ID   PATS1_DICDI             Reviewed;        3184 AA.
AC   Q55E58; Q8I7W7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Probable serine/threonine-protein kinase pats1;
DE            EC=2.7.11.1;
DE   AltName: Full=Protein associated with the transduction of signal 1;
GN   Name=pats1; ORFNames=DDB_G0269250;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 160-3123, AND FUNCTION.
RX   PubMed=12529423; DOI=10.1091/mbc.e02-06-0335;
RA   Abysalh J.C., Kuchnicki L.L., Larochelle D.A.;
RT   "The identification of pats1, a novel gene locus required for cytokinesis
RT   in Dictyostelium discoideum.";
RL   Mol. Biol. Cell 14:14-25(2003).
RN   [3]
RP   NOMENCLATURE.
RX   PubMed=18523161; DOI=10.1096/fj.08-111310;
RA   Marin I., van Egmond W.N., van Haastert P.J.;
RT   "The Roco protein family: a functional perspective.";
RL   FASEB J. 22:3103-3110(2008).
CC   -!- FUNCTION: May act as a serine/threonine-protein kinase and guanine-
CC       nucleotide releasing factor (By similarity). Essential regulator of
CC       cytokinesis involved in the binding to actomyosin cytoskeleton.
CC       {ECO:0000250, ECO:0000269|PubMed:12529423}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. ROCO subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO12857.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AAFI02000005; EAL71975.1; -; Genomic_DNA.
DR   EMBL; AY170918; AAO12857.1; ALT_FRAME; Genomic_DNA.
DR   RefSeq; XP_645923.1; XM_640831.1.
DR   SMR; Q55E58; -.
DR   STRING; 44689.DDB0191503; -.
DR   PaxDb; Q55E58; -.
DR   PRIDE; Q55E58; -.
DR   EnsemblProtists; EAL71975; EAL71975; DDB_G0269250.
DR   GeneID; 8616864; -.
DR   KEGG; ddi:DDB_G0269250; -.
DR   dictyBase; DDB_G0269250; pats1.
DR   eggNOG; KOG0192; Eukaryota.
DR   eggNOG; KOG0619; Eukaryota.
DR   eggNOG; KOG4471; Eukaryota.
DR   HOGENOM; CLU_225525_0_0_1; -.
DR   InParanoid; Q55E58; -.
DR   OMA; LQHTITN; -.
DR   Reactome; R-DDI-1483248; Synthesis of PIPs at the ER membrane.
DR   Reactome; R-DDI-1632852; Macroautophagy.
DR   Reactome; R-DDI-1660499; Synthesis of PIPs at the plasma membrane.
DR   Reactome; R-DDI-1660516; Synthesis of PIPs at the early endosome membrane.
DR   Reactome; R-DDI-1660517; Synthesis of PIPs at the late endosome membrane.
DR   Reactome; R-DDI-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR   PRO; PR:Q55E58; -.
DR   Proteomes; UP000002195; Chromosome 1.
DR   GO; GO:0042641; C:actomyosin; IDA:dictyBase.
DR   GO; GO:0005829; C:cytosol; TAS:dictyBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004438; F:phosphatidylinositol-3-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; ISS:dictyBase.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0099139; P:cheating during chimeric sorocarp development; IMP:dictyBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:dictyBase.
DR   GO; GO:0046856; P:phosphatidylinositol dephosphorylation; IBA:GO_Central.
DR   GO; GO:0006470; P:protein dephosphorylation; ISS:dictyBase.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 2.130.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   Gene3D; 3.80.10.10; -; 2.
DR   InterPro; IPR032171; COR.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR   InterPro; IPR030564; Myotubularin_fam.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   PANTHER; PTHR10807; PTHR10807; 3.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF06602; Myotub-related; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00369; LRR_TYP; 11.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50998; SSF50998; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF52799; SSF52799; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   TIGRFAMs; TIGR00231; small_GTP; 1.
DR   PROSITE; PS51450; LRR; 12.
DR   PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51424; ROC; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 2.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   3: Inferred from homology;
KW   ATP-binding; GTP-binding; Kinase; Leucine-rich repeat; Nucleotide-binding;
KW   Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase;
KW   WD repeat.
