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Database: UniProt
Entry: W2QMF0_PHYPN
LinkDB: W2QMF0_PHYPN
Original site: W2QMF0_PHYPN 
ID   W2QMF0_PHYPN            Unreviewed;      2628 AA.
AC   W2QMF0;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Guanylate cyclase domain-containing protein {ECO:0000259|PROSITE:PS50125};
GN   ORFNames=PPTG_08439 {ECO:0000313|EMBL:ETN13694.1};
OS   Phytophthora parasitica (strain INRA-310).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=761204 {ECO:0000313|EMBL:ETN13694.1, ECO:0000313|Proteomes:UP000018817};
RN   [1] {ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genome Sequencing Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Chapman S.B.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Hansen M., Heiman D.,
RA   Howarth C., Larimer J., Lui A., MacDonald P.J.P., McCowen C.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ETN13694.1, ECO:0000313|Proteomes:UP000018817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=INRA-310 {ECO:0000313|EMBL:ETN13694.1,
RC   ECO:0000313|Proteomes:UP000018817};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica INRA-310.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; KI669574; ETN13694.1; -; Genomic_DNA.
DR   RefSeq; XP_008900770.1; XM_008902522.1.
DR   STRING; 761204.W2QMF0; -.
DR   EnsemblProtists; ETN13694; ETN13694; PPTG_08439.
DR   GeneID; 20178243; -.
DR   VEuPathDB; FungiDB:PPTG_08439; -.
DR   OMA; WYQARRI; -.
DR   OrthoDB; 48945at2759; -.
DR   Proteomes; UP000018817; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0140326; F:ATPase-coupled intramembrane lipid transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 2.
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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR   InterPro; IPR001054; A/G_cyclase.
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; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR032631; P-type_ATPase_N.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR032630; P_typ_ATPase_c.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR24092:SF150; PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR24092; PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00211; Guanylate_cyc; 3.
DR   Pfam; PF16212; PhoLip_ATPase_C; 1.
DR   Pfam; PF16209; PhoLip_ATPase_N; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00044; CYCc; 2.
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; SSF55073; Nucleotide cyclase; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE   4: Predicted;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018817};
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        405..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        449..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1187..1208
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1220..1239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1267..1289
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1309..1326
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1338..1363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1383..1406
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1573..1591
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1597..1615
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1627..1645
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1657..1680
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1701..1723
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2105..2126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2146..2166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2203..2222
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        2242..2262
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1774..1903
