ID A0A067R2N5_ZOONE Unreviewed; 4788 AA.
AC A0A067R2N5;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=L798_08844 {ECO:0000313|EMBL:KDR17278.1};
OS Zootermopsis nevadensis (Dampwood termite).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Termopsidae; Zootermopsis.
OX NCBI_TaxID=136037 {ECO:0000313|EMBL:KDR17278.1, ECO:0000313|Proteomes:UP000027135};
RN [1] {ECO:0000313|EMBL:KDR17278.1, ECO:0000313|Proteomes:UP000027135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole organism {ECO:0000313|EMBL:KDR17278.1};
RX PubMed=24845553; DOI=10.1038/ncomms4636;
RA Terrapon N., Li C., Robertson H.M., Ji L., Meng X., Booth W., Chen Z.,
RA Childers C.P., Glastad K.M., Gokhale K., Gowin J., Gronenberg W.,
RA Hermansen R.A., Hu H., Hunt B.G., Huylmans A.K., Khalil S.M.,
RA Mitchell R.D., Munoz-Torres M.C., Mustard J.A., Pan H., Reese J.T.,
RA Scharf M.E., Sun F., Vogel H., Xiao J., Yang W., Yang Z., Yang Z., Zhou J.,
RA Zhu J., Brent C.S., Elsik C.G., Goodisman M.A., Liberles D.A., Roe R.M.,
RA Vargo E.L., Vilcinskas A., Wang J., Bornberg-Bauer E., Korb J., Zhang G.,
RA Liebig J.;
RT "Molecular traces of alternative social organization in a termite genome.";
RL Nat. Commun. 5:3636-3636(2014).
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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KK852747; KDR17278.1; -; Genomic_DNA.
DR STRING; 136037.A0A067R2N5; -.
DR EnsemblMetazoa; KDR17278; KDR17278; L798_08844.
DR eggNOG; KOG1426; Eukaryota.
DR InParanoid; A0A067R2N5; -.
DR OMA; HTNGVLY; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000027135; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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:UniProtKB-UniPathway.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR CDD; cd08664; APC10-HERC2; 1.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR Gene3D; 3.10.120.10; Cytochrome b5-like heme/steroid binding domain; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 3.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR004939; APC_su10/DOC_dom.
DR InterPro; IPR021097; CPH_domain.
DR InterPro; IPR001199; Cyt_B5-like_heme/steroid-bd.
DR InterPro; IPR036400; Cyt_B5-like_heme/steroid_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR037976; HERC2_APC10.
DR InterPro; IPR010606; Mib_Herc2.
DR InterPro; IPR037252; Mib_Herc2_sf.
DR InterPro; IPR009091; RCC1/BLIP-II.
DR InterPro; IPR000408; Reg_chr_condens.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR000433; Znf_ZZ.
DR InterPro; IPR043145; Znf_ZZ_sf.
DR PANTHER; PTHR22870; REGULATOR OF CHROMOSOME CONDENSATION; 1.
DR PANTHER; PTHR22870:SF437; X-LINKED RETINITIS PIGMENTOSA GTPASE REGULATOR-RELATED; 1.
DR Pfam; PF03256; ANAPC10; 1.
DR Pfam; PF11515; Cul7; 1.
DR Pfam; PF00173; Cyt-b5; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF06701; MIB_HERC2; 1.
DR Pfam; PF00415; RCC1; 17.
DR Pfam; PF00569; ZZ; 1.
DR PRINTS; PR00633; RCCNDNSATION.
DR SMART; SM01337; APC10; 1.
DR SMART; SM01117; Cyt-b5; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00291; ZnF_ZZ; 1.
DR SUPFAM; SSF55856; Cytochrome b5-like heme/steroid binding domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF159034; Mib/herc2 domain-like; 1.
DR SUPFAM; SSF50985; RCC1/BLIP-II; 3.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR PROSITE; PS50255; CYTOCHROME_B5_2; 1.
DR PROSITE; PS51284; DOC; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS51416; MIB_HERC2; 1.
DR PROSITE; PS00626; RCC1_2; 1.
DR PROSITE; PS50012; RCC1_3; 19.
