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Database: UniProt
Entry: M1V553_CYAM1
LinkDB: M1V553_CYAM1
Original site: M1V553_CYAM1 
ID   M1V553_CYAM1            Unreviewed;      1775 AA.
AC   M1V553;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   ORFNames=CYME_CMI198C {ECO:0000313|EMBL:BAM80070.1};
OS   Cyanidioschyzon merolae (strain NIES-3377 / 10D) (Unicellular red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Cyanidiales; Cyanidiaceae;
OC   Cyanidioschyzon.
OX   NCBI_TaxID=280699 {ECO:0000313|EMBL:BAM80070.1, ECO:0000313|Proteomes:UP000007014};
RN   [1] {ECO:0000313|EMBL:BAM80070.1, ECO:0000313|Proteomes:UP000007014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10D {ECO:0000313|EMBL:BAM80070.1,
RC   ECO:0000313|Proteomes:UP000007014};
RX   PubMed=15071595; DOI=10.1038/nature02398;
RA   Matsuzaki M., Misumi O., Shin-i T., Maruyama S., Takahara M.,
RA   Miyagishima S., Mori T., Nishida K., Yagisawa F., Nishida K., Yoshida Y.,
RA   Nishimura Y., Nakao S., Kobayashi T., Momoyama Y., Higashiyama T.,
RA   Minoda A., Sano M., Nomoto H., Oishi K., Hayashi H., Ohta F., Nishizaka S.,
RA   Haga S., Miura S., Morishita T., Kabeya Y., Terasawa K., Suzuki Y.,
RA   Ishii Y., Asakawa S., Takano H., Ohta N., Kuroiwa H., Tanaka K.,
RA   Shimizu N., Sugano S., Sato N., Nozaki H., Ogasawara N., Kohara Y.,
RA   Kuroiwa T.;
RT   "Genome sequence of the ultrasmall unicellular red alga Cyanidioschyzon
RT   merolae 10D.";
RL   Nature 428:653-657(2004).
RN   [2] {ECO:0000313|EMBL:BAM80070.1, ECO:0000313|Proteomes:UP000007014}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10D {ECO:0000313|EMBL:BAM80070.1,
RC   ECO:0000313|Proteomes:UP000007014};
RX   PubMed=17623057; DOI=10.1186/1741-7007-5-28;
RA   Nozaki H., Takano H., Misumi O., Terasawa K., Matsuzaki M., Maruyama S.,
RA   Nishida K., Yagisawa F., Yoshida Y., Fujiwara T., Takio S., Tamura K.,
RA   Chung S.J., Nakamura S., Kuroiwa H., Tanaka K., Sato N., Kuroiwa T.;
RT   "A 100%-complete sequence reveals unusually simple genomic features in the
RT   hot-spring red alga Cyanidioschyzon merolae.";
RL   BMC Biol. 5:28-28(2007).
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; AP006491; BAM80070.1; -; Genomic_DNA.
DR   RefSeq; XP_005536356.1; XM_005536299.1.
DR   STRING; 280699.M1V553; -.
DR   EnsemblPlants; CMI198CT; CMI198CT; CMI198C.
DR   GeneID; 16993616; -.
DR   Gramene; CMI198CT; CMI198CT; CMI198C.
DR   KEGG; cme:CYME_CMI198C; -.
DR   eggNOG; KOG0168; Eukaryota.
DR   eggNOG; KOG0170; Eukaryota.
DR   HOGENOM; CLU_000366_1_1_1; -.
DR   OMA; AEPLSQF; -.
DR   OrthoDB; 1093891at2759; -.
DR   Proteomes; UP000007014; Chromosome 9.
