ID   A0A1S3G3K7_DIPOR        Unreviewed;       713 AA.
AC   A0A1S3G3K7;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Biotin--protein ligase {ECO:0000313|RefSeq:XP_012882874.1};
GN   Name=Hlcs {ECO:0000313|RefSeq:XP_012882874.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012882874.1};
RN   [1] {ECO:0000313|RefSeq:XP_012882874.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012882874.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the biotin--protein ligase family.
CC       {ECO:0000256|ARBA:ARBA00009934}.
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DR   RefSeq; XP_012882874.1; XM_013027420.1.
DR   AlphaFoldDB; A0A1S3G3K7; -.
DR   STRING; 10020.ENSDORP00000024420; -.
DR   GeneID; 105994008; -.
DR   KEGG; dord:105994008; -.
DR   CTD; 3141; -.
DR   InParanoid; A0A1S3G3K7; -.
DR   OrthoDB; 317678at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:InterPro.
DR   GO; GO:0036211; P:protein modification process; IEA:InterPro.
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, ECO:0000313|RefSeq:XP_012882874.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671}.
FT   DOMAIN          440..638
FT                   /note="BPL/LPL catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51733"
FT   REGION          31..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   713 AA;  79110 MW;  87A2D1B5BC78DF65 CRC64;
     MEDRLQMDNG LIPQKIVSVH LQDSTLKELK DQAARGQVQS LKLAARPSPE PKPVQHADRD
     EPRAPGQDSC KQRTDGEGEP EEHSHLHLFS CHECLELENS TIESVKFASA ENIPDLPYDH
     SSGLEAVTDE LCPKREESRV NMVGKAPNIL VYVGPGTQDT LGRLEQVRSV LADCVDADSY
     TIYHLPEDSG LRDPWADNCI LLVIAALEPI PKDLYQKFMA YLSQGGKVLA LSSSFTFGGF
     QVTGEGMLRK TVQDLVFCKA DRSEVRLSVL SSGRFYKAGP REQLSPAGLH GHLDTEDKDR
     TILQVPFGSC GGEAVLCQVH LELPPSSPTV QTQEDFNLLK SSNMKRYEVL REILTTLGIS
     CDVRQVPALT PVSLLLATEE IRDPLMQWLG AHVDPKGVIK SSKLSLKFVS SCASEVEVTP
     SSIPVITDTE DFSSEHFNLD IYRQNLQTKQ LGKVILFAEV TPTTMNLLDG LMFEMPQEMG
     LIAIAVRQTQ GKGRGPNAWL SPVGCALSTL LISIPLRSQL GQRIPFVQHL MSLAVVEAVR
     STPKYQDINL RVKWPNDIYY SDLMKIGGVL VNSTLLGETF YILIGFGFNV TNSNPTICIN
     DLITEHNKQH KTALKPFRAD CLIARAVTML EKLVHTFQDE GPQSILPLYY KYWLHSGQQV
     RLGSTEGPQV SIVGLDDSGF LQVHQEDGRI VTVHPDGNSF DMLRNLIVPK QRW
//