ID A0A369GG13_9HYPO Unreviewed; 659 AA.
AC A0A369GG13;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=UBC core domain-containing protein {ECO:0000259|PROSITE:PS50127};
GN ORFNames=CP532_3923 {ECO:0000313|EMBL:RDA82694.1};
OS Ophiocordyceps camponoti-leonardi (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=2039875 {ECO:0000313|EMBL:RDA82694.1, ECO:0000313|Proteomes:UP000252748};
RN [1] {ECO:0000313|EMBL:RDA82694.1, ECO:0000313|Proteomes:UP000252748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCC 80369 {ECO:0000313|EMBL:RDA82694.1,
RC ECO:0000313|Proteomes:UP000252748};
RA Kobmoo N., Wichadakul D., Arnamnart N., Rodriguez De La Vega R.C.,
RA Luangsa-Ard J.-J., Giraud T.;
RT "A genome scan of diversifying selection in the zombie-ant fungus
RT Ophiocordyceps unilateralis complex supports a role of enterotoxins in
RT coevolution and host-specificity.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|RuleBase:RU362125};
CC -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009347, ECO:0000256|RuleBase:RU362125}.
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:RDA82694.1}.
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DR EMBL; PDHP01000275; RDA82694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A369GG13; -.
DR STRING; 2039875.A0A369GG13; -.
DR Proteomes; UP000252748; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016627; F:oxidoreductase activity, acting on the CH-CH group of donors; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd00195; UBCc; 1.
DR Gene3D; 1.10.540.10; Acyl-CoA dehydrogenase/oxidase, N-terminal domain; 1.
DR Gene3D; 2.40.110.10; Butyryl-CoA Dehydrogenase, subunit A, domain 2; 1.
DR Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR Gene3D; 3.10.110.10; Ubiquitin Conjugating Enzyme; 1.
DR InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR InterPro; IPR046373; Acyl-CoA_Oxase/DH_mid-dom_sf.
DR InterPro; IPR036250; AcylCo_DH-like_C.
DR InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR InterPro; IPR013786; AcylCoA_DH/ox_N.
DR InterPro; IPR037069; AcylCoA_DH/ox_N_sf.
DR InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR InterPro; IPR000608; UBQ-conjugat_E2.
DR InterPro; IPR023313; UBQ-conjugating_AS.
DR InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
DR PANTHER; PTHR42807; GLUTARYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR42807:SF1; GLUTARYL-COA DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR Pfam; PF02771; Acyl-CoA_dh_N; 1.
DR Pfam; PF00179; UQ_con; 1.
DR SMART; SM00212; UBCc; 1.
DR SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
DR SUPFAM; SSF54495; UBC-like; 1.
DR PROSITE; PS00183; UBC_1; 1.
DR PROSITE; PS50127; UBC_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU362125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW Reference proteome {ECO:0000313|Proteomes:UP000252748};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT DOMAIN 509..659
FT /note="UBC core"
FT /evidence="ECO:0000259|PROSITE:PS50127"
FT REGION 443..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 597
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10133"
SQ SEQUENCE 659 AA; 72102 MW; C28090705FDC468C CRC64;
MFTRPVLRNS ARLTRQPWRP VAAARVGFAS SSSSSSAPPF DWQDALNSRN LLTEEEIAVA
ETAERYCQEY LAPRVLQAYR DEHYDASMLA EMGELGLLGA GISGYGCAGV SSVAGGLITR
AVERVDSGYR SGMSVQSSLV MGGIDQFGSA EQKERFLPDM ARGRLLGAFG LTEPNHGSDP
ASMESVARPH PSRTGYYALS GAKTWITNSP VADLLMVWAK MHDTGRIRGF LVERSLCPAG
TLETPAIKHK TGLRASVTGM ILMDDCPVPE ANMLPDVEGL RGPFSCLNKA RYGIAMGVMG
ALEDCIARAR TYALERKQFR GNPLARYQLV QKKLADAATD AAYGTLAAIQ VGRLRDEGKA
SPEMISMVKR QNCDAALRNA RALQEIFGGN AVSDEYAVGR HVANLYVAQT YEGQSDIHRD
GSGLSFSPCL VRLDLLPGLP QIRPFSSPNT RSLPSPSKKN TSSPDVISSP PEKASFYRST
TQPPPTHQKN AREQKKSSLS STTLEAAVMA LKRINKELTD LGRSTGKRLL WDRYVSTDED
GQNGRLTDDG CKTDSPYAGG VFFLGIHFPT DYPFKPPKVN FTTRIYHPNI NSNGSICLDI
LRDQWSPALT ISKVLLSICS MLTDPNPDDP LVPEIAHVYK TDRNRYETTA KEWTRKYAV
//
