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Database: UniProt
Entry: A0A182UBY8_9DIPT
LinkDB: A0A182UBY8_9DIPT
Original site: A0A182UBY8_9DIPT 
ID   A0A182UBY8_9DIPT        Unreviewed;      1377 AA.
AC   A0A182UBY8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Anopheles melas.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=34690 {ECO:0000313|EnsemblMetazoa:AMEC017638-PA, ECO:0000313|Proteomes:UP000075902};
RN   [1] {ECO:0000313|Proteomes:UP000075902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM1001059 {ECO:0000313|Proteomes:UP000075902};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Besansky N., Howell P., Walton C., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Anopheles melas CM1001059_A (V2).";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AMEC017638-PA}
RP   IDENTIFICATION.
RC   STRAIN=CM1001059 {ECO:0000313|EnsemblMetazoa:AMEC017638-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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         Evidence={ECO:0000256|ARBA:ARBA00001433};
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; Evidence={ECO:0000256|ARBA:ARBA00000775};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   STRING; 34690.A0A182UBY8; -.
DR   EnsemblMetazoa; AMEC017638-RA; AMEC017638-PA; AMEC017638.
DR   VEuPathDB; VectorBase:AMEC017638; -.
DR   Proteomes; UP000075902; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR   Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR032171; COR.
DR   InterPro; IPR001611; Leu-rich_rpt.
DR   InterPro; IPR025875; Leu-rich_rpt_4.
DR   InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR   InterPro; IPR032675; LRR_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020859; ROC_dom.
DR   PANTHER; PTHR48051; -; 1.
DR   PANTHER; PTHR48051:SF26; NON-SPECIFIC SERINE_THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF16095; COR; 1.
DR   Pfam; PF12799; LRR_4; 1.
DR   Pfam; PF13855; LRR_8; 1.
DR   Pfam; PF08477; Roc; 1.
DR   PRINTS; PR00449; RASTRNSFRMNG.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00364; LRR_BAC; 8.
DR   SMART; SM00369; LRR_TYP; 8.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 2.
DR   PROSITE; PS50088; ANK_REPEAT; 2.
DR   PROSITE; PS51450; LRR; 3.
DR   PROSITE; PS51424; ROC; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   REPEAT          52..78
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          288..320
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          1018..1234
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   REGION          209..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          794..859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        829..859
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1377 AA;  149982 MW;  58C922E46CD52DF2 CRC64;
     MDPVDHTREQ IRSQKHRALR EAVTATDEAA VQLLLESIGS DREIIVNMAP GGANTLLFIA
     AQAGSERIVQ LLLEAGADGR AHAVTKYSPL YTAVHNGHTQ VAALLLDRFP ELVQQVTVER
     WLPFHAACIN GHCAVVELLI KHPYVEELLG VYRSPNGELE WRLPFDPNAQ DVAGQTALYV
     GCLLGNPQLV ETLLKWRVKC VRHTLASTTD HEQAKMGGSG GRDHGGGGGS SSSNPLSPTS
     RKISFGIQSI MSRLSLSGGR TDPSEEGEEG QLGEMRCPLD LDILCGAARE TALLAAVRGG
     FLDVVTILLE NGADPNVIAR AVEDQNDPKS SDEIYGFSNV PLAEATRQKS LPMVELLLKH
     GARDDQSVAL GIAVQNGDEP IICRLLAIKA HPDPDYKINK RALAGQEASA PEYGTAPLAF
     VGKLGGSFTY SSLFPSTATM INWHSNNCRL GLIRMAWVSE AVLQCNRKLR AHPKCHQLAL
     AALTRIDISH NTLTTLPAEL FALGSLRYLN AAQNKIERLP LPDEDAGGQG KRRGSAKPVD
     YQCPVLEELY LQDNRLECVP AVLFRLPNLA ILDVSNNKLQ ELPFEMWKAP KLKELNVAFN
     FLKDLPSLPL PELLLSCGQG QGGDGGRLEL PSPVTIAVEG GGGGGGGCGS SAAAAAMFHP
     YTGTSASFDD GTEALARNRH VTNLELVRHH IWARSLEVTE QELRLADARH DSALSQLSSL
     NLANNLFTSI PLALPCLAVN LTRLNMSYNS LRSMGHVTSY PASLKQLDLG HNEISCWPSL
     PRIAASDPHL MCYNPQEGKK HPTDSGGGSG GVGAGTGGGS GGKSGSRGGS GGGDTTPSSN
     ASTTSYGGTE MTTVVKSSTS SNSITSLRTA VLKSVCCHRR HLRLESLRTL VLADNSLTRI
     QLSTDDVTTL GESDDAEWSL IGMAKSRLIF PNLSMLDISN NCLKEIPASI HELTNLSVLN
     LSGNMDITEL PPHMGLLSRL WNLNTRGCSL QDPLRSMIDS KKYKTMDIVG YLKSVYEDAR
     PYARMKLMVV GVQGIGKTSL LEQLRAEGSA RGKKPVDHWA KRMGHRHINQ KTSRGINMST
     VGVDIGDWVC EKKVRGQSHH GPVVFRTWDF GGQREYYATH QYFLSKRSLY LVLWRIIDGR
     RGLAEVLQWL GNIQARAPNS PVIIVGTHYD AVGETLPAKK AEELQQIIRD RFIAVSDAEK
     IGLPRVLDSI EVSCRTGHNI KLLAGLIYDT AFSLRPPGCK EPLLYQRVPA SYLALEDVVA
     NIAASLRQHG ADPVLDADRY RQTVTHEMQL RGLKGFRDWS ELNQATMFLH DNGVLLHYDD
     ATLRDLYFLD PQWLCDMLAH VVTVREINPF ARTGVMKMDD LQHVFKSSCL GSNNNRG
//
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