ID A0A0V1H5R3_9BILA Unreviewed; 1390 AA.
AC A0A0V1H5R3;
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:KRZ05637.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ05637.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ05637.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ05637.1};
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004251};
CC Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
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:KRZ05637.1}.
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DR EMBL; JYDP01000135; KRZ05637.1; -; Genomic_DNA.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 CDD; cd06370; PBP1_SAP_GC-like; 1.
DR Gene3D; 3.40.50.2300; -; 2.
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; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR018297; A/G_cyclase_CS.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR011645; HNOB_dom_associated.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR028082; Peripla_BP_I.
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; PF01094; ANF_receptor; 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; SSF53822; Periplasmic binding protein-like I; 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:0000256|ARBA:ARBA00023170};
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 488..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 511..796
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 868..998
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1337..1357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 805..840
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 8..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1339..1357
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1390 AA; 156700 MW; 27BF57B12DFA0462 CRC64;
MAILPAKSAI SSDSSSSHRC ATSSPISPTM LPCNITYGHI ISGALKYAIE IVNANPDILP
GYQLDFIFAD TRGLTKQSVK ATMELWQKGV IAFIGPEDSC QTEAMMAASQ NLPMISYKCF
DHAVSDKSKY STFARTVPAE TEIGRAAISL LKHYSWRKFA IVYGHNDVNS HLLKTIVELS
TEEGLHILNI SRFEEPYRST NFDDRQRISE IVSETHLKTR IYLMFGSVSA LQQMLYAMDD
LELLSNGEYV IIYLEPSYTY LNPDDAMMNY FYRATLYTVE EFHNYPFVNR IVDLSRSVLA
IIPSPVTFTD KAWQEFWEKV NQYNAQPPFN FFNPVSNSHI GKYPVVREGR DIDDVNRYAT
YLYDAVMLYA TALHEELQAG GDPRNGSAII GRIFNRRYQS MQGFEMQINE HGDAEGNFTL
LTRQRLVDSR FNLTYGLIPS AYFIEKNETL PGLLFKHGLR VDWVGGKPPQ DEPECGFRGE
YCVDQPSYAV EIVCGAIGIL MLIMAVVSFI YYRNRKYEQE LAGLIWKINP KEIQFHPCTG
YDNLGGKSAD FSSWIVDPHG LGVYRGSLVA IKEIRYAKRT REITRATKIE MKKMRSLHHD
NVNRFIGIIV QPNFICVVRE YCAKGSLFDV LLNENIKLEN MFIASFVDDL LKGMIYLHDS
EIRVSDFGLS ELREGQIYMS QDSQLMGLLW TAPELLRESV DHMQPCKGTQ RGDSYSFGIV
LHEVFSRNGP FDVYYEDSLS GEEILKNIIH TPYFRPSLAL VECEKYISDT MIACWDERPE
CRPDFRQIRM RLKMLFKGIM KQNIMDHMMG MMEKYQSHLE ELVEERTEEL KEEKKRTETL
LHRMLPKVVA AQLMQGKDVV PETYDSVTIY FSDIVGFTAL SAESTPVQVV AFLNDLYTLF
DRIIRQYDVY KVETIGDAYM VVSGLPIRNG NQHAGEIATM ALELVEAVKA FQVPHKPDVA
CLLRIGIHTG PCAAGVVGKT MPRYCLFGDT VNTASRMESN GMPLKIHCSE STKLALDKLG
GYLLDERGLI PLKGKGEMRT YWLLGKQEAV VSSRPSEANV EEPLFSSSRF VRPCSVKQRS
RETSLISIRM ENARSKIRRE NTILENASVA AERTAQPFAA GNDLKMLGKY QMKCRRRESA
KQAPNRIADD FINRKRSNSY PENIHSLTAK GGTSAPTLRN TTLLTNALYC STQPSSSAAS
SGQPLTLIID NKDSSGGIIS TLADGRQGKR HSREDRSVCK FPVKRHSCSG PRVPKTKLNG
MSISMDEFAL PEHTPWRAQG NLWQVANNRG ERADMNDHLP NTCNGAESIS GSYPEECGVN
CPLLQPAEYF ENAKATDRQF RNESSSQLSN SPMASASHSD SAASLWMRFL KSSMTGGSGE
INAEQQPGIA
//
