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Database: UniProt
Entry: K5W668_PHACS
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ID   K5W668_PHACS            Unreviewed;      3574 AA.
AC   K5W668;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   28-JUN-2023, entry version 53.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=PHACADRAFT_174950 {ECO:0000313|EMBL:EKM54444.1};
OS   Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS   carnosa).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Phanerochaetaceae; Phanerochaete.
OX   NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM54444.1, ECO:0000313|Proteomes:UP000008370};
RN   [1] {ECO:0000313|EMBL:EKM54444.1, ECO:0000313|Proteomes:UP000008370}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM54444.1,
RC   ECO:0000313|Proteomes:UP000008370};
RX   PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA   Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA   Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA   LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA   Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA   Grigoriev I.V., Master E.R.;
RT   "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT   chrysosporium, to elucidate the genetic basis of the distinct wood types
RT   they colonize.";
RL   BMC Genomics 13:444-444(2012).
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; JH930473; EKM54444.1; -; Genomic_DNA.
DR   RefSeq; XP_007397136.1; XM_007397074.1.
DR   STRING; 650164.K5W668; -.
DR   GeneID; 18909697; -.
DR   KEGG; pco:PHACADRAFT_174950; -.
DR   HOGENOM; CLU_000215_0_0_1; -.
DR   InParanoid; K5W668; -.
DR   OrthoDB; 164548at2759; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000008370; 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   CDD; cd14270; UBA; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
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   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
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; PF00627; UBA; 1.
DR   Pfam; PF14377; UBM; 3.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   3: Inferred from homology;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1271..1311
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          3239..3574
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          200..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          953..1010
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1311..1420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1738..1760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1799..1835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2053..2198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2226..2276
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2427..2498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2578..2597
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2650..2676
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2870..2930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        204..220
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        232..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        972..1001
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1312..1365
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1399..1416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1738..1755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2067..2085
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2110..2197
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2259..2275
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2427..2464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2472..2491
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2870..2888
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2897..2930
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        3541
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   3574 AA;  395220 MW;  B1B7926E4A2D362A CRC64;
     MKILHKSRRS VPLIPVVAEL IDKLADTPTE ELSDALAQID HWRWPRSDLN AWVKILNKFD
     TIMEDVIRDY EIEKAQLKPF SASDKQLLCE ILRFERLLLE NSTNRKTYNS YDRLNSFMTT
