ID A0A3Q7UMB5_VULVU Unreviewed; 701 AA.
AC A0A3Q7UMB5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=MARK3 {ECO:0000313|RefSeq:XP_025868435.1};
OS Vulpes vulpes (Red fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Vulpes.
OX NCBI_TaxID=9627 {ECO:0000313|Proteomes:UP000286640, ECO:0000313|RefSeq:XP_025868435.1};
RN [1]
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (JAN-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_025868435.1}
RP IDENTIFICATION.
RC STRAIN=TameXAggressive cross {ECO:0000313|RefSeq:XP_025868435.1};
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_025868435.1};
RG RefSeq;
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 -!- 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 RefSeq; XP_025868435.1; XM_026012650.1.
DR AlphaFoldDB; A0A3Q7UMB5; -.
DR OrthoDB; 5475340at2759; -.
DR Proteomes; UP000286640; Unplaced.
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; cd12196; MARK1-3_C; 1.
DR CDD; cd14407; UBA_MARK3_4; 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; 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:SF1; MAP_MICROTUBULE AFFINITY-REGULATING KINASE 3; 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 Kinase {ECO:0000313|RefSeq:XP_025868435.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000286640};
KW Transferase {ECO:0000313|RefSeq:XP_025868435.1}.
FT DOMAIN 1..201
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 220..259
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 652..701
FT /note="KA1"
FT /evidence="ECO:0000259|PROSITE:PS50032"
FT REGION 264..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 526..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 701 AA; 78200 MW; 78511AC241F1E79C CRC64;
MKILNHPNIV KLFEVIETDK TLYLIMEYAS GGEVFDYLVA HGRMKEKEAR AKFRQIVSAV
QYCHQKRIVH RDLKAENLLL DADMNIKIAD FGFSNEFTVG SKLDTFCGSP PYAAPELFQG
KKYDGPEVDV WSLGVILYTL VSGSLPFDGQ NLKELRERVL RGKYRIPFYM STDCENLLKR
FLVLNPIKRG TLEQIMKDRW INAGHEEDEL KPFVEPELDI SDQKRIDIMV GMGYSQEEIQ
ESLSKMKYDE ITATYLLLGR KSSELDASDS SSSSNLSLAK VRPSSDLNNS TGQSPHHKVQ
RSVSSSQKQR RYSDHAGPAI PSVVAYPKRS QTSTADSDLK EDGIPSRKSS GSAVGGKGIA
PASPMLGNAS NPNKADIPER KKSSTVPSSN TASGGMTRRN TYVCSERTTA DRHSVIQNGK
ENSLTELFAY AASPASVCAT SSTCRLRHQK SMSMSASGHP TMMVPPVDSE GDNSKAVTIP
DPRTPVASTH SVSSAATPDR LRFPRGTASR STFHGQPRER RTATYNGPPA SPSLSHEATP
LSQTRSRGST NLFSKLTSKL TRRNMSFRFI KRLPTEYERN GRYEGSSRNV SAEQKDENKE
AKPRSLRFTW SMKTTSSMDP NDMMREIRKV LDANNCDYEQ RERFLLFCVH GDGHAENLVQ
WEMEVCKLPR LSLNGVRFKR ISGTSIAFKN IASKIANELK L
//
