ID A0A3L6SFW5_PANMI Unreviewed; 410 AA.
AC A0A3L6SFW5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=procollagen-proline 3-dioxygenase {ECO:0000256|ARBA:ARBA00012262};
DE EC=1.14.11.7 {ECO:0000256|ARBA:ARBA00012262};
GN ORFNames=C2845_PM02G32120 {ECO:0000313|EMBL:RLN19878.1};
OS Panicum miliaceum (Proso millet) (Broomcorn millet).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum.
OX NCBI_TaxID=4540 {ECO:0000313|EMBL:RLN19878.1, ECO:0000313|Proteomes:UP000275267};
RN [1] {ECO:0000313|Proteomes:UP000275267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30683860; DOI=10.1038/s41467-019-08409-5;
RA Zou C., Miki D., Li D., Tang Q., Xiao L., Rajput S., Deng P., Jia W.,
RA Huang R., Zhang M., Sun Y., Hu J., Fu X., Schnable P.S., Li F., Zhang H.,
RA Feng B., Zhu X., Liu R., Schnable J.C., Zhu J.-K., Zhang H.;
RT "The genome of broomcorn millet.";
RL Nat. Commun. 10:436-436(2019).
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the leprecan family.
CC {ECO:0000256|ARBA:ARBA00006487}.
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:RLN19878.1}.
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DR EMBL; PQIB02000005; RLN19878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L6SFW5; -.
DR STRING; 4540.A0A3L6SFW5; -.
DR Proteomes; UP000275267; Chromosome 2.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0019797; F:procollagen-proline 3-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0032963; P:collagen metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR039575; P3H.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR PANTHER; PTHR14049; LEPRECAN 1; 1.
DR PANTHER; PTHR14049:SF9; PROCOLLAGEN-PROLINE 3-DIOXYGENASE; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000275267};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 81..186
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 410 AA; 46091 MW; 4CB05D04308604AF CRC64;
MASTTASPPP AAGDHPRVLL RGFLSRETCK ELEFVHRSCG AAGYRPSVVS TSLPHLAATG
CGHLLLPFVP VRERLRDAVE SFFDCLFDVF IEFTGLISWC KGASIGWHSD DNKPYLRQRT
FTAVCYLNNH GEDYKGGILQ FQDGDPSSIV PVAGDVVIYT ADNRNVHCVT EVTEGERLTL
TLWFTRDRAY NEDPKLLTFL SQTSLSCEPT KQKSYIPMPA SDNMYWFSCD QSGFDIRCAR
VHVLGFSFHS SSGEYSTSVL PTEDDPLELL GKQLRLGRGD DVFDKIFSNS LHALQVVQFY
YWKAPELAAR REQSAVGSRT VRYPVIIHHS RGTELPLPCN HTLAQTIFGS VNTAEIAFKW
NDFALGVAMW ENYSEELKKQ LLTFLPFWLS NESIFVVDSS ELQCRPPFLT
//
