ID A0A1Y2HMQ8_9FUNG Unreviewed; 1948 AA.
AC A0A1Y2HMQ8;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=HECT domain-containing protein {ECO:0000259|PROSITE:PS50237};
GN ORFNames=BCR44DRAFT_48723 {ECO:0000313|EMBL:ORZ35839.1};
OS Catenaria anguillulae PL171.
OC Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC Blastocladiomycetes; Blastocladiales; Catenariaceae; Catenaria.
OX NCBI_TaxID=765915 {ECO:0000313|EMBL:ORZ35839.1, ECO:0000313|Proteomes:UP000193411};
RN [1] {ECO:0000313|EMBL:ORZ35839.1, ECO:0000313|Proteomes:UP000193411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PL171 {ECO:0000313|EMBL:ORZ35839.1,
RC ECO:0000313|Proteomes:UP000193411};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORZ35839.1}.
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DR EMBL; MCFL01000020; ORZ35839.1; -; Genomic_DNA.
DR STRING; 765915.A0A1Y2HMQ8; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000193411; 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 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; 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; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000193411};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1586..1948
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..565
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1194..1328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..103
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..121
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 534..552
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1058
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1228
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1252
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1310..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1915
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1948 AA; 204095 MW; 3FA363F31BAE1D34 CRC64;
MTSKTSAPSS FIASTPLRRS SRIASTPVPA VTPSSTSLSQ SLSQTKRGGR GVGRKAAAAL
RDLDSDSDLS SLSSSHSDSN SQSESDREAE LSDIGDLKVT RRKSSTKAQV THSRKRKLPA
SKTRTQQQGL EPPTKRSRHS APKTETASTD SPSRAASLSA STTTSAPLGG RRRSARFTTE
QPSTPTAVPT TAATATVGIT SASQSQSAVK KAKTKAKAKA KATARNARAD PSASSSSSSS
SSPIHDVIKL PKSSTSKHLQ AFKTQSTPKA NTPSAAARTS TRASTRRTRS SSSSSAMSAE
PTDPTIQIKS STDSGAAATA ADSSAMDVDP PSPAAAASSA APGSSAASSS SSSAPAAGDT
ASPTTPSAAT ASPLSPLSAL AAALSNASAS GPGTSSTSNP DPSSPNSILT ALLNSASAAG
GGPLSPTSQS NAQAALLAAM QQAAASASSS SATSMFGGFG GGGGLRVSAQ IRQLATTFKS
LAANLSQAED PTELYMALQQ IPELVLMNAE DTLAAVCMCT QNEYANAAAS QHDDQDQDED
EDNDEQDEDD EAALPAAAPT GTGPRNVIDH LVKRLIPLIA PTSAPTSDAI SELAYAMLGT
EVAVLAVRCV KALLDGLPSS GIAMLVRNRA PVALVTALGD VQYMDAADGV VDVVHHLVTG
GVDGAAAASL GGYLGAGGAT RTAQAALVDA GAVPVLVKYL DFLPLPSQRR AIQALAACIS
SAAGAMAFTQ DKHTWRAVLH LVSAPEGVVD AQLQKAAVGV WMNVVKYAAN VAEALMPRGD
QAGGEETPLA VLAKLVRENR EVTALLKVAC HRDAAARAAT AGASPTSADS SSNDDNKGVA
HALVQHGVLD LLLSPPAEAS ATTDQGADDQ NKQPTTAAAT AKFTLTADHI ALLTALVDAE
VQSTPGSAGN ADRAAQLVEC LLDMPDEVPG PVSATAMRPT FASIMNRGSA ASAAPTVAPH
WSLLLHVVQR AVQAGNAGAQ VVSPGLIDRV IAAIARGTVP KDHALPLVLV DAEPERCRRH
GLAEVVDEQQ EETMTKEVKQ VSPESPKSPT STTTAPAKKR SVRIDAPPAP LSSSTARIAD
LTAWEFMHLP WVQSPTACAV PTTLTPEDVH AAHSHIHVLI ARHLTQLPLV FDPRVSLRGP
GGALVSSQGG ASGEVTPEIV LVGVRVNVVA PVAVADRMGM GVAFGGIGRA AAGTGGPGGA
DGEMVQSEVE SEDDHHEDDE DEEDEDDDHH HSPDVQMDED GEMDDEFDAG IDGDGDIAMH
DVLPASASEA EDDDEHAEYA GGHGSETQQE SQATEAVPDL DGAQIEPPTT PIIPSDQLAS
GEDAPTTAAQ EEVEQVVEMG PFQIQAVARV RDVYRSLGID MAKWVITHDG RALELDDAVF
RPLWEHVQKL HREKCKADGK PVTVCPTEDV FRKQFRFQVV AKDKAPADAA AKEQQQVGEE
LAKSEAVAAP MCALLECAAR LNAQYHGLGA RPSAALVRHV QRQMNQVLLA STQSQPEWLA
AVVQGHFPLS RPPTDSAANH QEQQDSGMSS WRFLVPFATR RHYYACHCLG YARCLLRVAP
QAARLGKIPR QKVRIDRPHI LSSAYRTFDL FGAEYSMLEI EYRGEVGTGL GPTLEFYSLT
VQEIANRKDL WQTAAVPFLL PRGASVTDAE VDQVRAESEK PQVDKKMVPK DKLTHAHILF
LLGQVMAKAL MDDRTVDVPL HPAFLKLVFS QQPSAADMDG LRAVDPVVAK SMQAVLDMSD
PSALHLHFEY DGKPLIPGGE DVPVNTAEDA RRYVALVADR VAGVEGLGAA ARCVRLGFER
VLPVAPLASL FSADELLTLF SGSATEDNQY WTHQALLSPG GMQADHGYSL DSPAVRWLVD
WMVALPASDR RTFLTFLTGA PRLPLGGWKA LRPKFTVVHR SAPNPDTYLP SVMTCANYLK
MPSYSSRELL DQRMRMAMAE GQGSFHLS
//
