PF14634; zf-RING_5; 1.
DR   SMART; SM00184; RING; 1.
DR   SMART; SM00356; ZnF_C3H1; 1.
DR   SUPFAM; SSF90229; CCCH zinc finger; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50103; ZF_C3H1; 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, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00723}.
FT   DOMAIN          14..54
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          410..438
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50103"
FT   ZN_FING         410..438
FT                   /note="C3H1-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ   SEQUENCE   484 AA;  54476 MW;  6071D59B66A9F5CB CRC64;
     MPVQAAQWTE FLSCPICYNE FDENVHKPIS LGCSHTVCKT CLNKLHRKAC PFDQTAINTD
     IDVLPVNFAL LQLVGAQVPD HQSIKLSNLG ENKHYEVAKK CVEDLALYLK PLSGGKGVAS
     LNQSALSRPM QRKLVTLVNC QLVEEEGRVR AMRAARSLGE RTVTELILQH QNPQQLSANL
     WAAVRARGCQ FLGPAMQEEA LKLVLLALED GSALSRKVLV LFVVQRLEPR FPQASKTSIG
     HVVQLLYRAS CFKVTKRDED SSLMQLKEEF RSYEALRREH DAQIVHIAME AGLRISPEQW
     SSLLYGDLAH KSHMQSIIDK LQSPESFAKS VQELTIVLQR TGDPANLNRL RPHLELLANI
     DPNPDAVSPT WEQLENAMVA VKTVVHGLVD FIQNYSRKGH ETPQPQPNSK YKTSMCRDLR
     QQGGCPRGTN CTFAHSQEEL ENMGTVHNEL YKQQHVCAVK RAETCFSSQF FSPLEEPRER
     IQES
//
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