ID A3LNA3_PICST Unreviewed; 3268 AA.
AC A3LNA3;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 24-JAN-2024, entry version 106.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=TOM12 {ECO:0000313|EMBL:ABN64821.2};
GN ORFNames=PICST_81688 {ECO:0000313|EMBL:ABN64821.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN64821.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN64821.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
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}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00034494}.
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DR EMBL; CP000496; ABN64821.2; -; Genomic_DNA.
DR RefSeq; XP_001382850.2; XM_001382813.1.
DR STRING; 322104.A3LNA3; -.
DR GeneID; 4837043; -.
DR KEGG; pic:PICST_81688; -.
DR eggNOG; KOG0939; Eukaryota.
DR HOGENOM; CLU_000215_0_1_1; -.
DR InParanoid; A3LNA3; -.
DR OMA; DCHFSRE; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002258; Chromosome 2.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 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; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF06012; DUF908; 1.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF14377; UBM; 2.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 2932..3268
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 173..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1910..1947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1978..2071
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2090..2156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2269..2312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2396..2431
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1910..1926
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1991..2037
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2038..2052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2053..2071
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2101..2127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2128..2156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2269..2306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2413..2431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3235
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 3268 AA; 375085 MW; C5E4437883BEFDF9 CRC64;
MIVEKRDHLE RMEMAKPMRS LIDDLTSCSI KELPAKLEAN LKWEKPRGDL LHWVSVLNRM
DEIYEEIINK YDLENEFPRL QLFSQEEQTL ICSCLKFTYI LLDHCSDRQI YSSSERIFAL
LNTPTIDVRL HALEVAVLIS EKYAQSSSSR YSAPKQIKNK VLQMARSYPP IVPPSYAKAH
QEDPKAEESD KPSVMGDHFN FIDTLSSKKK YPSKWKSLEF PYYKTVLVND QKKSQQPGSD
RKKSEKTDKS DKSVHRSEGL STFHLSEESV RKLTLEQIYD KASDSIPKDS WFEFGLVASV
TKAFNTRSYE SIKLREKLLQ IKCLAIGFVC CMCSSQFTSS RLFEAEPYIF SFLVDLVSPT
NDDKVSTQVY YAATRALECI SSRKLWGSDI IRCMGGNVNH GILFQCIRHI NKMVRSEDPI
YFERGYIHFF NMLGNLINSK NLIPRLTSGG ILNDLMSFFD LRTKYRWSCS AAVHLTSNYL
KASPDSFEEF VNKDGFNLLI NTIRYEVNFA LQNPDYDGGA PTDAVVHYSI SFRQANYIKN
LMKLVSDLIQ SDSGDRLRNL FDSPLLESFN QVLLNPEIFG PLILSTTIDS VFFIIHNEPT
