ID D8RJ07_SELML Unreviewed; 636 AA.
AC D8RJ07;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EFJ27834.1};
GN ORFNames=SELMODRAFT_411779 {ECO:0000313|EMBL:EFJ27834.1};
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:EFJ27834.1, 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).
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DR EMBL; GL377581; EFJ27834.1; -; Genomic_DNA.
DR RefSeq; XP_002971236.1; XM_002971190.1.
DR AlphaFoldDB; D8RJ07; -.
DR STRING; 88036.D8RJ07; -.
DR EnsemblPlants; EFJ27834; EFJ27834; SELMODRAFT_411779.
DR Gramene; EFJ27834; EFJ27834; SELMODRAFT_411779.
DR KEGG; smo:SELMODRAFT_411779; -.
DR eggNOG; KOG0238; Eukaryota.
DR HOGENOM; CLU_000395_3_3_1; -.
DR InParanoid; D8RJ07; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR045774; MCCA_BT_dom.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF19331; MCCA_BT; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000001514}.
FT DOMAIN 36..503
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 155..342
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT REGION 592..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 69539 MW; D6DED70666829B06 CRC64;
MGNSASIARR SKRCWSSLAN PFSQAPPVEK SPAQQPIEKI LIANRGEIAC RIIKTARSLG
LKTVAVYSDA DRNSLHVRRA DEAVFIGPAS AQLSYLSTTS ILDAARRTGA DAIHPGYGFL
SENSKFAQAC HESGITFIGP SAAAISLMGD KSASKKLMSG ANVPVVPGYH GDDQSHELLQ
SEADRIGYPV LIKPVLGGGG KGMRIVHSRD EFLDSLRSAL RESAAAFGDT RVLIEKYIAQ
PRHIEVQIFG DRFGNVVHLF ERDCSVQRRH QKIIEEAPAP LMSDDFRNSI GQAAVNAAKF
IVDTATGDFF FMEMNTRLQV EHPVTEMVTR QDLVEWQIRV ANGESLPLEQ KSHAFEARVY
AENVPRGFLP AAGVLYHYNP PPASSTVRIE TGVEQSDAVA GLPTNIHFLK KLAKHPAFRA
GDLETQPLDF SERAKRDVKS FAALAAVGVC VRESFRRPES RTGGPWHTTS GFRVNNPYTR
KISLDWMPES ESLSCEPMSL DVTYSSDSEF LVKIHLVSNT AKRVASSGCD ITVDINGISS
TISYGYYLQA VEDLHGRVDA ATPAIHADER SRQDGREFEA LLVDSRVDGL AEREEGEAEV
GAGFQDGGED ESQFRFVESQ SNGLVSGNFW LTPADL
//
