ID A0A1C7NAE6_9FUNG Unreviewed; 2517 AA.
AC A0A1C7NAE6;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=mak2_2 {ECO:0000313|EMBL:OBZ86102.1};
GN ORFNames=A0J61_05845 {ECO:0000313|EMBL:OBZ86102.1};
OS Choanephora cucurbitarum.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Choanephoraceae; Choanephoroideae;
OC Choanephora.
OX NCBI_TaxID=101091 {ECO:0000313|EMBL:OBZ86102.1, ECO:0000313|Proteomes:UP000093000};
RN [1] {ECO:0000313|EMBL:OBZ86102.1, ECO:0000313|Proteomes:UP000093000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KUS-F28377 {ECO:0000313|EMBL:OBZ86102.1,
RC ECO:0000313|Proteomes:UP000093000};
RA Min B., Park H., Park J.-H., Shin H.-D., Choi I.-G.;
RT "Choanephora cucurbitarum.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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:OBZ86102.1}.
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DR EMBL; LUGH01000328; OBZ86102.1; -; Genomic_DNA.
DR STRING; 101091.A0A1C7NAE6; -.
DR InParanoid; A0A1C7NAE6; -.
DR OrthoDB; 1222064at2759; -.
DR Proteomes; UP000093000; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF13191; AAA_16; 1.
DR Pfam; PF01590; GAF; 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; SM00065; GAF; 1.
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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OBZ86102.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000093000};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 73..392
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1893..2118
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 2387..2510
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1623..1670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2290..2365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1623..1638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1639..1661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2290..2333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2439
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 2517 AA; 285367 MW; B23161862B527273 CRC64;
MIVFYAYWAI SIASYSVKLR IKLKLMMYNQ GIANPSLMLP MMTNIMPTQT GPIVTGTEIV
LTFEINIPNY TFGKAVELAG AGGLIAVSIG KRNKDNKVIL AKLSPHSVRL EREYYVTKRL
YSIPGGEKYV PNAIEYVSLV QDGLAALLYT DVEPNDYIYF EQDQAPNYFS LYYLAQLTQM
TLWQENEPKR DCDQIKFELF LSFSIECCST LQFLHENGVV HGELRPSAFM LRYQKELTTK
IWNFGGGLNS YEELLLTTSR WRSYMSHDHD EDRSMNLKTF NNNPSRFYSP KEFKSSLVYV
