ID Q4DE65_TRYCC Unreviewed; 1527 AA.
AC Q4DE65;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=ATP pyrophosphate-lyase {ECO:0000256|ARBA:ARBA00032597};
DE AltName: Full=Adenylyl cyclase {ECO:0000256|ARBA:ARBA00032637};
GN ORFNames=Tc00.1047053506493.70 {ECO:0000313|EMBL:EAN90818.1};
OS Trypanosoma cruzi (strain CL Brener).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=353153 {ECO:0000313|EMBL:EAN90818.1, ECO:0000313|Proteomes:UP000002296};
RN [1] {ECO:0000313|EMBL:EAN90818.1, ECO:0000313|Proteomes:UP000002296}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL Brener {ECO:0000313|EMBL:EAN90818.1,
RC ECO:0000313|Proteomes:UP000002296};
RX PubMed=16020725; DOI=10.1126/science.1112631;
RA El-Sayed N.M., Myler P.J., Bartholomeu D.C., Nilsson D., Aggarwal G.,
RA Tran A.N., Ghedin E., Worthey E.A., Delcher A.L., Blandin G.,
RA Westenberger S.J., Caler E., Cerqueira G.C., Branche C., Haas B.,
RA Anupama A., Arner E., Aslund L., Attipoe P., Bontempi E., Bringaud F.,
RA Burton P., Cadag E., Campbell D.A., Carrington M., Crabtree J., Darban H.,
RA da Silveira J.F., de Jong P., Edwards K., Englund P.T., Fazelina G.,
RA Feldblyum T., Ferella M., Frasch A.C., Gull K., Horn D., Hou L., Huang Y.,
RA Kindlund E., Klingbeil M., Kluge S., Koo H., Lacerda D., Levin M.J.,
RA Lorenzi H., Louie T., Machado C.R., McCulloch R., McKenna A., Mizuno Y.,
RA Mottram J.C., Nelson S., Ochaya S., Osoegawa K., Pai G., Parsons M.,
RA Pentony M., Pettersson U., Pop M., Ramirez J.L., Rinta J., Robertson L.,
RA Salzberg S.L., Sanchez D.O., Seyler A., Sharma R., Shetty J., Simpson A.J.,
RA Sisk E., Tammi M.T., Tarleton R., Teixeira S., Van Aken S., Vogt C.,
RA Ward P.N., Wickstead B., Wortman J., White O., Fraser C.M., Stuart K.D.,
RA Andersson B.;
RT "The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas
RT disease.";
RL Science 309:409-415(2005).
CC -!- FUNCTION: Could act as a receptor for an unknown ligand.
CC {ECO:0000256|ARBA:ARBA00002708}.
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:EAN90818.1}.
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DR EMBL; AAHK01000584; EAN90818.1; -; Genomic_DNA.
DR RefSeq; XP_812669.1; XM_807576.1.
DR AlphaFoldDB; Q4DE65; -.
DR SMR; Q4DE65; -.
DR PaxDb; 353153-Q4DE65; -.
DR EnsemblProtists; EAN90818; EAN90818; Tc00.1047053506493.70.
DR GeneID; 3543917; -.
DR KEGG; tcr:506493.70; -.
DR eggNOG; KOG0198; Eukaryota.
DR InParanoid; Q4DE65; -.
DR OMA; RCGSTFT; -.
DR OrthoDB; 146224at2759; -.
DR Proteomes; UP000002296; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004383; F:guanylate cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR48016; MAP KINASE KINASE KINASE SSK2-RELATED-RELATED; 1.
DR PANTHER; PTHR48016:SF29; MITOGEN-ACTIVATED PROTEIN KINASE KINASE KINASE 1A; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:EAN90818.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000002296};
KW Transferase {ECO:0000313|EMBL:EAN90818.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 206..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 526..553
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 732..860
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 1265..1525
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1048..1115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1048..1062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1069..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1527 AA; 168496 MW; D967859E96592F78 CRC64;
MGLEGDRLVT PRQETAKSHP ASVNRIEIPR LPMPWSARGQ QNSATGAGVQ LTTLPALGTV
GASTAASNLY SGDLGKQMAA AEVSNKISSR ALLNTTALRT ARSISCMEVM NNESSPDLSS
KEMGSIHAML LDASPRQGRK DFKAADAGAS GKETTPILVK RCSDCSPSTP LGINGLRIEE
TGEQNTVTLE EMLREASEVH GISLKWILYG VMLVTVLIFL MLLGEVHLFV KDNIIIPEEE
LVGISSATAM NQLEWLQYSV KNMLHNFELI QGDPHDTSTN YTLGILCRSI GGAPLVFARY
GPLGTPLLES YACPSATTKP VVPPTSIGTQ HKLPTGFPRM AVYRSDFIIA MMTLRAGSEV
LTVILHKEPV GRLLLANSIP TYSSLALKHS ATSFFLPDFS SLKIVVALHS LDAEYTRYDV
AQPTPLGQVL KNVFNSICAA GKFHTWHTVV RPDTNNLPMK ENDMNASHNA LPGAYVAYRG
LWGSVSRVVI CGVLCSEPEK NECSSDNPTR AWFIVDDEPL RRETEIALTA VSIVSSIAIF
LVFVTLVIAY LSISAPVQHL KSLVFNTVGD KWKKTKQQQW VFHHTRNCWP GDLQALVRSF
QVLSFCFRFN KKYVPQHVLE QQVVALRKRK DYLWRTIVEE IESDDDEEYD GEEEDMVPGV
NDRMDMEAFV KTVAIPDGVA AMGRFNGPEG MFQRELSWCG LISPDVEILE TSGNNFLGHS
NIDLAGGGMT LVEGATVLVV RLCAVELAYF TNYRAALKPH RRIMNLLLGR IRRYRGELFE
RSGDCIAAAW NAFESRTDHA QRAAACALSI ARMLSCYREA GFRVGIVLHQ GPFVCGVVED
NKEAFTTVFG TVPRQAIALA ELASSLPYFR VLVSEPVKQS LASLYECIMV DVIKYHEEDN
PIVMFELYEE RRPALVKGAL LSSSTFAEEH ARVFFDFRNH DFARAMMGIE QLRLRFPGIG
RRLLTRIEIL CKYYMYHENE LPMPYFRPFP IWPNFEAIAN TECPSDIGVQ STKEDSFLDP
PRYLRPPKSI YEDEAVNFRQ ELHDNVLASK RTQNQSPTLK AANVAPSKDA EANNAQSPRS
LTMLSQTQNM QRSTPSLEPE TGEGDDAASK EHQSKPLLRV AVVSPHEEHA EQCVEADKKR
CSGASAGKEE VNREEFAPSI REPTVNASAT AAASAAGSDE KGDPGDEEND GAGRQRFSLT
NRMGPAFPDC RSCSFFCGTD SLDSINSETM VTAPTFSLCN IDGSLTKVAS EIPTEIVAKN
GITYQRSSRI LGKGSFGCVY LGMDILSGRM VAIKFLPLPS EEEEIANVER EVVTMQKVKS
NQVVEFISYA FKSNLIIIVM ECMMAGSLQG MISAFGSIPG TTARLFIRDV LRGLHKLHSL
GVIHRDVKPQ NVLLTLAGNC KISDFGASAF LQELVRRRME GKGLQIQGTP VYLAPESARG
TPEEKSDIWS CGIMFIQLVT GKLPYAKPFL EMSPQILVYQ IGSGAAKPII PESLDEFDAE
FVCNCLKDDP NERLSAQRLL ELPLFAL
//
