ID A0A137QTN9_9AGAR Unreviewed; 3585 AA.
AC A0A137QTN9;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 28-JUN-2023, entry version 30.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE Flags: Fragment;
GN ORFNames=AN958_03824 {ECO:0000313|EMBL:KXN90585.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN90585.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN90585.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN90585.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; KQ962043; KXN90585.1; -; Genomic_DNA.
DR STRING; 1714833.A0A137QTN9; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
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 CDD; cd14297; UBA2_spUBP14_like; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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 InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
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; PF00627; UBA; 1.
DR Pfam; PF14377; UBM; 3.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50030; UBA; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1245..1285
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 3250..3585
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 196..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1222..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1287..1348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1659..1682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1723..1746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1971..2121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2403..2515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2592..2617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2654..2677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2894..2940
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1229..1248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1298..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1662..1682
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1971..1990
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2033..2082
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2095..2121
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2403..2436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2897..2940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 3552
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KXN90585.1"
SQ SEQUENCE 3585 AA; 397640 MW; D028C7B388C3E452 CRC64;
PTVVAEFIKK VLNVSDEQLA HVLASVESWK WPRSDLNAWT KVLNKFDSIL EDVINQYELD
KVQLINFPSQ TKALVSEILR FQRLLLENST NRKTFSSYDR LNSLLLCSDL DIVLLSLNVL
LRPAQQYSAQ SSVSHILSFT TPRLLALAKR WPFLREYGIN LIDLVSSKSK AEVEGLPADT
REVSFSFYKT DAGVRSSQEK KKEENELLAT PSKSQGAHTA SSSGPVNVLI SEATLSSESP
MKILADSVRT YEIPDEEKFE LLNRIRVSQA LFKDHESERE KLVIARLLSI AIYAHTHTES
QATTSFFLYE PDLIANVAEL LQVDPVQTAA IAVLDAFTRY RNRCQEVLTA VNAGVNHGIL
MALFRKTVNE VANPSSDIPQ SCVEALLQFV TLIATHTSGV NMIVGAGLIP LLVQLVDSKL
PNRLVIVSKT LQLIDSVLYS FQNGFSLFCA AHGVNVLVER IEYEVDSDIQ EHGRWSKSLD
ISSTGNDLPI PRSSVLKHLL RTMHRMMQSS GTSEGLRGLI DTSLVKSIRK IIDNRVLFGP
AVLPLAINIM ATFVHNEPTS LGIIQEAGLP EAFYKAIEAG IEPAIEVIQS IPNALGALCL
NEAGQIQLSN RPSIIPAIFA IFTSERHLKV LIDKENAVII GTAIDELVRH HPLLKAAVFT
ALKSILSTIE EIGKSYQVQD DLLHWYQLVP TASDSSDGDV KMEDARPVST QSTETEMVDI
