ID A0A0G4LNT0_9PEZI Unreviewed; 2714 AA.
AC A0A0G4LNT0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=HECT domain-containing protein {ECO:0000259|PROSITE:PS50237};
GN ORFNames=BN1708_013775 {ECO:0000313|EMBL:CRK23713.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK23713.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK23713.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK23713.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CVQH01016113; CRK23713.1; -; Genomic_DNA.
DR STRING; 100787.A0A0G4LNT0; -.
DR OrthoDB; 5471864at2759; -.
DR Proteomes; UP000044602; Unassembled WGS sequence.
DR GO; GO:0004865; F:protein serine/threonine phosphatase inhibitor activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011107; PPI_Ypi1.
DR PANTHER; PTHR46434; GENETIC INTERACTOR OF PROHIBITINS 3, MITOCHONDRIAL; 1.
DR PANTHER; PTHR46434:SF1; GENETIC INTERACTOR OF PROHIBITINS 3, MITOCHONDRIAL; 1.
DR Pfam; PF02492; cobW; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF07491; PPI_Ypi1; 2.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50237; HECT; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1112..1459
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1547..1584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1992..2011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2202..2249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2429..2450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2475..2525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2540..2576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2694..2714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..184
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..548
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1563..1584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2202..2239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2494..2519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2550..2572
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1427
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2714 AA; 298531 MW; EB13A5A1B3D5A409 CRC64;
MASAAQRPLQ RGSPAPSQTQ TVTAAPVRPN TRQTTLRLRG AHASSRPSVQ WADDVVDNEG
LGRKKSKVCC IYHRPKGIDE SSDESSSDSS SDGSDSENES GRRRVPDGDS KGKGKAKPHK
CDDHDHDHDH AHHHGRADKR GGDKGKEKRL PSPNAYERIP KPPKTKNDQG ENTKKHDKDK
QTWRRMAYIG YPAPLNSSLF LFSRSSDFRI SHTTMSHSHD DGASHSHSHD ASISAAEHGH
SHEILDGPGS YLGREMPIVE GRNWSDRAFT IGIGGELARL SRHDFALEDS QANADSSSSE
SDIHPSRPRR RPAHSRSMSV PFPSLFSSRK KQRPDPVHDD SDDSHNDPPV TRSAAKTHTR
GNMSQGNRDF ATGNCMTCNS LVRWPRDLKV FKCTVCVTVN DLSPEEHAGT NRSGGVPQWL
