ID A0A0L0DC78_THETB Unreviewed; 1394 AA.
AC A0A0L0DC78;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Guanylate cyclase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMSG_06250 {ECO:0000313|EMBL:KNC49942.1};
OS Thecamonas trahens ATCC 50062.
OC Eukaryota; Apusozoa; Apusomonadida; Apusomonadidae; Thecamonas.
OX NCBI_TaxID=461836 {ECO:0000313|EMBL:KNC49942.1, ECO:0000313|Proteomes:UP000054408};
RN [1] {ECO:0000313|EMBL:KNC49942.1, ECO:0000313|Proteomes:UP000054408}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50062 {ECO:0000313|EMBL:KNC49942.1,
RC ECO:0000313|Proteomes:UP000054408};
RG The Broad Institute Genome Sequencing Platform;
RA Russ C., Cuomo C., Shea T., Young S.K., Zeng Q., Koehrsen M., Haas B.,
RA Borodovsky M., Guigo R., Alvarado L., Berlin A., Bochicchio J.,
RA Borenstein D., Chapman S., Chen Z., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J., Yandava C.,
RA Burger G., Gray M.W., Holland P.W.H., King N., Lang F.B.F., Roger A.J.,
RA Ruiz-Trillo I., Lander E., Nusbaum C.;
RT "The Genome Sequence of Thecamonas trahens ATCC 50062.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; GL349458; KNC49942.1; -; Genomic_DNA.
DR RefSeq; XP_013757419.1; XM_013901965.1.
DR STRING; 461836.A0A0L0DC78; -.
DR EnsemblProtists; KNC49942; KNC49942; AMSG_06250.
DR GeneID; 25565460; -.
DR eggNOG; KOG0618; Eukaryota.
DR OrthoDB; 5406290at2759; -.
DR Proteomes; UP000054408; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR PANTHER; PTHR43081:SF1; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054408};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..1394
FT /note="Guanylate cyclase domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005537305"
FT TRANSMEM 830..858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..148
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 883..1014
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1177..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1255..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1301..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1380..1394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1394 AA; 145806 MW; 83ADD97B36AC0E81 CRC64;
MTIVMILLLG HFPCHTHALA SCSSQIFNST SGVTAGYVNI TGGYPAAVDC IYQFDYLQGG
LQLIFDSFDT KPPFDHLIVY RGLVGDWSEV LADMSGNSPV GARIGEPIFF NASQISIRFR
ALPPDNERDG VAFSWERRLG LDATDFAVPP EPAIPTCAYN ESSPGVWPSL DIDADISIEM
RVTVNSFSTQ TIFAFLGDNT RFIVGMFDDS NPQYGPDPDA DYAVTFSAGY SPGYIRYESD
APVGTFTQGV ERHIAGVFDA TTSTWTIYVD GAPTSSSWYR SAFFTYYTYG AKTATRGLYL
GRFDGSVRDV RVWNRTLSDG EVSSRASATL SGCEQGLVAL LRPNGIGDFA NLAGIGCGGA
SDITCSIPPN GVATNWTTLP LPVACGDGFR ESSEQCDDGN TNVGDGCDAS CNIVAPWSCS
GDAPTICLEP GYACLTPGAP CTTCAHPNGM DCAGTCDGNA ILDACNVCSG GTTNRLPNAD
RDDCGVCFGG NADRDDCGVC FGANTHKDGC GVCFGSNATC AGCDGVPNSG LVRDVCGVCD
GDGSSCLGCD GVPIPSGGAH FDACGVCGGN ATVCYVGCDG VYGSSIHYDC HSVCGGNATI
DSCGMCAGGN VSTPLPYNYH LDSCGVCFGQ DLTCTTCASG VLDACGVCDG DNSTCVGCDG
IRVSDGGALF DLCGVCGGDG SSCIMGCDGV LGSSAIYDCT GTCSGTAAID ECNSCAGGTS
LIPTANFFRD SCGVCFRGNA DRDSCGVCFG DDADLDSCGV CRGHNAAMDD CGVCFGSNLA
KDDCGTCYGN NTVCAGCDGI PNSGKTLKSC GMCSAADVEC PPNTKTTEGG LSIVTVAAMS
GALLVLCLVL IAAIVLLYRS RRSASVSAYH AALADKAPQG EIFIVTTDIQ DSTALWEANP
EQMILVLDKH NEIMRAAIAA TGGYEFKTEG DAFFVAYEDV EAMISFTCGV QRALMDVSWP
NWLLSLMAEG RPACWNGIRV RMGVHYGRVS SAFDVRAGRS QYFGGMANLA TLVTDAAWGG
QIALSRQVVD RIASARSSSP SPSTSRSAVA LAPLAVLVFS GLAQPCEIWE MLPADLASRS
LCFTDDRMRR IARSAILLTG DVFASVWPDE DAIPSDIVAA PALANRMTTK QALSSLGKST
TNTFPMASSL ATSSPPNTAA DPPSGVALVE ALVRHSIEGT SPSERLANSR GRSPSGTRLS
RPRSISLHST EYHVAGVISP RGHACLQDRN GSQTARAHTS SYEIERCAVR RTKTHRNMAR
TSPREPRALR TRSARNMVSS ASHGQVGTHL AVARARNSRI IDGDGNSSEA SGASDASNAS
KVSHAVTRKR RVRVRSSSRA RALSLSPALK PLPRDDTTPT PPGSVTLSRI NRIAHRRRRS
TNSVPTTAET KMTT
//