ID A0A2K6CEM0_MACNE Unreviewed; 874 AA.
AC A0A2K6CEM0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Holocarboxylase synthetase {ECO:0000313|Ensembl:ENSMNEP00000022118.1};
GN Name=HLCS {ECO:0000313|Ensembl:ENSMNEP00000022118.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000022118.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000022118.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC {ECO:0000256|ARBA:ARBA00009934}.
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DR AlphaFoldDB; A0A2K6CEM0; -.
DR STRING; 9545.ENSMNEP00000022118; -.
DR Ensembl; ENSMNET00000046371.1; ENSMNEP00000022118.1; ENSMNEG00000034742.1.
DR GeneTree; ENSGT00390000002960; -.
DR OrthoDB; 317678at2759; -.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000034742; Expressed in pituitary gland and 12 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005652; C:nuclear lamina; IEA:Ensembl.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0009374; F:biotin binding; IEA:Ensembl.
DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:InterPro.
DR GO; GO:0004080; F:biotin-[propionyl-CoA-carboxylase (ATP-hydrolyzing)] ligase activity; IEA:Ensembl.
DR GO; GO:0019899; F:enzyme binding; IEA:Ensembl.
DR GO; GO:0043687; P:post-translational protein modification; IEA:Ensembl.
DR GO; GO:0070781; P:response to biotin; IEA:Ensembl.
DR CDD; cd16442; BPL; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004408; Biotin_CoA_COase_ligase.
DR InterPro; IPR003142; BPL_C.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR NCBIfam; TIGR00121; birA_ligase; 1.
DR PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR Pfam; PF02237; BPL_C; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000233120}.
FT DOMAIN 602..800
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
FT REGION 176..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 874 AA; 97164 MW; BD624D05D0F9D959 CRC64;
MLITLCYLYL WARWGRRPAE LVRATVRRLR ASRCSFTFCG AAAQPPGARV CLSRGGRVFC
VSDSQSIEDL NKWALFLVSP FILEAEHIAF VTESIWVQSE NLQRSSSSSE TIVEWSDCCL
PLACRPGDPY RLIAEASVDN FSKLGVAFME DRLHMDNGLV PQKIMSVRLQ DSTLKEVKDQ
ASNKQVQILE PRSEPSLEIK PEQDGMEHVG RDDPKALGEE PKQRRGSASG SEPAGDSDRG
GGPIEHYHLH LSSCHECLEL ENSTIESVKF ASAENIPDLP YDYSSSLESV ADETSPEREG
RRVNLTGKAP NILLYVGSDS QEALGRFHEV RSVLADCVDI DSYVLYHLLE DSALRDPWTD
NCLLLVIATR ESIPEDLYQK FMAYLSQGGK VLGLSSSFTF GGFQVTSKGA LRKTVQNLVF
SKADQSEVKL SVLSSGCRYQ EGPVRLSPGG LQGHLENDDK DRMIVHVPFG THGGEAVLCQ
VHLELPPSSD IVQTPEDFNL LKSSNFRRYE VLREILTTLG LSCDMKQVPA LTPLYLLSAA
EEIRDPLMQW LGKHVDSEGE IKSSQLSLRF VSSYVSEVEI TPSCIPVVTN MEAFSSENFN
LEIYRQNLQT KQLGKVILFA EVTPTTMRLL DGLMFQTPQE MGLIAIAARQ TQGKGRGGNA
WLSPVGCALS TLLISIPLRS QLGQRIPFVQ HLMSVAVVEA VRSIPKYQDI NLRVKWPNDI
YYSDLMKIGG VLVNSTLMGE TFHILIGCGF NVTNSNPTIC INDLVTEYNK QHKAELKPLR
ADYLIARVVT VLEKLIEEFQ DKGPNSVLPL YYRYWVHSGQ QVHLGSADGP KVSIVGLDDS
GFLQVHQEGG EVVTVHPDGN SFDMLRNLIL PKRR
//