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Database: UniProt
Entry: B2B074_PODAN
LinkDB: B2B074_PODAN
Original site: B2B074_PODAN 
ID   B2B074_PODAN            Unreviewed;      1189 AA.
AC   B2B074;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Kinesin light chain {ECO:0000313|EMBL:CDP27347.1};
DE   SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 3, supercontig 2 {ECO:0000313|EMBL:CAP70755.1};
GN   ORFNames=PODANS_3_8170 {ECO:0000313|EMBL:CAP70755.1};
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:CAP70755.1};
RN   [1] {ECO:0000313|EMBL:CAP70755.1, 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:CAP70755.1};
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:CAP70755.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP70755.1};
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:CDP27347.1}
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 (APR-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CU638743; CAP70755.1; -; Genomic_DNA.
DR   EMBL; FO904938; CDP27347.1; -; Genomic_DNA.
DR   RefSeq; XP_001909622.1; XM_001909587.1.
DR   AlphaFoldDB; B2B074; -.
DR   STRING; 515849.B2B074; -.
DR   GeneID; 6193490; -.
DR   KEGG; pan:PODANSg6658; -.
DR   VEuPathDB; FungiDB:PODANS_3_8170; -.
DR   eggNOG; KOG1840; Eukaryota.
DR   HOGENOM; CLU_000288_125_3_1; -.
DR   OrthoDB; 2413181at2759; -.
DR   Proteomes; UP000001197; Chromosome 3.
DR   GO; GO:0005871; C:kinesin complex; IEA:InterPro.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR002151; Kinesin_light.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR46082:SF11; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR46082; ATP/GTP-BINDING PROTEIN-RELATED; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   Pfam; PF13374; TPR_10; 4.
DR   Pfam; PF13424; TPR_12; 1.
DR   PRINTS; PR00381; KINESINLIGHT.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   TPR repeat {ECO:0000256|ARBA:ARBA00022803}.
FT   DOMAIN          77..365
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   REGION          1079..1189
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1086..1106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1130..1149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1155..1189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1189 AA;  132353 MW;  CD677DE9426F8F93 CRC64;
     MGTKPTSQNQ PRTTSTYTHM FHADCLLIVS SSITEPSEQA SLNVLRDRQF VIRPHAGSNE
     ARTAVPPRRL ATQNDLEIAV ICALKTEADA VLALFDCRWD EPGWLFRGDT NAYTFGAIGR
     HNVVLIHMPH IGKVKAATAA AHCQRTFPNI GLALIVGVCG AVPFTSTGEE ILLGDVIISE
     RVVQYDFGRQ YTEGFVLKDT PKDALAAPNN EISGLLSKLK TYDHRKELQE QIALYIRTVQ
     DHPGLGSEYP GVEYDKRFPA SYRHATDDIS CEDCCDLGKL MPPSRLSQEP AVHIGMVASS
     DKVMRSANHR DAIARSSDVI GFEMEGAGVW GIFPCVVIKG VCDYADSHKA KGWQQYAAVT
     AAACMKAFLD HWRPSGRKPA AQTWFDVPYQ KNDHFVGQSD ILRKLRELPL KSASHTRVAL
     CGLGGIGLFL TRNRKTQIAI EFTYWIKGTY DDISVFWVHA SNHERFREAY TAIAQKYRIP
     GHEDPKAEVL PLVKSWLESK ERGQWIMAID NADDLELFFN RNGGLGRYLP ECAHGTILIT
     TRNLQVASRL TKGMASSVIR IGKMDEVETA QLLSTRLAEI DTMPGDYAGL SARLEHLPLA
     LVQAASFIQE NSITISRYIQ LLDESDQTLI GLLSEDFETV GRDSETPRAV AEAWIISFKQ
     IHNRNTLAGE LLSIMSFLDR QTIPYEFLFT YAKDHGAGEF QLIKALGVLK AFSFVTEDKD
     QKFDMHRLVH LVTRKWLVQN GIKQKFAERA LLVVTVCFPW GEYKNWTICN AYLPHTTAVL
     KLGEDISSRQ GKLARASLLH NAGALFSGRG DFQRAALYLK EVWEISQAHL GEEHPGTLTS
     MNNLASTYQS QGRWKEAELL QLQVVEIRKR VLGEEHPGTI TSMNNLALTY ESQSRWKEAE
     LLQLQVVETG KRVLGEEHPV TLTSMNNLAS TYKSQGRWKE AELLQLQIVE IRKRVLGEEH
     PDTLNKCLCL REKVLGLDHH GTINTQAEIA WSYMEQGRLP EAERIQAGML GKRKRILGEE
     HLHTLISMIN LAHTWKVMGR LEAAVELMQE CVRLRQKVLG SDHPDTVESL SALEEWQDLR
     GEGGGNGNTH GNSEANTAMK SGENAGGSSS HHEDVDNGTD DDAGYEGNEN GNNKAGQSSE
     SQQCQATRGG DEKGNIGDGI QDGEGRRSSE DGKTVEADES GYGPRPERF
//
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