ID F0UUZ4_AJEC8 Unreviewed; 1572 AA.
AC F0UUZ4;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=HCEG_08936 {ECO:0000313|EMBL:EGC49721.1};
OS Ajellomyces capsulatus (strain H88) (Darling's disease fungus) (Histoplasma
OS capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=544711 {ECO:0000313|Proteomes:UP000008142};
RN [1] {ECO:0000313|Proteomes:UP000008142}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H88 {ECO:0000313|Proteomes:UP000008142};
RA Champion M., Cuomo C., Ma L.-J., Henn M.R., Sil A., Goldman B., Young S.K.,
RA Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A., Borenstein D.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L., Lewis B.,
RA Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Klein B.,
RA McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA San-Blas G., Taylor J., Mendoza L., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Ajellomyces capsulatus strain H88.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DS990644; EGC49721.1; -; Genomic_DNA.
DR STRING; 544711.F0UUZ4; -.
DR VEuPathDB; FungiDB:I7I53_06285; -.
DR VEuPathDB; FungiDB:I7I53_06287; -.
DR VEuPathDB; FungiDB:I7I53_06288; -.
DR HOGENOM; CLU_245449_0_0_1; -.
DR Proteomes; UP000008142; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProt.
DR CDD; cd05120; APH_ChoK_like; 1.
DR Gene3D; 3.90.1200.10; -; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF30; MATERNAL EMBRYONIC LEUCINE ZIPPER KINASE; 1.
DR Pfam; PF01636; APH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 2.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000008142}.
FT DOMAIN 16..288
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 570..598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 543..570
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1199..1226
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 579..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1572 AA; 177618 MW; 04993C25F0177369 CRC64;
MKHSQLAPLP NDLPFRIVSK TIGQGAYACI KRACPLQSDS PVFAVKFIHK DYAARHGRIT
SKQLQMEVAL HKHIGRHNNI IYFHETGEDD CWRWIAMELA EGGDLFDKIE ADEGVGEDVA
HVYFCQLVNA VGYMHSKGVA HRDIKPENIL LSANGNLKIA DFGLATLYEY RGETKLSTTL
CGSPPYIAPE VINCSNRGKS KGQGYRADVV DIWSCGVVLF VLLVGNTPWD SPTDDSYEFV
EYVKTNAKPT DELWERLPTA ALSLLRGMMK VDASNRFSMD DIRRHPWFTR TNPYMSADNR
LSNPINLATT MLESLHIDFN RDPLSLSSQP QPTTTDTGAM EVDEPGSSVK FKFASTQPEH
PVDDMLDWDG PPRLTSQSAF SQPKSMDTDH VMLLNERLSQ DPSMSQFSTT PSVPLSRTQN
AVNFHDIVPA SRLTRFASAW PLGLLVPRVC EALQLLHVPA SPTSSDSADS TLIRIRTQDD
RKCPLHGNII IESITEGHVE VEFVKVKGDP LEWRRFFKKN LSNDDMEYEP TTGPTTDNTL
IQMREYLRKQ DEYLNRMNEY SDRMDRMMEK SLQKPGGNPD SRSRRDQEDI KQGEDEMDQL
TSAPQIYASA ADMLIQPLRR PTFMVTWSTK LTSYMDLPCS ESKAALRGIL NLGLDLPAMR
FSDICRDNSI WRQHSYEAAN HKLQGCNTLF HNLRPNTNTT SGVLDVLLTD QIQAGNIAKS
SKALHTDSDS SHNKRTIPLA TSASQWDPSY QGEQIDWYSE YIARNAPISV HWLQEPYAAA
VQDEDDAIIQ HEIKGMGLMK DNRYGGSDKV IGPLDDGTLC LWDLNRSSLS KRGARGKIVG
TSVRGSLTTD SSRRADAPFS SKPTNLDFIS IGECMSVDSF LQTAYIAVGN ILNEVDLSTL
QVISQQKYPW SIFALSQETE YSAPLTVGTT RNLNLYDPRF RGPGPDTRLC CPMSPDNGRY
VSLFQPVPLS ILHTPLPNIN SIVLAGRFSA ILLYDRRNLS SLLSTAHSGA RICSLAAIPT
CPRPYSFTHP ELQNNHTIVA AGEYKGHGSL DMFSISTPAN PGDYRTQDRS LFVRDGICLN
RQSEPYSKLL SVATHGTRLV FTDANGYIKW VERDGRTEVR RWNLTKNTKY RRRRLGLTHS
IPSSLHDPES YRWVDESAAG VSDIVRKILP TGYNYVLDDE LLIWTGDRIG RLHFSNKAGQ
DWDNEAEIYE EQMESARREE EQMYVRFCLR RFKLAYLWVH DNGLIIEVAA TDMFSLTARS
AVTFSMFTLG QFWQTQEPAN RSAFNPFTAF KGLFSPLPRD ADVSTPKAGH GQDISNSILG
IPLAIRLDDH RVLKKARNLL EPDIMKFVAA NTTIPVPKTY ETKFDEEQNT FYIIMDYMHG
KPLDKVWMNL TQDQQKSTCC QIANYLEELR QLTGKQIEGV NGTPVRVGCY YSRWGGPFKT
EKDFNHFMAP NAQQYPGHTH SIHFAHGDLS PRNILVNEDG DIAAVLDWEW AGWFPEYWDV
VRMFTDLPSK KQMPEYAKHL RSALSHQYER ELHAMVHVLK LEPPDPRWKT IHPAAPQLIK
CFASLFFSDA IE
//
