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Database: UniProt
Entry: A0A1L8G152_XENLA
LinkDB: A0A1L8G152_XENLA
Original site: A0A1L8G152_XENLA 
ID   A0A1L8G152_XENLA        Unreviewed;      1067 AA.
AC   A0A1L8G152;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=ribosomal protein S6 kinase delta-1 {ECO:0000313|RefSeq:XP_018120484.1, ECO:0000313|RefSeq:XP_018120485.1};
GN   Name=rps6kc1.S {ECO:0000313|RefSeq:XP_018120484.1,
GN   ECO:0000313|RefSeq:XP_018120485.1,
GN   ECO:0000313|Xenbase:XB-GENE-17337068};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|RefSeq:XP_018120484.1};
RN   [1] {ECO:0000313|RefSeq:XP_018120484.1, ECO:0000313|RefSeq:XP_018120485.1}
RP   IDENTIFICATION.
RC   STRAIN=J_2021 {ECO:0000313|RefSeq:XP_018120484.1,
RC   ECO:0000313|RefSeq:XP_018120485.1};
RC   TISSUE=Erythrocytes {ECO:0000313|RefSeq:XP_018120484.1,
RC   ECO:0000313|RefSeq:XP_018120485.1};
RG   RefSeq;
RL   Submitted (APR-2022) to UniProtKB.
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DR   RefSeq; XP_018120484.1; XM_018264995.2.
DR   RefSeq; XP_018120485.1; XM_018264996.2.
DR   STRING; 8355.A0A1L8G152; -.
DR   PaxDb; 8355-A0A1L8G152; -.
DR   GeneID; 108717713; -.
DR   KEGG; xla:108717713; -.
DR   AGR; Xenbase:XB-GENE-17337068; -.
DR   CTD; 108717713; -.
DR   Xenbase; XB-GENE-17337068; rps6kc1.S.
DR   OMA; GKLWNYA; -.
DR   OrthoDB; 5308056at2759; -.
DR   Proteomes; UP000186698; Chromosome 5S.
DR   Bgee; 108717713; Expressed in egg cell and 19 other cell types or tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd02677; MIT_SNX15; 1.
DR   CDD; cd07287; PX_RPK118_like; 1.
DR   Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR   Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR007330; MIT_dom.
DR   InterPro; IPR036181; MIT_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001683; PX_dom.
DR   InterPro; IPR036871; PX_dom_sf.
DR   InterPro; IPR042132; PX_S6K-delta-1.
DR   PANTHER; PTHR15508; RIBOSOMAL PROTEIN S6 KINASE; 1.
DR   PANTHER; PTHR15508:SF2; RIBOSOMAL PROTEIN S6 KINASE DELTA-1; 1.
DR   Pfam; PF04212; MIT; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00787; PX; 1.
DR   SMART; SM00745; MIT; 1.
DR   SMART; SM00312; PX; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF116846; MIT domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF64268; PX domain; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS50195; PX; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|RefSeq:XP_018120484.1,
KW   ECO:0000313|RefSeq:XP_018120485.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW   Transferase {ECO:0000313|RefSeq:XP_018120484.1,
KW   ECO:0000313|RefSeq:XP_018120485.1}.
FT   DOMAIN          1..132
FT                   /note="PX"
FT                   /evidence="ECO:0000259|PROSITE:PS50195"
FT   DOMAIN          787..1057
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          226..249
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..642
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1067 AA;  118351 MW;  C09B6888E6DBCFD3 CRC64;
     MMISQRDRGD LARFYTVTDP RRHQKGFTIY KVTARIVSRK NPEDVQEIVA WKRYSDFKKL
     HIDLWQIHKN LFKQQELFPP FAKAKLFGRF DENVIEERRQ CAEDLLQFSA NIPALYNSSQ
     LEDFFKGGEV HDGSDLIGPA EPTDFTDSLS DCSSDVRKDS CGPDDLTFTS VSECGGLSSD
     SDLISLTVDK DSLSGIDDGM ASNQTSPSKF LGVLPSPESS IQSVFASSHE ATKSEGEKDR
     QSSFPARLKQ KLSKPDYLTK AGSLITMAMK KESQEDYESA IEFYKKGVDL LLEGVQGEPS
     PTRREAVKKK TAEYLMRAES ISSLCLKHSQ EELSAPPGAL SSRPSWNLRS PAEELKAFRV
     LGVIDKVLLV LDTRTQETFI LKGLRKSEHC ATRKTIIPRL VPNMVRLQEY IISEESVFLV
     LQHAEGGKLW NYLSKFFSRS ADESFDIPPS KSSHSDEDLL KHLAPCPKSS LDSRGSSDRN
     MLSVQQLQSS LTISSQDDSS TQDEEGRESP LKWADSASSS DEECTTSYLT LCREYSQEKV
     QPDTLSVEPL LGLDGQEDFP PDFVEQEPSC TTSNSLNSQL TSEEPLFIEE SGHSVPKPVL
     MADALRKSRG SPMEFFRIDS RESNSDLGDH SSKAGTVDAY PSFQDDVDDD SEFEPERPSV
     GTSVIITHDA ISRGSNDSFP VISFKDAALD DVCSIDEGRP DLLVNLPGTE QMDETEVVFQ
     PNLLETDFME TKLLETPDVL LVNNSLEQLT GLNPNPLVAV EQTWGPHSQI TEQCQVNTNS
     KESSRSASID PLESRGTLSD LDTLLPASVT FPLSYSTTTE GVSQVPCETS SGIKNVYDPQ
     ETLALVSSEV SDELTTNLVQ LNIKIEDTDA CDVKKEFWGE KDIHKLFQEL DAKLSAASNF
     IIPETFIQKW AAEIVLALDG LHGEGIVCRD LNPNNILLND GGHIQLTYFS RWSEVEDSCD
     SDAIEKMYCA PEVGGITEET QACDWWSLGA LLFELLTIKA LVECHPAGMN THTTVSMPDY
     VSKEAQSLVQ QLLQFNPLER LGAGVAGVDD IKSHPFFAGV KWEELAR
//
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