DR PROSITE; PS50135; ZF_ZZ_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000027135};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT REPEAT 533..584
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 585..636
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 639..690
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 691..742
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 743..794
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 1218..1294
FT /note="Cytochrome b5 heme-binding"
FT /evidence="ECO:0000259|PROSITE:PS50255"
FT DOMAIN 1863..1936
FT /note="MIB/HERC2"
FT /evidence="ECO:0000259|PROSITE:PS51416"
FT DOMAIN 2681..2732
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 2736..2914
FT /note="DOC"
FT /evidence="ECO:0000259|PROSITE:PS51284"
FT REPEAT 2927..2978
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 2979..3032
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 3033..3084
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 3085..3136
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 3139..3190
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 3191..3242
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 3243..3294
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 3922..3973
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 3974..4027
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 4028..4079
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 4080..4131
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 4134..4185
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 4186..4237
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT REPEAT 4238..4289
FT /note="RCC1"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT DOMAIN 4428..4755
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1362..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1920..1956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2404..2442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3395..3460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1375..1389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1592..1607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2411..2426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3443..3460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4723
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4788 AA; 524371 MW; 7477AE64CE130A58 CRC64;
MSGQLDIVVH THSRLDGKWL KTDLQQALST DGLAQLWNEM VKDGELTGSF SDGLLNSVGI
TAHKGESGHY YCGLRVLTCP CCDGICGPQT GCNCSPCQRL DREEAARVEV KSADPAPSQL
