ID A0A183BCH3_9TREM Unreviewed; 1105 AA.
AC A0A183BCH3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN ORFNames=ECPE_LOCUS16908 {ECO:0000313|EMBL:VDP94182.1};
OS Echinostoma caproni.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC Digenea; Plagiorchiida; Echinostomata; Echinostomatoidea; Echinostomatidae;
OC Echinostoma.
OX NCBI_TaxID=27848 {ECO:0000313|Proteomes:UP000050740, ECO:0000313|WBParaSite:ECPE_0001695101-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ECPE_0001695101-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDP94182.1, ECO:0000313|Proteomes:UP000272942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Egypt {ECO:0000313|EMBL:VDP94182.1,
RC ECO:0000313|Proteomes:UP000272942};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001593};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; UZAN01066483; VDP94182.1; -; Genomic_DNA.
DR WBParaSite; ECPE_0001695101-mRNA-1; ECPE_0001695101-mRNA-1; ECPE_0001695101.
DR Proteomes; UP000050740; Unplaced.
DR Proteomes; UP000272942; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 2.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR45627; ADENYLATE CYCLASE TYPE 1; 1.
DR PANTHER; PTHR45627:SF12; ADENYLATE CYCLASE TYPE 3; 1.
DR Pfam; PF00211; Guanylate_cyc; 2.
DR SMART; SM00044; CYCc; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 2.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000272942};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 66..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..237
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 604..628
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 634..657
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 743..763
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 786..804
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 264..405
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 876..1019
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 1105 AA; 126472 MW; 4E67B6FCAA0244C8 CRC64;
MSKDDTVWGE QVRDVFLSNS YAEASIKTKF SIILRTLFQV VNQEFSTIGQ FYEEVSIRHL
VRRLRAGIRL TLIYSLIGIT EIGVMQGEVS ATRIVFVLIV ILSSVIFYCC SARMTTPGRV
FNSSFLIILQ NMALSVLLAA DDSEPQLAGF MTGVMLLVAL CLLLPVRYDL VVVLLVLYAS
AYLISDWLPA ELISSRWVEH RYQTEDEHRV RTTFWVNILI WLTALIGGIQ LHVWGILRQK
FAFLYLADSV HEYNACLELE KRQILTFKEL LPAYFLSKSM VRNSLTESDP ISDTFVEQSE
LQSVITVLDQ LSVRVGCEKL DIFGSTYFAY AGLDPVKAQN HCHLCIELGL VMCYMIKRVA
HKYKTPLRVR VGVHLTSTIF SALIGHIRPR IDLLSYDMNI VEKLQATGIP GRVRVTELTY
QQCKDKFQFA PGDPIELTQP NGELFLMDTY YVHPRSKSIS SFRLTPEEIK VASEEAIDRL
ELIMNRVPNP VNTIQIELEN RLRFSVIKSQ LQVDESLPRG SYSLDSELQL INTANKPTEQ
ELNQMAVQYL ANNIHEAPNY FRTQYLNTPI NFWTRCFVQR DVERIYQSQL SLESDRHLLD
SSSMIIITDM ISLTIHLFLI MLVIYVVIQP SGVMLLSFIL LCLVFCAPQI TILYLFIQMV
MAPTCQDTKP KCNPKFIHKW FVKNVVCEVL LFFQSMTPTL CLLTYMLVFF DNGVHDESAY
QLIIALEPLV YMTHIFPSRS RFVTRLCGIT ISVLIFASVN VYAQSASPLL CTYDRSKSDV
YRDQRVSIYL LEIWAIILMT WTGFRENDLI CRIVFYQRHE RNTQKKKKLS LSIQTHHLIS
ALIPTGLYKC VKAISLMELH HPRKLSAYWT ESLNAGVAHI GVINFRRAIQ SDDTQKTIRQ
IKTLHLLICA LDQLLANSSF GELDKIKSWQ HYYVVCSGLF SKQTRRSTDL RAHLVALMEY
CLLVLHQLNE FNNLHFPDSD GFKLAIGYHT GAIYAGISGS VRMTLNTWGD TVRLAHTLMQ
QEVVNQIVVH EATTLLLSHL YEFQPCGQLI LNTGYPEVNY IPVQMLETVK KNPEDLNDYP
TKPTVITENR TFVQAAADVV IAHEL
//