SPEQTGRTSN ALDHRADLYS LGIMFFIVLT HTPPFQGTAM HVIHLILSKN VPLVHTMRND
VPPVMSLIID KLTRKAVDER YDSAYGLRED LYECQRRLKA AESDEALVYF PLGLNDINPV
FKVSDAMYGR DHEAQLIRTI VENTHQFHQQ AKKKAQQIHP DTTKEDNSAL KEADNLRVNS
STSLDHTVCE VIVLKGPGGI GKSTLVSSLN VQARQYGYTA CAKFDKNQKR PYNGLLKCLS
SILRQLLTES EHVVREFYKD LKHNLGPQFS NVRLMVNMVP ELKPILCDSQ DNDTNLDDDA
LSSILNTETR FHSIYLNIIR AIAKRKLLTL CLDDLQEADE SSIRLINAFI SSRTTALVIL
TFRDGLETPK RVVEILEKCN NPVTNIQLHP LTLDDFKDLV LNTFYNISAN SLDQNKTAVQ
EHTETIMPLV TIIYHWTRGN PFYAKQFLKH VKRKDDIWFD WNEKHWKFRL DNIKGLMDAQ
KGDTPPNRIA RRSSHDMFHL GVDQAKQLNS THPTDHTFGV RNLVSHLKSL DVNARCFLKW
ASLLGHVFNF KRIKWLMLTT TEEDQTASHL RLSDSEENET YELQENQAML GLQVALNEGV
IQYNSGNEFC FIHDRYYQAA AMLITDSSQH ESMHLKIGQM LMLEEEQEGQ EEDNVFMMAD
HFLKSVRLIA MMNKRKPYRD VLIRAANEAT LSGALEMSAG YYECALSLLD PDMDKRWQDD
VDSSFTETLS LYMKILELKL LNNKDFHDTM TGHITTTTTT HKEENMIDNH KVVDQTTSLV
ADGNKLVKAT TFIMQDEMRD NMIQQIMERT KDKPYERSQA WRIQARIYFQ QSQYRKGIHN
ILEGLEELGI VVDTNITEQE VLNYYQLIKQ KIIQSGFDAL MESGSCQSSK QIAVMTLLNE
ACTGAYWVNP ILVDFFGLKL CELSLQYGYT PASGGGFIWV GCTATRVSEF TFAAELGKFG
VALCEKYAGN SEIARAIIVY HSLLAQWTGV HVREYIYQYQ RAYKYAIAGG DQLYSSMALF
HVATTLYWTS SNLFDLHWHL NHSLEECSKG SSKDVLILNI SLWRSVMVFQ GRTDITQDPE
KLMNDPDNSF DEPSFVEDLK SQSVNSGNPL NWHYSFKMIL LFHFGFAKAA SELGFKIFDN
SINEMVHRHV GIAMYYHSIS IVESLRDPNL DTATREKYTR QLYKNEKKLN DLATYSEVNY
RMYHKIVQAQ ISTLDLNNLS HTLQLYNEVM ELALKGKWHS FLGLTFELAS EHYMRCGLSQ
LAVPTLSRSI EFYARWGAIG KVQYLEKKYS KELQGQVVSG KEDMSVQTED VIVGTTTVAE
KNATVWDNNS SDGNTHDSSL KESYNEDNSS PNEDNRPEDT GESSVSDTVY PEDLKRVRED
ALFSLDMVDL ASIIKSSQVI SNEMNSFDEL LKKMMGIIMV NSGAESGAII IKEGHFGIAA
YSVRSSDTCQ TYEPLLALCD DDDKILTPIV HYVIHTTTSL FISNVQADTR FSIGEKRAAV
ICMPIMHKNS LVGVLYLQAN LNAFTRKHAN VLSILCDQIG ISITNALLFK SVQQATKANS
LMIQSQVKAL EEARASKEQA LRATKMKSNF LANMSHELRT PFSGFYGMIS LLSETRLDPE
QREFVTIAKQ SCEMLLHIID DLLDFSKLEA HKVKLLHGLF HIEDLIADRL ELLITLATNK
NVELSYFIDP DVPSMVFGDG NRIGQILMNL IGNAIKFTHH GEVVVHCGLD TSTELVEPDN
IVLKISVRDT GIGMSEEEIK GLFLPFSQVD GSTTRNFGGT GLGLSICLQL VKLMHGDIHV
DSVVNEGSTF SFTIQVKSSD AVSEVDASYD SRCNTINELR QQLGQPRLLV LSSERAYLMI
QGFIPWMEHI DHTSHADEAI EIAKRNIYDC VVIDSTNPDV FCNFVKSAEE TGINKTRVLV
LLAPAVDTIR RHLVNTASRE IMKDQRTHYQ ANSFHYYLFH PLVARLSKPI RTIKLLNALA
TLLSTRSDHL NEPLPSPGES SQLISSSNSI DTVASSDIPS SAHSLPPRDT NQHSSEMIDS
HKTADATEES SSSSNTSPPP MLVTPPYSRM NHEAFSPEEL ALFKGRKILV AEDNFIAQRL
IVKQLSRLGF MVEKCNNGFE CYDTWKSRGP GYFLLAWIDH HMPGCDGLEA TRKIRRHEKE
MSYSPALPII ALTADIQLTA QQSCLEAGMN DYVTKPLMQK DLATILRKYC LGPTVLQ
//
