ID W1QHP4_OGAPD Unreviewed; 1796 AA.
AC W1QHP4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Adenylate cyclase {ECO:0000256|ARBA:ARBA00021420};
DE EC=4.6.1.1 {ECO:0000256|ARBA:ARBA00012201};
DE AltName: Full=ATP pyrophosphate-lyase {ECO:0000256|ARBA:ARBA00032597};
DE AltName: Full=Adenylyl cyclase {ECO:0000256|ARBA:ARBA00032637};
GN ORFNames=HPODL_00568 {ECO:0000313|EMBL:ESX01166.1};
OS Ogataea parapolymorpha (strain ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL
OS Y-7560 / DL-1) (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=871575 {ECO:0000313|EMBL:ESX01166.1, ECO:0000313|Proteomes:UP000008673};
RN [1] {ECO:0000313|EMBL:ESX01166.1, ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RX PubMed=24279325; DOI=10.1186/1471-2164-14-837;
RA Ravin N.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V., Schneider J.,
RA Mardanova E.S., Smekalova E.M., Zvereva M.I., Dontsova O.A., Mardanov A.V.,
RA Skryabin K.G.;
RT "Genome sequence and analysis of methylotrophic yeast Hansenula polymorpha
RT DL1.";
RL BMC Genomics 14:837-837(2013).
RN [2] {ECO:0000313|Proteomes:UP000008673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 26012 / BCRC 20466 / JCM 22074 / NRRL Y-7560 / DL-1
RC {ECO:0000313|Proteomes:UP000008673};
RA Ravin N.V., Mardanov A.V., Eldarov M.A., Kadnikov V.V., Beletsky A.V.,
RA Zvereva M.I., Smekalova E.M., Dontsova O.A., Skryabin K.G.;
RT "Genome sequence of the methylotrophic yeast Hansenula polymorpha DL1.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays essential roles in regulation of cellular metabolism by
CC catalyzing the synthesis of a second messenger, cAMP.
CC {ECO:0000256|ARBA:ARBA00003896}.
CC -!- SIMILARITY: Belongs to the adenylyl cyclase class-3 family.
CC {ECO:0000256|ARBA:ARBA00005381}.
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:ESX01166.1}.
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DR EMBL; AEOI02000005; ESX01166.1; -; Genomic_DNA.
DR RefSeq; XP_013936000.1; XM_014080525.1.
DR STRING; 871575.W1QHP4; -.
DR GeneID; 25770039; -.
DR KEGG; opa:HPODL_00568; -.
DR eggNOG; KOG0618; Eukaryota.
DR HOGENOM; CLU_000430_4_1_1; -.
DR OMA; DFVHVDL; -.
DR OrthoDB; 1698689at2759; -.
DR Proteomes; UP000008673; Chromosome III.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR CDD; cd07302; CHD; 1.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR InterPro; IPR001054; A/G_cyclase.
DR InterPro; IPR048580; CYAA_C.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR036457; PPM-type-like_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR InterPro; IPR000159; RA_dom.
DR PANTHER; PTHR48051; -; 1.
DR PANTHER; PTHR48051:SF1; ZGC:77287; 1.
DR Pfam; PF21187; CYAA_C; 1.
DR Pfam; PF00211; Guanylate_cyc; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 4.
DR Pfam; PF00481; PP2C; 1.
DR SMART; SM00044; CYCc; 1.
DR SMART; SM00364; LRR_BAC; 7.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF52058; L domain-like; 2.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF81606; PP2C-like; 1.
DR PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
DR PROSITE; PS51450; LRR; 5.
DR PROSITE; PS51746; PPM_2; 1.
