ID A0A183S7X2_SCHSO Unreviewed; 1127 AA.
AC A0A183S7X2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=adenylate cyclase {ECO:0000256|ARBA:ARBA00012201};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
GN ORFNames=SSLN_LOCUS320 {ECO:0000313|EMBL:VDL85413.1};
OS Schistocephalus solidus (Tapeworm).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC Eucestoda; Diphyllobothriidea; Diphyllobothriidae; Schistocephalus.
OX NCBI_TaxID=70667 {ECO:0000313|Proteomes:UP000050788, ECO:0000313|WBParaSite:SSLN_0000033701-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:SSLN_0000033701-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDL85413.1, ECO:0000313|Proteomes:UP000275846}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NST_G2 {ECO:0000313|EMBL:VDL85413.1,
RC ECO:0000313|Proteomes:UP000275846};
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; UYSU01000202; VDL85413.1; -; Genomic_DNA.
DR STRING; 70667.A0A183S7X2; -.
DR WBParaSite; SSLN_0000033701-mRNA-1; SSLN_0000033701-mRNA-1; SSLN_0000033701.
DR Proteomes; UP000050788; Unplaced.
DR Proteomes; UP000275846; 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; 2.
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:UP000275846};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 66..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 666..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 695..722
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 743..766
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 778..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 304..431
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT DOMAIN 934..1077
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 547..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1127 AA; 127350 MW; 2D5A30069D1F36DB CRC64;
MREGNLLGHQ LTDILDVKNA SKSTKTQRLV NSIADIRYFF GLRTHLLSDF FDQLTLPHIK
SGFRMALTYA SLVLCIVLMV FYSRLPVGGN EISEALIFTG FLEIGILYLI SVKAFSVEVY
RYLSIILITT IGVCILATFS SMTVEVSLQH TLILLLAFVS HTNLQIPTSF LFCFQILLGV
GLSAVDTYQE EIPQHPWDTS DGHKAGSGKP AVESLIILLQ VISTTGLSIY VNGYNELRFK
AAFLRLCQGV EARARKNEAM RRQLEWFDVV MPPEIHTKYL EMLLKNRGRE RSSWLFCESY
QPVSILIADA VGMSRLVEQY TAYRVMTILN TMFTEFDTLC SNCKCEKIST LGDTYYCVSG
CPQPNADHAI SCAEFALAIM RSIKSVNAKF KMSLELAVGV HTGHVNAAVL GEERFRFDIY
SYDVNTTQNL QSSCPPGKIH ISGALQELLP SNYITTPAQT IEAKREEVSA IAGMKLSTVK
IPTFYLELTS KNLLDDKTLK RKIKSAFSVK LESLKSKSSS EDLSESIGVA RDIIRETTVC
RHETSRIRHL SSRQRPKNHW TVKNPWNKPP GDDRISSIRK SFFGQPVAQK DFLKSLSDFR
DLNAKDLQLI QQLRSDPDRH AQLFRAHPLD ALGLQFLDPA IEEQYWQEEY DRNKPIYIDS
LKLAPAFDMV VVFIYLTAFV VCSIVATAFD STAGGVLSIL TVAINFLGIL PVTFWINFSI
LVKDTKLTGM LQKKLVIWGR QRKLFEIMLF FIAQIPTIFT IIYYVGIRTE RFSVRHEHFI
LCFGTYAIFI HCLPMNSRFW IRILASSIST LTIETLLFVY AKDASAEIDR TEFGWFYESS
RFQPQTLGPA VVLFAAWVLV IGVSRKNESS CRLAFYMNVE AEKAYRNAMT AINDCDDLLH
NFVPVYVFNI LQAQGRTKLE SDTVNHAVLV QLAGIAFIRI TNFFDGYYRE DYQGGKQALG
LLNKIICMLD RHLRLAQFKD VEKLKSFNDS YMVAAGINME VRMQNMGAVD HVVTLMNFCH
SLFALMDRFN ADYIIGSEKF TIAIGLDVGS VTAGLLGTLK PSYDVWGHPS SQAYKLHRAA
KANQVLVKGN VKRLLESSFD FEPIDAKGTS WEKTSKLFCC KPRSVTE
//
