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Database: UniProt
Entry: A0A0B4HR42_METMF
LinkDB: A0A0B4HR42_METMF
Original site: A0A0B4HR42_METMF 
ID   A0A0B4HR42_METMF        Unreviewed;      2552 AA.
AC   A0A0B4HR42;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=ATPase-like, ATP-binding domain protein {ECO:0000313|EMBL:KID97733.1};
DE   Flags: Fragment;
GN   ORFNames=MAJ_06219 {ECO:0000313|EMBL:KID97733.1};
OS   Metarhizium majus (strain ARSEF 297).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium;
OC   Metarhizium majus.
OX   NCBI_TaxID=1276143 {ECO:0000313|EMBL:KID97733.1, ECO:0000313|Proteomes:UP000031176};
RN   [1] {ECO:0000313|EMBL:KID97733.1, ECO:0000313|Proteomes:UP000031176}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 297 {ECO:0000313|EMBL:KID97733.1,
RC   ECO:0000313|Proteomes:UP000031176};
RX   PubMed=25368161; DOI=10.1073/pnas.1412662111;
RA   Hu X., Xiao G., Zheng P., Shang Y., Su Y., Zhang X., Liu X., Zhan S.,
RA   St Leger R.J., Wang C.;
RT   "Trajectory and genomic determinants of fungal-pathogen speciation and host
RT   adaptation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:16796-16801(2014).
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KID97733.1}.
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DR   EMBL; AZNE01000030; KID97733.1; -; Genomic_DNA.
DR   RefSeq; XP_014576727.1; XM_014721241.1.
DR   HOGENOM; CLU_001037_0_0_1; -.
DR   OrthoDB; 1222064at2759; -.
DR   Proteomes; UP000031176; Unassembled WGS sequence.
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; 1.10.510.10; 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   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; PF00069; Pkinase; 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   SMART; SM00220; S_TKc; 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   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, ECO:0000313|EMBL:KID97733.1};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000031176};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          72..405
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1974..2199
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          2248..2372
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..515
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          535..590
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2470..2552
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..121
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        489..511
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        535..549
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        707..755
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2470..2490
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2509..2540
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2303
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KID97733.1"
SQ   SEQUENCE   2552 AA;  280458 MW;  402DF39D52354D27 CRC64;
     MDGAVLVPDD VLDSRPPPPP RLFERLRQIA GYTWDETKEP IHSSYDFWLV FGTRFVSSKP