QIDSWVWGPQ PSVEQLKLCI KSLNYEQKVL CHEAASSTLS ACRLRQRLMV AQRYFVALGR
HLPADDSRPL MKTTLNGAIG DHRGTKTAEK ATISLAKVGC RAALNFSFAF LRRAWRSGED
ADLCSELLTE SLEALQSLPE ATLFDENSVS PVWLEVIERS DRFLQQVVLG DVNSTRSWCE
VPVSDQHTAL CLLLELAVQR GALSNILDAV ILLLSLWDRG KYQVDNRVVS SGTSAPLIPL
LRRFEKVSCS KIGPLNAPWD ENAQIMISPT ECFLRYLQLP DNDSIAVDLK QAAVVIMSHL
DRLAAPHAPP ATFIKNMGQY QEVLAWGWLA WSSCTDSGMV PQCCETIGEL GVAQIVCAER
CLLILTNAGK VFIVYYSSEM LCPQQVEGFG DKEVVKLAAH PDGKHFLALT SDGGVYSWGS
GDGGRLGHGD SNSRDEPTLI EALDGKHMVH IACGSAYSAA VSSSGDLYTW GRGNYGRLGH
GCSEDHSVPT IVAGLKGHRV VDVACGSGDA QTLVVTDAGL VFSWGDGDYG KLGRGGSDGS
KTPKLIDKLQ DVDVVKVYCG AQFSLALTKT GSVYSWGKGD THRLGHASEE HVRFPKLIEI
LQGKRVVSLA VGSVHVLALT DEGEVYGWGR NDYAQVGETT GSSVLEPTLI TSLQGKVIIG
MACGPTQSFA WSSSSNWSIN LRVAFVVDVC EETFQMLDQL LSLVCEGVSG NLDWPPPQDK
ECMAVACLNL LKLQASTVIL PMFQLHAMLS HSVDVSCVGL GPNTNLLSSL KQHVVELASN
IGVLNTIQSA AQATLQAGWS ILLPTADERA KTLSALLPST DPSAVSAGHR FMTDLLVSSL
MADGGLETAL KAAFKVELGE HSENDERKVH MSDQALLETE SKRAKDASLH EKHNSTVPLL
HLVKLLLRNG SALTQARLQA VQNCGTVRHE SREKHERSPS LNLLLRFQRL LIAQIYSHSH
KMKSSNSQQD QDVLGAESLL TKYIYQLCNH ITETLPVASS LAATSSRHFS HVVSILKGDV
IDVLLPELIV CMILLQLEVP LLLHQVNWVQ LLVPLLDTLD KFNRLASGVD KEDAEDLSWP
GIIAPQHSLS GQKAPEDIPM IRKADLENHN RDGGLWIVVD RKVYDVQDFR AQAPCGSELL
QRYAGRDATQ PFHTAAHSQA AREMMQGFLV GYYMEPEQEV VQAVDVNNVG SPLMDVERNL
AFLLGLHAHW LSQSTALQPA EEEAQQWLHA VFLRGGLQVL QPPNPYEEEK GEARSTSSTA
GTTPTEPNTP KLEGLHKWTL DRAAPFLQAL AEHRSTDPYV RTFLSIVERY CKLHHLMMHG
DLSADHPVEE VGRLLMALLI KHQGLGFQVI ALIDQEIDGS GISVKIPKQL IDIIRTVHQT
KWNLIKTRQE MNRSYKEVCA PVLDKCRFLL HEIRAATSFE VKALHHLQLL HTVPRWKKTV
KNIISDNKLR KHMPCAKPED ILNASIQGVE AKCKENEEET ESWTRDEKKD EDEEEEGDKG
WDSTMNLLLQ IAEKQQNNMQ CPDSGKITNA VIDFVMQEES GDVETLRKAL YCQVQRARIR
IQGNEMMYEL LKRDYLISSV KYTLLNGWLG LAHKKHILRE GLSYCLENIQ SVNPYQKVEV
LLSQARITSW AVATLREHVL LAEQPRKTHK LKGKGSLNQG TYSWLRKLPW ARFLLTILGM
LTGHHHGNEI SLIVNSGVLA LIQSLMRQMG PEFSSCIEDK NKDLFAIYED TLQKNSPPAI
ILSGPELASM MKIGTRVVRG VDWKWGDQDG PPPGEGRVVG DLGEDGWIRV QWDNGSTNSY
RMGKEDRYDL KLAEPPTPAE TDTDSDTNDE ATKPPLRLNC KDAHPTKLLK QASLTLLRTI
SICCGINADQ VQPSSTKIFC SLLRDIIQTA NKASDSPSQT QLLALNHHVE WATLGFTRAI
ASSSAMCRAL STPAWLHLLL SIVSGQDSSI VITLPKQILS LRLLQAVLPA WDVNPTERLS
LLEKLFHLLG YTALLCPADS TVQHTVRVSL TASHSSTVAE ECITLLRSLH SLPVWNQALN
HILANKLSVA GDLLIEGPLF HVHQVSISTV QFNQSLGIQS AVMTALSVVG GLDSRPRIGG
LVIAEGLGQG TVCHITQHGK LVVQLHETGT VKKLSLSTVV PLQTAQFVLD KTLRSEHMLD
TWATLLSLLS QHHSDKRQPG AVPGMVNISL LRTQQKRLAA MNACIVLFRH QNLLRHVLKH
HTLGSSPSLE ILNEGEELDP VSETLLIQKL ISKATQPSPL KALAAALNIS QYLATEVKAQ
MKRGSEVATP ASDCSLPSPM SSSNKTGSKH KRVRPPSPPL SPLVGQLTEM GFARRSVECA
