ID D2HZI3_AILME Unreviewed; 978 AA.
AC D2HZI3;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
DE Flags: Fragment;
GN ORFNames=PANDA_018228 {ECO:0000313|EMBL:EFB16980.1};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|EMBL:EFB16980.1};
RN [1] {ECO:0000313|EMBL:EFB16980.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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};
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DR EMBL; GL193804; EFB16980.1; -; Genomic_DNA.
DR AlphaFoldDB; D2HZI3; -.
DR InParanoid; D2HZI3; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd16574; RING-HC_Topors; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46077; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR PANTHER; PTHR46077:SF2; E3 UBIQUITIN-PROTEIN LIGASE TOPORS; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 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};
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 38..77
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 450..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 938..978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 544..579
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..678
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..833
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 938..968
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EFB16980.1"
FT NON_TER 978
FT /evidence="ECO:0000313|EMBL:EFB16980.1"
SQ SEQUENCE 978 AA; 112277 MW; D631D52A8A3F9D63 CRC64;
QIMASAAKEF KMDNFSPKAG TSKLQQTVPA DASPDSKCPI CLDRFDNVSY LDRCLHKFCF
RCVQEWSKNK AECPLCKQPF DSIFHSVRAE DDFKEYVLRP SYNGSFATPD VPRFRYRTTM
TRDRSASVYS PNNTMSRRTT TPPDSGVLFE GLGISTRPRN GEIPQLMRQI AIRRPTTADE
RSLRKIQEQD IINFRRTLYR AGARVRNIED GGRCRDISAE FFRRNPACLH RLVPWLKREL
TVLFGAHGSL VNIVQHIIMS NVTRYDLESR EFVSDLRPFL LNRTEHFIHE FISFARSPFN
MAAFDQHANY DCPAPSYEEG SHSDSSVITI SPDEAETQEL DINVTTVSQA PWDDETPGPS
YSSSEQVHAA MSSLLNTSDS SDEELVTGRA ASQIQGVQTN EDLNNDSDSS SDNCVIVGFV
KPLAERTPEL VELSSDSEEL GSYEKMETMK MQEQSYSSGD SDVSRCSSPR SVLGKDEQIN
KGHCGSGKRI KSKKEEKHSA SLSSPRDLSS SIRGDRVYSP YNRRHRRRGR SRSSDSRSQS
RSGHDQKNRR KHHGKKRMKS KRSRSRESSR PRGRRDKKRS RTRDSSWSRR SQTLSLSSES
TSRSRSRSSD HGKRRSRSRN RDRYYLRNNY GSRYKWEYTY YSRNKDRDGY ESSYRRRTLS
RAHYSRQSSS PEFRIQSFSE RTNARKKNNH SERKYYYYER HRSRSLSSNR SKTASTGPEW
VRNEKPGGKR KYKTRHLEGT NEVAQPSREF ASKVKEGHYQ KSSSKLDGSH KNESDSFSDS
RSSERETKYK RKKRRTRSLS VEIVYEGKAT DTTRHHKKKK KKHKKKHKKH HGDNPSRSPV
VITIDSDSDK DSEVKEDIEC DNRGPQDSVQ NEFLPPPLEP FEAKDVVTIE DEFGILDKEC
SITTLNNNLS NANKTVDNIP AQAASVEQTL DIREETTFAS DLENQPSNVS IQTEPSRQLP
SPRTSLMSVS LGRDHDMS
//