     SDLDVLIYSL NLLLRPAQQY SAQPAVSHAL SLNTSRLTSL SKRWPSLHDY DINLVALAGE
     QGRAQVDSLP NEAREVAFTF YRKDGSQSKK EEKKEPEVDP FEAPPPQTPR KGASSSPSAT
     SANGPVTVHI DSQSLETKPA MQSWAEANET YSVPDDERFE LLCRIRSAKA LARTHAEDRE
     KLVIVRLLAI GLFCHTHPEQ TTFNNLFLYE PDLVHHIAEL LQLDRGIDIQ VQTAAVYALD
     AVGRYRNKIQ DVLTAVNAGV NHGILMALLR KTITELANAE SSTPQAFVEA LLSFVTYIAA
     HAAGGNMVVS AGLIPLLVQV IENRLPNRLY ALSKTMQLLD NILYGYTNAF QLFCNARGID
     VLVGRIEYEV DTGLDEHGGG KPAAEIPILY GKISVGRATV LKHIMRSMHR MMQSSGTSEG
     LRGLLDSSLV QSVKKVMADR SVFGANVLAI AINIMATFIH NEPTCLPVIQ EAGLPEAFYT
     VVESGLEPVI EVVQSIPNAM GALCLNQIGQ DQLASRPGII PGFFSIFTSE KHQRMLQEKE
     NAVIIGTAVE ELVRHHPSLK NQVFEAIKQT MAKIEELGNA YQVPEENKHW YVLRATRTTN
     ASVGTSDVDV DMDASAQPSS SSIAASAEPE ATPHIFEDSS FKSHDNAIVS FIDVLGKFLE
     GYFQHVPHCR DFLSSTDGLD RLARLTALPC IPYDFANSVA SDSLVQVVRT MVEASTNESL
     AFIVKIVNES LIATASLRDD NAGNSKYLEL ATVEDEQQAA EANTAFRNLV TLHVRIMLLS
     DIFATAGYSQ GRALATLLQS VTGTGTGDIL LGLGSLHRSS IWENVMLKEK MTIRPEDKQQ
     TPEAFAPVET PMSVSSEATT PGPSTTANGS QPENSATATP KPEHPTKKDP KEMNMRALRH
     LASQLPNSLA PFFQSVVRLF QTRRNPDQAQ KQRILDAADV VADVAVKHLS ARQTDDKRNL
     FTYYTMMLGL VTILLIDERT NSKVAHTVLL QAFLRKGGVD AIVTLCREFI ATIDEITPIT
     PEERTELQSQ TLIHAHGGLK VALHLIHPLV SFKPIVDSPQ SGFLLATDKK DTEPGWFDPR
     NLVVQLRVAI LPLLKDIWQS SWLMSAPLGV SKSVIQVVLE LLNTDQEEIK EVEPAAPSMV
     PAIPIATRTI GPDENRIRQL TDMGFPRSAA ERALIRARNN VSHATELLLA QPFPLPPDPE
     PEPAAPAPEP ADSAPEPADP APEPIVPAPE PIVPAPEPAA PAPAAPTVED APAQQPAADE
     AAATAVIAPA PAPTESTPVP EAEASSSSSS SPPLAPQKSH EEWLKELNDL REPLKESLGS
     RILSLVDEHP ALVFDVQKVF VGPSAPYRDQ AVNRLTEDVK KFSSAALDHH EQPLSVRFRI
     LALVLNDPSS PLAAMPEAEA TSLMDTLIGL LLSTPINIEN GHVTIPKWLA SHLLVTEAVL
     MMGEEPRSVG LPTKEDEPLP EIDAVETGPK FNEKRPVVLD FCLRLLHVPQ LPRDELLSSL
     RLFMLLTRDH ALALEFVKRD GISALFRLLR DSPTSASAPG THPYIASILR HIVEDPVTLK
     QIMQQEVKAF LSHPRHRHLE AGSFVRTCGA MALRDPKVFV QATAEVCQLS NPYGPLKNLN
     LKESHKSNSD GTSGAEGSGE MHIDVSVSQR PSSESLDSLV HFLISELIKS VKVPEQKLSS
     EGAATQAPLS GSSTAVQPAD SSTSTSTEIK DSSPTPSIDH TYSCFVMQCL TELLFSYDSC
     KVSFLSYSPK KRTHTPAKEK HRTHALQFLI NDLLSFGTIN PSPPSEAKQQ IMLCNWAMSV
     IVALCVDTTP TEIKDVPSER ASVRKFVLDA INRAIKDLPG SEMGEARYSR LLALADLCYR
     LLTVRFNTGT RKINDDAPTH IAKVMLEKNF VATLTNALAE VDPNFPDIRG VVTGILRPLE
     YLTKIAIKMS RASDKQKDSP LDKEESIDSE ISEEDEDEEM EDADREEAPD LYRNSSLGMY
     GGEMEDVHFG HDDEMDEDAE DEDDDAEMYD EEETGSEDTS ATDEEDEEAL EQELEDETGD
     SEGGWNEAEE EEDLVENEEG HEDADEDSED GEEAGEEAEV MWQPIPTDLN AREGDQMFWH
     GMVRSGRRRG EDDGLDIFGR PRTTSTGIPE GTTHPLLLDP NTAAPTSQSR SSRRAHRGTI
     AGFPQDLLHS IEHALGEGAI QLFQHIIQGR GGAGETIRID VPANQLIPQL GRHGRAGISA
     HIRLERAPRN DGRSDTRGFE PLLTRDRWAE EVKSLHGRFE QSRITKITGH VVLALLPEAI
     EAHKKAKLEE EKEAARRREA QQKAEEEAVR KREEEEKVRQ EEERAKAEKE RLEAEARAAE
     AESADQSADA DTEMADATTQ GQPSAAEEGQ PEAGSSSVPE RVTVLIHGNE VDITDTGIDP
     TFLEALPDDM REEVLNQHIR DQRAARVERP VDSQISPEFL DALPPELRAE IIQQENLERA
     RRQAQQPTAA PAQPAVPAEM DPADFLASLD PALRQTVLMD SDEMFIQALP PHMLAEVGLF
     RDAQNAARSR AQPAPQLAVR QGGRQPPAGP GKPPASREAI QLLDKHAIAV LIRLLFFPQV
     LRKNLLSKVL VNLSENGKTR TDIFNLLLGI LQDGTGDLSS IDRSFAQMSF RNTKSSAQIT
     PHTPGKATLP QPEVVPELVA QRCLDALTYI TATNEASSLF FLTEQELPTG LRRSSSKKGK
     GKEKQTSQAY YPVVLLLGQL DRQTLLRTPS LMESVAGLLS LVTKPLTSLK DAQKEKEKEK
     EKDANPEADR SVTAPLEIQP TAPSGITAQL PQGNSSAPSN IPETTGTQAL PPTADKVLLS
     HPPNIPQQVL RHVVNILTAG ECSGRAFSHT LALIQHLSFV SGARDVIAQE LRTRAQEFGQ
     RLYSSLDELA TALQESLQEL RTEDVALTVA SKFSPASSDQ AKLLRVLKTI DYMYSPKSIA
     SAADATNEDV EKVQSIYESF RFTTLWRRLG DCLSVIEERP ELEHIATVLL PLIESLMVVC
     KYVGPKASSS TTSRAVRASA SPRTPTTARE SMEDLFVSFT DAHRKVLNLM VRNNPSLMSG
     SFSLLVNNPR VLDFDNKRNY FNQQLHRRLH SREHHGTLQL NVRRQRVFED SFQYLQRKSG
     EQIKYGKLSV RFYDEEGVDA GGVTREWFQI LARQMFDPNY CLFQPCAADR LTYQPNKASS
     INPEHLSFFK FVGRIIGKAI YDGRLLDAYF ARSLYRQILG KPVDYRDVEW VDPEYYKSLC
     WILENDPTLL DLTFSVEADE FGVTKLIELK ENGAHIPVTN ENKREFVQLS ANYRLYSSIK
     DQIEALLTGF YEIIPKDLIQ IFDEKELELL ISGTPDIDVD EWRAATEYNG YTSSDPVIVW
     FWRALKSFNR EERAKVLSFA TGTSRVPLGG FVDLQGVQGV QRFSIHKAYG EVDRLPQAHT
     CFNQIDLPQY SSYEMLRQQL LLAIHEGGEG FGFA
//
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