ID A0A1H3T609_9PSEU Unreviewed; 495 AA.
AC A0A1H3T609;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Adenylate cyclase {ECO:0000313|EMBL:SDZ45318.1};
GN ORFNames=SAMN05421504_1182 {ECO:0000313|EMBL:SDZ45318.1};
OS Amycolatopsis xylanica.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=589385 {ECO:0000313|EMBL:SDZ45318.1, ECO:0000313|Proteomes:UP000199515};
RN [1] {ECO:0000313|EMBL:SDZ45318.1, ECO:0000313|Proteomes:UP000199515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CPCC 202699 {ECO:0000313|EMBL:SDZ45318.1,
RC ECO:0000313|Proteomes:UP000199515};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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DR EMBL; FNON01000018; SDZ45318.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3T609; -.
DR STRING; 589385.SAMN05421504_1182; -.
DR OrthoDB; 368920at2; -.
DR Proteomes; UP000199515; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
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 CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR PANTHER; PTHR16305:SF28; ADENYLATE CYCLASE 10; 1.
DR PANTHER; PTHR16305; TESTICULAR SOLUBLE ADENYLYL CYCLASE; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00672; HAMP; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00304; HAMP; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000199515};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 216..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 239..291
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 323..446
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
SQ SEQUENCE 495 AA; 51946 MW; DEAEC90BCE21469E CRC64;
MRKPAHLGRF RLVLRTSLGF AALGLGSSVC GSGVVALLLF FEGSPSQLGD RSWVLGATAA
GLVAVSLVVG SLWTAWLQRR TAIWFVLGRP PTESEARLAL RLPVDMAIVS GTLWLIGTIV
LGTLSYVLGA GEEAFAVALT ILLGGLTTVG LTYLAAEWVA RPVMTIALKV LPPTGSLPVT
VLRRLVLTWA LASGVPLLGV LLVSSPPELI GEGNHTASLI MLSVIGLVVG ALGTALLARA
VAAPLHRLRI ALNQVARGST DVSVPVDDSS EIGMLQTSVN DLVAGLREQD RMRDLFGRHV
GADVARHALE FGASLSGDVR EVVALFVDVV DSTALAYRTP PEELVTKLNR LFTSVFDEVN
ARGGLLNKFA GDAALCIFGA PTRLADPATS ALSAARAIRD AVLDWGELDL GIGVASGPVF
AGQLGTSSRL EYTVIGDAVN EAARLTEHAK TVPGRILASE AVLKACTSSE RTLWTPDGDL
ELRGRQVPTP TWTTT
//