FT   CHAIN           1..3184
FT                   /note="Probable serine/threonine-protein kinase pats1"
FT                   /id="PRO_0000358889"
FT   DOMAIN          842..1348
FT                   /note="Myotubularin phosphatase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00669"
FT   REPEAT          1391..1412
FT                   /note="LRR 1"
FT   REPEAT          1416..1438
FT                   /note="LRR 2"
FT   REPEAT          1439..1460
FT                   /note="LRR 3"
FT   REPEAT          1467..1488
FT                   /note="LRR 4"
FT   REPEAT          1491..1512
FT                   /note="LRR 5"
FT   REPEAT          1514..1535
FT                   /note="LRR 6"
FT   REPEAT          1541..1563
FT                   /note="LRR 7"
FT   REPEAT          1564..1585
FT                   /note="LRR 8"
FT   REPEAT          1587..1608
FT                   /note="LRR 9"
FT   REPEAT          1610..1631
FT                   /note="LRR 10"
FT   REPEAT          1633..1654
FT                   /note="LRR 11"
FT   REPEAT          1656..1678
FT                   /note="LRR 12"
FT   REPEAT          1680..1701
FT                   /note="LRR 13"
FT   DOMAIN          1716..1910
FT                   /note="Roc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT   DOMAIN          2247..2519
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REPEAT          2745..2785
FT                   /note="WD 1"
FT   REPEAT          2790..2829
FT                   /note="WD 2"
FT   REPEAT          2909..2947
FT                   /note="WD 3"
FT   REPEAT          2949..2986
FT                   /note="WD 4"
FT   REPEAT          2990..3040
FT                   /note="WD 5"
FT   REGION          369..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          913..1013
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1716..1910
FT                   /note="Small GTPase-like"
FT   REGION          2528..2609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2652..2671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3055..3164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        381..516
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2528..2586
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2594..2609
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        2379
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         1729..1736
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT   BINDING         1797..1801
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT   BINDING         1854..1857
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00758"
FT   BINDING         2253..2261
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         2274
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   CONFLICT        160..161
FT                   /note="NK -> II (in Ref. 2; AAO12857)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3184 AA;  356654 MW;  D919E3E7F2F7A69B CRC64;
     MEILNLSIEF HIPDGNTLKK MVRVDNTTKI GEMSRLLLDK FGRSDFDPSQ FQLIVPQKTA
     TISFHVLSDL NKSLSSYNIK NNDELIFKKR QKKTNPGNAK LVSKKKPESI FKTLFSMSTL
     EMKLGEDKSA PEISEVENQI DDLGILFKAL EILTNSFNQN KDIEDIVSSF QYVGNESEIA
     DLVKIVLSNN DGLSSNSNNN SSSNIGSMLN SGGGGSGSNL GLGLSSGTGG SFNGNSSGSS
     SSSSYYYNNN NNNNNIELTA QQKNPKVLCS FILHLLQIIF SQTSLTYSLY ITYLKTNNNN
     NNNNNNNSSS PSNTDLSRST YFYDIPVKSR IILKHIMLFL YNLTQRDASL LDSLSNIIGP
