ID A0A0L0HCH4_SPIPD Unreviewed; 2365 AA.
AC A0A0L0HCH4;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=SPPG_06169 {ECO:0000313|EMBL:KNC98468.1};
OS Spizellomyces punctatus (strain DAOM BR117).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Spizellomycetales;
OC Spizellomycetaceae; Spizellomyces.
OX NCBI_TaxID=645134 {ECO:0000313|EMBL:KNC98468.1, ECO:0000313|Proteomes:UP000053201};
RN [1] {ECO:0000313|EMBL:KNC98468.1, ECO:0000313|Proteomes:UP000053201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOM BR117 {ECO:0000313|EMBL:KNC98468.1,
RC ECO:0000313|Proteomes:UP000053201};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Engels R., Freedman E., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA Saif S., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T.,
RA White J., Yandava C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA Lang F.B.F., Roger A.J., Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Spizellomyces punctatus strain DAOM BR117.";
RL Submitted (AUG-2009) 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}.
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DR EMBL; KQ257460; KNC98468.1; -; Genomic_DNA.
DR RefSeq; XP_016606508.1; XM_016754372.1.
DR STRING; 645134.A0A0L0HCH4; -.
DR GeneID; 27689495; -.
DR VEuPathDB; FungiDB:SPPG_06169; -.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR InParanoid; A0A0L0HCH4; -.
DR OMA; AEPLSQF; -.
DR OrthoDB; 1093891at2759; -.
DR Proteomes; UP000053201; 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; 3.30.2160.10; 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; 2.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
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; SM00185; ARM; 2.
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:UP000053201};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 2020..2365
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 792..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1014..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1466..1546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1893..1920
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..816
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..835
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1120..1144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1152..1168
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1520..1546
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1570..1587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1603..1651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1893..1914
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2332
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2365 AA; 255712 MW; 38C2CD40B5569B66 CRC64;
MDSTDKLNLK VEQDPVATVS GNRRSARIQT SSNSSVTYPP QSTQQRSPRK RKSSEPNIGS
LSGSLESTVD WTRENNPASG PSSRRSSRLS SRTSSVSRET KSLSAASSRK GKGKAAGNTS
KIGTSQSSTS KRVKNVPQAS VQPPDATKKS SKKRRRPSIS SDEKESEDNP TPQEHVTKRR
RHAAVRASET ITSISSSGKK GSSTLEKVDM GKDKSKSKGK LKEGDDLQVG QHEVQAPQSE
RKKSNTTKEK SKGRRGKKND ESAAEASSGS KGSRGSEHDL AEDTAPTVKA SRKKRGRTQK
STSPDLSSSA SHTEEPGRSD DHYHESDDPS YDDDDDMDAD FGRDDVSGPT VHRSNLSTLF
GFGGGISIGG SGAMGGSSRF SSMLRQLKQK NDPTMQMVAL QELSEVLSMA TEDMFIGNGS
HNLAGFNTNE FVKALVDILK GPADMGGAFG ADFPLEVLDE LGMSASELGF GGGMGPNPEL
MLLACRCLSN LIEAHPSSTM HVLQHGAVQV LVGKLMEVEY IDLAEQVLSV LGKISQEYPS
AVVRANGLLA VLQYIDFFSL HVQRTALTIA ANACRGLNSV SMGGGITSRI MGGDSSASSA
NSDTGPQTVE QVFGMVKEVM PILERLLVYS DQKLVEQAVR CLGRIVDWCW KYEDKLENLV
TPSLLKTVIG LINPTGTASS GPVASNPHMF TQLVKLVANV SKGSARLGTA LIEEYGIVEV
IKNYLTGGFV GSSSEQDADT DMETVATAVT NVVVNRPVEQ VLEVLNLALA VVPSLPRDGM
WNTTIIKDET LVEGQPNSDS PTKRIGSIFS RGRSRSPEKN STSRDPMDID QRESGSVKDV
SSPAARTSSD SAESAMTESP TQNKKPALDE RDARRLELLR RQPEAMQKYA SQLLPIMIEV
FGATVNANLR RKVVECVAKG IWYLDQPEFL AHALAKNQVF GKFVSELLSL REIAFRKSVP
DKERKEALVL VAGGVQIALV VMNRCGEKFK AWFAREGTME ELVKIVAMND LEKEKEVEKK
DESPVQSPVR TETPSTHLPT PMGRRLSDLV KDLKRLRDQV AGHIGTSSTG TASSEASSSA
VGPAADKHSE VEELLETVEA LAKGSGEGTG MDERGDTTQK SHSSSSLRID TGRKDSTSTA
GGDAEAASEM SESGASVASP TSPGSSLLHG MRSMLERLGR GSHSTTSASR RQISTAGSVI
GLNGERVAET EMRSWIVAEC KSILEVCPAT PMSSEKAGLV LEDLRRLGAI LRGHATVDGD
DPLMLSVLHA IAEHFAGRKD TDTEVGVTGY EMLESGVMDA MADFLTKPGI PDVAAPDPDA
EKPRYTLPLT ARLKAFLHVF MNGPTPDPQN RPFFVQGAFK RLVQRLQESL SRVERFEVAA
AVPSSTGFSY EPIFGSMFGA SGGHLREASN PSMQLTRQLK VKLMAAEPDT VPRQYQALLI
SVHAVATYKA LEDYLKGRVA MAPQPTATRG ATEATKDGQE VGAEVSENTP ETPSRTVDEQ
GDIEMGDAAI TSADAQVSAG DDEADIEDED MEDEFDDDDD DDLDDDMLNV SDLLLHSEEA
RRRRRRGESF TSQASAVSDG HSEDTANQPD LSGRRDSVVD VRADMPSQTN TTAPTPASPN
IPSSTSSTPA SAPTSSLSST PSAASTTGTS TATAGRSYAS AAASSTNFTI EFSVGNIVVP
RDTTIFGSVY KLEQQKLGTT GAPPNVWGQV YTVKYRKVYP EAKEEGVKEE VQTTRNGSAD
RQMAVKLPFP TMMPEGISLD TSPGKILYLL RLLYGLNSRW AEVYANEDAE LDGVHEGGTS
ALPLQEGSQP MTRVAVTSRT DAPVSIDMLP PAAFANTKLT AKLNRQLDEP LIVASHVLPS
WCSSLAKDFS FLVPFETRLV YLQSTSFGYS RSMGRWQQQQ QQGNGGSGSG TGRGSADGAS
HLGRIQRQKV RIARQRILDS MIKVMELYGS TQALLEVEFF DEVGTGLGPT LEFYANVCRD
LRKKDGIAFG SGEKIKIWRD DDSLDSQAVK DDNRSTKAGL VPDDYLNPAL GFFPAPLTPA
EVDTEKGRKI LMLYKALGTF VAKALLDSRI VDIPFSAMFL EMVVGEEEEE ESAAEAALGT
AGRKGAEFHL LRHVDPSLYK SLLDLKKYVH IKRSLEADPT LSPAERAARI SNITVKGARL
EDLFLDFTLP GYPSAELIPN GKDIALTLDN LEHYIDRVVE MTVGEGVQRQ VEAFRRGFDR
VFPAADLRSF TVQELAVLVG GAEEEDWAYD VLIDSIKADH GYNSDSRTIK HLATFMSTLN
PIQRREFLQF VTGSPKLPLG GFKALNPSLT VVRKNVEAGK KPDDYLPSVM TCVNYLKVPD
YSELEVMKMR FEVAVREGQG CFHLS
//
