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Database: UniProt
Entry: A0A0D2WUL7_CAPO3
LinkDB: A0A0D2WUL7_CAPO3
Original site: A0A0D2WUL7_CAPO3 
ID   A0A0D2WUL7_CAPO3        Unreviewed;      1772 AA.
AC   A0A0D2WUL7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=guanylate cyclase {ECO:0000256|ARBA:ARBA00012202};
DE            EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202};
GN   ORFNames=CAOG_009003 {ECO:0000313|EMBL:KJE96405.1};
OS   Capsaspora owczarzaki (strain ATCC 30864).
OC   Eukaryota; Filasterea; Capsaspora.
OX   NCBI_TaxID=595528 {ECO:0000313|EMBL:KJE96405.1, ECO:0000313|Proteomes:UP000008743};
RN   [1] {ECO:0000313|Proteomes:UP000008743}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 30864 {ECO:0000313|Proteomes:UP000008743};
RA   Russ C., Cuomo C., Burger G., Gray M.W., Holland P.W.H., King N.,
RA   Lang F.B.F., Roger A.J., Ruiz-Trillo I., Young S.K., Zeng Q., Gargeya S.,
RA   Alvarado L., Berlin A., Chapman S.B., Chen Z., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D., Howarth C.,
RA   Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., White J., Yandava C., Haas B., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capsaspora owczarzaki ATCC 30864.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KE346371; KJE96405.1; -; Genomic_DNA.
DR   STRING; 595528.A0A0D2WUL7; -.
DR   EnsemblProtists; KJE96405; KJE96405; CAOG_009003.
DR   eggNOG; KOG0192; Eukaryota.
DR   InParanoid; A0A0D2WUL7; -.
DR   Proteomes; UP000008743; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   PANTHER; PTHR11920:SF335; GUANYLATE CYCLASE 32E; 1.
DR   PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 2.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293};
KW   Kinase {ECO:0000313|EMBL:KJE96405.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008743};
KW   Serine/threonine-protein kinase {ECO:0000313|EMBL:KJE96405.1};
KW   Transferase {ECO:0000313|EMBL:KJE96405.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        727..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        899..918
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          815..1185
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1653..1772
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          828..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1115..1167
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1224..1266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1326..1346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1402..1426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1118..1167
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1402..1422
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1772 AA;  194385 MW;  BE8C7F758C565EF8 CRC64;
     MSHLDAHADG LARHSAQNER DNVRKTRSIG MAEIATLTLA EPTHQKFRRR HHRQASSSSL
     RPVLSAISLL LVALLLLSGN VRAPSTLPVG GGGGFLQSAP FGGVDALPSN NRHSDDADAD
     ALEPPFHLED EPLVVQQVRS GGGMEGALGS AHELNEQDGE ARKNDAFQRS QGQAAAMHRR
     PRELAEDDNL TEQADGDSAA SISPNNSKVF MEQASASPTA PTGTTIRLVW YDHRGCKALQ
     TVTSLYPEQN VHVEVACLPA EEYNQIPLTP DGAKAYSMDL VTFSPYLLGE AVSTGMLLQF
     PDGVLDTTST SFFAENLALH GEFPPNSNRF YGVPLEGDVP LLAYRNDILQ LAAITNPELF
     GSAGLRAPQS LSDLIQFSRF FYNSSFVPYG FAASWCGTET YLTKACRGQT TLVATNFIWG
     ADGLLFNETT FRAFVSEPYN SNANIGLAVV NALYQTSAKD MTGGESEAIK LFCTGQAAFL
     MVWTSVVNEQ LGDLCRGFFD TPPPYPTLSS NNLIIWDPKD SVLKRRQVDA IDDNDDAFDD
     NADEMDNSQA HFRKSKLPVH RRAPGDPFTV SYQVLPLTQR RAGVGSHQAG GWSLGIASTT
     PNLEAAARVL DWIFEIDQQV QLESLGMLPT QRSLVLDRYF LEQLAPSFGL AYALSFPSAT
     SILSTEVTRQ VTRLSDLYFS QAIFGTLDIR SAMTVYRTRA DAILVDAYPC GPECPPVPSS
     HLSAGEYVAI IVPAAVVMII LLVVCLYRRA EKRINAMEKK QYQIDYNELE NIEDPSCELH
     TTAFYSANQQ PVFISRVDPV KVAPLLASAG IITRARMSKS AASGGLDVEA AGGSPDADGG
     PDGAAVAPRR TSWQQSVRDT TNNCISILPG LISAHRTWRI SRESSQALKR LRSLKHPNVV
     EFLGITVAPQ CFAVYEFMVK GSLLTVIERD GLPHDMDFKC SMAADIARGM LYLHSHGVLH
     KHLRLTKILL DNRFVCKISG ASEQHNLLQQ REYNHHPHHH SAIESSAMAA LAAGALGTAI
     PPDQLANYQA TTTPGRRASS MSTSSNSSAL SALRVRALLG QGGDGLGNDR AEHPVDQRIA
     DGRQELLTET STSAKPWYQQ RTTSWPALFA NKAKGAFRRP SASTQSAESQ TPTSSRKGSA
     IDAAAAPQQQ QQQQQQQQQS QMRQANNTAR VALAPALSTI EEPSVDDAVV LASTGNTNNQ
     QSAAGRTATQ NSAVVFVPAA GEEMSQLPRT TDNSAAQQPR RHWLHHRANG TASDDDEDED
     AYDGVERNEL SSIDESMESV TDEDRAAEYS IAQDQLRSLA QVRDIMNARG RRKSAIDITL
     PPILRSASSK RSSESTRSSQ QSQHAAVLVP SNVIVEMPHP LDAQAKESTS SHAHSRRESY
     QSHLAPLVIP HDDNHSEARA NSKLVEPTDE QKQDEQTDHL EGQDQPLEPV VSGISLASAS
     PGSTSPTRAP LASRRVTITH AINTNVNPEH LLWMAPEVLQ EKILAHSRVD EKLYMTEKAD
     VYSFGLIIYC LFMDITHPFD LELQPEAIFD AIVKRQVRPE LDDTLELTDV EMQVVQLIQQ
     CWQPHALFRP NFRTLLESFE KLYPAENKGF EKMAFMLEKY STHLEEIVDS RSTQLKEEKL
     RAETLLTNML PVTIANRLRS GAGFIADEFP TCTVFFSDIQ GFTAMAHQAS PNEIVRMLNK
     LFTRMDRLAG KYELEKIKTI GDAYMAACGV PTYIENHAEK VVQFAMHVLR NNTCDIHNQP
     IRMRIGIHTG PLIAGVVGTR KFTYDLWGDT VG
//
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