ID A0A161WK02_9PEZI Unreviewed; 2533 AA.
AC A0A161WK02;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE SubName: Full=Cytosolic regulator pianissimo {ECO:0000313|EMBL:KZL84958.1};
GN ORFNames=CI238_09586 {ECO:0000313|EMBL:KZL84958.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL84958.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL84958.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL84958.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RICTOR family.
CC {ECO:0000256|ARBA:ARBA00008878}.
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:KZL84958.1}.
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DR EMBL; LFIW01000750; KZL84958.1; -; Genomic_DNA.
DR STRING; 1573173.A0A161WK02; -.
DR Proteomes; UP000076584; Unassembled WGS sequence.
DR GO; GO:0031932; C:TORC2 complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro.
DR GO; GO:0031929; P:TOR signaling; IEA:InterPro.
DR CDD; cd17966; DEADc_DDX5_DDX17; 1.
DR CDD; cd01169; HMPP_kinase; 1.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR CDD; cd19367; TenA_C_ScTHI20-like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 1.20.910.10; Heme oxygenase-like; 1.
DR Gene3D; 1.10.287.160; HR1 repeat; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR016084; Haem_Oase-like_multi-hlx.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR004399; HMP/HMP-P_kinase_dom.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR028268; Pianissimo_fam.
DR InterPro; IPR028267; Pianissimo_N.
DR InterPro; IPR013749; PM/HMP-P_kinase-1.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR029453; Rictor_IV.
DR InterPro; IPR029451; RICTOR_M.
DR InterPro; IPR029452; RICTOR_V.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR004305; Thiaminase-2/PQQC.
DR NCBIfam; TIGR00097; HMP-P_kinase; 1.
DR PANTHER; PTHR13298; CYTOSOLIC REGULATOR PIANISSIMO; 1.
DR PANTHER; PTHR13298:SF11; RAPAMYCIN-INSENSITIVE COMPANION OF MTOR; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02185; HR1; 1.
DR Pfam; PF08543; Phos_pyr_kin; 1.
DR Pfam; PF14663; RasGEF_N_2; 1.
DR Pfam; PF14666; RICTOR_M; 1.
DR Pfam; PF14664; RICTOR_N; 1.
DR Pfam; PF14668; RICTOR_V; 1.
DR Pfam; PF03070; TENA_THI-4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00742; Hr1; 1.
DR SMART; SM01303; RasGEF_N_2; 1.
DR SMART; SM01307; RICTOR_M; 1.
DR SMART; SM01308; RICTOR_N; 1.
DR SMART; SM01310; RICTOR_V; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF48613; Heme oxygenase-like; 1.
DR SUPFAM; SSF46585; HR1 repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
DR PROSITE; PS51860; REM_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01207};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584}.
FT DOMAIN 99..179
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 2111..2139
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 2142..2317
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 2329..2492
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1317..1376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2015..2036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2508..2533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2111..2139
