ID A0A016V2L4_9BILA Unreviewed; 1412 AA.
AC A0A016V2L4;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 Name=Acey_s0020.g155 {ECO:0000313|EMBL:EYC20963.1};
GN ORFNames=Y032_0020g155 {ECO:0000313|EMBL:EYC20963.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC20963.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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:EYC20963.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JARK01001356; EYC20963.1; -; Genomic_DNA.
DR STRING; 53326.A0A016V2L4; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
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 GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd06352; PBP1_NPR_GC-like; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 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; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR008737; Peptidase_asp_put.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR11920; GUANYLYL CYCLASE; 1.
DR PANTHER; PTHR11920:SF68; RECEPTOR-TYPE GUANYLATE CYCLASE GCY-4; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF05585; DUF1758; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 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; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 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};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 92..105
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 823..1115
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1170..1321
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 826..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1377..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1412 AA; 159816 MW; F8F7A23FC7EC2A12 CRC64;
MGKESATAQQ KRNAPAGTPP IVKHVKHDRG KTPQRQNCAV TSDIQTLPET EDREASSLCV
SNTELTPRQN NVLLLTGVAK VRNEKSGKLQ DIEILLDTGA DRSFILRQLA EDLELPIMDK
VDLSVYTFGD KFPKRQQYDV SRLQIWDALG DTHNLHLCKT DTITEKAKQV RLTPEDVEYL
QKKSITLSKK EDTPVNPQIL LGCDQLWPLL STTSPQYMLP SGLMVIPSKL GYLLSGRQER
SSDKQHQRRK SEDFNMARIG TLDTEDIDKW DHYWSLDSSG IEEFGGAKHE EKAHINTKIL
QFFNKTIERR QDGYYVRLPF KETCETLPTN KTLAYRRLIS AWNMLKSNGD LLHQYHKVFQ
EQLEKGIIEE VPTTENSSLL VHYLPHQPVV TPQKQTTKLR VVFDASSHLK GCPSLNDALH
QGPLILPELY GMLLRFRMKP HVVISDVEKA FLQVRLNEQD RDVTRCFWIR DTSLPPEKDN
IVTYRFTRVT FGLNVSPFLL AATIRYHLNH EVEDQKLACE IGENLYVDNL ILRGDSEEEI
LQKSLKTREV FLQMNMNLRE FLANNSKVQE KFSSEIRASK TTQKVLGISW DATNDTTSIE
CKFMETPKIT KRAIARQIAS IYDPLGWLGY CVVRLLKEFE WDNLSIIFTS NVVNYCDDIV
ADVEAAISDD NSYNPVIVYK EQINKSDTDP FHNALSEIRL RSRIVLICLD SAKERRDFLI
RTSQMGMSTD EFVYVFMGMR GFAFGQSGAG KEVLPNGLTP IWEDVTNGNA DRMDDVAKEA
AKRVLLVDLS AEVEDPSLTE SFKSHVVARV RSDPLYCSTP ACMNNTNLPA DGRSRRSLQS
GPSTLTSDST FDPNTSKFEL YMLNKEPVLV TRHTPVLITS SEQELFVKLR KLEHDNVNKF
IGASIDGSEH LVVWRMCARG SLQTIISKGV FTIDSFFIIC IIRDIAEGLH YLHRSFVGAI
GNLTSATCLV NDAWQVKISG FGIPFFIDRQ LQKESLWVAP EHLAEDPVGE SKPGDIYSFA
IICSEVITRK PAWNIVERKE TTHDLLYRIK RGGHTLMRPE LTLDGVEIGS GLLNLVRDCW
SQDPADRPST EFILSQIRDM NKCWKNANLM DHVFSMLEEY TTSLELERKV SQFLKNDILL
TLEGKRIKEQ VAERLKLGQT VEPEGFDSVT IFFSDVVKFT QLAAKCSPIQ VVSLLNELYS
SFDAIIDEHN VYKVESIGDG YLCVSGLPVR NGSAHIKEIV DMSLAFMEYV RGFRIQFLPR
DKVELRIGVN SETNSQQHLL AAARYLLPSC VGGGCVAGVV GLSMPRYCLF GDTVNTASRM
ESNGKAGHIH LSPTAHSLLT SKFPSQYKTE PRGEVIIKGK GVMETYWVLD RHSSSRAMQD
PVSDSVERAE DCHSQTNSSV NDSDYRKHLS QQ
//
