ID A0A093YQ39_9PEZI Unreviewed; 1721 AA.
AC A0A093YQ39;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=PPM-type phosphatase domain-containing protein {ECO:0000259|PROSITE:PS51746};
GN ORFNames=V490_01110 {ECO:0000313|EMBL:KFY01040.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFY01040.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFY01040.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFY01040.1,
RC ECO:0000313|Proteomes:UP000029320};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the PP2C family.
CC {ECO:0000256|RuleBase:RU003465}.
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:KFY01040.1}.
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DR EMBL; JPJS01000309; KFY01040.1; -; Genomic_DNA.
DR STRING; 1437433.A0A093YQ39; -.
DR HOGENOM; CLU_002827_0_0_1; -.
DR Proteomes; UP000029320; 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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR CDD; cd00143; PP2Cc; 1.
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 Gene3D; 3.60.40.10; PPM-type phosphatase domain; 2.
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 InterPro; IPR000222; PP2C_BS.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_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; PF00481; PP2C; 1.
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 SMART; SM00332; PP2Cc; 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 SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01032; PPM_1; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU003465};
KW Reference proteome {ECO:0000313|Proteomes:UP000029320};
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 139..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 372..399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 855..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 884..904
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 925..953
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 983..1005
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1026..1045
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1256..1686
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT REGION 1..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1692..1721
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1703..1721
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1721 AA; 189222 MW; 76969C9840CC2817 CRC64;
MANPPEKEGP RIQWNADDVE SASRPRALHR SNSQFSIHSS HSRRGSIDPS HALPIQYRAV
SFQIDESFDQ ELLKAKKHKT SAIKELENLD WHLVSPREIF ERLSTSKTQG LSTEQAKKNI
SEYGKNVPSH PPTHYTKQIF GYFFKGFGSI LLVGGILVFV SWKPLGEPAP AIANLALAIV
LLAVFIIQAA FNAWQDWSSS RVMASITTML PDHCIILRDG LQATVFASDI VPGDILYVKA
GNKLPADVRF IEVSSDAKFD RSILTGESAP LPGTVDSTDP NFLETRCIGL QGTHCISGSG
LGVVVSTGDK TVFGRIAKLT NEPSTGMTPL EKEVLNFVFV IISIMVTMIV LFIIVWAAYL
RKNHPGWISV PALIVSCVSV AIAFIPEGLP IAVTAGLTIT ANIMRKNKIL CKSLKTVETL
GSVSVICSDK TGTLTKNKMY VTEAAIGAFD MSVEGSRDEM IRQKNANDSQ NSVSQLRTIA
ALCNSGNFDA ATYHLPLHDR KIHGDATDQA ILRFSESLGP VAEARDAWIK SFELAFNSKN
KYMIRTFTLA NRDGLDLALS LTEANNFRQN STLLTIKGAP DVLIGRCSMF IDRDGVSKPL
DEATRFSISC MKDRWSSQGK RVILLGRKTL SHEQIKSTPT DARFEDEIIE QSRTGLTFVG
IVGIVDPPRD EIPSVVGILR RAGIRIFMVT GDFALTAQAI AAECGIITNL PGAVKTVAAL
TRDEISAPSS INKSFDPTPQ PLTSIVVSGP ELITLNECQW DQLCRYDEIV FARTTPEQKL
RIVREFQSRD EIVGMTGDGV NDAPSLKAAD IGIALGSGSD IAIEAADMVL LESFSAIVHA
VQYGRVVFDN LKKTIAYLLP AGSFSEFWPV FGNVIFGIPQ ILSSFLMIVI CCFTDCAAAI
VLAYEAPEAD VLLRRPRKPK VDRLVNWQLM LQTYAFIGIL ESLASFAMAF WYLERQGIPF
SVFWFQYGAL PDNLDADFVA SKLAVASSIY FVNLVVMQWF NLLGVRTRRL SIFQHPPLFK
KETRNWLLFP AMGFALVMVF FWLYVPEFQR VLGTAEVPVE YFFLPARPWT ITDTYGFIAT
YLSIPPGHGH PSRLLRSRLP TFSRSYRSAS YIPILANSSL DNPPIIKQGD DISDRPLQLH
QRRCVLPRPQ RRHFHNYFVT HLPSSSLHPD SRSPHHKLPR AASVPHTGSG PPPTAVPPLA
GSSRELTVVR IPIQSAKHHF GGKTSRGTRS YNEDRFEAGT IEIPAFANRA PISLTRSDTG
SGQGGEATSA DSASGDPQVF YFGVFDGHGG SECSEFLKHE LHHYVEDAAK QFGLQSSLKR
SPDSMEDPAM GAAIPEVGVA AEEDLSKKVK ESLNSVHMKT KEETKPPDTR SPKEQVAERP
PDAERLKSED PLKQRMDKPK ALELEASLLD QWKSTVGGYF RRFKPDYFDV KVKYQHRNHK
STIEPAASPA ASAPSIETVL MYAFLRCDLD FIIAQASKPD KESTFDLPLN NDEILGRPSA
PAHSIGGPTR FKGGSTASIA MVSTPSPTPF WHPSSPSTLL VAHVGDTRIL LCDTATGLAV
PTTTNHHPSS PIESTRLHRY AATFVTDSFG EERMSGLANT RAFGDMKSKR IGVSAEPEIV
RVALAPAQYS FLVLVSDGVS GTLTDQEIVD IVKEAKTPEQ GAQEVVTFAT ETTKDGDNAT
CLVVRLGGWE RRGEGGSGSL GTKEVRDFRR QEATDPRRNR R
//
