ID G0RY44_CHATD Unreviewed; 4034 AA.
AC G0RY44;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=CTHT_0005350 {ECO:0000313|EMBL:EGS23830.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS23830.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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; GL988032; EGS23830.1; -; Genomic_DNA.
DR RefSeq; XP_006691072.1; XM_006691009.1.
DR STRING; 759272.G0RY44; -.
DR GeneID; 18254573; -.
DR KEGG; cthr:CTHT_0005350; -.
DR eggNOG; KOG0939; Eukaryota.
DR HOGENOM; CLU_000215_0_1_1; -.
DR OMA; ADEMKYG; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000008066; 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 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 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; 3.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
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:UP000008066};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3698..4034
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 220..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1531..1567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1588..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1980..2038
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2066..2107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2358..2407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2424..2554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2568..2598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2829..2924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3002..3029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3083..3103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3179..3211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3317..3387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3499..3520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 770..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1617..1636
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2013..2032
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2424..2448
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2461..2542
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2570..2598
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2829..2890
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2906..2924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3002..3019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3089..3103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3194..3211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3317..3338
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3339..3363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3365..3386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4001
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4034 AA; 450748 MW; 2D673082FCCD6D1F CRC64;
MGKITKTMQP RHKETLSPWL KDYVQTAASL PLPLIPQKLE EFPTRWPFPR GDLYHWIPLL
NRFDSILEAF CATYELNKGF QMRDFGCDLL MNKGAPVEYC DQQGWSKERL AQLGYGEDGD
CQLIVSILNF TRVLLQHCGN RSIYASSMHL NDLLNTTYLS VVYATLEVGL ELAQRYQASI
KRVAQPTRQV SSALLANHYN IDLDRVQVLS QPFVKTPVAP VAPRFPVDGP PQTPASASKG
KEKTSGSHKP PAPVYANDLT ALVAPGSPDD GRWNGWGDIK IVYYPKTDPS GTSAADASAE
NRPSPSTNVP ATPTPLRRSS TGPSQPSQHT PRPSRTSGVD ESPGSRNQEA NVDEHGPKTI
EIRQATVQSS SIYELLRLCP VDMPKVSRYE FLNRLRICKA LFGSTEDRQL AVAVRLLAIT
NLAYIHSENT FAEKVLKQDN DEPRRYQLVY QLAELIHPSV AGAPETPLWL QAIAFAALEA
ISVVPAKYAD VLSALNANVN HGVLLYVIRK AVASMREDPV EADEGKVTDA DHWRGSLFAL
TLHMAMSSRI GQEMASAGLL DILVEILNIR SKTATRNYSM VLAFLDTLVY TYQGAFSNFS
SAGGLDAISR LIVDTVAQSR DLVAQGLGTK PEFHAQLVDY EIPFYHQQTL KWLLKFIHHI
MTNAFSFGAN TDRLLRNLVD NSSLLRSLRV IIENTRVFGS VVWTNAASLL SDFLNNDPTS
