ID D8RSC7_SELML Unreviewed; 1827 AA.
AC D8RSC7;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=UPL3-1 {ECO:0000313|EMBL:EFJ25045.1};
GN ORFNames=SELMODRAFT_149458 {ECO:0000313|EMBL:EFJ25045.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ25045.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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; GL377588; EFJ25045.1; -; Genomic_DNA.
DR RefSeq; XP_002974090.1; XM_002974044.1.
DR STRING; 88036.D8RSC7; -.
DR EnsemblPlants; EFJ25045; EFJ25045; SELMODRAFT_149458.
DR Gramene; EFJ25045; EFJ25045; SELMODRAFT_149458.
DR KEGG; smo:SELMODRAFT_149458; -.
DR eggNOG; KOG0168; Eukaryota.
DR eggNOG; KOG0170; Eukaryota.
DR HOGENOM; CLU_000366_1_0_1; -.
DR InParanoid; D8RSC7; -.
DR OMA; AEPLSQF; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR CDD; cd00078; HECTc; 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; 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; 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 Ligase {ECO:0000313|EMBL:EFJ25045.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1507..1827
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 625..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 904..1010
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1195..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..86
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 904..947
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 956..978
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1794
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1827 AA; 193661 MW; A385C57AFF06A472 CRC64;
METRSRKRAE ATGRRPPPAQ SSSRASKRVR VGASSSSSGA AAAAAAAPPA PAPVAAAAAG
ASSSRSRPST RRNTASQAGT SVSNSSGEKD DKGKEKEACR NRDARDRAAG ASVEADDDDG
GDGVSTLQQN LASASSALHG LLRKLGAGLD EFLPSSTPAH QSSRLKRILS GLKAEGEEGR
QLEALSQLCE LLSIGTEESL SSFSVDSFVP VLVSLLNHEY NPDVMLLAAR ALTHLCDVLP
SSCAAVVHYG AVPCFCARLL SIEYIDLAEQ SLQALEKISH EHPAACLRAG ALVAVLSYLD
FFSTGVQRVA VSTAANICRQ LPSDGVNFVM ESVPILTNLL QYQDPKVVDH ASLCLTRIAD
SFANSSEKID VLCSHGLIPL AARLVSVSNP NGAMVPQTSL SASTYTGLIR LLSSCASGSA
SASESLLLLN ISSILKDILT GAGLTSTTSV APSISRLPEQ LFEIVNLVNE LLPPVPDVGA
APLPNGVDST SSSKVTQASP RIQLLQDRPE LLLGFGADLF PVLVQVYGSS VTSSVRHKCL
AAIHKLLYFS TPEMLHSLSK DTNISSFLAG VLASKDPSVL LTALHITELL MQKLPGVFAK
TFVKEGVVHA IDTLIACEQQ LGKTSDSQKT RRATSGRRRS GSTSDVHPDD PGGSSSAPVG
SPPNADSPLH TARLGLLSTA VAKAKFLRGA HFCNGITDGG ATESLCRLKS LCSKLTADST
PEVKGKGKGK AKACGSTTSL SEEQLLAAIS GVFGELENGE GVSTFEFVNS GIVSALLNYL
SCGSVDGRSR QQALNRLKNF LAVALSSDIR EAPLTVLVRK LQNALGSLER FPVILSHGPR
ATGSTASIAA GLSALTQPFK LRLCRASGEK VLRDYSTNVV LIEPLATLAA IEDFLWSRVK
RHDSSPSSTV AASSDCVSSP PASTTPTAST STPSRPSTRS RTAAAGSGDA TPSKGKGKAK
TFEARATTES RGPETRNAAA RRRAAAAAAS AAVTKQRAPI DSEDDDADAS PVEVEDAVAM
DEDDVSEDEE ELFGEEPAEV CVGDRVHDVQ LGDSADAGAV ATSATTSETP SPFGTGAAGS
STPVLIGTGA SGSRATAAVG KGALSFAAAA MAGANASKNS KDRKSLAAIA SANVPPKLSF
YLGGKLLNRS LTIFQAIQRQ TAMDEDDDER YAAPDHPLGH GRRLWDEVYT ITYQRADPTE
KTSPGGVSST KSGVAGSSSQ GLDGLQQASL LDAILQGELP CDLDKSSSTY NILLLLRVLE
GLNRLAPRLR AQGVIDAFAE GKVSSLSLSE ASTGGASVLQ EEFLSSKLTP KLARQMQDAL
ALCSGGLPAW CHQLTKACPF LFPFETRRQY FHSTAFGLSR ALQRLQQQQS ADGTSSANER
ELRVGRLQRQ KVRVSRTRIL DSAAKVMELY SGHKAVLEVE YFGEVGTGLG PTLEFYTLVS
RELQKNSLDL WRTESRPGSP QQADTEMPDI NEDVLDEPSE NQASVQPVEQ NIDYVTAPHG
LFPRPWHPAS TDARYTKTVE HFRLLGRVMA KALQDGRLLD LPFSIPFYKL VLGQELDLYD
VKAIDPELGS TLDELQGLVR RKQYLEGVCH QMSDGLRFRG SRIEDLCLDF TLPGYPEFHL
KEGGNEIMVT LDNLEEYVAL VVDATVKMGI SAQMEALRSG FSQVFQLSSL QIFTEQELDN
LLCGRRELWT PETLVDHIKF DHGYTSASPP VRHLLEIMGE FTAEEQRDFL RFATGAPRLP
PGGLAALNPK LTIVRKHPTG GNGSSVVLGS TPPGAASAMG TTLADGDLPS VMTCANYLKL
PPYSSREVMR ERLMYAISEG QGSFDLS
//
