ID V9KKF4_CALMI Unreviewed; 633 AA.
AC V9KKF4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
DE Flags: Fragment;
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|EMBL:AFO98428.1};
RN [1] {ECO:0000313|EMBL:AFO98428.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Heart {ECO:0000313|EMBL:AFO98428.1};
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
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};
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DR EMBL; JW865911; AFO98428.1; -; mRNA.
DR AlphaFoldDB; V9KKF4; -.
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:InterPro.
DR CDD; cd20363; BRcat-RBR_RNF19B; 1.
DR CDD; cd20355; Rcat_RBR_RNF19; 1.
DR CDD; cd16776; RING-HC_RBR_RNF19B; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 2.20.25.20; -; 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; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR11685:SF427; RBR-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF01485; IBR; 2.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
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:PRU00175}.
FT TRANSMEM 252..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 305..338
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..242
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 24..72
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 553..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AFO98428.1"
SQ SEQUENCE 633 AA; 68161 MW; 613FCE60C2AE5925 CRC64;
APTGSFPALS PTPARKVSAG FLECPLCLVP HPQENVPEIM TCQHRSCLDC LRQYLRIEIT
ESRVNISCPE CTERLNPHDI RLILNDQTLM DKYEEFMLRR YLASDPDCRW CPAPDCGYAV
IAYGCASCPK LMCGRDGCDT EFCYHCKQLW HPNQTCDTAR QQRAQELRVR TTQSSGLSFG
PESGTTDDIK PCPRCGAYII KMNDGSCNHM TCAVCGCEFC WLCMKEISDL HYLSPSGCTF
WGKKPWSRKK KILWQLGTLI GAPVGISLIA GIAVPAMIIG IPVYVGRKIH SRYEGKKMSK
HKRNLAITGG VTLSVIASPV IAAVSVGVGV PIMLAYVYGV VPVSLCRGGG CGVSTANGKG
VKIEFDEDDG PITVADAWRA LKSPSIGESS VEGLTSVLST SGSPIDGVSV TQGNYSETTS
FAALSGGTLT GGALTGSNGH HSRMQIQADI QKESFNLNKD SISLGATSDN ASTRAMAGSI
ISSYNPQDRE CNNLEVQVDI ETKPTHLCLA SGSSLDESLH LRSQSTEGLC CGGEKDSERR
SASLTSQTCD VTLAQPESVK SDEDSTDTQS DDLPDMTSDE CDSPSPANGS HLEISALDAK
SLNNENVPSD HVQQREDSAE PVEQETESVV HYA
//