DR PROSITE; PS50200; RA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW cAMP biosynthesis {ECO:0000256|ARBA:ARBA00022998};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000008673};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 386..461
FT /note="Ras-associating"
FT /evidence="ECO:0000259|PROSITE:PS50200"
FT DOMAIN 1093..1370
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51746"
FT DOMAIN 1406..1544
FT /note="Guanylate cyclase"
FT /evidence="ECO:0000259|PROSITE:PS50125"
FT REGION 1..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1777..1796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1796 AA; 200862 MW; 8F0F86E3BF3CBD93 CRC64;
MTGIANKQQI LEHDSEFPTN HSIPQFNSKY TAESFGASEA LTSSAQRKNK SQESSPLASP
TTSRRSSRFP SVNPVSPSSS SLALNQDAQR TSHTSSVHEL SDNGSRRPSS SQGDIGVPPS
YKGFHGRRDG SEKPVPPLMT PIKPKKSRRG TSFFNKFLPS RRDSDPKARR QGSSHSSRFS
RRSDQSLSSR TASTDSEKGG SPRESVSFSS RLKNPISQAL PFGSSDKKAS PFNLDLDTDN
EQMADITRLS NSRLSRMGST VSMIPQPPLE RTEWRPPESW KVKNTRENSD PLTHYPGIQE
RTSSMSSSES STASSGRSLV PPRKASAITS PSTSSPKSDN HLDGHREKRD SKSTITEDSG
RVYHAKELKG AARSSVRIFI GDKSSVLPCT LDTTCKDVLD SLHRKRFLKN DEDHIIVLKC
GGLIRTLSLD ERPLKIQRTM LFLYGYTQRD NLDYIERTDL SFLFKFVVQD RGVELISNER
RRMINPQNVN LNNWNLQDIP NFLYAEPIVS LDVSQNPSFE FTKEFMHDCR NLLNLSFTRS
GNPKFPTPVV YAPRLQELNL EVNYIKLIPP EISKMTTLTT LNLACNRIST LPASFAELQS
LQSLNLSSNR LKNIPEPLTK IAGLKRLDLS YNSISEIPDS VSNLVNLEVL QLAANRLSRD
LPSFFRQLKT LIKIDIRFNK FDSIDALKNL PALEVIRATG NNISVFKSSA ANLFEVELNI
NPVTLVKFDQ VMTKLKIVDF SKDKLTSCSF VSMLPAIEKL TMDYNHLVSL PDDIYKMKNL
THLSVFRNNL TSLPSAIGSL TRLRYLDLHL NNISFLTPEI WNLSSLEYFN ISSNLLEFFP
DPPEQFVPFT GFSSLGRTAT QRARNHQSSI VAPSTKRRTS EISTMTMSNY DSVGLEKSLK
VLSLNDNKFT DSVIQTVSMF KNLVVLNLSY NELFDIPPGH LNNLTKLQKL YLSGNHLSSL
PVDDLEAFTQ MDTLHLNGNR FHTLPAELSK ITNMTALDVG SNNLKYNIGN IPYDWNWSYN
PKLKYLNFSG NKRLEIKPLH KREGMEDSLD SFLVLKDLKL LGLMDVTITT DLVPDQSVDV
RVRSTVSQLG KYGYGISDTL GNKSSLTTRD VVIERFRGNS NEKLITIYDG KNCSDESGDK
ISKIIQETFE IHLAKELEGQ DSGKTIEDAL RAAFLTMNSE MSILINKDKS STFSSAAAHR
TTTTDELTME KDGLTGCCAT VIYIRGDELY VANIGDIMGI LTKADGEYSV LTIKHEPYAP
EEYARIRESG GFVTTDGYLD GVSDVSRAVG YFKLIPHINA VPSISKYKLT QNEEMIAIAT
SEIWKKVPYD LAADIVRQEK SNPGIAAEKL RDFAISYGVS DKATAVVLSL RQFTTKQKYH
ERGSLPEDSL LRKLDEEIEP PTGELAMVFT DIKNSTLLWD TYPVAMRSAI KVHNAIMRRQ
LRIIGGYEVK TEGDAFMVSF PTPSSALLWC FTVQSQLLTT DDWPAEILAS DQGCEIKDEE
GNIIFRGLSV RMGVHWGRPV CERDIVTKRM DYFGPMVNRA SRVSSVADGG QIAMSTDFYY
EFEKLRNLHE QVKSGAGDIS QVYGSKTLGQ ILESQMNQVD QIGWVEESIG SRKLKGLEAP
EKIWLIFPAH LAQRLKLLTR TNGEIDNRAG KLLMGGLTAE SVWRLRKLSL RLEKICSFCA
GSTTQLISNK AKILPSDLIS SSAEETFINQ IANAEMDLLL FIEHIVTRIE NAVGILTVRK
CASPEEANGL LMGTMDELYR AMHLMVHQAE EAARAKSQLM EELPEELSQD GAELVN
//
