ID   SCYL1_XENTR             Reviewed;         827 AA.
AC   Q28FH2; A4QNQ1;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=N-terminal kinase-like protein;
DE   AltName: Full=SCY1-like protein 1;
GN   Name=scyl1; ORFNames=TEgg006d23.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulates COPI-mediated retrograde protein traffic at the
CC       interface between the Golgi apparatus and the endoplasmic reticulum.
CC       Involved in the maintenance of the Golgi apparatus morphology. Has no
CC       detectable kinase activity in vitro. {ECO:0000250|UniProtKB:Q96KG9}.
CC   -!- DOMAIN: The protein kinase domain is predicted to be catalytically
CC       inactive.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR761974; CAJ81390.1; -; mRNA.
DR   EMBL; BC136057; AAI36058.1; -; mRNA.
DR   RefSeq; NP_001016149.1; NM_001016149.2.
DR   AlphaFoldDB; Q28FH2; -.
DR   SMR; Q28FH2; -.
DR   STRING; 8364.ENSXETP00000050005; -.
DR   PaxDb; Q28FH2; -.
DR   DNASU; 548903; -.
DR   Ensembl; ENSXETT00000050005; ENSXETP00000050005; ENSXETG00000023113.
DR   GeneID; 548903; -.
DR   KEGG; xtr:548903; -.
DR   CTD; 57410; -.
DR   Xenbase; XB-GENE-5843537; scyl1.
DR   eggNOG; KOG1243; Eukaryota.
DR   HOGENOM; CLU_010392_0_1_1; -.
DR   InParanoid; Q28FH2; -.
DR   OrthoDB; 1074965at2759; -.
DR   PhylomeDB; Q28FH2; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000023113; Expressed in 2-cell stage embryo and 14 other tissues.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR021133; HEAT_type_2.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50077; HEAT_REPEAT; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Reference proteome; Repeat.
FT   CHAIN           1..827
FT                   /note="N-terminal kinase-like protein"
FT                   /id="PRO_0000249545"
FT   DOMAIN          1..309
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REPEAT          345..383
FT                   /note="HEAT 1"
FT   REPEAT          384..422
FT                   /note="HEAT 2"
FT   REPEAT          502..540
FT                   /note="HEAT 3"
FT   REGION          586..827
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          788..817
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        591..619
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..682
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..771
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        789..827
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   827 AA;  91324 MW;  63B5911162C04E64 CRC64;
     MWFWSRDPAR DFPYDVTGER EELPAGWGVQ KGKKKTGGDA VSVFTYEIRP GAEEQTQAAK
     TALKRIKTLK HPNILSYVDG LETDKCLYIV TEPVTPLGTY VKLRTDSGGV SELEISWGLH
     QIVKALSFLV NDGNLIHNNV CMSAVFVDRA GEWKLGGLDY MYTAGAEDTA PLKGIEMEKY
     NPPEKTDRSK TSKEKWSADM WCLGCLIWEV FNGPLPRPTA LRSLGKIPKS LVPHYCELVG
     ANPKVRPNPA RFLQNCRSPG GFFCNSFVET NLFLEEIQIK DPAEKQTFFE QLSENLDSFP
     EDFCRHKILP QLLTAFEFGS AGAVVLPPLF KIGKFLNADE YQQKIIPVVV KMFSSTDRAM
     RIRLLQQMEN FIQYLNEPTV NAQIFPHVVH GFMDTNPAIR EQTVKSMLLL APKLNENNLN
     MELMKHFARL QARDDQGPIR CNTTVCLGKI APYLNPATRQ RVLISAFSRA TKDPFSPSRA
     AGVLGFAATH NFYSLTDCAG KVLPVLCGVT VDPEKNVREQ AFKAIRSFLD KLETVSEDPS
     QLAELEKDVH TASVSPSVVG GWAGWAVTGV SSLTSKFIRT GGGAQDAAAS EGASAPSTAS
     EASKPDTAPS SSAPPAAAST APTSYEPEEE KGAPDNSLDR WDDEDWGSLE DAEQNRGQTE
     NDDWDTDWGH GKTQEKTVDF SSSRSKTKQV SPPPNRTSAL DDGWGWDDAF QTVPPSKEHT
     ASKSQQLEGT RPASDYNWDT SGSSGRQGDF FASLSEPSSQ KNDNRNSDSA GDWGGDDNWE
     SVEADQGLSK AEMARKKREE RQKEIEAKRA ERRAAKGPLK LGVRKLD