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Database: UniProt
Entry: A0A090CGV1_PODAN
LinkDB: A0A090CGV1_PODAN
Original site: A0A090CGV1_PODAN 
ID   A0A090CGV1_PODAN        Unreviewed;      2440 AA.
AC   A0A090CGV1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Signal transduction histidine-protein kinase {ECO:0000313|EMBL:CDP27381.1};
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:CDP27381.1, ECO:0000313|Proteomes:UP000001197};
RN   [1] {ECO:0000313|EMBL:CDP27381.1, 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};
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|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).
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DR   EMBL; FO904938; CDP27381.1; -; Genomic_DNA.
DR   eggNOG; KOG0519; Eukaryota.
DR   InParanoid; A0A090CGV1; -.
DR   Proteomes; UP000001197; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR041664; AAA_16.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR43047:SF46; HISTIDINE KINASE_RESPONSE REGULATOR, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G12550)-RELATED; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CDP27381.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000001197};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          98..406
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1949..2174
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          2246..2370
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          57..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          467..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..589
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          695..747
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2201..2238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2402..2440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        471..507
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        549..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        698..747
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2201..2224
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2301
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   2440 AA;  268687 MW;  3539BEDB449E8F6C CRC64;
     MDTAARLLDE QLESPARLFE RLHQISGYVW DDSRPPFHST YDNWHIYGTR FVSPFSSGGA
     VPTSPAPHNS PASQPGVAGF TLPPAHRPSS RDHRPSTSSQ LSEVGSERSA TSLPVIPPTG
     SDVPVIEEPV VARVSYHVLR EERTFHIFKS LIAHTDSSAE RERIVKPLDI IRLPALPGDR
     GAVIVTVYED PGPNYLWDVL DLGPAFYYAK KHGDGWEPSR PGHTGHKLAP PISLQHFLDF
     AIGSAQSLEM IHHGQGTIHG EIRGDTFHYN VETNKVKLVC LGSGLRSFEH GLTSTGWSAL
     SRELGAKHKL QYISPEQTGR MPAEPDTRTD IYSLGALFWS LLTQHPVFHG ESPLDVVQGV
     LSRRIPSIST FRIDVPEVIG RIIQKCTAKN VNDRYYSASG LRHDLTWVKK LLGVGDLQAL
     KDMKIGTNDV SSFFRLPSSM IGRERERAEL LKVIDRVAKR HSLALNGAAA HRQSDGSNVS
     TEVDAADVSS DGASSAEGTN RFGTSVTNKD RRSSLYHSAV GVDSVGAYTE VNSSGAVRPP
     RPWDRQHSVS LKESVQSAEA STSEPSWRSA AVATNGTDSS AASISRPLGP AKYRKQGQCE
     IVMIEGAGGL GKTCLVQSVL VDARRMGYCA TAKFDTARRT AYGPLIKLLS SLFRQVWGER
     NTDTPFHQAL KQSVRPTWPT LHKVLGLPEH MLPRLDTPLG RSSSSPQPPK SNNLRRRPSS
     PEFSGASSKL GASSASSSAQ STQEFLRGGS TTKVNRLANI FLDVLRLFTR HKFICFCLDD
     LHYADDESLE LITQIVSAKL QMVLIITYRP DEMSPEKLYT ITNPPKSEDH LRACYPITTK
     ITLDPLSEEE IREYVSTTLS LPKDQVVSLA LVLQSKTAGN PFYMREMLSA GHRKKCIWYD
     YTEGRWKFDL DRLFEHFRGE QDYDVLDTAF ITRRLGELPQ ESRSILAWAA LIGQTFSLDL
     IEKLMEGEFY YTDDNQDGSD DCAILPHGKQ DIFAGLEAAI QAYIIIPGDR DDQFRFAHDR
     YIQAASALRE CNSLKMHFVI ARTLLAHFPK SQENTASHIC ESIEVIKKRI SERAPFRKVL
     MERAGEAVES GARPTAAKYY SNALALLQSD PWNDDAPDVS YEETLQLHRR AAECFLYMGR
     PPSANMLLQT MIENARSPLD KTPAWVLQSR IFAQSGDSAQ ALTSLRQCLR AFGVNVDECP
     TMKKCDEQFE KLSVKIQNMD RQDVMNPLAS SDPPPESLVS LGAVLAETTS AGWWSDCVVF
     YQLALLMVET HFTKGPYPQS GMAFLHMSMI ALSRFNMVDF AQSLASICFD LLQKSSDPFS
     LVRGYMIYAN FIGNIQDLTG ATVEQLEANV LAAAPLGDRV SVILSFGLLA LLKFFASQDC
     AELEVYCQFA CDDIPSWHLD TKGGTLLISV RQLCRALQGK TRASQPLEVM NDDQHDASTY
     KNWLNTHTNN GGRSLLLYET MEIVPLFLYG HYGRAIEIGK ACLEQAELLW SARNTRLAMF
     FYGLALAGTV LREQQDPREP PKGDPKVRRD EAIRKVEELN RKIKDWKAVH NVNYLAWSKL
     LDAQVSEMLG NHGIAIRQYE EALDHASEHG FVFEEALGNY LMANIFIRNA ARRSARSALR
     DAVSLYRQFG ATGIADLIET EHSILLHGPA GNLRTCDAGV QTDFFGDTAS VQYRGVDTEE
     SQQSTRAAVA ALKGERMMAW RGSMQPEAGA GLPALDMIDL HGILTSSQAI SSVLRVDELL
     RTMCSVILQA CSGSATFAAI IVQDEGSVDW CVAASGDSEN GATAHIPGIP LSGTDLVPEN
     VILYCTRLRE KVFLQDLVND ERFGNVSDQW LRKNPNSKAV IAVPIRHGNS KPLLGVLYLE
     GLPGSFTDRN VTVLELLVGQ ISISYSNALS MKSVERVSAE NISMVELQKQ ALATAIEAEA
     KAKNAEAEAI RNVKLAEEAT KAKSIFLANV SHELRTPLNG VIGNSELLRD SGLNREQMEM
     ADSIRVSADL LLTVINDILD FSRMEADKMK LYIIAFNPEE MVREVVRAVS YSNREKTSKK
     NVKIVQDINL PPMLIYGDPI RLHQVLGNLI GNSLKFTEDG SITIGARIDE ETPDKATLTF
     WVKDTGIGIS QQHLENLFQP FSQADASTAR KYGGSGLGLS ICKSLIETMM EGTIQLESEE
     NVGTTAWFTV TFEKAKPEVV AGDEQALANG DDGLLPVESA YRQQQSNSEN SSDSTTLTGG
     FQPSSSHPPL PPAPPNLTQI PKNELRICIA EDNAINAKIA MQYMQRLGYP NVDTYENGLK
     AVEGLREKAK EGRPYHIILM DVQMPVLDGY EATKLLRTDE LESVRKVLVI AMTASAIQGD
     REKCLAAGMN DYLAKPVRGE VLKRKLEAYL GAGGTTPASG GPVNVASAAV GGVVGNGVEK
     KKVAGGEVEG EKTVEVDGER DKTEVKGKED ERDKGGGDGH
//
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