SVGEALNSTE EAVLKSHDNT VVSFIDVLCR FLEGFFQHAP HCSDFITLSD GLRFIGRLTN
LPCLPYDFSN SVASDSLVQV MRTLVDSATN ETLLYLAEIV RESLQDTRAF WDVSQTSSEL
LPLLELNAAN REDHNSNFRS LVTLHIRTAL LSDVFGTIGY SHGRGAFALL QTLMGSCGSR
TIPELGALHR ATIWENIVLN AALSKKGIPQ SSPSQSPLGA SPNLSTTNLV EAADALNTGA
STANGIQSGG DTEPSGVEST NSKQDESPIT RNAAALKYLT HGIPNVLAPF FQSIVKMFHA
RRSLEASQKK QIQESASTVA KVLLSHLQIQ KFDDVPSVYT YYSVIFGLYT LLFVDERTST
NTLHTVEVHA FYQIGGFDEV LRVCTTLTKS IEEITEVREE DRSDFFNKTL IHAYGGLKVA
LHLLHPIISA KPLFESPQTL LLITRDKKET DLGFFDPNSF LVRLRFKVTP LLRSLWEAPW
LVQAPLGVSR SIVRSVLELV HGENEQSKPE TTTESAVPNI TRPTGPDENR VQTLVDMGFP
RHAAERALVQ TRNNVTAATD FLLSHPFAFP EPAQPQPPAT QSNDTAGEPT PEENAEQTAE
TPGGTPMASH AEAGLSQPEE DSTEEVKTIE EWKRALDEAR TPLQGLISRQ ALLLVDEHQS
LLFELRAAFV WASPNQSQAV RDLVDDVKSF SPYAYDVQEQ PLANRCRLLA LVFCENPSSL
NEGLRKELLD SLLALLLSGI DPENPPKWLA SHLLVTEALL ILAEEPCTIT LPKEDEPINS
QPLSIGLHRS DAKDIIPEFC LRLLAVRDLA SDEFLSVLRL LVHFSKDKKT VKQLLEGNGL
THLFKRLAAS EITGGSSYVI TILRHIVEDR VTIRNIMSES VKRYFQHPRN NTVDVNTYVR
TCNAMAFRDS GVFLDVTQSL CSLSHPFGFN PQIALKVSES GEDKATPGEK DVTQEEKKEE
GVDMEMRVDQ PAVVPVANDS YAENVIHHLF TELMTTIKSI HETPTSSSAQ VPDASRVESN
TSTQTPGNTN DKYQYACFLM QCLTELLFSY DTCKLAFLSF YPKKKAQTPA KESTSKFRSM
TLQFLFNDII NPGTINPSPS DSNRQHLSLC NWAMLMIVSI CVDTSTSPHE PKDISPELVA
VRKFVLETLS RSLKDVSTVE NIQVRYGKLL AYADLCHRLL TVRFNNTTTS GRKQQDEIPT
HLAKIMLEKN YVSTLTNALT EVDLNYPHIR TLVDFILRPL QYLTKIAIKM SRGSKNKDSP
DTKRDDSESS SLSPEEDEAS NMSEDETREE TPDLYRNSAL GMYGGEMDDG HYSGSDEMDE
DEEDEGDVEM EFDGTGSEDT SEATEEEEED ELGEDEDEAE EDWHTAGAER QEDQDLVENT
EDDEDDEDDE DVIDDEVDEE VDEDGNLLWE SFEYLAHFEA QDVPPPGGGL GPIGEDIDDE
DDHGVPIQII HHEEDLDMAS DDEGFRFEGE VFGAEAGLPF TAPFINIAAG RDPPPVFLSR
RSRSDNEDIQ VFGRTRNAPA PPPETITHPL LLDTTTNSTR LPPNVRRGAR YNHRNVAVGA
DLFQNLDEIM GPGSTQFLQH ILTAGGAHAF QLDVGNMMNL DRGHRRPTHG VISAAIRVER
GPGPRAQSPR QGREFDPLLT LQRWAEEAKI LNGDFVSERS GKLVNHVILA LLPAAAEARK
KAKAAEEAAE RDAAREREEE RLRQEAETKQ EEERARAVAA TTPAPDATVA TDVERTSDAS
AAPTSVDEPA IEDQAMEVVT PDQDTPMDDV TAAEGRGATP AEDGNAGAST SSQPPQRITV
LIHGSAVDIT DTGIDPTFLE ALPDDMREEV LNEHVRDQRA ATIERPADSQ ISTEFLDALP
PEIRAEIIQQ EAMDRARQRA EESASAQPGQ PADIDPASFI ASLDPTLRQT VLMEQNEGFL
QTLPPHILAE AGGLADGQRR AAHRTTARST GVPPAAPRKF TIDHDAIQLL ERSGIAALVR
LLFFPQVSKK NLLFKVLVNV CENAKTRAEL FNILLRILQD GPADLAAVDK SFSQLTVRGT
SKPQTPKSVG KQKASDYFTT LMTSPSTRTE AVPDLVVQRC LESLTYIVSS NELASLFFMT
EHELPAGLRK VSGKKGKGKE KQAPQTHYPI VLLLGLLDRR SLIRTPAIME SLVGLLATVT
KPLASLKPKE ADVLPPNSTI TDATPQTIPA TSSGASTTEG EGQASSNIQP APNQTTATAT
LTKDSKPTLE ALEEKILLAN PPQVPHAVLR LIVNILTVGE CSGRTFQQSL ALIQHLSYIP
DARDVIAQEL RSKAEEFGHA LHADLNELVT ALQGSQDSLN AVAAKFSPAS SLQAKLLRVL
KTIDYMYSSK APSLNTTTEA DIDRVQTIYE SFRFTPLWQR LGDCLSIIED KPDTEHIAIV
LLPMIEALMV VCKYVGSRTP SAIPRALRGS MSPRTPTTPR ESMEDLFISF TDAHRKVLNV
MVRNNPSLMS GSFALLINNP RVLDFDNKRN YFNQQLHRRP ATREHYGTLQ LNVRRARVFE
DSFQYLQRKT GEQIKYGKLS VRFYAEEGVD AGGVTREWFQ ILARQMFDPN NALFQPCAAD
KLTYQPNKNS WVHSDHLSFF KFVGRVIGKA IYDGRLLDAY FAKSLYRQIL GKPVDYRDVE
WVDPEYYNSL CWILENDPTV LELNFSVEAD EFGVNRIVPL KENGEAIPVT QENKREFVQL
SAQYRLYSSI KDQIENLLNG FYEIIPKDLI TIFNEQELEL LISGTPDIDV DEWRAATEYN
GYSSSDPNIV WWWRALKSFN REERAKVLSF ATGTSRVPLN GFVDLQGVQG VQRFSIHRAY
GEPDRLPQAH TCFNQIDLPQ YSSYEMLRQQ LLLAINEGGE GFAFS
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