ID   A0A2K6M2E4_RHIBE        Unreviewed;       379 AA.
AC   A0A2K6M2E4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   Name=MARCHF11 {ECO:0000313|Ensembl:ENSRBIP00000029945.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000029945.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000029945.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000029945.1}
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   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   AlphaFoldDB; A0A2K6M2E4; -.
DR   STRING; 61621.ENSRBIP00000029945; -.
DR   Ensembl; ENSRBIT00000053902.1; ENSRBIP00000029945.1; ENSRBIG00000038853.1.
DR   GeneTree; ENSGT00940000160025; -.
DR   OMA; QPWTCLC; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000233180; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:UniProtKB-UniPathway.
DR   CDD; cd16810; RING_CH-C4HC3_MARCH11; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR047906; MARCHF11_RING_CH-C4HC3.
DR   InterPro; IPR046356; MARCHF4/9/11.
DR   InterPro; IPR011016; Znf_RING-CH.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46053; E3 UBIQUITIN-PROTEIN LIGASE MARCH4-LIKE; 1.
DR   PANTHER; PTHR46053:SF1; E3 UBIQUITIN-PROTEIN LIGASE MARCHF11; 1.
DR   Pfam; PF12906; RINGv; 1.
DR   SMART; SM00744; RINGv; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51292; ZF_RING_CH; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233180};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        220..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..286
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          139..199
FT                   /note="RING-CH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51292"
FT   REGION          1..139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        17..33
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..54
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        117..135
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   379 AA;  42094 MW;  B13B9A6430040C5D CRC64;
     PLLSRFRRAP KPTRVSAQTV APPPGPRHIP PAHPVTVSGP AASPLPPPSP LTRAAVGHPP
     RNRRERQRVQ PVEAAEGSPT SSPRRLPEVA AAKGGPGESE ASAGGEGERR GAGDQPETRS
     VCSSRSSSSG GGDQRSGHQH QHHLPICKIC FQGAEQGELL NPCRCDGSVR YTHQLCLLKW
     ISERGSWTCE LCCYRYHVIA IKMKQPCQWQ SISITLVEKV QMIAVILGSL FLIASVTWLL
     WSAFSPYAVW QRKDILFQIC YGMYGFMDLV CIGLIVHEGA AVYRVFKRWR AVNLHWDVLN
     YDKATDIEES SRGESSTSRT LWLPLTALRN RNLVHPTQLT SPRFQCGYVL LHLFNRMRPH
     EDLSEDNSSG EVVMRVTSV
//