ID B2B6M1_PODAN Unreviewed; 1116 AA.
AC B2B6M1;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE SubName: Full=Podospora anserina S mat+ genomic DNA chromosome 2, supercontig 2 {ECO:0000313|EMBL:CAP73448.1};
GN ORFNames=PODANS_2_8180 {ECO:0000313|EMBL:CAP73448.1};
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:CAP73448.1};
RN [1] {ECO:0000313|EMBL:CAP73448.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP73448.1};
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:CAP73448.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S mat+ {ECO:0000313|EMBL:CAP73448.1};
RA Genoscope - CEA;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CU640366; CAP73448.1; -; Genomic_DNA.
DR RefSeq; XP_001911621.1; XM_001911586.1.
DR AlphaFoldDB; B2B6M1; -.
DR GeneID; 6196364; -.
DR KEGG; pan:PODANSg8665; -.
DR VEuPathDB; FungiDB:PODANS_2_8180; -.
DR HOGENOM; CLU_000288_34_2_1; -.
DR OrthoDB; 1765294at2759; -.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR46082:SF6; AAA DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR46082; ATP/GTP-BINDING PROTEIN-RELATED; 1.
DR Pfam; PF12796; Ank_2; 3.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 8.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 7.
DR PROSITE; PS50088; ANK_REPEAT; 7.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023}.
FT REPEAT 860..892
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 895..927
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 943..975
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 979..1011
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1013..1045
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1048..1080
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1083..1115
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ SEQUENCE 1116 AA; 120784 MW; 615A6812F3610BE2 CRC64;
MDAQAATEPR THSDYTVGWV CALPKEQTAA TAMLDHKHVD LPKPPNDHNT YTLGSIGNHN
IVIACLPKGE IGTNSAATVA TSMANAFPSI KIGLMVGLGG GIPPKVRLGD VVISSPVGQY
PGVVQWDLGK AKEGGKFERT GSLNNPPASL RTALTKLETE HEMSGSKIPQ YLEDLKRKWP
RLALKYASRD HLEDPFGVPD DPPRSQKAIQ GLPSMESGAK QVDEYCDATF RDRLDEEFGG
YVLCVEMEAA GLMNNFPCIV IRGICDYADS HKNKDWQEHA AAVAAAFAKE LLQYVSYSPV
GVTVYVLIIG VVHKEISATR EDVTQIKSKF QKEEDKEVLD WLTTIDYGPQ QSDYLNRRQP
GTGQWLLDSE KFKGWLSASN QTLFCPGIPG AGKTILTSVV LDHLGSKFHN DPKIGIAYIY
FNFQRQDKQK IDDLLASVLK QIAESQPSVP GSVKDLFDKH KAKRTRPSLD EILRVLQSVA
ATCSCVFIVV DALDECQTSE SCRERFLSEL FNLQKMHGIN IFATSRSIME IVDRFKTSIS
LEIRASTADV AQYLEGHISE LPSFVQQDRR LREEIMAGIS EAVDGMFLLA QIYLNLLYDK
MTPNDIRSTL EVFRNQGQGR DEIQKVGALT SAYNQAMMRI NGQMPGCKKL AMEVLTWITC
AKRQLTTLEL QHALATKPGK SELDDGDLPC IGDMVSVCAG LVTVDENNGI IRLVHYTTQE
YLEGTRSRWN PNAELAITTT CVTYLSFTVF ETGFCTTNRK LKERLQSNPL YDYAARNWGH
HAHKAATSSQ VVIHFLESKA KVEASSQALM ATNWSRSYPI GSQHVPRNMT GLHLSGYFGV
IEAADELLRS RPGPDLKDTC RRTPLWYAAQ NGHEAVVKKL LAAGADVNTA AASFDGRTAL
QAAAGRGHLK VIEKLLAAGA DVNAVAATSG RWTALQAVVA TSGSWTALQA AARGGHLEVV
EKLLVAGADI NAAAATSIDG RTALQAAAEG GYLKVVEKLL VAGADVNTAN SSNGRTALEA
AAGGGHLEVV EKLLAAGADV NIIAATSGRW TALQAAAKGG HLEVVEKLLA AGADVNAAAA
TIDGRTALQA AARRGHLEVV EKLLVAGADV NTAALF
//