ID D8SDC5_SELML Unreviewed; 1194 AA.
AC D8SDC5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFJ17598.1};
GN ORFNames=SELMODRAFT_420859 {ECO:0000313|EMBL:EFJ17598.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ17598.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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}.
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DR EMBL; GL377613; EFJ17598.1; -; Genomic_DNA.
DR RefSeq; XP_002981410.1; XM_002981364.1.
DR AlphaFoldDB; D8SDC5; -.
DR STRING; 88036.D8SDC5; -.
DR EnsemblPlants; EFJ17598; EFJ17598; SELMODRAFT_420859.
DR GeneID; 9647252; -.
DR Gramene; EFJ17598; EFJ17598; SELMODRAFT_420859.
DR KEGG; smo:SELMODRAFT_420859; -.
DR eggNOG; KOG0370; Eukaryota.
DR HOGENOM; CLU_000513_1_0_1; -.
DR InParanoid; D8SDC5; -.
DR OMA; FPFNKFP; -.
DR OrthoDB; 309at2759; -.
DR UniPathway; UPA00070; UER00115.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central.
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:UP000001514};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 227..423
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 785..978
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1045..1186
FT /note="MGS-like"
FT /evidence="ECO:0000259|PROSITE:PS51855"
SQ SEQUENCE 1194 AA; 130265 MW; 5380C540B7A36E44 CRC64;
MAAEMLAPRF RGIDAPAFSD FTENRLKHAA AGCRDWNSRR SHRGLAVRAS GSGAWHWNPS
QYRHARKKWE ARSVEQEVES LPFIEWSKKG NVCKGKKRTD LKKILILGAG PIVIGQACEF
DYSGTQACKA LKEEGYEVVL INSNPATIMT DPDLADRTYI APMTPELVEQ VIAKERPDAV
LPTMGGQTAL NLAVALAESG ALDKYGVELI GAKLDAIKKA EDRDLFRQAM QKIGVKTPPS
GIATTLEECF QIAETIGEFP LIIRPAFTLG GTGGGIAYNR EELETICKAG LTASITSQVL
VEKSLLGWKE YELEVMRDLA DNVVIICSIE NIDPMGVHTG DSITVAPAQT LTDKEYQRLR
DQAIAIIREI GVECGGSNVQ FAINPEDGEV MVIEMNPRVS RSSALASKAT GFPIAKMAAK
LSVGYTLDQI PNDITRKTPA SFEPSIDYVV TKIPRFAFEK FPGSQAILTT QMKSVGEAMA
IGRTFQESFQ KAVRSLETGH SGWGCEDSKE LKWDIEELKY KLRVPNPDRM YAVYAAMKRG
MSAEEIHELT FIDPWFLGEL KELFGVEEFL SNTKLTELSK DDMYEIKRRG FSDRQVAYAT
KSAEAEVRAH RIALGVVPAF KRVDTCAAEF EAKTPYMYSS YDDECEANSG SKRKVLILGG
GPNRIGQGIE FDYCCCHASF VLREAGFETI MMNSNPETVS TDYDTSDRLY FEPLTTEDVL
NIIDLEKPDG IIVQFGGQTP LKLAVPIQNY LDDFKPLSAS GDGYVKIWGT SPDSIDASED
RKRFESILNQ LGIKQPPGGI ARSEEDALAI AKRVGFPVVV RPSYVLGGRA MEIVYSNDKL
KKYLETAVEV DPGRPVLVDK YLTDSSEIDV DCLADGNGGV VIGGIMEHIE QAGVHSGDSA
CSIPTQTIPA VALATIRDAT TKLAKKLNVC GLMNCQFAIT QSGEVYIIEA NPRASRTVPF
VSKAIGHPLA KYAALVMSGK SLGDLGFSQE VIPAHVSVKE AVLPFDKFQG CDVLLGPEMR
STGEVMGIDY SFDKAFGKSQ IAANQKLPLQ GTVFISLNDQ TKAQAVPIAR GFHALGFNIV
STSGTAKFLE EQGIPVERVL KLHEGRPHAG DLVANGQIQL MIITSSGDAL DEKDGRQLRR
SALAYKVPIV TTIAGGLANL QAVKSLKECP VEMLALQDFF KADKVVAEIA SVVV
//
