ID G5AQ66_HETGA Unreviewed; 997 AA.
AC G5AQ66;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=GW7_13939 {ECO:0000313|EMBL:EHA99176.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHA99176.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHA99176.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
CC -!- SIMILARITY: Belongs to the Arkadia family.
CC {ECO:0000256|ARBA:ARBA00007622}.
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DR EMBL; JH166450; EHA99176.1; -; Genomic_DNA.
DR AlphaFoldDB; G5AQ66; -.
DR STRING; 10181.G5AQ66; -.
DR Ensembl; ENSHGLT00000079590; ENSHGLP00000039060; ENSHGLG00000017832.
DR eggNOG; KOG0800; Eukaryota.
DR InParanoid; G5AQ66; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016605; C:PML body; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16681; RING-H2_RNF111; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR029306; RNF111_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16200:SF1; E3 UBIQUITIN-PROTEIN LIGASE PLR-1-RELATED; 1.
DR PANTHER; PTHR16200; RING ZINC FINGER; 1.
DR Pfam; PF15303; RNF111_N; 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 945..986
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 63..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 507..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..149
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..521
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..680
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 997 AA; 109130 MW; BB1A75BF239E92EC CRC64;
MSQWTPEYNE LYTLKVDMKS EIPSDAPETQ QSLKGILLHP EPIGAAKNFP AGVEMINSKV
GNEFSHLCDD SPKQEKDMNG NQQEQEKSVV RKKRKSQQAG PSYVQNCAKE NQGVLGLRQH
LEAPSDEEND SSFSDCLSSP SSSLHFGDSD TVTSDEDKEV SVRHSQTILS AKSRSHSARS
QKWPRTEPES VSGLLMKRPC FHSSSLRRLP CRKRFVKNNS SQRTQKQKER ILMQRKKREV
LARRKYALLP SSSSSSENDL SSESSSSSTE GEEDLFVSAS ENHQNNSAAP SGSIDEDVVV
IEASFTPQVT ANEEINVTST DSEVEIVTVG ESCRSRSTLG HSRSHWSQGS GSHTGRAQEP
RSRSRVSTVI QPLRQSAAEV VDLTVDEDEP TVVPTTSVRM ESQTTSASVN NSNPSTSEQA
SDTVSAVTSS QPSTVSETSP TLTSNSTTGT SIGDESRRTA SSAMTETGPP AMPRLPSCCP
QHSPCGGPSQ NLHGLGHAHT GCFQQHGHHF QHHHHHHHPP HPAVPASPTF SDPACPVERP
PQVQVPCGGN SGSSTSYHDQ QALPVDLSNS GIRSHGSGGF HGASAFDPCC PVSSSRAAIF
GHQAAAAAPS QPLSIDSYGT SLVAQPQPQP PPQPSLSSCR HYMPPPYALT RPLHHQAPAC
PHSHGNPPPQ TQPPPQVDYV IPHPVHAFHS QMTSHATSHP VAAPPPTHLA STAAPIPQHL
PPAHQPISHH MPAAAPPSQR LHPHEVMQRI EGQRRRMMQH PTGLFMFCVS RRAHERPPPH
PHRMHPNYGH GHHIHVPQTM SSHPRQAPER SAWELGIEAG VTPATYTPGA LHLGHYHAPP
RLHHLQLGAL PLMVPDMAGY PHIRYISSGL DGTSFRGPFR GNFEELIHLE ERLGNVNRGA
SQGTIERCTY PHKYKKVTTD WFSQRKLHCK QDAEEATEED TEEKCTICLS ILEEGEDVRR
LPCMHLFHQV CVDQWLITNK KCPICRVDIE AQLPSES
//