RGANPSTSCS ASPPDQPARP VDKSGTKEIS LEHTKSLVHS CLQKYLVQVV RQGKAAEKQR
GPSSGHPHSP IAQDDHSIGH RIATNPATPD SVSQRTQKEE PATYMFSEQP TLRQNPHQQS
PRSYSSSYPA RPLVHSIFGE ESIRPAAPLQ PEIDGKRLFK PLEDYLVSCF SSLQCVNSSF
LPSRPHYTAR PESDDSQPVF PAQSTGDATR SVFAPEPKGG NVRRQTAVAR SDPKCAESQS
QLVDLDPKLL LLGNFAENGM WWTGNQRESQ QHAQSKGRKT SEAAHSVVSM RCPQIEWDQV
ASWFSIFKDL TSGFLTFRLI RQNEKKYEAK VDVIEGLIPN MSTGRSAASL HAALGTSSSS
KKKPKEQPKK MTRRCNHAGX TDPEDMRFLL ILLENPLLYA IPSYYRGSKQ SGTGGSRGGK
NGSDSTHARG GPISGQHSVV IKRILGLMSN ASNSCHTHLI AWFARYPESR FSIFKDLTSG
FLTFRLIRQN EKKYEAKVDV IDGLIPNMST GRSAASLHAA LGTSSSSKKK PKEQPKKMVY
HDDWQIRAAA RVLALLFAAN NTLGVRRADA TMLGNSSVVL REGVQVFGQV LPTSDFYNSM
IDYADLIADF EAWETKRSKF AFCQYPFLLS IWAKSQILEY DARRQMTTKA RDAFFDSIMT
RKNVTQHLTL DVRRDCLVED SLAAVSEVIG SGGEDIKKRL RIEFRGEEGY DAGGLRKEWF
LLLVREVFNP EHGLFTYDEE SQLCYFNPNS FETSDQFFLV GVVIGLAIYN STILDVALPP
FAYRKLLAAA PISSIPSSAH PRPVMTYNLE DLAEWRPRLA AGLKQLLDYD GDVEETFGLD
FVVPVEKYGT VLQVPLCPGG EWKPVTNANR REFVDCYVRY LLDHAVTRQF EPFKRGFYTV
CGGNALSLFR PEEIELLVRG SDTALDIDSL RAAAEYDNWG TKNPDGTEPV IGWFWDTFKS
AKPSEQRKLL SFITGSDRIP AMGAALLPIK ISCLGEDEER YPIARTCFNM LSLRRYGSQE
RLEHMLWTAV HESEGFGLKR SLSRFLSSIV AFCFFLSTAP WRSISSTSFI SACSSGVGRT
GWAPVSARKR AKISSERWFF MSILTTRSSA AGGAALEVSM PDEGGWMRTA GSAPAAAASE
RKFPETTPTS NTPDDSWQNE TVASPAMHRA LSSRWLRSAL RIGDRAALAE VPGYLCPALS
LSAQRGRGVA HQMTVAHGQR RCLHAESNLH ESNLSESLER LPSDPADANA LALAKLPLQC
HGCGAFTQTT EPDQAGYYDL NRKSVQKFAA SEHEYEIKKG EIEEDFVVTK ALEGLDEHKL
QELNLDPRTL LAGEDLETDI PSFPPAPNAT PLCNRCHALV HHRKGTPIFH PSVDALRETI
EESPFKNNHI YHVIDAADFP MSLVPKLHQL LGDVSLRRRN RRSRAGRYYK DRKFDMSFII
TRSDLLAPTE KQVNALMPYL REVLRSALGE FGDVVRLGNL KCVSARRSWW TKDLKQEIYK
RGGAGWMVGK ANVGKSQLFQ AVFPKGTTAD IPFKNAVEVS MFSREEEDEN LKYLDDGAEN
YDERLDLDAL LPPARPESNY PEMPTVSSLP GTTASPIRIP YGNGKGELID LPGLVRSDLE
LFVQEDKRQA LVMQDRLKPE QHSIKPGQSL LLGGLIRITP RTPDLIFLGY NFTPLPEHLT
STEKAVAFQA QTRTAAQVDN ICTPDAADKM QLAGSFPLRH DVTKLRAGPI TRKNAINIKV
ENLPYRVLST DILIEGVGWV EMTAQVRARQ LFAKPEAKAA EPVVDDTSED KPQDPFDAIL
SRVHGAEKER PKEPPVADKK TNSKAGGLDG PAELNWPVVD VYSPLGKFIG VRAPMNGYML
NKPRVLAKHK KARPRRSMKG AKKRDKMARR HAAAASASAS TRAINGLPGR DQLAEACIER
LGVQTLLLQL LQLLELRLSS RGLELPPRLP PDGDESGLAQ VKLGVGGGAL GVGHGAVVGL
EAVEVEGGVG GRGSCEVAAA AGTASVRPNT QQTTLRLRGA HAPSRPSVQW ADDVVDNEGL
GRKKSKVCCI YHRPKGIDES SDESSSDSSS DGSDSDNESG RRRVPDGDSK GKGKGKAKPH
DFPNIIPFLF SRSSDFRISH TTMSHSHDGG ASHSHSHDAS ISAAEHGHSH EILDGPGSYL
GREMPIVEGR NWSDRAFTIG IGGPVXXXXX XXIDVSGGDK IPRKGGPGIT QSDLLVVNKT
DLAEIVGADL GVMERDARKM REGGPTVFAQ VKKDVGVDHI INLLTSAWRA SGAEGNRKAA
GGPRPTAGLE ELNA
//
