ID V4AKJ8_LOTGI Unreviewed; 1977 AA.
AC V4AKJ8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=RBR-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012251};
DE EC=2.3.2.31 {ECO:0000256|ARBA:ARBA00012251};
GN ORFNames=LOTGIDRAFT_170560 {ECO:0000313|EMBL:ESP04724.1};
OS Lottia gigantea (Giant owl limpet).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Patellogastropoda; Lottioidea; Lottiidae; Lottia.
OX NCBI_TaxID=225164 {ECO:0000313|EMBL:ESP04724.1, ECO:0000313|Proteomes:UP000030746};
RN [1] {ECO:0000313|EMBL:ESP04724.1, ECO:0000313|Proteomes:UP000030746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23254933; DOI=10.1038/nature11696;
RA Simakov O., Marletaz F., Cho S.J., Edsinger-Gonzales E., Havlak P.,
RA Hellsten U., Kuo D.H., Larsson T., Lv J., Arendt D., Savage R.,
RA Osoegawa K., de Jong P., Grimwood J., Chapman J.A., Shapiro H., Aerts A.,
RA Otillar R.P., Terry A.Y., Boore J.L., Grigoriev I.V., Lindberg D.R.,
RA Seaver E.C., Weisblat D.A., Putnam N.H., Rokhsar D.S.;
RT "Insights into bilaterian evolution from three spiralian genomes.";
RL Nature 493:526-531(2013).
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; KB199652; ESP04724.1; -; Genomic_DNA.
DR RefSeq; XP_009044623.1; XM_009046375.1.
DR STRING; 225164.V4AKJ8; -.
DR EnsemblMetazoa; LotgiT170560; LotgiP170560; LotgiG170560.
DR GeneID; 20241454; -.
DR KEGG; lgi:LOTGIDRAFT_170560; -.
DR CTD; 20241454; -.
DR HOGENOM; CLU_234325_0_0_1; -.
DR OrthoDB; 443445at2759; -.
DR Proteomes; UP000030746; Unassembled WGS sequence.
DR GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; cd20335; BRcat_RBR; 1.
DR CDD; cd22585; Rcat_RBR_DEAH12-like; 1.
DR CDD; cd00590; RRM_SF; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR031127; E3_UB_ligase_RBR.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR Pfam; PF01485; IBR; 2.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00647; IBR; 2.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030746};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
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 DOMAIN 1761..1977
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1765..1814
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 45..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 418..481
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1543..1570
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 49..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1977 AA; 225519 MW; 3B9FC9402F4365FA CRC64;
MDRILPEFLK KLWRNHNNGD RDKADPEEGR DCTKIDIFDN VLFDPLPART PSSDQQTNGS
DIKNVAKSHD KIVIAETRNK YDWKILPYPK ESTNKFKSDG RLTTPSKQSS FRQYDPSASS
RYRPTLMSES PTELDRTERR REHRETLKDS YPNKQFDGQN IPIKPRSTLD NKAKPALSTN
SFTKNEVGLP HQSRENRGTQ NGSLSSRSFG SSDLSNDEEA RLQHTREVLK RTTDKIRKSE
SKESKTCTDY PGIRLSSTSF GSCNISNDKV ATLQHRRDVL KRDTGQIRKS DRKESTLCRP
SAYPVVPKRN EFCDESKKNT KCPMTQYDHL SSTTRLSFES SDGTDVDTSK SRVNYIKMIS
PRPFIYRQSN SLENKTAKES GNGSSSTKVI DTYTKKIHDS RDGYQQFNME TSTVDTKYKG
VATDKRTPTD KQPIVDKQPL VDKRPPVDKG NATDKRKPVD KQPVDQRTSA NDSSEIDKYT
KKNHSQLDKL LSDCVEKSRN DCLKKSGKLC DAENAGEHSL STLEIGTLAK YHSQGARPKD
SSFINKSKNM SPNLAETSGG RNDVKGLEPT SQHTKFDTRQ EANDHSKRSK NNETLNLDQS
KVKSANPDLT ENSRRQSYVN RKSETNQKAS HKIIAATASE QKGSTSLHER NNSLNQDQSK
SKKKRNRRRR KSNNHEATKD NHHVTSATPL RQPEIGNSQP LERSQSSSQN QSRSNVVKNP
KKPETTPINP TIIQDKPIPS KVHLTNHFQK IATCPKSKPS RSFYVVLLKI EMSVPLVALL
DIILGPDSER TILSIEDEPI LDLESATLNF SDVQKAEQAL KQLREFNCQN LLCTWTTVDK
RIEILKTYFN DFEFHSSDIL KTHDEKIQAI RKQLESCAFD EKEALKMRKE ELILQLREFT
SFSKTVRESL RRSILLEDEQ SPPDAAIQTA IETLEELGSI KDDRITDIGK WLVKIPLEPR
FGCMIKKGFE MGFAYDTIVF TALCSSSGSI FYRGGNDQQK KRSDLKKLTF CDTKGDAFTY
LKIYKEWEQV TEKRKNKWCF DNALNSKSLR GARELVNEIC SIFKHNWSIL VKKTFSTKVE
LEEALQNIIL FAFYENIAHS LGHNRMGYYI PNLRQRVFVH PSSALNSLND SSQWLVFINI
LKTSRDYITV VTPVEESWIR KITSLKTKQF DIDEAKRKSV CSVRNQFFGS TTYSFFVGPA
HSKLKAYEDL LYESVQVPVV IEADRKTGEV KFICGFNVAL PGDLIDNWIV EARSHVIQRT
AEYKVGSNNQ AGGVRIVLGL GGEGQLILMP DEYRNIHIKS SGKETSKETV VDKFKRFGQI
VDCWEDKRSY HRWGRVTFST PEAAAEAVRR TQDDPKHAAT PEFKIQKHAF FQYQATIEWV
RRKPTGLVFV DMDYLEAMSV KSLREVRILG QSCSISLDKK KRGTVLLRKV PTMVTEQDIQ
YCFPQHSQRR AITKISIIRE KTFTNPNEIP YFQQQIHDQF QEFDHDMKFV VDVMKPYDSN
INFRAFIKFN DASQGTMACD ALRGRLIING QKANLTPKLS SSLSVSEQVY QLLEDEIEDF
TAELRENGTE FKLDSKKLKN ERRVFNISAS NSNDLVQIRL GLAAIVQGEV IEYWSNENNR
YLFLKSGREF LRSLEKRTNT ILQVDNRLLS LRVFGLEDNI LMAQNAIDQY LGNMVEGDGR
REIKLDGKSQ PKGLMKTLVT RYDLELEGFV QASGLQSALL NHHNQTLKIS GDSASIEKAT
GLIESLATEL RNKITKTKIA ELPDCCTCLC PVQSMDYIYR LEACGHVYCL DCIKRQITVA
VQSKELPVLC GNCQDPLVWS DFEFCFKRLQ INPLDLVRTA VSVYMIRNKD GYRHCPTPDC
PMVYRITKKS DVFNCNECGM RICTSCHVEY HDGLTCAMLK SSSDVDSDME KYLRENATRV
KRCPKCSTPI EKKSGCNHMT CSGCKIHFCW LCCQAFTTTS SVYGHLNAQH GGIFDFR
//