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Database: UniProt
Entry: A0A060SGR5_PYCCI
LinkDB: A0A060SGR5_PYCCI
Original site: A0A060SGR5_PYCCI 
ID   A0A060SGR5_PYCCI        Unreviewed;       568 AA.
AC   A0A060SGR5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Acyl-CoA dehydrogenase/oxidase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN946_scf184909.g13 {ECO:0000313|EMBL:CDO71419.1};
OS   Pycnoporus cinnabarinus (Cinnabar-red polypore) (Trametes cinnabarina).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=5643 {ECO:0000313|EMBL:CDO71419.1, ECO:0000313|Proteomes:UP000029665};
RN   [1] {ECO:0000313|EMBL:CDO71419.1, ECO:0000313|Proteomes:UP000029665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRFM137 {ECO:0000313|EMBL:CDO71419.1,
RC   ECO:0000313|Proteomes:UP000029665};
RA   Levasseur A., Lomascolo A., Ruiz-Duenas F.J., Uzan E., Piumi F., Kues U.,
RA   Ram A.F.J., Murat C., Haon M., Benoit I., Arfi Y., Chevret D., Drula E.,
RA   Kwon M.J., Gouret P., Lesage-Meessen L., Lombard V., Mariette J.,
RA   Noirot C., Park J., Patyshakuliyeva A., Wieneger R.A.B., Wosten H.A.B.,
RA   Martin F., Coutinho P.M., de Vries R., Martinez A.T., Klopp C.,
RA   Pontarotti P., Henrissat B., Record E.;
RT   "The genome of the white-rot fungus Pycnoporus cinnabarinus: a
RT   basidiomycete model with a versatile arsenal for lignocellulosic biomass
RT   breakdown.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|RuleBase:RU362125};
CC   -!- SIMILARITY: Belongs to the acyl-CoA dehydrogenase family.
CC       {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:CDO71419.1}.
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DR   EMBL; CCBP010000101; CDO71419.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A060SGR5; -.
DR   STRING; 5643.A0A060SGR5; -.
DR   HOGENOM; CLU_016513_1_0_1; -.
DR   OMA; FQGAMFM; -.
DR   OrthoDB; 5489386at2759; -.
DR   Proteomes; UP000029665; 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   Gene3D; 2.40.110.20; -; 1.
DR   Gene3D; 6.10.250.600; -; 1.
DR   Gene3D; 1.20.140.10; Butyryl-CoA Dehydrogenase, subunit A, domain 3; 1.
DR   InterPro; IPR006091; Acyl-CoA_Oxase/DH_mid-dom.
DR   InterPro; IPR036250; AcylCo_DH-like_C.
DR   InterPro; IPR009075; AcylCo_DH/oxidase_C.
DR   InterPro; IPR009100; AcylCoA_DH/oxidase_NM_dom_sf.
DR   InterPro; IPR041504; AidB_N.
DR   PANTHER; PTHR42707; ACYL-COA DEHYDROGENASE; 1.
DR   PANTHER; PTHR42707:SF2; ACYL-COA DEHYDROGENASE FAMILY MEMBER 11; 1.
DR   Pfam; PF00441; Acyl-CoA_dh_1; 1.
DR   Pfam; PF02770; Acyl-CoA_dh_M; 1.
DR   Pfam; PF18158; AidB_N; 1.
DR   SUPFAM; SSF47203; Acyl-CoA dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF56645; Acyl-CoA dehydrogenase NM domain-like; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU362125};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU362125};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU362125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029665}.
FT   DOMAIN          8..163
FT                   /note="Adaptive response protein AidB N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18158"
FT   DOMAIN          172..286
FT                   /note="Acyl-CoA oxidase/dehydrogenase middle"
FT                   /evidence="ECO:0000259|Pfam:PF02770"
FT   DOMAIN          297..456
FT                   /note="Acyl-CoA dehydrogenase/oxidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00441"
SQ   SEQUENCE   568 AA;  62407 MW;  B5A9DF90A10259D6 CRC64;
     MRVEEGFQPV PFIEGNPYTT DPVLPVLLKR ILPSDVFQDV DKDLQRFGGE VLTTMRELTK
     RATPPQLVQY DNWGRRVDDL RTSEGWRGLK DVFHREGIVS IAYERKYREH SRPYGFAKLF
     IAAADSDVTD CPMSMTDGVA RVLELIGSPA LKQEVLPRLI SRDPARAYTA GQWMTERPGG
     SDVSRMETVA TPVPGAASPY GPQDKIDGFK WFSSATDSDV ALALARTGRP DDGSRGLSLF
     LIPVRLPLVR APGAPRPPAL TNNIYIHRLK NKFGTKIVPT AELSIQGADA YLLGEPNQGV
     KLITPVLNIT RTHSAIGSVA YLRKCLAIAT AHSNGRAIKG GRQLLRNTPL HVAELAKLHV
     LYRALVHFVF GSVVLLGKAE CGVATENEGL RLRLLTPAIK AFAADKCVTA MEECMTMLGG
     EGYMEENGIT KLIQDGLVEK IWEGTITVLS LDLVRAVEKS AALDAFVKWA NDIMASCPSQ
     LAESLREPLA LLRKGLDVLT GTYDAPMHPL VPRPALFLFC HIACSVYLLE HALWAVKTSE
     PGNENDIEVF KRWVEEGGLY TALENSMA
//
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