     FILGNVLLDP PPPPPSNSSP PISKSTSNNN LNVSNYHNNN NNNNNSNSNL SNSGNGDESP
     DFQSQNLVKS YNRENSGNSL NSMLHQTSLP NNNNSNVVNN NNNNNNNNNN NNNNNNNNNN
     NNNNNNNNNN NINNNSTSSN NNNNNNSNNN NSQIPPLIQV RQPSSDFTTT SSGNLRSLSN
     TENSLCKKVA IDLIQNIPLY LLFSHLKIQQ LEGEKILFSA ENIFCVDKCN FPPNKAMLGE
     IWVTNFRIIF INSNSNSSTI PNSTSSTSIS SFASTQNLSI LSIMTLFGSY NGNGGSGPTN
     ATLSGGGSTS SSSNLNTPIT TSPIHTSTNS NGAILNPINN SLINSNNNNN NNNINNNINN
     NINNINNNIN NINSNSNNNI NSIINSNSNN NNNNNNLNKL STLDNTEIPL SMIYRWKMVK
     TGSLYDSFKI YCKDFRCKII GFQINSHVLV KFKDLLTKCS VPTLDTIFAY NSKESSFGNT
     ECFPDHSLLQ EYNRIGVSWD LWRTTTQSKL CEHYPPTSVV PKSVSDNIVV TSAYYRSYGF
     PVLAWSHPTQ KSSITRATSP EDQNNGSSNY LLTPNSPNSS SSNLANNNNS NNNNINNNNN
     NNNNNNNNNN NNSNNNNNNN NNNNNNNNNN NNNNGGGSGS RSTTIDNGQT SILNKNISNT
     PLIQSPTPNL PPSQHSLNLL MSPQTSSPRI HQSISSSSIP QVCQEDIDFL RGILDIKSSS
     MLNVFDTGSG GSYSSTMIGC QIEFLNLPPP NKVRERFNRL LHLHLGNPDS EWSETIRFFW
     LDPLKPILSA AINIAMHVDQ GRSVLIQNSS SGPDIELQLS SLAQILLDPY YRTMDGFKVL
     IEKEWLSYGY PFSKRCHHKT SDDGFSPIFM QFIFLVWQIW KEFPTHFQFN EYYLLTLLDN
     VYNSRFGTFL CNNYKERMEN NVYSSTKSFW SFQQQNQSRF TNLFYRPSPS SSSSSSSSSS
     SLSNGYNSSV QHLKCLRVFQ DTMWNEYFFR YCFKSSLAIE QFEDRIKLSL LDIEMTVNSA
     ITSTANALLP FLETLDLSNL RLYYLPSEST LYHLVGLREL NLSKNNLNSI SCSLSSLVKL
     EKLSFEENSI TNLPIETVVL LAEKLTSLTE LNLSSNQLID LPIEFSMFSK SLKKLHLKNN
     RFSAIPEVLG MLENLIELDL SELDLSSSTN SGVGIPTKLS KLCILNLNQT RIVELPKEFG
     DLKSLEKLYL DFNSLVTLPH SFRQLTNLEE LSLSFNSMTE LPREVCFLIN LKKLMIEGNQ
     IQFLPNEISQ LSKLMILNVC KNKLDSLPAS IGQLSQLVSL NLNNNSQLVS LRPTMGLLSN
     LVELKLDGTR LKTPPPEIVS LGLKSILLYL KDLIKGQEQC YKMKLMIVGQ ENVGKTTLLK
     TLKEKKKKAT PSGPNISTDG IAIDQWVFSC LFEELDETSQ NGRLIKKKQD ITLSIWDFAG
     QEIYYTTHQF FLSERSVYIV AWNCALAEEE SRVEFWLQSI TTRAKDAPII IVGTHLDDVN
     RTTAKMQKKR MKEKYLIRYQ NIKAIKLVSC TSGKGITSLR EKLEALVQSQ SNMGESLPRS
     YMLLENLVKE ETKKRIIPTI PWTEFIQMGT ICTITDEAEL LRATMFLHQL GSLVYFPKEP
     GLKQFVILDP QWITTMLSSI ITTKHSYAKD GILNHKSLKQ IWRPPQYPTH LHPHLISLLE
     KFEISYNLSP DSTSFETGTS LIPSLLLNDR PAIFPSLWGS FNQLVRQFGR IYQFEFVPNG
     FFSRLMVRIL NFARVEAKCY WKNGMILQHD EETIFLEMNN AKKSLSFTVR GGANSTTLSR
     DVIETIQSLL DDSFQLPTYV FVPCFHCIFL SLPQCYYFPL DVCENAAVKG TGYLKCLTYD
     ANVRTDLLVP DLVMSNFTGA KIPFDQLMIE ELIGEGGAAL VYRARWQGQT VAVKKLKTIE
     NLDSPIEIND ISLSKAFNEF RRECWVMSEL EHPNIVQLKG LCLDPLCIVT EYLPHGNLYS
     FLHKPEMEFS WLFRLKVALD ISSGMAFLHS STPPIIHRDL KSPNILLASI NENAQTIAKV
     VDFGLSGLQH TITNRGVENP LWLAPEILNK TKEASTQTDV YAFGVILWEL VTRKDYFGEI
     GFMTLIEEKV INGERPKIPE DCPEMYSKLI VECWQTDASQ RPKFSEIEDR LIKIAEAMFP
     DIHLSNIYQQ QQQQQQQQQQ SSPSKSSSTS PIIKSLNLST VSELGESSNQ TPKQNITTTT
     TTTHSDHKRQ LSTDSGSSYR NKSHDTISHS TSVASDLLDI DNTLTVATTP RNRSKTNDDN
     IINTSNGRII TNSINNSNSN NEQPLSPNSL LQHSQSQQQL ENVGLSALLD ALPNSPIVSS
     TAAPSTTSTN KKVMYTSIVG DSARTRRGSV SIQPFQNEFN RELLPNQGTI QCLIKVGGNG
     CQVWAGTGNG FISTWKIEGQ EKYIQRLFEA NKDKKRIHCL YPYMNTVWCG SADDSITIWD
     IDTYQKIKSY SVEGPSCITR VGNTMWVGTI VNTIHIYDLK KKTKYKGKIS LDSPIECLLR
     RDQEVWVATL GNIARIDVNS LRVVQMTKAH ERAIHAMIQV DDHVWTASSD GTIKVWSSTC
     QSVHTIENAH SSRIFTLELV GDFVWSGSWD TTIKIWSTKD YHLVSENSGK HKDAISSFVY
     ISNDQPLQTN ERPIQKQVWS GSWDSSICVW ALPNDTNSRS NTIFSSDSQF NLNGGSSNSI
     TNSNSNSNNN LNGNLNNSNN SINNNYNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNYYY
     SNNVNSPNQA SQSAGHLGTI HEQTSPNSAT PLSSTPPGSK GLMQRRTVSF MNVLERFSND
     KNRK