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Database: UniProt
Entry: B2B6K7_PODAN
LinkDB: B2B6K7_PODAN
Original site: B2B6K7_PODAN 
ID   B2B6K7_PODAN            Unreviewed;       318 AA.
AC   B2B6K7;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Choline kinase {ECO:0000313|EMBL:CDP25835.1};
DE   SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 2, supercontig 2 {ECO:0000313|EMBL:CAP73434.1};
GN   ORFNames=PODANS_2_8080 {ECO:0000313|EMBL:CAP73434.1};
OS   Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)
OS   (Pleurage anserina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Podosporaceae; Podospora;
OC   Podospora anserina.
OX   NCBI_TaxID=515849 {ECO:0000313|EMBL:CAP73434.1};
RN   [1] {ECO:0000313|EMBL:CAP73434.1, ECO:0000313|Proteomes:UP000001197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197}, and S mat+
RC   {ECO:0000313|EMBL:CAP73434.1};
RX   PubMed=18460219; DOI=10.1186/gb-2008-9-5-r77;
RA   Espagne E., Lespinet O., Malagnac F., Da Silva C., Jaillon O., Porcel B.M.,
RA   Couloux A., Aury J.-M., Segurens B., Poulain J., Anthouard V.,
RA   Grossetete S., Khalili H., Coppin E., Dequard-Chablat M., Picard M.,
RA   Contamine V., Arnaise S., Bourdais A., Berteaux-Lecellier V., Gautheret D.,
RA   de Vries R.P., Battaglia E., Coutinho P.M., Danchin E.G.J., Henrissat B.,
RA   El Khoury R., Sainsard-Chanet A., Boivin A., Pinan-Lucarre B., Sellem C.H.,
RA   Debuchy R., Wincker P., Weissenbach J., Silar P.;
RT   "The genome sequence of the model ascomycete fungus Podospora anserina.";
RL   Genome Biol. 9:R77.1-R77.22(2008).
RN   [2] {ECO:0000313|EMBL:CAP73434.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP73434.1};
RA   Genoscope - CEA;
RL   Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Proteomes:UP000001197}
RP   GENOME REANNOTATION.
RC   STRAIN=S / ATCC MYA-4624 / DSM 980 / FGSC 10383
RC   {ECO:0000313|Proteomes:UP000001197};
RX   PubMed=24558260; DOI=10.1534/genetics.113.159988;
RA   Grognet P., Bidard F., Kuchly C., Tong L.C.H., Coppin E., Benkhali J.A.,
RA   Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Genetics 197:421-432(2014).
RN   [4] {ECO:0000313|EMBL:CDP25835.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Grognet P., Bidard F., Kuchly C., Chan Ho Tong L., Coppin E.,
RA   Ait Benkhali J., Couloux A., Wincker P., Debuchy R., Silar P.;
RT   "Maintaining two mating types: Structure of the mating type locus and its
RT   role in heterokaryosis in Podospora anserina.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000256|ARBA:ARBA00006219}.
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DR   EMBL; CU640366; CAP73434.1; -; Genomic_DNA.
DR   EMBL; FO904937; CDP25835.1; -; Genomic_DNA.
DR   RefSeq; XP_001911607.1; XM_001911572.1.
DR   AlphaFoldDB; B2B6K7; -.
DR   GeneID; 6196170; -.
DR   KEGG; pan:PODANSg8651; -.
DR   VEuPathDB; FungiDB:PODANS_2_8080; -.
DR   eggNOG; ENOG502RW01; Eukaryota.
DR   HOGENOM; CLU_021768_4_0_1; -.
DR   OrthoDB; 2342810at2759; -.
DR   Proteomes; UP000001197; Chromosome 2.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR21310; AMINOGLYCOSIDE PHOSPHOTRANSFERASE-RELATED-RELATED; 1.
DR   PANTHER; PTHR21310:SF55; APH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:CDP25835.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW   Transferase {ECO:0000313|EMBL:CDP25835.1}.
FT   DOMAIN          43..255
FT                   /note="Aminoglycoside phosphotransferase"
FT                   /evidence="ECO:0000259|Pfam:PF01636"
SQ   SEQUENCE   318 AA;  36805 MW;  AD1C543717CD49A6 CRC64;
     MMPSPPETEQ ECDSKDPVDI LSDRDLARYI AKARQHRESD TIENNTLLLT SRYITKFYTT
     LSHAKDVEVA ILQAHALGIR VPELKRVIKA KDGTYECIMT RIQGVTLESC WPDLSLFTTI
     RLAVQLRTIV QRMRRMTRPT AGSLGTGICR SFWLEEFYGV PSHASAAVVG QIVNFWCGFQ
     SYGRERRKTL AEHRESCEMV EQDARGQELV FTHHDLAPRN IIVESGTSKL WLVDWDESGF
     YPRYFEYAGM RNLEYPPEWG WYGEWRWKIF CWIVAGFCSY DKQAEMLRDI RQKAGRFPGG
     RRFNIKAGVT PSERPVDD
//
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