ID G0V900_NAUCC Unreviewed; 689 AA.
AC G0V900;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=BPL/LPL catalytic domain-containing protein {ECO:0000259|PROSITE:PS51733};
GN Name=NCAS0A13910 {ECO:0000313|EMBL:CCC67949.1};
GN OrderedLocusNames=NCAS_0A13910 {ECO:0000313|EMBL:CCC67949.1};
OS Naumovozyma castellii (strain ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC
OS 1992 / NRRL Y-12630) (Yeast) (Saccharomyces castellii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX NCBI_TaxID=1064592 {ECO:0000313|EMBL:CCC67949.1, ECO:0000313|Proteomes:UP000001640};
RN [1] {ECO:0000313|EMBL:CCC67949.1, ECO:0000313|Proteomes:UP000001640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 76901 / BCRC 22586 / CBS 4309 / NBRC 1992 / NRRL Y-12630
RC {ECO:0000313|Proteomes:UP000001640};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Type strain:CBS 4309;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Genome sequence of Naumovozyma castellii.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HE576752; CCC67949.1; -; Genomic_DNA.
DR RefSeq; XP_003674329.1; XM_003674281.1.
DR AlphaFoldDB; G0V900; -.
DR STRING; 1064592.G0V900; -.
DR GeneID; 11529409; -.
DR KEGG; ncs:NCAS_0A13910; -.
DR eggNOG; KOG1536; Eukaryota.
DR HOGENOM; CLU_006150_1_1_1; -.
DR InParanoid; G0V900; -.
DR OMA; HHAFYSN; -.
DR OrthoDB; 317678at2759; -.
DR Proteomes; UP000001640; Chromosome 1.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0036211; P:protein modification process; IEA:InterPro.
DR CDD; cd03144; GATase1_ScBLP_like; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR019197; Biotin-prot_ligase_N.
DR InterPro; IPR004143; BPL_LPL_catalytic.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR12835; BIOTIN PROTEIN LIGASE; 1.
DR PANTHER; PTHR12835:SF5; BIOTIN--PROTEIN LIGASE; 1.
DR Pfam; PF03099; BPL_LplA_LipB; 1.
DR Pfam; PF09825; BPL_N; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Reference proteome {ECO:0000313|Proteomes:UP000001640}.
FT DOMAIN 375..606
FT /note="BPL/LPL catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51733"
SQ SEQUENCE 689 AA; 76083 MW; 3CD08240AE4EFF65 CRC64;
MNVLVYNGPG TTPGSVKHVV ETLRHFLEPY YAVSTVTAKT LETEPWSSKA SAVVFPGGAD
LPFVKECKPI IPLLKQFVSK QGGVYIGFCA GSYFGSGRVE FAQGNPEMEV TGSRDLKFFK
GIARGPAFNG FQYNSELGAR AAKLSCLDGL EFSTYYNGGP VFVDADHYDN VEVLARYIEP
LDVSYTDSKD RLSIKAPAAT ILCTVGKGKA LLVGAHPEFI PKMLKRSDDA KFISDVVNKL
ETQEESRLKF MHFILAKAGL TCNTNWEMKR EPGLTPIIAA TAPDKNYILE DFENNIAKHT
SNIENKADHV EFKDQNDTFD LYLGLDKYEQ ANATLVDKDV IETSKPIILS NKNETFSLPK
AAISFNIQKY FDFLSPNNSI GSFLLYGEVV TSTSSLLDNN KTMLSCLPEN TVLHVGSVQV
TGRGRSGNSW VNPRGVCAST AAISLPLKSP KTGESISIVF VQYLSMLAYC KAITSYAPGF
EDLPVRIKWP NDLYALKPDY YYNKKMSLVG KSFDHTLVPL TDIEPAYVKV AGLLVNTNFI
NNKYSLLLGC GLNLTNDEPT TSLKKWVDIL NSERLGLGLA CIPRIEVEVL LAKYMNYLQI
LLETFINYGA STILPEYYKY WLHSDQIVTL TTLGNARAKI LGITNDYGLL IAKELMSGSD
SCFTGNVYHL QPDGNTFDIF KGLIAKKAT
//
