ID A0A261BRE8_9PELO Unreviewed; 1042 AA.
AC A0A261BRE8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
DE Flags: Fragment;
GN ORFNames=FL83_12998 {ECO:0000313|EMBL:OZG12305.1};
OS Caenorhabditis latens.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG12305.1, ECO:0000313|Proteomes:UP000216463};
RN [1] {ECO:0000313|EMBL:OZG12305.1, ECO:0000313|Proteomes:UP000216463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PX534 {ECO:0000313|EMBL:OZG12305.1,
RC ECO:0000313|Proteomes:UP000216463};
RA Fierst J.L.;
RT "Caenorhabditis latens genome sequence.";
RL Submitted (JUL-2017) 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:OZG12305.1}.
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DR EMBL; NIPN01000095; OZG12305.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261BRE8; -.
DR STRING; 1503980.A0A261BRE8; -.
DR Proteomes; UP000216463; 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; cd06352; PBP1_NPR_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; 1.
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; GUANYLYL CYCLASE; 1.
DR PANTHER; PTHR11920:SF375; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-13; 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};
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:UP000216463};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1042
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012153049"
FT TRANSMEM 452..478
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 516..787
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 861..991
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 508..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OZG12305.1"
SQ SEQUENCE 1042 AA; 117433 MW; 845F8CE25266A7E7 CRC64;
MVYIILILEM IFLLILDMAT SVGWQTSASA IEIAMDRINS ERLIDNIDIN FIYVFDDCSE
SKAAGLSSKL MMDANVSAII GPTCNAAGLA VVNLAGYYNT PVLTWGLTIS SNFIDTARYP
TTVTLVPVAK SIAAAIHEVM IQFEWTEFVY VFVEDEKCGY FRDDLEQITA DSNYTSLSRT
IQIYDQSYTN LVRQLEKLKT VSRIFTVCLP EAGDIKRRFM LAAYDLQMTT EEYVYLFAGP
KSTAYQQTSS TGDVVGIWVD WSDDPDGRDE EAKLAFMRTM VIVATPVQGD KYAAFKKDVI
ERMKLPPYNC IEECSDKKYQ EAAEYADQLH DTVYLYALIL NKTIEEQGIE QIANGSNIVT
RGAGIEFEGM SGVVRMNGIG YRLPNMNLAN LDSNATQRTV AFMDIDASSV NWTYAIIDQR
LIWDAYNGHV PQTRPECGYT GKSCPVNFFV DYLYIVVIVA IIIFLCCAAA LIAAYMVIKA
RRDEELRLDD QWIVPHGMLQ TIMKGRKESH HSSRSLQSNS TTTTGTTGIS SRSVFFPETE
SQGFFIYMNE PVLARKYQLR VPIFKQDRAE LRMLRSIEHD NVNRFIGLSI DGPVYMSFWR
YCSRGSIKDV IAKSSINMDG FFIYCLMKDI AAGLQYIHHS PIKQHGNLTS ECCYINDRWQ
VKIGAYGLSF MQGVEKRSED AMLHTAPEVL REALVSGSQA GDIYSFAIVC SELVGHCSAW
NLENRKEEAD EIIFMVKRGG RTPFRPSLDE ADEDINPAML HLIRDCWDED PKQRPNIDMV
NKLMKNMNSG RSGSANLMDH VFSVLEKHAS SLEDEVQERM KELVEEKKKS DILLYRMLPQ
QVAERLKLGQ SVEPEAFESV TIFFSDVVGF TVLANKSTPL QVVNLLNDLY TTFDAIIEKN
DSYKVETIGD AYLVVSGLPR RNGTEHVNNI ANMSLELQDS LLSYKIPHLP QEKVQIRIGM
HSGSCVAGVV GLTMPRYCLF GDTVNTASRM ESNGKPGFIH LSSDAHELLT SLYKEYLTES
RGEVIIKGKG VMQTYWLLGR KE
//
