ID G9MI28_HYPVG Unreviewed; 1042 AA.
AC G9MI28;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Ca2+ transporter {ECO:0000313|EMBL:EHK25905.1};
GN ORFNames=TRIVIDRAFT_189022 {ECO:0000313|EMBL:EHK25905.1};
OS Hypocrea virens (strain Gv29-8 / FGSC 10586) (Gliocladium virens)
OS (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=413071 {ECO:0000313|EMBL:EHK25905.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK25905.1, ECO:0000313|Proteomes:UP000007115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gv29-8 / FGSC 10586 {ECO:0000313|Proteomes:UP000007115};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(2011).
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:EHK25905.1}.
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DR EMBL; ABDF02000003; EHK25905.1; -; Genomic_DNA.
DR RefSeq; XP_013960098.1; XM_014104623.1.
DR AlphaFoldDB; G9MI28; -.
DR STRING; 413071.G9MI28; -.
DR EnsemblFungi; EHK25905; EHK25905; TRIVIDRAFT_189022.
DR GeneID; 25789384; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_189022; -.
DR eggNOG; KOG0583; Eukaryota.
DR HOGENOM; CLU_003954_1_0_1; -.
DR InParanoid; G9MI28; -.
DR OMA; HGRIQQP; -.
DR OrthoDB; 1024at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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 PANTHER; PTHR24346:SF91; CAMK_CAMKL_KIN4 PROTEIN KINASE PPK1; 1.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000007115}.
FT DOMAIN 212..506
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1008..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 241
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1042 AA; 113719 MW; 8F5A0E5E4CA94930 CRC64;
MPRAHQHHHR AAVASDTSAP VNSRIPTSAT RAADQHSRAD RLSTAPIAPP RTSSNNPAHS
SDKMNNSPRR GQADGSRIAS RGDTNGAADP ARSKRAQSYH MPQDSVSAQP TSTRGSHAAE
AHSSIPVPIR THQTTTNSKP SREASESLHR VISNGEEANG RSAAYHNSTH DDDPAAPPPV
VSMNAGSEER RGGRSRHDHS RNNKATTKFG EFILGNTIGE GEFGKVKLGW KQDSNVQVAI
KLIKRDTVGH NPSRLAKIKR EVTILRGIHH PNIVRLIDMV ETDRYIGIIL EYASGGELFD
YILNHRYLKD NSARRLFSQL VSGVGYLHKK GIVHRDLKLE NLLLDRNRNI IITDFGFANT
FDPHDELTEE EELNLSDREY VKRLGIDKVK PNGMRKGDLM QTSCGSPCYA APELVVSDSL
YTGRKVDVWS CGVILYAMLA GYLPFDDDPA NPEGDNINLL YKYIVTTPLT FPEYVTPHAR
DLLRRILVPN PRKRADLFEV ARHSWLSEYA HVVEFITSST TSPSEVQSVS ATGSDYAEAP
MVTRSASVRE APKQKSPQPA VVGGLAKTHG KIDSPTEPTQ RTSKDAKRRT VQVEYVAPVT
QTQRGGTEEV SRHQARPTSR HHHEPALEDL SLDDRNLARP QSKRGPATGQ TSGIPQPTRP
VRDVRATSDH TYAVGVPVAT ARPRTGNSMQ SATSLGLQSG GNYGQPVPPT IADTNVQGRI
QQPSNAAEDD ALGRTSTNVP PKFARMSGFN EPKSSDGKGH KRSNTIGEIG SKLLGRSGSM
FGRKGKKSEQ SAEKAKKYPP ISMANTGMAA GDEPRSRPSI DSKASRRSFT LGLGKKASGS
INGSQDSIDK KERRRFSLLP ASFSLKSLSA PKDYGSAHPS EQDLPIQNPR TADLGRIVTT
HGGSTPFFDN GYDGQQPDMV VSTPPVQNQN HNLAPADRRP NAIPQYMQQG AHLNSASETS
VDMRQPPAGA RQGPYQYGYT QSEGFDGRAI GTGRGVLQKS HKRFTDAYDQ GDYRGHEGSS
GAAKRVMDFF RRRGKARGGD DR
//
