ID A1CTM1_ASPCL Unreviewed; 1817 AA.
AC A1CTM1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=ACLA_083530 {ECO:0000313|EMBL:EAW06658.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW06658.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW06658.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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 -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
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DR EMBL; DS027060; EAW06658.1; -; Genomic_DNA.
DR RefSeq; XP_001268084.1; XM_001268083.1.
DR STRING; 344612.A1CTM1; -.
DR EnsemblFungi; EAW06658; EAW06658; ACLA_083530.
DR GeneID; 4700333; -.
DR KEGG; act:ACLA_083530; -.
DR VEuPathDB; FungiDB:ACLA_083530; -.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR HOGENOM; CLU_000366_1_1_1; -.
DR OMA; AEPLSQF; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
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 Ligase {ECO:0000313|EMBL:EAW06658.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1461..1817
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 705..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..762
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1080..1097
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1126
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1158..1188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1784
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1817 AA; 200031 MW; BA6769DE9C215B79 CRC64;
MSSRITRSAA RLAADPHSSS GSGPSPSNPA AGSAPTRKRK SQARRDRSLD APEEINPSSP
PRKTKKQRLT PSSQPAAAPA PTRRGTRNRP SMSQPGSSSN APEEPSTTQT SPPPSRRKSS
RHGGKISQDH LPATQSPPPR RQKKRASKMN PDVIMKEAEE EMESHDPTAD RETSPSDDSN
DGTTPSGMDD DDADLFHNSL FGSRSPLGLQ STLRALSGMM SGMSSRLREI LSHLRMKDDP
SIQLIALQEL SDLLLVSNED NLSGQFSPDP YVKELVSLMQ PNEFGEENPE IMLLACRCLA
NLMEALRGSV ANVVYGGAVP ILCQKLLDIQ FIDLAEQALS TLAKVSVDFP ASIVREGGLT
ACLTYLDFFP TSTQRTAVTT AANCCRNLPH DAFPVVRDVM PTLLNVLASN DPKVVEQGCL
CVSRIVESFK YKPEKLEELI EPAMLKAVLR LLLPGTTNLI GPHIHTQFLR VLAIVSKASP
RLSVELLRMH VVDTLYQILT GVSPPENLET TGVKMDSVLV MQALIHRPRE QVFETLNVIC
ELLPEVPDRH GSSVDRMLAS SAADNSALES KSTQGQQSAE KRRSLLMECT VELKRFAMIL
LPTLTDAYSS TVNLGVRQKV LLAQLKMLHN LDAALIEEAL RSVPYASFLA AILSQKDHPS
LVSLALRCAE LLFKRLEHVY QYQFHREGVV SEIVRLAETP LATDKQLKSS HDSPDLVPMD
ISSDSPRKPK SITSEDEAHD FDRQADEDDD DEQDDENEDI SDSESSSSFS SPYNTTRMED
ASKDLAIRDA RAFVELYEAS EAKAMRDKAL QILTELQHLA ADIEACYLGD GDGDGLPLFT
KLAYYFDGDA LESITSSELL NSGVINVLLD VFGDLKSPSM REARAAFLQA FMGSTISAKA
QSQSTATTPF SVLIQKLQDL LSRTEHFEVI TVSHNSLENT RSNATHMLGK QLRLKLVADE
DSDIPRPYRN IMVSIHAIAT FKSLDDFLHP RISLSDRPKP SRSRDTILSQ IASAARLRDQ
LTGGGEFHGS DLLNPSRASG STHQESGHEG SRAPDKSSSA ERPDPASRAK PSGGQLPAPE
GHNEEHDDEP LECADERHLS EDDEDEDDDD DEEAGEELNA IVDDLEDDLS EDHHHDPTAV
NMEVASTGKI TARKEDGTRV ATPSQSTPAS KSSASIPTMA ANPTGSSNSL ATAGRPFASY
AAAMTAIPQD WHIEFSVDDK PVSSDTTIYR AVHHNREHVD ASARNVWSAV HTVKFKRVGG
PPPPEPSTLT ANSVEASSGD GTEMPSSLSK DPTTAPILRL LRSLHEMNAT LDDILAETKE
LVALKPEPLA QFINTKLTAK LNRQLEEPLI VASSCLPSWS EDLARLFPFL FPFETRHLFL
QSTAFGYSRA MMRWQNSQNA EDTRHDHRRD DRPFLGRLQR QKVRISRSRI LESAMKVMEL
YGSSPSVLEV EYFEEVGTGL GPTLEFYSTV SKEFSKKKLK IWRENDCNND EEFAFGRRGL
FPAPMSEEQA ASESGKRQLS LFKTLGKFVA RSMLDSRIID ISFNPAFFRI ADSGSSVAPS
LGTVKAVDRD LANSLLLLKR FASVKKTIEG DKSLSKAQKS QALQNVEVDG VKVEDLSLDF
TLPGYPSIEL IDNGSNIPVT TDNVDQYVDR VVDMTLGRGV QHQVDAFRAG FSQVFPYSAL
RTFTPSELVM LFGRAEEDWT IETLMDSIKA DHGFNMDSKS VRNLLQTMSE LDTQQRRDFL
QFVTGSPKLP IGGFKSLTPI FTVVCRPSEP PYTPDDYLPS VMTCVNYLKL PDYSCLDVLR
ERLSVAIKEG QGAFHLS
//
