ID L8FQ12_PSED2 Unreviewed; 4091 AA.
AC L8FQ12;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN ORFNames=GMDG_05560 {ECO:0000313|EMBL:ELR02594.1};
OS Pseudogymnoascus destructans (strain ATCC MYA-4855 / 20631-21) (Bat
OS white-nose syndrome fungus) (Geomyces destructans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=658429 {ECO:0000313|EMBL:ELR02594.1, ECO:0000313|Proteomes:UP000011064};
RN [1] {ECO:0000313|Proteomes:UP000011064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4855 / 20631-21 {ECO:0000313|Proteomes:UP000011064};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C.A., Blehert D.S., Lorch J.M., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The genome sequence of Geomyces destructans 20631-21.";
RL Submitted (SEP-2010) 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 -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00034494}.
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DR EMBL; GL573288; ELR02594.1; -; Genomic_DNA.
DR RefSeq; XP_012743990.1; XM_012888536.1.
DR VEuPathDB; FungiDB:GMDG_05560; -.
DR HOGENOM; CLU_000215_0_1_1; -.
DR OrthoDB; 164548at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000011064; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
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 InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF06012; DUF908; 1.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF14377; UBM; 3.
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:UP000011064};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 3755..4091
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 205..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..971
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1556..1624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1653..1686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2020..2064
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2096..2154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2392..2647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2705..2739
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2894..2992
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3063..3087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3373..3430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..223
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..950
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1557..1576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1583..1624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1660..1682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2042..2064
