ID A0A1R3K7V8_COCAP Unreviewed; 1185 AA.
AC A0A1R3K7V8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OMP03171.1};
GN ORFNames=CCACVL1_02520 {ECO:0000313|EMBL:OMP03171.1};
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:OMP03171.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMP03171.1, 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:OMP03171.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=2 ATP + hydrogencarbonate + NH4(+) = 2 ADP + carbamoyl
CC phosphate + 2 H(+) + phosphate; Xref=Rhea:RHEA:18029,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:456216; EC=6.3.4.16;
CC Evidence={ECO:0000256|ARBA:ARBA00043687};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl
CC phosphate from bicarbonate: step 1/1. {ECO:0000256|ARBA:ARBA00005077}.
CC -!- SIMILARITY: Belongs to the CarB family.
CC {ECO:0000256|ARBA:ARBA00009799}.
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:OMP03171.1}.
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DR EMBL; AWWV01006114; OMP03171.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3K7V8; -.
DR STRING; 210143.A0A1R3K7V8; -.
DR EnsemblPlants; OMP03171; OMP03171; CCACVL1_02520.
DR Gramene; OMP03171; OMP03171; CCACVL1_02520.
DR OMA; FPFNKFP; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01424; MGS_CPS_II; 1.
DR Gene3D; 3.40.50.20; -; 2.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR Gene3D; 1.10.1030.10; Carbamoyl-phosphate synthetase, large subunit oligomerisation domain; 1.
DR Gene3D; 3.40.50.1380; Methylglyoxal synthase-like domain; 1.
DR HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006275; CarbamoylP_synth_lsu.
DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR InterPro; IPR011607; MGS-like_dom.
DR InterPro; IPR036914; MGS-like_dom_sf.
DR InterPro; IPR033937; MGS_CPS_CarB.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR NCBIfam; TIGR01369; CPSaseII_lrg; 1.
DR PANTHER; PTHR11405:SF5; CAD PROTEIN; 1.
DR PANTHER; PTHR11405; CARBAMOYLTRANSFERASE FAMILY MEMBER; 1.
DR Pfam; PF02786; CPSase_L_D2; 2.
DR Pfam; PF02787; CPSase_L_D3; 1.
DR Pfam; PF02142; MGS; 1.
DR PRINTS; PR00098; CPSASE.
DR SMART; SM01096; CPSase_L_D3; 1.
DR SMART; SM00851; MGS; 1.
DR SUPFAM; SSF48108; Carbamoyl phosphate synthetase, large subunit connection domain; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52335; Methylglyoxal synthase-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
DR PROSITE; PS00866; CPSASE_1; 2.
DR PROSITE; PS00867; CPSASE_2; 2.
DR PROSITE; PS51855; MGS; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyrimidine biosynthesis {ECO:0000256|ARBA:ARBA00022975};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 214..410
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 772..965
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1032..1185
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
FT REGION 62..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1185 AA; 129889 MW; 415A5876FD5CBB61 CRC64;
MSSCRNLSSA ISHFSYITNP SLPKSLNFKF FFSSSSHSKT HPKTSFHLRS WPQQRGHYQV
ATKPVTAQAS STATAEEKAP KLGKRTDLKK IMILGAGPIV IGQACEFDYS GTQACKALRE
EGYEVVLINS NPATIMTDPD MADRTYVTPM TPELLEQVLE KERPDALLPT MGGQTALNLA
VALAESGVLA KYGVELIGAK LDAIKKAEDR ELFKQAMKKI GIKTPPSGIG NTLDECIEIA
NEIGEFPLII RPAFTLGGTG GGIAYNKEEF EAICKSGLAA SLTSQVLVEK SLLGWKEYEL
EVMRDLADNV VIICSIENID PMGVHTGDSI TVAPAQTLTD KEYQRLRDYS VKIIREIGVE
CGGSNVQFAV NPVDGEVMVI EMNPRVSRSS ALASKATGFP IAKMAAKLSV GYSLDQIPND
ITKKTPASFE PSIDYVVTKI PRFAFEKFPG SQPILTTQMK SVGESMALGR TFQESFQKAV
RSLECGYSGW GCAKVKELDW DWDQLKYSLR VPSPDRIHAI YAAMKKGMKV DEIYELSFID
KWFLTQLKEL VDVEQYILSR SLSELTKDEI YEIKKRGFSD KQIAFATKSS EKEVRDKRIS
LGVTPTYKRV DTCAAEFEAN TPYMYSSYDF ECESAPTEKK KVLILGGGPN RIGQGIEFDY
CCCHTSFALQ KAGYETIMMN SNPETVSTDY DTSDRLYFEP LTVEDVLNVI DLERPDGIIV
QFGGQTPLKL ALPIQHYLDE HQPLCASGVG HVRIWGTSPD SIDAAEDRER FNAILNELKI
EQPKGGIAKS EDDALAIATD IGYPVVVRPS YVLGGRAMEI VYSDDKLVTY LENAVEVDPE
RPVLIDKYLS DAIEIDVDAL ADSHGNVVIG GIMEHIEQAG VHSGDSACSI PTQTIPSSCL
NTIRSWTTKL AKRLNVCGLM NCQYAITASG DVFLLEANPR ASRTVPFVSK AIGHPLAKYA
ALVMSGMSLN DLNFTKEVTP QHVSVKEAVL PFEKFQGCDV LLGPEMRSTG EVMGIDFEFA
IAFAKAQIAA GEKLPMSGTV FLSLNDLTKP YLERIANTFL GLGFRIVSTS GTAHFLELKG
IPVERVLKMH EGRPHAGDMV TNGQIQLMVI TSSGDALDQI DGKQLRRMAL AYKVPIITTV
EGALASAEAI KSLKSCTINM IALQDFFETD LETGTSKDLL STSSL
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