FAAISESGLI QSFLSTLTGR EVTLPKPPGS PKPEQEGEDV SSPDYSDDSI TFEPDTRPHP
PTAEMLEEPR ENLAQGILAS SDAINVIPPI LNSISLNNQG MKMVVASNAL ESYLEIFESP
DHVQVMSLVD PDLAGVVGSS FDELARHHPK LRPSISNAVI DMVARVLHIA KTKAAAAGWG
AKLLVVDPTG QKVTADESLL ANLEGVTKGK GKATPDDMDV DMVDVIPPGP STPTGGDAEG
ESGLEKPIGA HHEITPYILA LAQFLGSIVT NSSLRSTFVQ DGGIELLLEL SEAPSLPEDF
DNTQASRTLS QVIAQLIESS PVLGIPSLLN RIHAAIDDLQ PLVSKERSQS FFAPFIVPGS
SLVNTQGEWD ATQVRKVASG TRVVKALVKL QTLVKTLYQS FPYASRQGMV TMPAVNAYDL
FRSLIRRLGP LLHGIITEEM AIAALVPQHW TGTKPVTQDG TELPAPPVAS SGIGDESKDD
SNITDTISNK KPAAATEPKK PTQEERSTVQ FQNYFVIHQL LHSLTPSTLP FFQTIGKTLL
LKRATDRDNH LRSYHLSIAD ALAETVLEQL KTSQDQLTAR DLHYWIVMFH TLREMLIEPP
RHGDRSVNAQ LILPVLVALK ERGGLEMLNA MLQKFSDEIR NGNPDGDDAH KVRLATVGMK
KILEIYHLIA NGKNVNDSLS QTSLYPRNMH RDRDYGHQLV VELRYAILPV VRKLWESDIA
EKAPTPVLSK IIDILKTIAA GDQELSAWRK SDKISPQPIF KNREPLRFPW ATHSNTIKSL
TEHFDEDLVR EAVYRANGKV DDASEYCRAH SKGIAGKRNP IPKEDEYQRT SSPKPQQPRK
HLDAEEEQQL RATADAMQFL RDMGEHVFGE SSDHSSDESH DHSSHDIGAE DSPIPVQEAS
SRATTKMETD SGPSSAAAAD SRPAWVTKED LDEERTKLQK DLIERCLDVV RAHPDSVFEI
SDLVDITLLR SDNEEKRTEV GEILANALMS FAMNDDVERR ENGQGISAYA HLLSLLLQNR
PFFESTLPTL KQNIEDYLGF LKVSPASSNE ELPSWLPYIL LIFEILLSDD QQPVEVHWKP
PVTDDEPLEQ PVWKVKEPSV SDEHRSSLLR AILDILPRVG KEESLAISVL RILVILTRDH
AMAKIVGEKR NLQRLFVMAK QSCSGGSARL NQTHISDNIM IILRHIVEDE DVVRQIMQTE
IRQFLSSAQR NPRSYDVYSY LRHLSHVALR SPKLFVEVTN DLVKLSRWVS LDTGISRGHH
SLALKEQPAE NPEPPKDGSV EPAVQATEDL TIEDVKPTTE SADKEMPDAP KGPFEIKRPV
LENPDGVIHF LLCELLNYRE VDDKELPVPT SKDQRAEGEP SSAGGDTVST SSDDQPSESK
EKDKKSLKPV FKAEEHPIFV YRCFLLNCLA ELLQNYNRCK VEFINFKRSA PMQTNTPIKP
RSSILNYLLN DLLCLGPAGI PLDSTAIKKK AATSNHAQAV LCALVARTPE KPIDRSRDHY
EYDDDPDLLF VRRFVLDTIL RAYKEASQPG EPIEIRYGKM MCAAELMSLM IGEKDRDAQP
RDNRGTDPVI VRSQMQLKRL MYEKGYIAAL TSSIADIDLT FPNVKRTIKY ILRVLRSLTK
TAYHLSQLDI IPATVTDQPE DDFLSSSSLS DLDDDREETP DLYRNSTLGM LEPGREEDFS
DEDEDDEDAM YDDEAYDDEL DYGDEMSQDE EENPSDDDEE ELDEMGEIEG LPGDPGVVEV
IMGENDDDVD EDMEEEDEEP SEEDEGDEDD EMGSDDMEDV EEQVEIVDEE GNPIDDDGAS
GWESATDEEG EEGDEDLEYE GEGQDMHDAV HGHGMDRIPD ILRTVVDGED LDGEDIDDHY
IDDGGEDDEE EDEDDMEDDE VYYDQGHHHD DYPPPNMPSG LGWDIAVEPG HRVRHGGVRS
PFPSGPLIMG HSGHDFRHFF GPSHHSRLIR APGDDGTNPL LLSSSRHAQD QITRASQQQL
IRLGFPPHAF GGPGMDGPLA IINDLMQTIP LSARAGAGIP VSLQLRSEGP SGEIRHLNIP
LGNMAQATRD TRREVYQEPH QAVAFIPQST AERWQEEAKI IFTSNHIDKS RVLANFILGM
LMPAAIKEEK EAKAREEEER RKREEERKKR EEEERKERER KEAEERAARE KKEAEERERR
ERERAEAEAA RATGQEGAAE EPQAMEGVES TTTQAEQAQP SAPRPRVLTT IRGETVDVTD
LGIDPDYLAA LPEEFREEVI AQTVSARRSE ARQQAADNGE NTEVFQEFLD ALPAELRMEI
EQQERQERRR REREEQRRQA AAAGQSLGPS DMDAASILLT FPPALREQVL LEQGEEILDQ
LPPDLAAEAR ALAQRHGLHR AAVQAARAQN AGRQPQATEP KPQRRTIVQM LDKSGIATLL
RLMFVAQQGS IRNYLFDVFA HVCENRQNRL EVISTLLQIL QDGSTDMDAV ERSFGQLSLK
AKQPKDNKDT KTPQSLKRTF TSISTSNQTT GSSEVSPLLV VQQCLDLLSE LATKNPHIPS
LFLTEHESVA TTLKRSLSRK GKGKDVSSKA HKFAINSLLG LLDRNLVMES SSVMQLLADL
LNKVTYPLQA LERRRKEAEE EAKKKAGKAN EEERAAAGES AETSNTQAST TTEQPSGQTG
EQQAEGVVKD KESEQKQDEK KVRQLIPPTI PDHNLKLVIK IFVARECSSK TFQNTISTIK
NLSSIPGAKK VFGEELVVQA KALSENIVQD LDDLLPHILK AESGTEIQGI ALAKFSPGAS
EQNKLLRVLT ALDHLFDNKK SNGESSPSSP ASPAEGKEIK ESTKDELLGS LYHNETFNVM
WDKLSACLSA IRQRENMINV ATILLPLIES LMVVCKNTVL KETAASQASS QTVLGKNMPL
STPPPEDRMA SLFFTFTEEH RRILNELVRQ NPKLMSGTFS LLVKNPKVLE FDNKRNYFNR
SVHAKSRDQQ RQQYPTLQLS VRRDHVFHDS FKSLYFKSGP EMKYGKLNIR FHGEEGVDAG
GVTREWFQVL ARQMFDPNYA LFEPVSADRT TFHPNKLSGI NPEHLLFFKF IGRIIGKALY
EGRLLDCYFS RAVYKRILGK PVSVKDMESF DPEYYKSLIW MLENDITDVI TETFSIEDEE
FGVKKVVDLI ENGRNIPVTE ENKHEYVRLI VEHKLLTSVK EQMEHFLKGF HDIIPADLIS
IFNEQELELL ISGLPDIDID DWKSNTEYHN YTAASPQIQW FWRAVRSFDK EEQAKLLQFV
TGTSKVPLNG FKELEGMNGV NRFNIHRDYG SKDRLPSSHT CFNQLDLPEY DSYETLRSQL
LKAITAGSDY FGFA
//