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2096..2112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2113..2136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2438..2486
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2498..2535
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2547..2572
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2593..2616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2617..2647
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2894..2940
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3063..3079
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3373..3395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4058
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4091 AA; 452206 MW; 85685F5E0561EAFE CRC64;
MVKILKTIQP KHKETLSPYI QSFVQNASTA PWHTLPQALA DFPTRWPFPR GDLYHWIPLL
NRFDSDLETF CATYALNNGP QVKDFGCELL QKGGATDEQV SEAGFGPEGD REVIERILHF
SRILLENCGN RSIYSSSTHL SDLLNSTSLS LLAATLQIGT QLAQRYQATF RRIASSHRQT
NATLLANHYN IDLDKVQQLS QPFSRTVTST ETSAPTVPNT PVTPNAKGKD KAYFSIPVAG
SKTTTSTSYA NDLVSLVRSG TLPDLSPKGR KAASTSSQTS AEVDWNEWGD VRITYYESQS
RGEEAPPSAT HNASAAPVTP TPVRRTSMLG NQHGNRAPRA PAPEEAPATP SRSSTLPAAA
PAEEKATSSL KVIDIPASKV SEHSVQELLQ EYLPSVPDAS KYTLLTKLRV AKALSHSLDT
RRQMLAVRLL AVTNLAYIYP EPSFLEKVLK QDSDEPRRQQ LIYQLAELIH PPAQGDLGIP
RSLQTIAVNA IEGLAQHQHK YQDVCTALNT NVNHGVLLYI VRKAVAEMAT DEPGDKHTEN
DEWHSALFAL LSHVATLPRA GNELVTAGLV PILVEVLTLR TAVAEGSYPR VLNFLDAIVF
NVKDAFQVLA NADGLDAISN LIVHEVQSST EVASKSEGMP ADYRSPSIDY EIPYYQQQSI
KWLFKFIHHM MNQAGGYGGN FDRLLRNLID SPQLLGSLRQ IISQAKIFGS SVWTNAVSIL
NDFINNEPTS FAIIAEAGLS KAVLEAVLGH EITVPAPKDG APQPESTNEE GSPAQTDDDS
IFSVVVDETP HPPTKEMLEA PRPGPLARGI MPSSEAIIIV PEAFGAICLN NAGMKMFLES
NALQSFFEIF ESPAHVKVLD NDTNNLATSL GSTFDELVRH HPALKTAILN AVLDMVARVS
HLCKTRTERE KLGAKLLVTN ANGDVVVADR SLLSEGSDED KGKGKSVDTD ADVEMTGVST
EAAEPSKVSK PVIPAEDDRE NSVTPYIAAV ANFLTQLFNN AGVRNLFMEN GGVESILDLA
ELPVLPNSPS DERSHRNMHT VIALLAEQKA HILVPSLMKR AQAAVDTLTP FTQHKGREAY
FAKFIEGCKQ SDDRTENILL ARGTSLVEAM VTAQNLCMAL RQCISSPIFS RNQASSFSSM
NLADYYVRLV KSLGAILAAS IKEDFKLMRL APRHWRRAGR QSVQMFMNDA PEPLIPTIDS
TEEALHSLLP EAQGTAPMAT LVTDSSGAEN PIHKVNQTKT LTTEEKHSPE FKNFQNLHYL
LGKMPISMSI FFQVIGKGLV PKRTPDSFQR QSNISIANAI VETVLSELTS VGDESSSETY
TFWVLMLRTV KDILVNNART AEKPQECITI VVQAFMKAGG FNTINHMLEL FDAEVRNNAD
KAVNFNDVDL LLRNDLATLG IKHILELYGP LVTGKNVGES FQSTTLHSRS DRDRNSPNYF
SAGQFVLEMR MAILPAVQKL WESDIVEKGS KIIPNKLIDI IRNVMETDLE EGAFRNGDKA
IVPSKQGKKK WRVNRENLVK LQAAEYDEEL AVEALFRCNN SYSSALEYCK AQLSERSGGR
NRFRKDDIDP NVGPDDAPGH ETRPSTGSIT PDQGAAQGGN GTNEAPNDGA SAQSPEEFSP
HASVPPNLQQ MLLENMNRTL ENAEAGNLFA AISGGGEQTN LPERVPNQQP SSSSSDKTLE