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   DOMAIN          2310..2525
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          573..600
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1036..1077
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1454..1474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2584..2628
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..600
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1038..1077
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1454..1473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2628 AA;  293935 MW;  09409BD14440F92B CRC64;
     MALPLPQNAI RSGRSSFPGD VALVSQKVDA TSSANTVITS QSKKRHNKFD LLTSLLRRNR
     VIDNTSEPSD NTQELIKSRL LFVNDVKRTM EYATYMQKFH HADPYSANTV RSSKYSALNF
     LPKSLFEQFR RVANFYFLII SLLQLCTDLS PTNEYSTIGP LMLVLTATMI KEGLEDRARH
     QQDWVVNHGK VETLDGMVEP GKKLKSAGDI SRTNHLGDFQ SIFWKNVRVG HVIKIHDQEQ
     VPADMVLLFS SQETGEAMCE TSSLDGESNL KVRHCIKWNH IIPHTPKEFG DSVHAEIRCE
     APNKRLYSFD GVMRISRSKT QAIGEPPRSY LEARSLENGD EENAPEAEEI PITIENVLLR
     GMKLCNTKWA IGVVVGGGND TKLVQNMKSI PSKFSRLDRI ANRCIFLIFS VLFGVCCFSS
     IQASLFVVKV HRKPGYASAY PFIAKFHPAY VLEAWVTYLI LYNNMVPISL YISLEVVKWY
     QARRIENDPK MYCPTTGRGV TARTSNVNED LGQIKYIFSD KTGTLTKNQM LFKVCSIGGI
     IFDGSNMQHR RAAQAGSDDL SIGSDMMLKF GSASTVRGSS TGREGSADGR RKSKHVSVTE
     KDVRSYSQMM KFVENPSRFS GKELHAVELA RPFFRCLLLC HSASVAIEDP SGHADAHSTA
     SRTPTESSIR TESRRHSAGY NSFTSNLAAA EATDAFPSLI KGDHKFFGSS PDEVALLNAA
     LEFDCVYERR DGDVIHIRLF GIPESYQLLA LNEFDSTRKC MSVVVKRLNR DDCHDSKLAR
     VQDNLGDLEH TDLDGLINES ESEEQDILVF SKGADTVMFA NASKDQDINK LALHVHYFAA
     MALRTLLLGY RTLSMAEYME WKSEFDLAKK ALSNREQLCV EVARKIEKST KLLGATGVED
     LLQDGVRECI SQLSLGGINI WMLTGDKDET AISVAHMCGL IGPKSKIIII KGKTKQDCLD
     EIAKARRKLK REGVWVPGVA SQDISLVING EALELLLADA LTSSKIKSQI SYINGNQTSP
     NAEPHSATID ALRSERDTRF SGSMSAKSMG NLPFPATPNS RHRSSSRPGS TRSSITDTNG
     NVQLAHELFL ELASQCRTVV ACRLSPMQKA QVVSLMKAAP GTPLTLAVGD GGNDVSMIQE
     AHVGIGIYGH EGMQAVRAAD FAIATFRHLS RLLLVHGRWN HRRVARVILF SFYKNMALIM
     TLFLYSFYNG YSGQTLYESY LMVGWNVLYT VLPIFVLGIT DEDIRDSAVL RFPFVYRSSL
     RKSELSIRIL SFWVANALFH SLLVFYFVMK TMGGVSSKHS HTNGLFPDGT AVYGALIITV
     TLKASLHTQC LYRWTRAHYI SLVGGFLAYI LFVGAYSQAY RMFPTFDVFR DFQGLAHILF
     SEMLYWAMLF YTSVTCLCVD LAVMYLRKMY LPSSNDIILE IDSGLGDIPS LPVRNADGSI
     DNSRAAKLIY SSSGRSEEGS YSGASSAVGG STKGELTPSL LEGEWSQQFR DFDLPTEHDE
     LSKQLVSIQR ELAQEIGHPD PLTQEDDAHS SRALRVQPPV HPLTLEFMGE EHQRLEMEYE
     ITFAFRERSR VMLCLKVMAF MVPLYAAYEL LWERESSYIY IRVGYFVCDV LFMRFARTKY
     FVQYYQIAIL LPYCMSGMAL TLTISDTGKF AAALYPVVLF VVIRVKFLYA LMLSIYNFAF
     YMLADRLSSM NYNNSVDLTD LMLFALYLVF VITFGAYACY SLQITMRRDF LQSRSLLIEQ
     KRSTQILKNM LPEHVVQRMQ KGDTNISEDE QDVTILFCDI ADFASFVNRF SPTEVVSLLD
     RVYSLFDQIC QKHGVRKMET VGKTYMACAG LQGKDHGREA ALRAVSMALD MLACLDKCRA
     SNGSGIKLRI GVHSGRVVSG LVGMKKQQFS LFGDTVNTAS RMQSTGVTGR CQISQITYKK
     LVGHFTFEER QIDVKGKGTM TTYLVGEPLT EVAQLSCLGQ LEFSSKRDSV MMSSSIINVR
     RAFEQDFLAA TRNKILHSAR QRWKKYDPIR MLLGTPPDLA SWGGTDTSES VEQHMLTEIR
     LLNMCFKDDD MENKYLESTL SNRVEGARTT LLALAAYASF TCMRDLLVEV FSVISAYAPQ
     KEISATMYAI LLFIRSPFVI VAILVARRVR DEFVFYSETK LRNVLLGFYL VGLFVFTLTQ
     ALLWGLNYEA DLDTSPRYVN LCLDTVLAMF VVSNGRSILY RHVVVFNVIA LFMVSITTLV
     SLQRYHQDAA KFNSKFKTSY PIVLTYFSVV ANIIASQSVE FFTRRQIWLK TRTQLETMNA
     DRLLYQMLPA AVVMRLKEGE MVCDQHQQVG ILFSDIKGFT SIASQAATAQ VVNILASLFC
     AFDKLTEKHG VFKMQTIGDA YVIVSGLPYV DMSLGPGVVT SSASTADMSI ADVGSTSTPS
     IAGIASGFMR ISSNRVLPLE RKTEVMEGQN GSPRGSGSKL RSHLLRRSTL KHKHQMHLRS
     HIRDLLAMAR DMHKEVRKVQ DPNTGERLQM RIGIHIGNII GGVIGTTTLR YDMWGPDALT
     ANELESNGVP EKILVSPVVQ EVVKDMIDIR CTFHRKINFT NVPMMDTYLV EFIEPDGTGG
     RASGCIAGSN VRENSGIPPE QLNPAPGYVG SDDDTTRPQS PREHTTPN
//
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