     SPPSSGHNES SLGSITKLQS GRPSLSEHGN HVPPSETQST ETPKTPLPHR PSTPISSPPS
     SADGPPIVEE SVVARVSSHN LREERAFQIA KNVAGTADPL GEHIAKPIDL LRLNPGPGDR
     NHITVAIYQY PGANYLGKVL DFGPAFYQAR KEGDAYVSYR PATSSHLRPP INLEYFLDFA
     IGAVQCLEIL HHGQGIIHGE IRGDAFHFNA EENKVRIVAF GTGLRSFEHG LTSTGWLTLS
     KEVGVKNKLL YISPEQTGRM PAEPDTRTDI YSLGILMWTL LTQQPVYTGD TPMDIVQGVL
     GRRVPNVATV RMDIPDVIGR IIQKCTAKNV ADRYHSASGL RHDLVNVQQL LSDGDSTALK
     DLEIGTKDIS SFFILPTNMI GRTAEQSELV KVIDRVSRNH SLGSNRNRFP DGSGLANELV
     VRDDVSSEGG ASSVRSVEGT NRRSGSFNLG GGSSEYKFPR NSFHPSILSD TQTLSNETVS
     SNQSGPQLRP TRPWERHHSI SVETASAVES TGGPESGRIG GMTESSGSSL SRQLGAAKFR
     RRGQCEVVAI EGAGGLGKSF LVQSVLGEAR RRGYCATAKF DTARRTAFGP LLKLLSSLFK
     QVWGETNTET PFHQVLKQYV RPVWPMLHRV LGLPEFLLGP PESASPMVGR PSTNNSQQAG
     QRSGVKSSSG KRRGSSPGSS PSPLSQHQVA NAAAAATAGS QSSQDYLCAG TSTKTTRLMN
     TCLDILRVFT THKFICLCLD DLHFADDESL ELITQIIGAK MKMLIIMTYR PEELPRERMD
     RIIYPAQLEE NHRNGRPRVT RISLEPLSET EILDYVSATL SRPKEEILSL ALVIQAKTAG
     NPFYMREMLS ACHRKKCIWY DYRDSIWHFD LDRLFAQFQG EKDYDVLDTG FITRRLDELP
     SAARAVLSWA ALLGNSFSFE IISRLMKGEF DYGDDDIPNC CPNLSKRSYT EAESIAGLQA
     AIQAYIIVPS ETDDRFRFAH DRYVNASAAL KECNARRMHF IISQTLLKYY AVEARQREST
     ACHICEAASI IKMRVPVRQE FRKLLIDCAQ AATENGARPT AAKYYGAAIQ LLQGDPWSDD
     ADDVSYEETM QLYLRAAECH LFMGQLSLAN DLLSTLFANA KSAMDKAPAY VLQSRIFAQN
     GNALAAFISL KECLAALGVP LEDEPTYEKC DKKFHKLAKQ VQGMDRQALM NPKKNTAPVT
     ASIGAVLSET ASAAWWSDCL QYYHLTLVML DMHLTRGAFP QSGMAFLQMG VVGLARFNMT
     QFAVDMGTIC QDLLYSARDA FSMARGQMLH SCFIGHVQYS MSLSTSQMDD AIELASVGGD
     RLSTILSYGL CAVTKLFASE NLSDLEAFCQ YGCEDIVNWS LDTRGGALLV AVRQLSRALQ
     GKTCTHEPLR VMTDDQHDSV GYKSWLTSQT QESNRSSLFY ESLELCALFL YGHYERAIDI
     GQKCVEKLPM LWSARNSRLI LLFYGLARAG QLLRLMQDPR SQTDDFTAQT EEIVNELTGF
     VKMMEDWSVV SDVNYRSWSR LLNAQVAELS QDHGQAIQHY EEALDHAAEH DFIFEEALGN
     YVMAGFFIRR RARRSARAAL QDAVGLYRQI AAAGVASAIE EEHSLLLHGP TRNHRTVEVG
     IQTDFVADPP PAQYRPVDGV DGDELTQVPS NAMSEFRGER IGAWRGSMRM PTEDGVGLPA
     LDMIDLHAIL VSSQVISSVL QVNELLKTMC DVILQTCGGS ATRAAIIIQD NDTESWCVAA
     SGDPERGASA HEPGLPLSGS TLIAENVVLY CTRFRESVFI PDLFADERFG NVNGGWLQRY
     PGGKAIISIP ILHGTKPLLG VLYLEGEPGS FTDRNVTVLQ LLVNQIGISY SNALSMKNVE
     KISAENRGMV SVQKRALAKA LEAETKAKHA EAEAKRNVKL AEEAAKAKAI FLANVSHELR
     TPLNGVIGNS ELLRDSDLNR EQLEMADSIR VSADLLLTVI NDILDFSKME ADKMKLYIIA
     FNPEEMVREV VRAVSYSNRE KTSKKNVKII QDINLPPMLI YGDPIRLHQV LGNLIGNSLK
     FTEDGSVTIG ARLDAETKDS ATLTFWVRDT GIGIPAQQLA KLFQPFSQAD ASTARKYGGS
     GLGLSICKSL IEIMMKGKIQ LESEESEGTT AWFTVTFEKA KADVSAGDAL GKASPPIDRY
     SLMTSPFDRV ASPNPFMDLS QVSKEDVRIC VAEDNPINQK IAIQYAHRLG YPNVVAYENG
     LKAIEGLRKK AAEGEPYHIV LMDVQMPVLD GYEATKLIRK DSIEAVRKVL VIAMTASAIQ
     GDREKCLAAG MNDYLAKPVR SEVLKKKLDA YVDVSKAGVI DTVQSPISPI SPTTPNDLEA
     NGTSLASIAS SNKVFRDTRA PNSSIIDPMQ EDAVYNMPLD STSLQAADSP VLSVNNNDQR
     TLSMHLPQLT RNSTNHSDSQ PSTEASTPEA VSTGDPVALQ PKRQPKKLTK TRANSDAHGD
     AEAKPVDKDG EKHKGVLTKK QPLADDPNGD AS
//
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