ID A0A0V1H633_9BILA Unreviewed; 957 AA.
AC A0A0V1H633;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Guanylate cyclase {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
DE EC=4.6.1.2 {ECO:0000256|ARBA:ARBA00012202, ECO:0000256|RuleBase:RU003431};
GN ORFNames=T11_4246 {ECO:0000313|EMBL:KRZ05636.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ05636.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ05636.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ05636.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001436,
CC ECO:0000256|RuleBase:RU003431};
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-4/guanylyl cyclase
CC family. {ECO:0000256|RuleBase:RU000405}.
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:KRZ05636.1}.
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DR EMBL; JYDP01000135; KRZ05636.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1H633; -.
DR Proteomes; UP000055024; 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:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 6.10.250.780; -; 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; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR011645; HNOB_dom_associated.
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; PF07701; HNOBA; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00452; GUANYLATE_CYCLASE_1; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW cGMP biosynthesis {ECO:0000256|ARBA:ARBA00023293,
KW ECO:0000256|RuleBase:RU003431}; Coiled coil {ECO:0000256|SAM:Coils};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000405};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000313|EMBL:KRZ05636.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..363
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 435..565
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 904..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 372..407
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 906..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 107404 MW; 6F611D1E0E520831 CRC64;
MDWVGGKPPQ DEPECGFRGE YCVDQPSYAV EIVCGAIGIL MLIMAVVSFI YYRNRKYEQE
LAGLIWKINP KEIQFHPCTG YDNLGGSRVS LTSQESADFS SWIVDPHGLG VYRGSLVAIK
EIRYAKRTRE ITRATKIEMK KMRSLHHDNV NRFIGIIVQP NFICVVREYC AKGSLFDVLL
NENIKLENMF IASFVDDLLK GMIYLHDSEI RVHGNLKSTN CCITSRWSLQ VSDFGLSELR
EGQIYMSQDS QLMGLLWTAP ELLRESVDHM QPCKGTQRGD SYSFGIVLHE VFSRNGPFDV
YYEDSLSGEE ILKNIIHTPY FRPSLALVEC EKYISDTMIA CWDERPECRP DFRQIRMRLK
MLFKGIMKQN IMDHMMGMME KYQSHLEELV EERTEELKEE KKRTETLLHR MLPKVVAAQL
MQGKDVVPET YDSVTIYFSD IVGFTALSAE STPVQVVAFL NDLYTLFDRI IRQYDVYKVE
TIGDAYMVVS GLPIRNGNQH AGEIATMALE LVEAVKAFQV PHKPDVACLL RIGIHTGPCA
AGVVGKTMPR YCLFGDTVNT ASRMESNGMP LKIHCSESTK LALDKLGGYL LDERGLIPLK
GKGEMRTYWL LGKQEAVVSS RPSEANVEEP LFSSSRFVRP CSVKQRSRET SLISIRMENA
RSKIRRENTI LENASVAAER TAQPFAAGND LKMLGKYQMK CRRRESAKQA PNRIADDFIN
RKRSNSYPEN IHSLTAKGGT SAPTLRNTTL LTNALYCSTQ PSSSAASSGQ PLTLIIDNKD
SSGGIISTLA DGRQGKRHSR EDRSVCKFPV KRHSCSGPRV PKTKLNGMSI SMDEFALPEH
TPWRAQGNLW QVANNRGERA DMNDHLPNTC NGAESISGSY PEECGVNCPL LQPAEYFENA
KATDRQFRNE SSSQLSNSPM ASASHSDSAA SLWMRFLKSS MTGGSGEINA EQQPGIA
//
