ID A0A4D9E8U3_9SAUR Unreviewed; 1109 AA.
AC A0A4D9E8U3;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Polyamine-modulated factor 1-binding protein 1 {ECO:0000313|EMBL:TFK04875.1};
GN ORFNames=DR999_PMT12485 {ECO:0000313|EMBL:TFK04875.1};
OS Platysternon megacephalum (big-headed turtle).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Platysternidae; Platysternon.
OX NCBI_TaxID=55544 {ECO:0000313|EMBL:TFK04875.1, ECO:0000313|Proteomes:UP000297703};
RN [1] {ECO:0000313|EMBL:TFK04875.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK04875.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK04875.1};
RA Gong S.;
RT "Draft genome of the big-headed turtle Platysternon megacephalum.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TFK04875.1, ECO:0000313|Proteomes:UP000297703}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DO16091913 {ECO:0000313|EMBL:TFK04875.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:TFK04875.1};
RA Gong S.;
RT "The genome sequence of big-headed turtle.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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: Membrane {ECO:0000256|ARBA:ARBA00004287};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004287};
CC Cytoplasmic side {ECO:0000256|ARBA:ARBA00004287}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TFK04875.1}.
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DR EMBL; QXTE01000125; TFK04875.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4D9E8U3; -.
DR STRING; 55544.A0A4D9E8U3; -.
DR Proteomes; UP000297703; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd05040; PTKc_Ack_like; 1.
DR CDD; cd09539; SAM_TNK-like; 1.
DR CDD; cd00174; SH3; 1.
DR CDD; cd14274; UBA_ACK1; 1.
DR CDD; cd14328; UBA_TNK1; 1.
DR Gene3D; 4.10.680.10; Cdc42-like binding domain; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR030220; Ack1_UBA_dom.
DR InterPro; IPR015116; Cdc42-bd-like.
DR InterPro; IPR037085; Cdc42-bd-like_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR021619; Mig-6.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR049587; TNK-like_SAM.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR14254; GENE 33 POLYPEPTIDE; 1.
DR PANTHER; PTHR14254:SF6; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR Pfam; PF09027; GTPase_binding; 1.
DR Pfam; PF11555; Inhibitor_Mig-6; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SMART; SM00165; UBA; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50002; SH3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR630220-
KW 2}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR630220-2}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000297703};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 206..465
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 468..528
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 167..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..833
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..883
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 332
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-1"
FT BINDING 212..220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-2"
FT BINDING 238
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR630220-2,
FT ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1109 AA; 122464 MW; CD4F708A58D10F90 CRC64;
MRGPGPCAPL SAAASRPGGG RGPGSPPARQ PREPAAGSGQ TPGSPRPMGE APHYQRLGPG
REEDEGEIGL GRRAAPCQRT LPCSMESDEG TDWLLELLTE VQLQQYFLRI RDDLTVTRLS
HFDYVKNEDL EKIGMGRPGQ RRLWEAVKRR KAMCKRKSWM SKVFSGKRPE AEFPPQPQPT
FPKLSSPPPA EEGQQALTCL ISEKDLTLFE KLGDGSFGVV RRGEWGTPTG KTLSVAVKCL
KTDVLSQPEA LDDFIREVNA MHSLDHRNLI RLYGVVLSPP MKMVTELAPL GSLLDRLRKN
QGHFLLSTLC QYAVQIATGM AYLESKRFIH RDLAARNILL ASSDLVKIGD FGLMRALPKN
DDHYVMQEHR KVPFAWCAPE SLKTRTFSHA SDTWMFGVTL WEMFTYGQEP WVGLSGSQIL
HKIDKEGEQL PRPEDCPQDI YNVMLQCWAH KPEDRPTFVA LRDFLLEAQP TDMRALQDVE
EPEKLHIQMN DVITVIEGRA ENYWWRGQNK RTLKVGQFPR NTVTSVAGLS AHDISQPIKN
SFIHTGHGDT NPQQCWGFPD KIDELYLGNP MDPPDVLGVD LNTARPTQLP SRAKKPSYDP
VSEDDSLSTG LKRLCLRKPG PPKGLKLVKP SAWVSATKVG ERQLSRAKGG GPSCGEAPLI
DFGDEPPPAT PSPVGELGAP SLARLAMEAF SLLDKTPPQS PTRALPRPLH PTPVVDWDAR
PLPPPPAYDD VAQDEADFEV CSINSVEGLV GRPAWDEDEK AVGERGSAPL EDNLFLPPHG
AKQRSLAQTT EIFQELQQEC MKRLHVPRSP APGPGDDKPQ IPPRVPIPPR PLRRNEPGRW
SGELSPASGG EEDRPPQIPP RDPLSQPTSR TPSPMALQVG SPQQRASLCS PLASLSTSPG
KAMPTTQSFA SDPKYATPKV ILAQDKDSAR GPCILPIVRD GRKVSNTHYY LLPEPPGYLH
KYEKFFTAAR SPEEPAPRAV STATVRPMVQ QPNCSANNSN PGPRGALRAS CSVQNIVYDS
SSHGCRAAEK VRLVQEMVHG VTTEECQAAL QNHGWNVQRA IQYLKVEQLF CLGLKTRGEC
LRVLETFDWN LEQASCHLLD PASAARQKR
//
