ID S7NHT4_MYOBR Unreviewed; 1189 AA.
AC S7NHT4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=D623_10028433 {ECO:0000313|EMBL:EPQ16856.1};
OS Myotis brandtii (Brandt's bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=109478 {ECO:0000313|EMBL:EPQ16856.1, ECO:0000313|Proteomes:UP000052978};
RN [1] {ECO:0000313|Proteomes:UP000052978}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23962925; DOI=10.1038/ncomms3212;
RA Seim I., Fang X., Xiong Z., Lobanov A.V., Huang Z., Ma S., Feng Y.,
RA Turanov A.A., Zhu Y., Lenz T.L., Gerashchenko M.V., Fan D., Hee Yim S.,
RA Yao X., Jordan D., Xiong Y., Ma Y., Lyapunov A.N., Chen G., Kulakova O.I.,
RA Sun Y., Lee S.G., Bronson R.T., Moskalev A.A., Sunyaev S.R., Zhang G.,
RA Krogh A., Wang J., Gladyshev V.N.;
RT "Genome analysis reveals insights into physiology and longevity of the
RT Brandt's bat Myotis brandtii.";
RL Nat. Commun. 4:2212-2212(2013).
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 EMBL; KE164307; EPQ16856.1; -; Genomic_DNA.
DR RefSeq; XP_005880969.1; XM_005880907.2.
DR AlphaFoldDB; S7NHT4; -.
DR GeneID; 102244880; -.
DR KEGG; myb:102244880; -.
DR CTD; 54542; -.
DR eggNOG; KOG3161; Eukaryota.
DR OrthoDB; 2909513at2759; -.
DR Proteomes; UP000052978; Unassembled WGS sequence.
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 CDD; cd16782; mRING-HC-C3HC3D_Roquin2; 1.
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:UP000052978};
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"
FT REGION 527..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 131592 MW; 156093F020938E15 CRC64;
MPVQAAQWTE FLSCPICYNE FDENVHKPIS LGCSHTVCKT CLNKLHRKAC PFDQTAINTD
IDVLPVNFAL LQLVGAQVPD HQSIKLSNLG ENKHYEVAKK CVEDLALYLK PLSGSKGVAS
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 EKYRLRNKKI NATVRTFPLL NKVGVSNTVT TTAGNVISVI
GSTEATGKIV PSTNGISNAE NSVSQLIPRN ADSTLRALET VKKVGKVGTN GQNAAGPSSE
SVTENKIGSP PKTPVSSVAA TSAGPSNVGT ELNSVPPKSS PFITRVPVYP QHSENIQYFQ
DPRTQIPFEV PQYPQTGYYP PPPTVPAGVA PCVPRFVRSN NVPESSLPPA SMPYADHYST
FSPRDRMNSP YQPPPPQPYG PVPPVPSGMY APVYDSRRIW RPPMYQRDDI IRSNSLPPMD
VMHSSVYQTS LRERYNSLDG YYSVACQQPS EPRTTVPLPR DPCGHLKTSC EEQIRRKPEQ
WAQYHTQKAP LVSPALPVAT QSPTPPSPLF SVDFRTDLSD SVSGTKFEED HLSHYSPWSC
GTIGSCINVI DSEPRDVIAN SNAVLMDLDS GDVKRRVHLF ETQRRTKEED PIIPFSDGPI
ISKWGAISRS SRTGYHTTDP VQATASQGSA TKPISISDYV PYVNAVDSRW SSYGSESTSS
AHYIERDRFI VTDLSCHRKH SSTGDLLSIE LQQAKSNSLL LQREANALAM QQKWNSLDEG
RHLTLNLLSK EIELRNGESD YTEDATDTKP DRDIELELSA LDTDEPDGQS EQIEEILDIQ
LGISSQNDQL LNGTAVENGH PVQPHQKEPL EQKRQSLGED HVILEEQKTI LPVTACFSQP
LPVSISNASC LPITTSVSVG NLILKTHVMS EDKNDFLKPV VANGKMVNS
//