AFSILNEAKV VDTILDNFHT LFIPSGNLLV SLPEVIGAIC LNNDGLKKVK EKGTISTFFQ
LFQDLECSKE LVRSDMATNM GCSFDELGRH YPSLKPVILD ATKKLIEDIV PYANEKMAGA
RFYTSSKGAL YYSEEEEIIE NEEGKNEIEN WDSTDMAYIL DNVFFFLGGL LQDSGQWGTD
SMKVIPFQLW LNFLTMPNAP FDYITSNGVS TLLGILKYFD DEGREYGFPE LFSRLKEQLE
NPIIQEFLNF DDPSVSFFSR FEEEEEMGTM FIQEFNILHT LLYIMTEIYV NPISLFHERF
QQVLNVFGGT GLSTVTDVGL LLKRVVLEET IIRTNLPLEV CKQTERARSV APEIPPLPIC
ASEPSSKSLK QDFTSSKFKN TLQLRTFNHN FQTYTSSIFC SLGRVCSSKR PDFALTSWRR
DAVALTIEVG RVLSTIFDVQ IDNEYYWECY VLNIATVVLY SLTLRDRIKD SLYTSLAISL
FQNGFFEKLK DFAHRLWMKI LQIEPEEMKK TKEYSYISRD ESSVVKNALN SSLAIFVKCV
NTESFSNIPS AKLYFHTGYG KDADNRVTCA LLVQIRLVAL EFFQSIIGTQ VLETSGLVDS
RWGHPENIPS PVMEQVISIA KHVYLGRKET LDAEFIPLHV SNVSPPAEQV SYLVSLGMTR
SEADHYFRHL QDVRDIANKK WPDCPQFDIS EEQWEKYGQM IREENANFDL TFPTYRKSSE
LRELRKSGKN SLVVEFLAIA KQFPRTVDAI NEFFLTIFVD VQEVVGKIFE SIVYLVDIQN
DKGQNLAVSI HLLQLLLRNE RWSRSSGPIY EKFATFIASE IENHGELINE DYFSHSLTLF
EQILVFRDFP VPEPTEYNEI KYNDIVLPFV IDEEKNSQIF EGILNLKNFT SMTSVIAVTR
ILVLYARNET YVMRIIKSDL FKELITLPKL LSKNVAGVEL LKTPLVILIR RCLETTDVLH
SHFAEEVRSQ FGSSFKRTKD LRSFLREAAP CVMRNPEAFV DYISTCIRLE GYDGHPSFFE
DKLPIVRIKT QTVEDVEMSE ADEQKPVEEQ KVLGSSGVMY ILLKNLMEAV RSDWTTDTTE
ESNESVVTGT GNYNYICFLV KTIAELLGSY KQSKLEFLTF SRKPNTDEKV KPRPTALNFF
IHQLIPKHSL EKPSVIELSR RSMVSALAKL AITSLVSTPL LTEKTVQTIK DEDIEMSYIR
KYFVEILSRI FKDTANSSAV NTLKYGKLAD LFELCSSVIS TKYREEGGLQ LDSEGTKWDI
FFITKALLEK QIPGQITSIV ADLDLNYPDI DKVIKASLKT VTAIAKAKVE DSEVHEGEHQ
GDKEDDDIVP EEVDDREETP DLFRNSTLGM YDVDFDSDEE EDELDYFEEG PLEVLMSGED
ISASEDSSGL SDLDSDMEDE DIEDGYQEVE DINQDVSEDE LNEDLDSEGS IDDIEIIDEL
DLGSHSDRGD NETEEGDNES TDASDFYDFE DDGEVSEYDS EVLDGWIEEF EREDDSANEG
DESDLLARLG RNIMDGTRRR SRNADDNDNE SSGSISDSEG DDLEFNPSNT NRSVLDSNGF
PSPALAVLLD NFFRDADFAV QVNGIETRFD GNRDGSITRY FENVMRNRHK SDSDPVSHIH
IKSVKDRWND YLRIFYPNKN KDAILFRAIP GIVNRIESDS IDLFRRNKEE ADRKRKERED
KRRQQEEEER KRKEEEAHER ELHATNTTPH EPVIVRIADR EVDISGTDID PEFFEALPDD
MREEVFTQHV RERRANATST GSDAREIDPD FLNALPDQIR DEILQQEELA RDYGIHERLD
SGESEDEQEE WYEEPRFYSR NEETEETKKP KSRKVFYTPL VDRQGVSALV RILFAPLTIN
QRENVFHTLQ YLCYSKQTRL EVMSMLIAIL HECFTNQRTI EKIYAQICSR ASGSKEIKKH
SHLPVGSTTI SIGIQIIEAV DYLLERNTHL RYYILTEHEN PFILKKVNKK LKLKDFSKEY
KYSINYLMML LENNLVKNDQ TFMDILARVL QISTRPLHVL QKLESEGEKN EKKQAPPFPP
PVIPNSNFRQ IIKILTANEC SNTTFRRTIS AMQNLSVLSN AQNIFSLELS EQAAALGLSI
VGDLKSLTTE LTQSTSFNTE SKSFGKFSAA SSDQAKLLRI LTALDYMFES REKDRDIESD
AAALGKLGEI QELTDLYKKL GLGNLWDALS DCLRELEDKQ DLANVATALL PLIEALMVVC
KHSKVRELQI KDVVKYEAKK IDFTKEPIER LFFSFTDEHK KILNQMVRTN PNLMSGPFGM
LVRNPRVLEF DNKKNYFDRK LHLEKNENSK LSINVRREQV FLDSYRSLFF KSKDEFRNSK
LEINFKGESG VDAGGVTREW YQVLSRQMFN PDYALFSPVA SDETTFHPNR TSYVNPEHLS
FFKFIGRVIG KAIYDNCYLD CHFSRAVYKR ILGRPVSLKD METLDLEYFK SLMWMLENDI
TDVITEDFSV ETDDYGEHKI IDLIPNGRNI PVTEENKHDY VKKVVEYRLQ TSVAEQMDNF
LIGFHEIIPK ELVAIFDEQE LELLISGLPD ISVIDWQSHT TYNNYSPSSL QIQWFWRAVK
SFDNEERAKL LQFATGTSKV PLNGFKELSG ANGTCKFSIH RDYGSTERLP SSHTCFNQID
LPAYETYETL RGSLLLAITE GHEGFGLA
//