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; 3.30.2410.10; 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; 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; 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:UP000007014};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1378..1775
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          1..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          898..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1321..1351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        82..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        911..927
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        984..999
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1071..1085
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1321..1342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1742
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1775 AA;  193985 MW;  1EE89B1ADB49EFE9 CRC64;
     MARGRRRSAL SRAQQHVERN TGAREETVTE GANVAKRAAG LARQEAETTT VESGQHAGAV
     ESAALEKTEV ARNTQRAVES QALDGHRYRK RRSACLEKEP VGRVLETRSE SKIAAEEPHA
     ATTRQGSKRM RRSRSRQRAL REATAGMLGG SDSTGADNDG LSSINSSESR SRRRYHSRYR
     RHTEPNTSAS LPLETNDDIP EASSLGFPLE HQSGRRRGAS PRGPSSLPPE TGGTLQGLLR
     HLGAGLSEIL PSFGHGGFGG SSVPARLRRI ASELRSLTTE GNTETDTVAL MALLNELCEV
     LSIGVEDVIL NFSFEQLVSP LVWILQNCPE LPELLILAAR ALAYMVEISP SVGASIAQSR
     AVPALCGFLL HVEYIDLAEQ CLQALERLSY NFPNHIVRSG GLRAILQHLD FFPTSIQRMA
     SSAAANCCAR VNDSALSQVE DALELLSHLL DSDDTRIREH GVTAYARLVA NFSASSNAQE
     VLRRIANDGG AMEKLVAVLA AGEASLDKRH RGLVLSTLSS LASADEGLGT RMLTSPAQGG
     LGIGAILANL LGVASDAEES TSTGQLLGAA DVHAVPLNRA TQTETLIGSA LMLVDALAPD
     RLLVQRLQTV LELNVRAPMH DQTSREGRRR AISAMKKTLF ALESEQEIQS FSMQLVPTLG
     YVLYDPIDED ERASVMCMIE HMLERVQDLG PLGELFVKEG VLHVLEQSAV ETDAAQKILD
     RFGDTLRSSG RQRIRKLCEL VERIKKGDHE SLIALFPELE HCSVFEVQMC GLAGALDAYL
     SVQPGAASEL ATRYSHLLVA AIRAPGALRR LVRSLVAIFT NTERFQVVRN MAANGSVSAG
     IRLLSQPFRL QLQRGGGCSG SRLRDFPASL VLVEPLASAQ TIEEFLYERV TGDAAELNEL
     SDEPVFETGT DENGSDDSGA FEVATESTAD TSDDEHAIFF DEDALSGSVE SDEPGEHRTR
     RRQAGSRPSL AGETALAAAE ETASGSEEDS DEFSDLGETF DELGPEHGLE NPNLSGSLPA
     VDIEFSDEVS GTGSPVREQE HSGRDSRRSA SETYAARAGR CAGAPCPSSE IDRGRRSRGI
     RLKRDGERRR ARLSLCIRGH TLLPQETILH ALVTTLGGQA LGPRLWSETH ALTYADCQSS
     RMGQVSSQPI SNGDGKPGGH QFEGPFAEFE LVQVAELQFQ VPRSFHLNEV TVAQDVSSYL
     SLLGKLYWMN NHHAELHAWI QASRTQSGST LDAAWSHNVH WPPADDPLVP EADIFASSSL
     ENKLGAQLSD PLAVAAAALP PWCFIVPRVC PGLFSLQTRR LLVQVSSFGI ARALSAVQTR
     ADTQRQQHAT ASSSTGRSDL GAHTSGAEQE ARIGRIQRQK VRVHRARLLE SAELIMENFA
     DQKALIEVEY FNEAGTGLGP TLEFYSMVSR ELQRVDLKLW WEDSSKAAER ERLLRSGKAL
     PPELRERLCY VVSAGAGLYP APIGPRERGA PVQERLQRFQ FIGRFCAKAF LDGRLLDLRF
     SPAFWRLVRA LAEARFLVSE GLNGHRAIFR AAKKRLDFSL RRLGEVDAEL ARSLHSIACM
     RDADACDIAA LCLDWTLPGQ PHIEMRPRGR SMTVSKDNLA DYVRQVKEHV LFDCAARPAY
     AFLEGFQSIC SIWALLGIFN PNEEVNVVLC GPDLHPWTEQ ELLSALRFDH GYTSENVAAR
     NFVRALCSLN EDDRRHFLLF ATGSPRLPMG GFHALLPPMT VVKRTPEAGL TPDECLPTVM
     TCTNYVKLPE YSSFEILLDR LLYTIREGQN SFDLS
//
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