UniProt: B2AS80

Database: UniProt
Entry: B2AS80_PODAN

LinkDB:  B2AS80_PODAN 
Original site:  B2AS80_PODAN

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Ontology (6)   
   GO (6)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (26)   
   InterPro (16)   
   Pfam (5)   
   PROSITE (2)   
   SMART (3)   
Literature (2)   
   PubMed (2)   
All databases (40)   

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ID   B2AS80_PODAN            Unreviewed;      1767 AA.
AC   B2AS80;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=DNA topoisomerase 2 {ECO:0000256|ARBA:ARBA00019635, ECO:0000256|RuleBase:RU362094};
DE            EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895, ECO:0000256|RuleBase:RU362094};
GN   ORFNames=PODANS_1_22630 {ECO:0000313|EMBL:CAP67253.1};
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:CAP67253.1};
RN   [1] {ECO:0000313|EMBL:CAP67253.1, 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:CAP67253.1};
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:CAP67253.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S mat+ {ECO:0000313|EMBL:CAP67253.1};
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:CDP24664.1}
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.
CC   -!- FUNCTION: Control of topological states of DNA by transient breakage
CC       and subsequent rejoining of DNA strands. Topoisomerase II makes double-
CC       strand breaks. {ECO:0000256|RuleBase:RU362094}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-dependent breakage, passage and rejoining of double-
CC         stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185,
CC         ECO:0000256|RuleBase:RU362094};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC   -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
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DR   EMBL; CU633897; CAP67253.1; -; Genomic_DNA.
DR   EMBL; FO904936; CDP24664.1; -; Genomic_DNA.
DR   RefSeq; XP_001906582.1; XM_001906547.1.
DR   STRING; 515849.B2AS80; -.
DR   GeneID; 6191059; -.
DR   KEGG; pan:PODANSg3615; -.
DR   VEuPathDB; FungiDB:PODANS_1_22630; -.
DR   eggNOG; KOG0355; Eukaryota.
DR   HOGENOM; CLU_001935_2_0_1; -.
DR   OrthoDB; 1944951at2759; -.
DR   Proteomes; UP000001197; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   GO; GO:0061982; P:meiosis I cell cycle process; IEA:UniProt.
DR   CDD; cd16930; HATPase_TopII-like; 1.
DR   CDD; cd00187; TOP4c; 1.
DR   CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR   CDD; cd03365; TOPRIM_TopoIIA; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.30.1490.30; -; 1.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.670; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR   Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   InterPro; IPR001241; Topo_IIA.
DR   InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a_sf.
DR   InterPro; IPR013759; Topo_IIA_B_C.
DR   InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR   InterPro; IPR002205; Topo_IIA_dom_A.
DR   InterPro; IPR001154; TopoII_euk.
DR   InterPro; IPR018522; TopoIIA_CS.
DR   InterPro; IPR031660; TOPRIM_C.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034157; TOPRIM_TopoII.
DR   PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR   PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR   Pfam; PF00204; DNA_gyraseB; 1.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF16898; TOPRIM_C; 1.
DR   PRINTS; PR01158; TOPISMRASEII.
