ID G9MSI3_HYPVG Unreviewed; 1131 AA.
AC G9MSI3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN ORFNames=TRIVIDRAFT_150738 {ECO:0000313|EMBL:EHK22987.1};
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:EHK22987.1, ECO:0000313|Proteomes:UP000007115};
RN [1] {ECO:0000313|EMBL:EHK22987.1, 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:EHK22987.1}.
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DR EMBL; ABDF02000006; EHK22987.1; -; Genomic_DNA.
DR RefSeq; XP_013957187.1; XM_014101712.1.
DR AlphaFoldDB; G9MSI3; -.
DR STRING; 413071.G9MSI3; -.
DR EnsemblFungi; EHK22987; EHK22987; TRIVIDRAFT_150738.
DR GeneID; 25788092; -.
DR VEuPathDB; FungiDB:TRIVIDRAFT_150738; -.
DR eggNOG; KOG0203; Eukaryota.
DR HOGENOM; CLU_002360_4_1_1; -.
DR InParanoid; G9MSI3; -.
DR OMA; QQPPIFN; -.
DR OrthoDB; 203629at2759; -.
DR Proteomes; UP000007115; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 2.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00121; NAKATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000007115};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..392
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 915..938
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 967..987
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1021..1041
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1062..1082
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1094..1110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 123..196
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1131 AA; 123735 MW; 24C489A472B04EC8 CRC64;
MADANDKGDP EKGNTGPGRA AKRRIRYFDD EIQPVDSSPA NYNGKLKRKG STYSIHSLSS
IRSGQRVVEP AAALPVLYRT LSIDMERTQG KYNVAMEKKE AGNKAIAGKF TDQAIIIDLG
DLEWHIIPVQ EVTERLDTSI ETGLSAQGVR DKAAEFGANT PTPPKSQLFQ KIFFYLYGGF
GSILFGGSIL VFISWKPLGE PAPAVANLAL GIVLAIVWLA QAAFNAWQDF SSSRVMKSIT
GMLPEDCSVL RDGSRILVPA SQVVPGDLLY FSAGNKLPAD IRFVNVSTDA KFDRSILTGE
SDPLSAVTES TEKNYLETRC IGMQGTHCTS GSGVGIVVAT GDNTVFGHIA KLTNKPKSGQ
TPLQKEIFRF VIIIATLMVL MVVVIVALWA GFIRHKYPDY ISVSTLIVDC VSVAIAFIPE
GLPIALTASL TITAGIMKKN NILCKSLKTV ETLGTVSVLL SDKTGTLTKN QMAVTDCLIG
SSALTVTEAI QQIAEESPSR KKTALKQLRV TSAVCNAGEF DPTTIHLPIH ERKILADATD
QAILRLSESL GPVTKSRGLW NKRFDLAFNS KNKFALRVSS PSSQSSLEST LSASEINGFD
VQKDYILMIK GAPDILLSRC IKYVGEDGEV HNLDEAVRSS IEAIKNSWSS QGKRVLALAR
RSLSGSTMQS NPEDNTFEKE ALEFARTDLT LIGLVGIVDS PREEVPGVIE TLHRAGIRTA
MVTGDFQLTA QAIARSCGII SVSDSEVHSV KNLPRVPPSI EPKKNTKSNH LPSETKAIVL
TGQDLMTLLP HQWHTLVTEY SEIVFARTTP EHKLQIVREF QSRSYVVAMI GDGVNDAPSL
KQADIGISPA SGSDIAIEAA DMVLLDTFSA IPEAVLYGRV VFDNLKKTIA YLLPAGSWSE
FWPVFTNVAF GLPQILSSFL MIIICCFTDC ATAISLAYEK PEANLMLQPP RDVVNDRLVD
WKLLLQAYGF VGTLETVLSF TMSYWYLQRN GLTFSSLWFS FGSIPTPDGQ SADDVNMHLT
VASSVYFITL VVIQWFNAMA LRTRHLSIFT HPPLFNLKTR NWLLFPAILF SLVIALIFTL
VPDITYLGCA PVPVEHWFIP MALGLGLLCI DELRKMMKRR YPGGLIARCA W
//
