ID A0A364L4T8_9EURO Unreviewed; 722 AA.
AC A0A364L4T8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=E2 ubiquitin-conjugating enzyme {ECO:0000256|ARBA:ARBA00012486};
DE EC=2.3.2.23 {ECO:0000256|ARBA:ARBA00012486};
DE AltName: Full=Ubiquitin carrier protein UBC2 {ECO:0000256|ARBA:ARBA00042190};
DE AltName: Full=Ubiquitin-protein ligase UBC2 {ECO:0000256|ARBA:ARBA00041569};
GN ORFNames=BHQ10_006840 {ECO:0000313|EMBL:RAO70828.1};
OS Talaromyces amestolkiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1196081 {ECO:0000313|EMBL:RAO70828.1, ECO:0000313|Proteomes:UP000249363};
RN [1] {ECO:0000313|EMBL:RAO70828.1, ECO:0000313|Proteomes:UP000249363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIB {ECO:0000313|EMBL:RAO70828.1,
RC ECO:0000313|Proteomes:UP000249363};
RX PubMed=28649280; DOI=10.1186/s13068-017-0844-7;
RA de Eugenio L.I., Mendez-Liter J.A., Nieto-Dominguez M., Alonso L.,
RA Gil-Munoz J., Barriuso J., Prieto A., Martinez M.J.;
RT "Differential ?-glucosidase expression as a function of carbon source
RT availability in Talaromyces amestolkiae: a genomic and proteomic
RT approach.";
RL Biotechnol. Biofuels 10:161-161(2017).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAO70828.1}.
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DR EMBL; MIKG01000013; RAO70828.1; -; Genomic_DNA.
DR STRING; 1196081.A0A364L4T8; -.
DR OrthoDB; 5481790at2759; -.
DR Proteomes; UP000249363; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IEA:UniProtKB-EC.
DR CDD; cd20524; CYCLIN_CCNH_rpt1; 1.
DR CDD; cd20525; CYCLIN_CCNH_rpt2; 1.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 1.10.472.10; Cyclin-like; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR031658; Cyclin_C_2.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR015368; UBA_C_fun.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR24067:SF347; E2 UBIQUITIN-CONJUGATING ENZYME; 1.
DR PANTHER; PTHR24067; UBIQUITIN-CONJUGATING ENZYME E2; 1.
DR Pfam; PF16899; Cyclin_C_2; 1.
DR Pfam; PF09288; UBA_3; 1.
DR Pfam; PF00179; UQ_con; 1.
DR SMART; SM00212; UBCc; 1.
DR SUPFAM; SSF47954; Cyclin-like; 2.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000249363};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 4..153
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT REGION 160..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..368
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..722
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 91
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 722 AA; 80096 MW; 87D5BBF4959C4B99 CRC64;
MASNRNRRIA KEIADIHNDP HSQVTAEPMG AEDDLTHLRG SFRGPPATPY EDGTFFVDIK
IPTEYPFRPP IMKFETKVWH PNVSSQTGAI CLDTLSSAWS PVLTIKSALL SLQSLLSTPE
PKDPQDAEVA NMLLRKPKEF ERVAREWAIA YAGAPKKHLA EGSGGATDAS IREQERKAKE
DEERDALAAY DGYNKDLVDR FCGMGFDIDR VVAAFKHVGI DRNNGADYEL EGEAVGDVTA
FLLELVMARG ICEINLISLD FLLLKDEKPT DEASFNRIFR LRDLQAYKQG STPTCVAIMI
EDEIYKTSTQ FRIWSYTKES LKSLRANTNA AASERLRAAQ NRAREAPRSA TPSTSGNLTP
NPSDNNDSKV EAALGKDVDC LSVEEELMFV RYYCELALDF GDKYKPALPT MVRATAIQYL
RRFYLSNSVM TYHPKTIMPC ALFLATKTDN YYLSLNEFAK QIPKIDKPAD VIAPEYTLTQ
GLRYTFDVRH PFRGLEGGIM ELQAIAQGEG QPGPFITGKT SESMKQAINN IDPLPGVEKG
SPSSRISAAH SKARDLLKTA AQMTDAYFFY TPSQIWLXAL LVADKPLAQF YLDSKIGPGV
TPVPTDSKNP LEMIRTKLMT TLSDCANLLE SYTPIASNPG TLQDLKAIAK KVYQCQMIEK
LDPAAPGSGQ KRSTGSLPGA EGASESELER VAKKRRLERE RREQESKDIF GGELVAQRKK
AD
//