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 1..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1318..1333
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2533 AA; 278801 MW; AA92EC77854ECECE CRC64;
MLGASSQSQK ALSPQQSASS VNTLNPRPSF EREASAGGLQ PPSASANASR SLGASGVSFG
PRGSSLNPSI APGSFSSELR SQMMPSRSGS RGDIYSIDKV DEEDSATAAE QTLAALREQL
NREMKIKDGS ENMLEALNAK KAKQTKEQRA KVEAELNASN QRIKVLRQKI ADASRFKATP
TTPIRQRANE ALFSSANNGL RSPPSASRSG AGSDNEEATE QSPTFLLAEL LQALEQEGMP
PEYYVSRGNS LVDLFRRHPT LKYDLVWSVF GLRMQVMLLS EAREVVAAGY RMIRYAISDV
SSLKKIRSLN TDIIVVTSLI KDRKADLERE QALKFVRAFL DVKDGVKELS RAVVRTVAAV
AEQAEDRLRS ICLETLAEIM LRDPALAVAS GGLSPLSEAL IEGTYKSPES LTASYMQILD
NPQKRVYLRS GYDLEVLFTA FTDIILANES LLKQNAKAIT KILKSWPGLM ILTMHDSRAL
KSLLTSMVLP QPTIRETVID LIYLLLRIKS PSWASSFLAG RRLTTYGRVA SLKSMSNHNP
SATSTPIEED SGEQNFMDHY TALLLATFVK AGLLENLLQV ARTSEPQLSR KTCLLIGEVL
KLASRLLPSS WSNDLPLLPE LFAAATQFKD DNRFIASGIV YQISSVSKTL YRSSPSVATA
GTLPSHDSMG NLADMHRKSN AGIVVQEGAI RQLLVESNVL NSSNYLKWNW DVISRIIEGP
LQDGKRLDEV NRVSKFMNRI MSFYRPFKHR FSDLSSNKNT QKYVRVGCAL MHTLLQSHEG
VDYLQDHKML RQIAECLAQC DPSSGLTSTD PMFSPGRLQS TLCAGYFPML GVLSGDPRGL
ELLQRWRMFN MMYHILGHKQ RPDLIKLLLS NFDYSIPGHP RVLIEQALTS GTREIRITAT
NALRKYATRP FDTSQPSHGK VDWKWAIEKL CDQLYDPEVE VCRTAVKILE KACNKKAYLE
YVVQCRPTMD HLGEIGAPLL LRFLSSSIGY HYLDGVDYIS NEMDDWFLGR NDSYVGVIET
SLAKAFLENP EEHQNRMNMV DEAQAEAEPE NHIPPHFYRE LARTQEGCKL LSDKGHFAEF
ASTIKDYGMQ SEDPELMLKV KASMWAVGNV GSMELGAPFI ESCDVVEDIV KIAEEHEVMS
LRGTAFFVLG LISRSAHGLE ILSECGWDAN LSPRGESLGF CIPNDLSKFF SFKPWKHAIA
SKITLPDTQK TFLTPPPPTE ARPPLEKEEL PAFTNEAATN QRILDLVVDL GNMVLYKRAM
GELMQIRQHK VPGFRCPKMF KRVMTMLEYN HYRLPIRRMV IEMFDKSVLR RIVFDEDSDS
GSDEDEDDEE GASSSGDENR TERQRSISDP SELVKDTPTR TDRSNSQSSA DTEGSAETAG
IFVLSQTAGR RSLWPLRFAT ALNMVQGRVL VIAGSDNSGG AGLEADQKVI AAHGCYAMTA
TTALTAQDTT GVHDIHHVPQ EFLVKQIDAC VSDIGVDVVK TGMLASPATI GTVVEALKRH
KIPKVVVDPV MIATSGAELL PREAVAELLE GLLRLTTVLT PNIPEAKLIL EDSGHKPIEV
KGVKDLEEMA KSVQALGPEW VLVKGGHAPF KADLTVAETE EEKSVVVDVL YGHGEFLHIQ
SPYQSSKNTH GTGCSLASAI ASNLAKGLTV PEAARSACRY IEAAIKTAPG FGKGHGPLNH
FHSVQTLPFA PGRFIEYMLA RPDVRDVWKT FVYHPFVMAM GDGTLPMESF KQYLIQDYLY
LVHFARANAL ASYKAKTIAD IAAGATIVSH ITREMSLHID YCKGFGITVP EMEATEEHQA
CTAYTRYVLD VGMSEDWIAL QMALAPCLLG YGAVAKQLHG DVRTKRDDNT YWKWIENYVA
DDYVGAVETG SEASHAVRCS LPYSISFDRS GVDAAVPLEA KNCTRKEVPL PAEGHPRPND
LQSFIDGIRN THAKSEKGFL ESWRPRQGER ARVKNLVAEL AEVPYRESYL LSYPTDKGRA
GPRAPANMSY GGGYGGGGRG GGGGYGGGGG YGGGRDRNDR GGRDGGYGGG GYNGNGYGGG
GGYGGGGGDR MNNLGAGLRT QEWDLNTMPK FEKSFYKEHE EVANRSPAEV ESFRRKHQIA
IAGNDVPKPV ETFDEAGFPR YVMDEVKAQG FPAPTAIQSQ GWPMALSGRD VVGIAETGSG
KTLTYCLPAI VHINAQPLLA PGDGPIVLIL APTRELAVQI QQEISKFGKS SRIRNTCVYG
GVPKGPQIRD LSRGVEVCIA TPGRLIDMLE AGKTNLRRVT YLVLDEADRM LDMGFEPQIR
KIIGQIRPDR QTLMWSATWP KEVRALASDF LTDFIQVNIG SMELAANHRI TQVVEVVNES
EKRDRMIKHL EKMMDNKENK VLIFVGTKRV ADEITRFLRQ DGWPALSIHG DKQQNERDWV
LDQFKTGKSP IMVATDVASR GIDVRNITHV LNYDYPNNSE DYIHRIGRTG RAGALGTAVT
FFTTDNSKQA RDLVNVLREA KQEIDPRLAE MTRYGGGGGG GRYGGWGRGR GGGRGGGGGH
NANNAPLGGA RRW
//