NQPEIPTVER LNAERLKIRS NLIERCLEVI NAHGEFTFEI ADLITTVIDK SPEQAEMRAT
MGGTLVVALT SFLSDDVREV GKKIASYAHL LALMLQDPQF YKASLEELKS NLGNLLEFVK
LSPDHKSEES SPWVAHILLI VEVLLSDDAE PRETEWKIPT SETASLEKPV LKAPELVVST
EDRATLFEAI LDMLPRIGKD ESLALAVMRI LVILTRARHI AVAMGEKKNI QRLFVMAKQL
AGAATPRIQS PLMLILRHIV EDDETIKQIM RSQIKVFLDP SSSRSSRHPD ITLYLRSMSN
LVVRQPELFV EVSNEMVKLV NWTTTTADQP GRQQIELQDK YKRTRRGKPE DAVLPTLKPT
EELSMEDVKP STETAEGEAA EGSKAVEHKV PIVENPDGVI YFLLCELLNY RDVEDKEPAA
PAPAEDKEKT TATTSETTTP STLGAESSST SASDAPQIRP PNPPKPETKK AKPEFKAEEH
PIYIYRCFLL QCLTELLASY NRTKVEFINF KRNAPTHAAT PSKPRSNVVN YLLFDLIPSG
SLDHGETLTM RKKVYTSSWA DSTITALLSK TGEQILDRER DNTDSDDEPD LLFVRKFVLE
NIIKAYREAS TSTEPLDIKY SRMLSLADLM SHIMAGKDNI GGGSDPNVTI RSQQQLKRIM
FEKGYIGALT ASIADIDLNF PGAKRAVKHI LRPLKALTQT AIELSEVGKV ALTPGQHDED
EIASASSVSD VDDDREETPD LFRNSTLGMF EPDRDHESSS EGEDDDEEMY DEDGYEEEME
GYEDGPIEDD EDNISDEDEE LEGMGEIEGL DGDHGMDVEV IMDDDEDDDE SGSSDEDDED
EDDDMDEDDE DDRVQIIDNE GNPHPLAELD DEEDWESEDE DEEEDYEGMA AEEEEEAMHA
GGHGPLGRLV HAFGGDPHHH GEIDNLLQRI EDERGGDPDM DIEYLDDDHE EEDEVDEEEE
DMDDDEDMYE EYQPEPGMPF TFEWNDEQEP PMIISHRGPR AHAAPQPSPY FFGAQRDPLG
VRDYYRGSYR SHRPGPTPRD NNDGTNPLLQ RGDRARGDAG LVGSTPFIGR ETLFNIVGRG
PFGAEAGGPA AILNDLFTQL PFPGGAIPTA GRNGGALHFH VTGGPGGADA REFQAMFGGM
RPGMARGHER GPGPAEPGAA TTFTTQLTAT RWSEEARLLF GPRHPDMALR VLMGLMAVVV
PAALEVEKKA IQEKKEAEEK KRKEDEEKAA QAAKEAEEKA AKEKKEAEER EAKERARAEE
AAAAAAAAPP AEEQPQEGEN AQPMEGVESG EAAAAGQEGE GAPTEDRPRV TIPFRDGTLD
ITDLGIDLDY LDALPEELRE EVITGAIAQR RSDAAATGAP PSEIDQEFLN ALPDEIRAEI
IQQERQDRRR RERDEARRQA AANGAPVLVP QEMDAASILA TLPADLRAQV LAEQDEDVLA
QLPPEYIAQA RASMGGHPLR GLTRVGVLDG ARPGHPSGGE IVKPVRRSIV QMLDKPGVAT
LLRLMFIFQQ DSLRNTLYQV LQNISENRHN RGEVISTILH ILQDGSADMT AVERSFAHLS
LRAKQPKDKD PKTPLSLSRK NTGTGLAALT TVPNTDISPL MVVQQCLGAL IYLCKVNLHV
PSFFLTEHES AVSGLKRNAS RKGKGKDTKA LKFPLNSLLV LLDRKLIMES SPVMESLSDL
LSRITAPLQT FERKQKEADE AAKKAEEKPA EGEGEGEAGP AEQQAENMDT GCPAPAVTED
PPAEAGASTA DALKAEVDKA DDKTKEAEKK KVRPFVPPVV PDGNLKLVIN IFVARECSAK
TFRETLSTIK NLSCLPGAKA VFGKELIAKA QELGEVILLD LEELFPQIQK ASNSTELQGV
ALTKFSPSGS DQNKLLRVLT ALDHLFDPKH ARKDATAEAE AGSETAETEK QDLLATLYEN
STFGPMWEKL SACLSAIRQR DHMLNVATIL LPLIESLMVV CKNTTLKDQP LRGKDNMLTS
PVPESRMESL FFTFTEEHRK ILNDLVRNTP KLMSGTFSLL VKNPKVLEFD NKRNYFNRSI
HNRNNPARQS YPPLQLSVRR DQVFHDSFKS LYFKSGDEMK FGKLSIRFHG EEGVDAGGVT
REWFQVLSRQ MFDPGYALFI PVSSDRTTFH PNLTSSINPE HLMFFKFIGR VIGKALYEGR
VLDCHFSRAV YKRILGKAVS VKDMESLDPE YYKSVVWMLE NDITDIISES FSVDNDKFGV
VETVDLIENG RNVPVTEENK HEYVRLMVEF RLTGSVQEQL DNFLKGFHEI IPAELVAIFN
EQELELLISG LPEIDVDDWK ATTEYHNYTA SSPQIQWFWR AIRSFDKEER AKMLQFVTGT
SKVPLNGFKE LEGMNGFSRF NIHRDYGNKD RLPSSHTCFN QLDLPEYESY EMLRQQVLTA
ITTGSEYFGF A
//
