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Database: UniProt
Entry: A0A2I3H7Z3_NOMLE
LinkDB: A0A2I3H7Z3_NOMLE
Original site: A0A2I3H7Z3_NOMLE 
ID   A0A2I3H7Z3_NOMLE        Unreviewed;       777 AA.
AC   A0A2I3H7Z3;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN   Name=MARK2 {ECO:0000313|Ensembl:ENSNLEP00000039597.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000039597.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000039597.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000039597.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) 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   -!- SUBCELLULAR LOCATION: Cell projection, dendrite
CC       {ECO:0000256|ARBA:ARBA00004279}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC       protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}.
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DR   EMBL; ADFV01079336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01079337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01079338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01079339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01079340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01079341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01079342; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01079343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01079344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01079345; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I3H7Z3; -.
DR   Ensembl; ENSNLET00000060218.1; ENSNLEP00000039597.1; ENSNLEG00000004656.3.
DR   GeneTree; ENSGT00940000155031; -.
DR   Proteomes; UP000001073; Chromosome 4.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd12201; MARK2_C; 1.
DR   CDD; cd14072; STKc_MARK; 1.
DR   CDD; cd14406; UBA_MARK2; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR028375; KA1/Ssp2_C.
DR   InterPro; IPR001772; KA1_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR049508; MARK1-4_cat.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR015940; UBA.
DR   PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR   PANTHER; PTHR24346:SF56; SERINE_THREONINE-PROTEIN KINASE MARK2; 1.
DR   Pfam; PF02149; KA1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00627; UBA; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SMART; SM00165; UBA; 1.
DR   SUPFAM; SSF103243; KA1-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50032; KA1; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001073}.
FT   DOMAIN          43..293
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          312..351
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          728..777
FT                   /note="KA1"
FT                   /evidence="ECO:0000259|PROSITE:PS50032"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          362..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        367..396
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        403..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..436
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   777 AA;  86691 MW;  B723E19D1C9047BF CRC64;
     RTFTRTPLPT LGHLDSKPSS KSNMIRGRNS ATSADEQPHI GNYRLLKTIG KGNFAKVKLA
     RHILTGKEVR TGTGDMHDPR YFIFQLFREV RIMKVLNHPN IVKLFEVIET EKTLYLVMEY
     ASGGEVFDYL VAHGRMKEKE ARAKFRQIVS AVQYCHQKFI VHRDLKAENL LLDADMNIKI
     ADFGFSNEFT FGNKLDTFCG SPPYAAPELF QGKKYDGPEV DVWSLGVILY TLVSGSLPFD
     GQNLKELRER VLRGKYRIPF YMSTDCENLL KKFLILNPSK RGTLEQIMKD RWMNVGHEDD
     ELKPYVEPLP DYKDPRRTEL MVSMGYTREE IQDSLVGQRY NEVMATYLLL GYKSSELEGD
     TITLKPRPSA DLTNSSAPSP SHKVQRSVSA NPKQRRFSDQ AAGPAIPTSN SYSKKTQSNN
     AENKRPEEDR ESGRKASSTA KVPASPLPGL ERKKTTPTPS TNSVLSTSTN RSRNSPLLER
     ASLGQASIQN GKDSLTMPGS RASTASASAA VSAARPRQHQ KSMSASVHPN KASGLPPTES
     NCEVPRPSTA PQRVPVASPS AHNISSSGGA PDRTNFPRGV SSRSTFHAGQ LRQVRDQQNL
     PYGVTPASPS GHSQGRRGAS GSIFSKFTSK FVPLNSPSLC FLRNLNEPES KDRVETLRPH
     VVGSGGNDKE KEEFREAKPR SLRFTWSMKT TSSMEPNEMM REIRKVLDAN SCQSELHEKY
     MLLCMHGTPG HEDFVQWEME VCKLPRLSLN GVRFKRISGT SMAFKNIASK IANELKL
//
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