ID A0A177BZ07_9PLEO Unreviewed; 1837 AA.
AC A0A177BZ07;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=CC84DRAFT_1222269 {ECO:0000313|EMBL:OAF99928.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAF99928.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAF99928.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAF99928.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-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 -!- 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; KV441560; OAF99928.1; -; Genomic_DNA.
DR RefSeq; XP_018030294.1; XM_018183348.1.
DR STRING; 1460663.A0A177BZ07; -.
DR GeneID; 28766834; -.
DR InParanoid; A0A177BZ07; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000077069; 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; 3.30.2410.10; 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:UP000077069};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1482..1837
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1280..1309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 735..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..776
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 777..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1088
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1113
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1179..1198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1804
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1837 AA; 201175 MW; 8000D7E100CF4A3C CRC64;
MSSRVTRSSA RQSSGSSPSN QPNPPAPPPP PARAGSTRKR KASAREPSPD EPPAQPEPPA
RAGRSKRTKV EQQDPPAPSA ARSKKGKGKS AMSTPGQPTD SPEEKAQPSS SKRGKSNRRS
GGQGDEPQRP PKLPTAKPGT DSAPSSSSRR GSRKSNAKND DDVAMEDAPG MNETPQGGSG
PGRPDTSDGS NVDGQDIHYD EDEDDDDDDP FGSGFLGRHP GGLSALRHLT GMAQLMSNTN
NRLRGILEQL QSQDPTIQMI ALQDLSEVLL ISTEDNLAGH FSPDAYVKEL VKLLQPNEFT
GEENPDIMLL ACRCLANLME ALPQATANVV YGGAVPILCS KLLEIQYIDL AEQCLSTLEK
ISVEFPASIV REGGLTACLT YLDFFATGTQ RTAVTTAANC CRNIPEDSFA TIRDVMPILG
NILKNNDQKV VEQGCICVSR IVQSFKQQDS KLEELVSPEL LRAILGLLLP GTTNLIGPNI
HTMFLQVLAY TAKASPRLSA ELFKLNVVDT LYQILTGVSP PAGTEDIATK IDTVVIMQAL
IHRPKDQVFE TLNVVCELLP AVTREDLTYL DDLVDAGYPG ENAPPLSASR TSNAAGDNRL
ELLEDCKEQV KRFAVILLPT LTDVYSSTVN LNVRQKVLTA QLKMLSNLDT DILEESLRAV
PYASYLASIF SQQDHATLVT YALQAAELLL KRLEPIYRYQ FYREGVISEI AKLASRPCKT
LELRPKGSRT TIEVEAAADS NASSSSTGEV DMDQDIEEEI DVEVHSEDEE DDHGNDDDEP
HDHSDNREDD DDSDSSSSSE HYHPPPMPNA EDIITLRAKK FIEVHENDDA KAIRDKATDI
LETLKSLATE IRQCVLQGGS GNCIELFTRL AAYFEGDALE SITSYELMSS NIVDVLLDVF
TTEPAKGVEP HALFLEAFMG TSSKNKIKTA SSASPATPFS VLVSKLQDLL SRAEHFEVIT
VHQHSYDSRG SATSMLAKQL RLKLMADDES GIPKTYRNMM VSIHAIATFK ALDDYLRPRI
AIAERPRPPR ARDAAAYAQA LAEGRLPVPP PPHTPSESTN RSSARKSKAK TSASTPSVQA
GPSSASQEKP RRSSRRQQAQ PPPPPPPPPQ LNSDHDPVEC ADEERLSDPD SMDESSALNA
IMDGLDDDMD EDQPDPSAVS VEVAPTGKVT ARKEDGTRVA TPVQSQTPSR PPAQERMSTP
SRLSSLLRGA AAHQGLAGAL SYAAAMQSTP QDWHIEFSVN DQPLSNDTTI YRAVHFSQGQ
PGDAPHRTVW NAIHTIKFKR VSGPPPTESS SITPPLESKS GTAGIPQSLS DHPITTGILR
LLSILHNLNA NMDDLISDNR VQLKANAEPL SQFVNTKLTA KLNRQLEEPL IVASNCLPSW
SEDLARLYPF LFPFETRHLF VQSTSFGYSR SMTRWQNAQP ATDSRHDRHR DERPFLGRLQ
RQKVRISRAR ILESAMKVMH LYGSSPSVLE VEYFEEVGTG LGPTLEFYSS VSKEFSKKKL
KLWRENESSG DDEYAFGKRG LFPAPMSTAQ AGTENGTKIL ELFKTLGKFV ARSMLDSRII
DVSFNPTFFR VGDGTVAVAP SLGVIKSVDY DLAKSLKLLK QFADAKKQIE GDDSLTAAEK
ASALKDVVFQ DCHVEDLGLD FTLPGYPIEL VEDGADKQVT IENVEMYVEK VLDLTLGSGV
QRQVEAFRAG FSEVFPYSAL RAFTPDELVM LFGRVDEDWS LETLMDSIKA DHGYNLDSKS
VRNLLQTMSE FSATERRDFL QFITGSPKLP IGGFKSLTPM FTVVCKPSEP PYTSDDYLPS
VMTCVNYLKM PDYSSMQILR EKLRVAIQEG QGAFHLS
//
