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Database: UniProt
Entry: A0A1X2HHM8_SYNRA
LinkDB: A0A1X2HHM8_SYNRA
Original site: A0A1X2HHM8_SYNRA 
ID   A0A1X2HHM8_SYNRA        Unreviewed;       704 AA.
AC   A0A1X2HHM8;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   28-JUN-2023, entry version 21.
DE   SubName: Full=Carbamoyl-phosphate synthase L chain, ATP binding domain-domain-containing protein {ECO:0000313|EMBL:ORY97946.1};
GN   ORFNames=BCR43DRAFT_457179 {ECO:0000313|EMBL:ORY97946.1};
OS   Syncephalastrum racemosum (Filamentous fungus).
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Syncephalastraceae; Syncephalastrum.
OX   NCBI_TaxID=13706 {ECO:0000313|EMBL:ORY97946.1, ECO:0000313|Proteomes:UP000242180};
RN   [1] {ECO:0000313|EMBL:ORY97946.1, ECO:0000313|Proteomes:UP000242180}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 2496 {ECO:0000313|EMBL:ORY97946.1,
RC   ECO:0000313|Proteomes:UP000242180};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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:ORY97946.1}.
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DR   EMBL; MCGN01000004; ORY97946.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X2HHM8; -.
DR   STRING; 13706.A0A1X2HHM8; -.
DR   InParanoid; A0A1X2HHM8; -.
DR   OMA; FVEICSH; -.
DR   OrthoDB; 1459320at2759; -.
DR   Proteomes; UP000242180; Unassembled WGS sequence.
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   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.700.40; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_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; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 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   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 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:UP000242180}.
FT   DOMAIN          31..478
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          150..348
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          628..703
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   704 AA;  78048 MW;  891152F2454C97E4 CRC64;
     MFRLCTQYNT KPWRFSLSAR HAYSTQARNT LFEKILIANR GEIACRVMRT AKKLGIKTVA
     VYSEADANAQ HVKMADEAFL IGPPPSAQSY LSIDKILNVA RMTGSQAIHP GYGFLSENAE
     FADRVTAEKL AFIGPSGDAM RSMGSKSESK FIMEDAGVPV VPGYHGENQD VKFLKEQADK
     IGYPVLIKAV KGGGGKGMRI VRSPSEFEEM LESSKNESIK SFGDDKVLVE KYLERPRHVE
     VQVFADKHDN VVHLFERDCS VQRRHQKVIE EAPGPGLTEE IRAQLGAKAV AAARAVGYEN
     AGTVEFIMDN VDKQFYFMEM NTRLQVEHPV TEMVTNTDLV HWQLEVASGN RLPMTQEELR
     LMGHAFEARI YAENPSNHFL PDTGTLFSVR TPEPSEDVRV ETGFIQGDQI SVHYDPMIAK
     LVVRGEDRNE ALRRFRRALE QYQIVGLNTN IDFVKRVAEH PEFIKGEVET GFIQQFEKDL
     LKPAETPSPL TLATAANGLL LQEYARIQVS QKDPFSPWST LHSNFRLNGK DPREFTFISS
     HGEHKVAVTP SQQAGSVDIT VTLGQDQAPT TYTNVSSHWT DDGQVVSSID DKKVKSNVVT
     KGEKVTVFDE AGRTDLTLPT PGYILASAAG VAGTGSVKTP MPCKISQVLV KPGQQVEKDT
     TLIVLEAMKM EHVIKAPMAG TIDQVLYAVG DLVDENKNLV TFAE
//
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