ID A0A1R3I953_COCAP Unreviewed; 792 AA.
AC A0A1R3I953;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=procollagen-proline 4-dioxygenase {ECO:0000256|ARBA:ARBA00012269};
DE EC=1.14.11.2 {ECO:0000256|ARBA:ARBA00012269};
GN ORFNames=CCACVL1_13906 {ECO:0000313|EMBL:OMO79115.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO79115.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO79115.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO79115.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290;
CC Evidence={ECO:0000256|ARBA:ARBA00001961};
CC -!- SIMILARITY: Belongs to the GPAT/DAPAT family.
CC {ECO:0000256|ARBA:ARBA00007937}.
CC -!- SIMILARITY: Belongs to the P4HA family.
CC {ECO:0000256|ARBA:ARBA00006511}.
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:OMO79115.1}.
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DR EMBL; AWWV01010466; OMO79115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3I953; -.
DR STRING; 210143.A0A1R3I953; -.
DR EnsemblPlants; OMO79115; OMO79115; CCACVL1_13906.
DR Gramene; OMO79115; OMO79115; CCACVL1_13906.
DR OrthoDB; 5488227at2759; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0090447; F:glycerol-3-phosphate 2-O-acyltransferase activity; IEA:UniProt.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:InterPro.
DR GO; GO:0004656; F:procollagen-proline 4-dioxygenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06551; LPLAT; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 2.60.120.620; q2cbj1_9rhob like domain; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR002123; Plipid/glycerol_acylTrfase.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR044862; Pro_4_hyd_alph_FE2OG_OXY.
DR InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR15486; ANCIENT UBIQUITOUS PROTEIN; 1.
DR PANTHER; PTHR15486:SF91; PHOSPHOLIPID_GLYCEROL ACYLTRANSFERASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
DR Pfam; PF01553; Acyltransferase; 1.
DR Pfam; PF12710; HAD; 1.
DR SMART; SM00702; P4Hc; 1.
DR SMART; SM00563; PlsC; 1.
DR SMART; SM00254; ShKT; 1.
DR SUPFAM; SSF69593; Glycerol-3-phosphate (1)-acyltransferase; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
DR PROSITE; PS51670; SHKT; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000313|EMBL:OMO79115.1};
KW Dioxygenase {ECO:0000256|ARBA:ARBA00022964};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023209};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Transferase {ECO:0000313|EMBL:OMO79115.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 218..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 613..735
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT DOMAIN 750..790
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
SQ SEQUENCE 792 AA; 87820 MW; CDD17017FC33904E CRC64;
MDGTLVRGRS SFPYFALVAF EVGGILRLLF LLLTSPIAGI LYYFISESAG IRVLVFATFV
GMKVSDIESV ARAVLPKFYS VDLHPETWRV FSSCGKRCVL TANPRVMVEP FLKDYLGADL
VIGTEIHVIG GRASGLVETP GILVGKNKAD ALDKAFKDDP TVPDIALGDR KTDFPFMKLC
KEKYVVPKKP EVKAVSLDKL PKPVIFHDGR LVQKPTPLMA LIIVLWIPVG FLLACLRIAA
GTLLPMPLVY YAFWALGVRV YIKGTPPPPA KKSIGQSGVL FICSHRTLLD PIFLSTALGR
PIPAVTYSLS RLSEFISPIR TVRLSRDRAT DASMIKKLLE EGDLVICPEG TTCREPFLLR
FSALFAELTD ELVPVAMANR MSMFHGTTAR GWKGMDPFYF FMNPSPAYEV TFLNKLPYEL
SCSAGKSSHE VANYIQRMIA SSLSYECTSF TRKDKYRALA GNDGTVVEKP KLSPNKIEAN
QGVFLMDSRC FLGFFLLIFL HLCLVSAEIN GSVIKMKRGT SSVPFDPTRV TQLSWHPRAF
IYKGFLSSDE CDHLITLAKD KLEKSMVADN ESGQSIESEV RTSSGMFLQK AQDEVVADIE
ARISAWTFLP VENGESMQIL HYEHGQKYEP HFDYFHDKAN QELGGHRIAT VLMYLSDVES
GGETVFPNSE GKLAQPKDDS WSDCAKNGYA VKPRKGDALL FFSLHPDATT DANSLHGSCP
VIKGEKWSAT KWIHVRSFDK LERRSANGDC VDENENCAMW AKAGECEKNS AYMVGSEESF
GYCRKSCNAC SS
//
