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Database: UniProt
Entry: F7H7Y8_CALJA
LinkDB: F7H7Y8_CALJA
Original site: F7H7Y8_CALJA 
ID   F7H7Y8_CALJA            Unreviewed;       702 AA.
AC   F7H7Y8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 3.
DT   24-JAN-2024, entry version 69.
DE   SubName: Full=Methylcrotonyl-CoA carboxylase subunit 1 {ECO:0000313|Ensembl:ENSCJAP00000009366.4};
GN   Name=MCCC1 {ECO:0000313|Ensembl:ENSCJAP00000009366.4};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|Ensembl:ENSCJAP00000009366.4, ECO:0000313|Proteomes:UP000008225};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000009366.4}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSCJAP00000009366.4}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
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DR   AlphaFoldDB; F7H7Y8; -.
DR   Ensembl; ENSCJAT00000009901.5; ENSCJAP00000009366.4; ENSCJAG00000005103.6.
DR   eggNOG; KOG0238; Eukaryota.
DR   GeneTree; ENSGT00940000156941; -.
DR   HOGENOM; CLU_000395_3_1_1; -.
DR   TreeFam; TF105650; -.
DR   Proteomes; UP000008225; Chromosome 15.
DR   Bgee; ENSCJAG00000005103; Expressed in testis and 6 other cell types or tissues.
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; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.700.40; -; 1.
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; 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; 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; 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:UP000008225}.
FT   DOMAIN          49..495
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          168..365
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   REGION          678..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..702
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   702 AA;  77901 MW;  CF25E2A9B59FEDBF CRC64;
     MAAVSAVSAL LAAAAERNRW QRLPSLLLPP RTWVWRQRTM KYATTTGRNI TKVLIANRGE
     IACRVMRTAR KLGVQSVAVY SEADRNSMHV DMADEAYSIG PAPLQQSYLS MEKIIQVAKT
     SAAQAIHPGY GFLSENMEFA ELCKEEGIIF IGPPPSAIRD MGIKSTSKSI MAAAGVPIVE
     GYHGEDQSDQ CLKEHAGRIG YPVMIKAVRG GGGKGMRIVR SEQEFQEQLE SARREAKKSF
     SDDAVLIEKF VDTPRHVEVQ VFGDHHGNAV YLFERDCSVQ RRHQKIIEEA PAPGIKPEVR
     KQLGEAAVRA AKAVNYVGAG TVEFIMDSKH NFYFMEMNTR LQVEHPVTEM ITGTDLVEWQ
     LRIAAGEMIP LSQEEIPLQG HAFEARIYAE DPSRNFLPGT GPLVHLSTPP ADPCTRIETG
     VRQGDEVSVH YDPMIAKLVV WAADRQAALT KLRYSLHQYH IVGLHTNINF LLNLSGHPEF
     EAGNVHTDFI PQHHKELLPS WKAAAKETLC QAALGLILKE KAMTDAFTLQ THDRFSPFSS
     SSGRRLNISY TRNMTLKDGK NNIAIAVTYN HDGSYNMQIE DKTFQVLGDI YSKGDCTYLK
     CSVNGVASTV KLIILENTLY LFSKEGNIEI DIPVPKYLSS VGSEGTQGGP LAPMTGTIEK
     HTIKAPKDGT VKKVFYREGA QASRHTPLVE FEEEEPDKRN SE
//
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