ID A0A0U1M565_TALIS Unreviewed; 1907 AA.
AC A0A0U1M565;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=PISL3812_07803 {ECO:0000313|EMBL:CRG90758.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG90758.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG90758.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG90758.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) 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 -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CVMT01000008; CRG90758.1; -; Genomic_DNA.
DR STRING; 28573.A0A0U1M565; -.
DR OMA; AEPLSQF; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000054383; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000054383};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1553..1907
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1086..1266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1347..1383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..256
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..849
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 850..870
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1086..1100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1124..1152
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1192..1225
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1249..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1874
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1907 AA; 210465 MW; 19854A969C064427 CRC64;
MARRTTSADH QDSLDPYPPP PAVSAPPSSS VAAFQVAAAA SPASRNTRSA ARNAAAESAT
NSTVDPAAIR STSQPSRKRK ATVRRDKVHE ETENPSQAAS PPRRTKRQRT ASTAPTHLES
STVASAPATG SRRPARNRPA MSQPSSSSQA SDAASRARAS SSNARRKSSR NSKTRLSDKD
ALPLRPGSRG EFSDSPFTAD PDARSSQSSH RRRKKQSPKQ SPDTPMRDTE DVPSDPEPTR
DDEDDEEDDE DAESSPPSES NDSTHPPGMM DDDDADPFRS GLFGSRTPLG LQNTLRALTG
MMTGMSSRLR DILGRLRMRD EPSMQLIALQ ELSDLLLVSN EDNLSGQFSP DPYVKELVAL
MQPSDFGEEN PEIMLLACRC LANLMEALRG SVTNVVYGGA VPVLCQKLLD IQFIDLAEQA
LSTLAKISVD FPASIVREGG LTACLTYLDF FPTSTQRTAV TTAANCCRSL PGDSFPVVRD
VMPTLLNVLS SSDQKVVEQA CLCVCRIVES FKYKPEKLEE LIEPAMLKTI LRLLLPGTTN
LIGPHIHTQF LRVLGIVAQA SPRLSVELLR MDVVDTLYQI LTGVSAPRDV EAGVKIDNVV
IMQALIHRPR EQVFESLSVI CELLPSSDNN DASSRFDDAL ATAGIRSRFG SQSSSKAKES
AEKRRALFME CKTELKRFAT VLLPTLTDAY SSTVNLGVRQ KVLLAQLKML QNIDANVIKD
ALRTVPYASF LAAILSQKDH PVLVSCALQC AELLFERLQD IYQYQFHREG VIFEISGLAE
RPLINENTAD SSSTKAGDEL GTPVRNTDDQ FDSRATSEDP SATRDDSQDE DNDEDDDDED
QDNDNDDMSE SESSTSFSIH RPLSQSMDSV MNDNVTTTAR AFLHMYEKSE TTKSTSEKAT
RILKELETLA SDIKSSYLGE STEDPVVLFQ KLATYFEGDA LENITSSELL KSGIIEVLLD
IFGSASSGRD ARTNFVQAFL STTIPEKSRS QISSKTPFSV LVQKLHDLFS RTEHFEVMTV
GHNSLENTRS NATYMLGKQV RLKLVADEAS DIPRPYKNMM VSIHAIATFK SLDDFLRPRI
SLSDRPRASR NRDLLSHLTG GERFRESPNA SQGPLDGEPR NPTLASSRAD TTPRQQRTSS
NSKNTSTTPR SPAAGRDRRH GTRRSSRNQP SNLDDDEPRD DRPLECADEK QLSDENNDEE
EIGDNGEDEL NAIVDDLEDD LSDDPGPEPT AVNMEIASTG KVTARKEDGT RVSTPSQSQT
LGRGSSSASA SALAALSGGG SLAMAGRPFS SYAAAMASVP QDWHLEFSID DHVIKNETTI
YKAIHHSREH IDDAGRNIWS AIHTVKFRRA PGPPPPEASS LGSGSEDEAA RDDKTDLPQS
LSKHSTTASI LQLLRVLHEL NAHLDDLIAE SKELIAVKAE PLSQFINTKL TAKLNRQLEE
PLIVASSCLP SWSEDLAREF PFLFPFETRH LFLQSTAFGY SRSMMRWQNS QPEDSRRDQR
RDDRPFLGRL QRQKVRISRS RILESAMKVM ELYGSSPSIL EVEYFEEVGT GLGPTLEFYS
TVSKEFSKKK LKLWRGNESD SRNDYVFGRH GLFPAPMSDR QAESESGKRQ LQLFKALGKF
VARSMLDSRI IDISFNPTFF RVVSSSFTPS LGSVKTVDRD LANSLLLVKR FVNAKKRVSE
DLSLSTNQKS QAVQDIEVDG VRVDDLGLDF TLPGYPSIEL ISNGSNIAVT IENVDTYLER
VIDLTLGSGV RPQVEAFRSG FSQVFPYSAL RAFTPNELVM LFGRVDEDWS IETLMDSIKA
DHGFNMDSKS VRNLLQTMSE LDAQQRRDFL QFVTGSPKLP IGGFKSLTPM FTVVCRPSEP
PYTSDDYLPS VMTCVNYLKL PDYSSLEVLR ERLIVAIQEG QGAFHLS
//
