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Database: UniProt
Entry: A0A176VQG2_MARPO
LinkDB: A0A176VQG2_MARPO
Original site: A0A176VQG2_MARPO 
ID   A0A176VQG2_MARPO        Unreviewed;       538 AA.
AC   A0A176VQG2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   08-NOV-2023, entry version 20.
DE   RecName: Full=Cytochrome P450 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AXG93_1953s1080 {ECO:0000313|EMBL:OAE23148.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE23148.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE23148.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE23148.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|RuleBase:RU000461}.
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:OAE23148.1}.
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DR   EMBL; LVLJ01002920; OAE23148.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VQG2; -.
DR   OrthoDB; 306875at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd20618; CYP71_clan; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR47944; CYTOCHROME P450 98A9; 1.
DR   PANTHER; PTHR47944:SF4; OS09G0441700 PROTEIN; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW   Metal-binding {ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202}.
SQ   SEQUENCE   538 AA;  60873 MW;  F7C602729DA8A49D CRC64;
     MKWSIVLAST CTVLTSFSVA QFLLWIKGNR LPRHGKLPPG PPSWGPLVGN LPQFRTSMRT
     PHVRAQELAK TYGPVMRVQM GGKVLIFISD PKIADRCFKD NDHNFANRPS IAAQKYLLYG
     GDHPSLAPIG DFWRSARKLY TTELLSGKKL QEFQVVRSEE MGQAVQDIYE ASARDASINM
     HDLFTKLFTN VITRMTMSRR FFNSANSAAK TLNETDSEAG SGNAELNDSM GNEWQQLIDS
     NHELMTRLLL EDVSPALAWV DILTGVRPRM QNSFARMDRL LQKVVDDHKA ELSSREKDSE
     NLDFIDVLLM LRDSSKTQFL SDRTIKAFSL DTIGAASETS TVTSEWALSE LLTNPEVMDK
     AREEVDSVVG KDRTVLESDL PNMPYIRALV NESLRLHPPL PWLVPHTNLM DCTLEDYNIP
     ANSILMFQVW AMQRDPLLWE RALEFDPSRF LNSDMDVKGM HTGLMPFGAG RRMCPGYNLG
     LTVLQYTLAR LIHSFDWSTT DPQVPLDMTE KFGLTSLRRA SVLHAKARPR LPHHLYTT
//
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