Basic Information | |
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Species | Fragaria vesca |
Cazyme ID | mrna19789.1-v1.0-hybrid |
Family | CBM57 |
Protein Properties | Length: 1028 Molecular Weight: 116344 Isoelectric Point: 8.4095 |
Chromosome | Chromosome/Scaffold: 3 Start: 1107167 End: 1114878 |
Description | Mo25 family protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
CBM57 | 28 | 206 | 3.4e-25 |
INCGGGETTVNGETYEQDNDTSSFFTSPNKNWAYSSSGSGGFLEGNTSYIKNMTCGVSIAEAPLYDRARLSPVSLKYYAFCLREGKYNVTLKFAEIFYTD DTDYTSLRKRAFDIYIQDDKIKRDFNIEEQAGGPDKPITRSFTAVVNKTNPLLKIHLYWDGKGSIGVDGPALNGPLISA |
Full Sequence |
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Protein Sequence Length: 1028 Download |
MKLNYVLPTL FISDLFTIML PADHSLFINC GGGETTVNGE TYEQDNDTSS FFTSPNKNWA 60 YSSSGSGGFL EGNTSYIKNM TCGVSIAEAP LYDRARLSPV SLKYYAFCLR EGKYNVTLKF 120 AEIFYTDDTD YTSLRKRAFD IYIQDDKIKR DFNIEEQAGG PDKPITRSFT AVVNKTNPLL 180 KIHLYWDGKG SIGVDGPALN GPLISAIAVT PEFKVHDQKL HPLHITLIGI GSTFAVLLLL 240 AFAWMVWLRS RSSPKIKVGE EKKGEEIQDK HVTLKELIDA TGKFSDKNKI GTGSLEKVYK 300 AELLGQVKTT VAVKKLSSHF KENIQKLKKE IKWLYELEHE NLIKLFDYHI EKDLQILVYE 360 YMENGSLEDA LTTGDSNTRS LKFTWDTRFK MCLGIARGLE YLHEHRKLNI AHMNIKAVNI 420 LLDGDLNPKI SDFGLAHLYV EEDQFKVIKS DVLQGYTAPE YFHGKFSNKG DVYSFGVILL 480 EIVCWKKNVI KSHHGTEVLV DKANENHERG RLEDMIDKTL QGVDTKQALT ILQLAVKCTN 540 IAPSVRPTMS QVVSVLLDKM KIDELFRPAP PNVGEKIMGT RDLASVDATS MELTLMPSTS 600 SPSPKTKDEL ENTGGIFMLG RFSNGLWQHK NQHKTKDTIG ICASKQSRHW RASRPESGLS 660 PPSPPRQHIS QQLIRSLSQS STSSQSQRMK GLFKSKPRTP ADVVRQTRDL LIYAQRGGTD 720 SRESKREEKM AELSKNIREL KCILYGNSES EPVSEACAQL TQEFFREDTL RLLITCLPKL 780 NLEARKDATQ VVANLQRQQV HSKLIASDYL EANIDLMDVL IQGYGDTDMA LHYGAMLREC 840 IRHQSVARYV LESQHMKKFF DYIQLPNFDI AADAAATFKE LMTRHKSTVA DFLSKNYDWF 900 FAEYNSKLLE STNYITRRQA VKLLGDILLD RSNSAVMTRY VSSRDNLRIL MNLLRESSKS 960 IQIEAFHVFK LFAANQNKPA DIVGILVANR SKLLRLFADF KIDKEDEQFE ADKAQVVREI 1020 AALEPKE* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
smart00219 | TyrKc | 5.0e-40 | 287 | 482 | 207 | + Tyrosine kinase, catalytic domain. Phosphotransferases. Tyrosine-specific kinase subfamily. | ||
cd00192 | PTKc | 5.0e-40 | 288 | 556 | 288 | + Catalytic domain of Protein Tyrosine Kinases. Protein Tyrosine Kinase (PTK) family, catalytic domain. This PTKc family is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers. | ||
smart00221 | STYKc | 6.0e-41 | 289 | 482 | 199 | + Protein kinase; unclassified specificity. Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase. | ||
cd00180 | PKc | 1.0e-41 | 290 | 487 | 205 | + Catalytic domain of Protein Kinases. Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and 550 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. | ||
pfam08569 | Mo25 | 8.0e-138 | 689 | 1025 | 339 | + Mo25-like. Mo25-like proteins are involved in both polarised growth and cytokinesis. In fission yeast Mo25 is localised alternately to the spindle pole body and to the site cell division in a cell cycle dependent manner. |
Gene Ontology | |
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GO Term | Description |
GO:0004672 | protein kinase activity |
GO:0005524 | ATP binding |
GO:0006468 | protein phosphorylation |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3zhp_B | 0 | 689 | 1024 | 6 | 336 | C Chain C, Human Mst3 (stk24) In Complex With Mo25beta |
PDB | 3zhp_A | 0 | 689 | 1024 | 6 | 336 | C Chain C, Human Mst3 (stk24) In Complex With Mo25beta |
PDB | 3gni_A | 0 | 693 | 1024 | 5 | 334 | A Chain A, Structure Of Strad And Mo25 |
PDB | 2wtk_D | 0 | 693 | 1024 | 5 | 334 | C Chain C, Structure Of The Heterotrimeric Lkb1-Stradalpha-Mo25alpha Complex |
PDB | 2wtk_A | 0 | 693 | 1024 | 5 | 334 | C Chain C, Structure Of The Heterotrimeric Lkb1-Stradalpha-Mo25alpha Complex |