DR   PRINTS; PR00418; TPI2FAMILY.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00433; TOP2c; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR   PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362094};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362094};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362094};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW   Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT   DOMAIN          557..671
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1188..1216
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1294..1369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1385..1767
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        55..71
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1188..1202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1294..1324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1412..1447
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1464..1483
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1491..1511
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1581..1612
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1651..1666
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1750..1767
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1767 AA;  197143 MW;  B6E60B8348E59368 CRC64;
     MDSDVESVFD TAQSESDGYS PEKTKAKAAP KKAPAAKAAK MVQTKLTVGK AKAAPKKRTK
     PDSDDSDDDR PLSSTPPMAK KQKKAPAKKS SGKPLAEIEN DSMLIDDEPA LAAASKSSKS
     ATETYQKLTQ LEHIIKRPDT YIGSVERTDQ KMWVFNKTEK LMENRVVSFV PGLYKIFDEI
     LVNAADNSQR DASMTFLKVT IDSETGEISV ENNGKGIPVE MHQKEGCYIP ELIFGHLLTG
     SNYDDDEKKT VGGRNGYGAK LTNIFSLKFT LECQDSVNGK RYKQTWTDNM SKMEKPKITA
     NKTNDFVRVT FLPDYKRFGM ENGIDDDLEA LMYRRVYDMA GTMASVKVWL NGEQLKIAKF
     KGYCQLYAKS IAAERGDVVP EGEKPTAANV EYEEVRDKGR TWQVGFTVSD GSFQQVSFVN
     NIATTSGGTH VNYIADQITE ALLKELNKKK KGHGLKPANF RNYIFIFINC LVDNPAFTSQ
     TKEQLTTKVS AFGSKCILSD AFLKKVQKSE VIANIMEFAE RKADKMLAKS DGNKRARVSN
     EKLVDANLAG TKRGHECTLI LTEGDSARAL AVAGRAVLDP DRIGVFPLRG KMLNVRDAST
     EQIMKNKEIE NIKKFLGLKH KQVYTDTRGL RYGHLMIMAD QDLDGSHIKG LLINFLEVQF
     PSLLRIPNFF QQFITPVVKV WQGTNPKKPL RPKSFFNLVE YETWKENNKN ELRKWKYKYL
     KGLGSSSNED AQVYFTDLDR HLKEFETLKP EESQMLDMIF SKKKADARKE WLGNFVPGTF
     LDSTAQRISY SQFLQNEFIL FSMADNIRSI PSMIDGFKPG QRKVIYSAFK RNLVNDQKVV
     ELAGYISEQA AYHHGEQSLQ QTIIGLAQTF VGSNNVNCLE PSGNFGSRLS GGKDSASARY
     IHTRLSPFAR KVFSKLDEPN LEYQFDDGNM IEPKVYAPIL PMVLVNGADG IGTGWSTSIP
     NYHPMHIVEN LRRRMGRFDP DDTEEKPFVP MAPWWRGWKG TPEQEAPNKW RFNGIIRQDE
     QNPNEIHVTE LPIRMWTDDF KAKLEDIIQN DKTPTFIKDY KEFNDHKTVH FIIDMDEKHR
     EAALREGLLE KFKLTTTVST TNLVAFDTQG KIRKYDNVEE IMEEYYHYRL KMYTERKKHW
     LKVYHADYRK LKNQYRFITE IIDNKMVVNR KKKAVLVQEL RDRDYEAFPP KEDKKVKSPD
     EEMAAEEAED DDTAGGARDY DYLLSMPVWS FTSERLERLK NQIAAKKAEH DELQALSEKD
     LWVKDLDAFQ EEWETQLKLD DEIATGIRRM GRRKSDKLGV GKGGGRRRKD DDAYEPEKKS
     RAKAVKAAPV PIKTEKTQQR FAEAFQAKSK PKPVADKTLP DVEAGGGISD DDFALLGKKA
     MPINTKVKEE SEAPTATNGR TKRAAAAKSK YVVSDDSDED FMDLGKPSVD EDVDMASEPE
     EAVAEKPPVK RVAAAAAKAK PSYKLSDNES DEEVEEKPPV KRAAAAKAKP SYKLSDDDSE
     DDFEAKPPAK RAAAAKAKPM YKLSDDSDSD DSLKLGDVGA MVKGIGAPAS SSSGGRLSLF
     AMSHSGGGDT SVLPKMKSKP SKPSLDLDDH DDTNYEALAR SSPLKTKEDN LDDFLSDDDV
     PAAKPAPKAA SKAKAPLSVV PAPAKKRGRP AGSKSTKDKD EATAPKAKAA VTKTAKTAAA
     KPKAPHLSPA AKAYAAKKAK AQKGLSDDEG DEAMEDAPDS PPAARPKARP GRAAAVKKKP
     IVIDSDEDDS IGGGGGDDES DDFDMSD
//

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