IKFFGIASEI PPSPETLVGW LLERPDHALC NSDTVSSFDG LSDTDSISEE VEDMTASHTE
GAVSSAGYNQ RSDFLSNDEY AMYIRDNIAD GMLVRCCKTY EEVHEGDVGR VLKVDNEGLH
DLNVQVDWQH KGSTYWVRFI HIELLGFPPS NPSLHPIKVG DRVKVKASVK NPKYKWGSVN
HTSVGVVTNI SSNGKDVSVD FPQQTNWTGI IAEMEIVPCC HQGISCDGCL MYPVTGPRFK
CKACDDFNYC ENCFYTKKLH RHSFNRIAEP GSAAVFAGKP GRYYRQDMSL ALNTGLIEDW
SKCIKTVSVS SRETWAHRLV DGSDNYWQSC GSQGKHWIRM EIQPDMLVHS LKMTVDPSDS
SYTPSLVVVS GGDSFTAMNE LATINIRNTD TVVSLLSDLK EYYSCIEIAI KQCKNGGIDC
KIHALNVIGK KRTTEGQLPT ALSFLASDND DIQQKGHVMD SRPELHTKVL VWGLNDKDQL
GGLKGSKVKL PVSSEALSAL KPIHIAGGSK SLFVVSLEGK LFACGEGTNG RLGLGHCNNV
SVPRQLTALS QYVVKKVAVH SGGKHAMALT LDGKVFSWGE GEDGKLGHNN RLSLDKPRLI
ESLKSKRIRD IACGSSHSAA ITSNGELYTW GLGEYGRLGH GDNVTQLKPK LVKSLLGHRI
VHVACGSRDA QTLALSDEGL VFSWGDGDFG KLGRGGSEGC NTPHNIERLN GMGVCQIECG
AQFSLALTKY GQVWTWGKGD YFRLGHGTDQ HVRKPTLVEG LRGKKIVHVA VGALHCLAVS
DTGQVYAWGD NDHGQQGNGT TIVNRKPAPV HGLEDVHVNR VACGSSHSIA WTTFNMQLPN
MHEPVLFVSS NDPLGASTLG IFESGAEDKS QVQQTNNTAN NSPHVSLSQI ILSLDSNISK
QHALQHVLNA LQVLHARDAV VAALSSHSNI AGFTSGGPTV KVRTPDSPPE GLASHSSSNP
LYEDGLEIAQ GGGEAPASVA EAVGLSSHST PESEQSPMAA FPSMSSSVSL SSRASKLSAS
AMSVIAATMT SNAQVVGQTE EADPLHPNLD DFTSLLGQDD ARMLVDLLKL AVAGRAIDTA
KETIVSVLVA MGSSCTDIRD MLLELCVTEL EDVALNTHSI HLAPQPVIQE SSHPYTDDAT
LSGHVKISGV KGLRVEFDRQ CSTERRHDPL TIMDGTGRTV SIRSGREWSD WSTEIRITGD
ELRWRFTSDS SVNGWGWRFT VYPIVTYAGP HELGSDRAIL SQPSVELVMC LLDARLVLSS
DRNLITRLAT ALASCAQLSS LAASQRMWAL QKLRKLMVSR LGKLLNIPAL LKMEQGLNTD
SALPTLVKGL PQALLRQYEY EDPAVRSGKH LMHSSFFKVL VALACDLGLD SLPCCSENHK
WSWFRRYCMA ARVAASLVNR TALPHGFCIE VRKKITEMIP ECDTTVWDHE NNEMFKQAHD
EQLLLWLHRR PEDWTLSWSG SGTIYGWGHN HRGQLGGVEG AKVKLPTPCE ALSALRPVQL
LGGEQTLMAV TADGKVYATG YGAGGRLGIG GTDSVMVPTL LESIQHVFIK KVAVNSGGKH
CLALSAEGEV YSWGEGDDGK LGHGNRSSCE RPRVIEALRG KEIIDIACGG AHSAAITCNR
EVYTWGKGRY GRLGHGDSED QLKPKVVEAL LGYRVMDIAC GSGDAQTLCI TDDDNVWSWG
DGDYGKLGRG GSDGCKIPMK IESLAGLGVI KVECGSQFSV ALTRSGSVYT WGKGDYHRLG
HGTDDHVRRP RKVAALQGKK IICIATGSLH CVACSDQGEV YTWGDNDEGQ LGDGTTNAIQ
RPRLVVALQA KKITQVACGS AHTLAWSTNK PVSASRLPVS TPLEYDLVRD FPLPTLRNRL
VLLHHFSELF CPGVAMFPID GEGSLDKLRG ILVSSTKEAA FKKVIQATMV RDRQHGPVIE
LNRIQVKRSR SKGGLAGPDG IKSVFGQMVT KMSLLAQEAL FLPHRVWKVK FVGESVDDCG
GGYSESITEM CDELQNGSLP LLIPTPNGRD DAGTNRDCFL LSPMAKSPLH MNMFRFLGVM
MGIAIRTGSP LSLNLVEPVW KLLAGMTLTP ADLTEVDRDY VPGLLCIRDM EPDTKVFQTL
EMPFSTPSAY GNEVPLSTRY HRIMPDNRLE YVRLALNYRL HEFDEQVSAV REGMAKVIPV
PLLSLFSGYE LETMVCGSPD IPLNLLKSVA TYKGVDVNAS LIQWFWDVME EFTNQERSLF
LRFVWGRTRL PQTIADFRGR DFVLQVLDKY NPPDHFLPES YTCFFLLKMP RYSCKAVLRE
KLKYAIHFCK SIDTDEYARV AMPGSGGASS NCDSDELESI ASDHAASI
//
