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Database: UniProt
Entry: A0A2T7PVF7_POMCA
LinkDB: A0A2T7PVF7_POMCA
Original site: A0A2T7PVF7_POMCA 
ID   A0A2T7PVF7_POMCA        Unreviewed;      1100 AA.
AC   A0A2T7PVF7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=C0Q70_00005 {ECO:0000313|EMBL:PVD37415.1};
OS   Pomacea canaliculata (Golden apple snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX   NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD37415.1, ECO:0000313|Proteomes:UP000245119};
RN   [1] {ECO:0000313|EMBL:PVD37415.1, ECO:0000313|Proteomes:UP000245119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD37415.1};
RC   TISSUE=Muscle {ECO:0000313|EMBL:PVD37415.1};
RA   Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA   Zhang G., Qian W., Fan W.;
RT   "The genome of golden apple snail Pomacea canaliculata provides insight
RT   into stress tolerance and invasive adaptation.";
RL   Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
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:PVD37415.1}.
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DR   EMBL; PZQS01000001; PVD37415.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T7PVF7; -.
DR   STRING; 400727.A0A2T7PVF7; -.
DR   EnsemblMetazoa; XM_025231817.1; XP_025087602.1; LOC112560179.
DR   Proteomes; UP000245119; Miscellaneous, Linkage group lg1.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IEA:InterPro.
DR   Gene3D; 1.25.40.430; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR015661; Bub1/Mad3.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR013212; Mad3/Bub1_I.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR14030:SF4; BUB1 KINASE, ISOFORM A-RELATED; 1.
DR   PANTHER; PTHR14030; MITOTIC CHECKPOINT SERINE/THREONINE-PROTEIN KINASE BUB1; 1.
DR   Pfam; PF08311; Mad3_BUB1_I; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51489; BUB1_N; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245119}.
FT   DOMAIN          1..89
FT                   /note="BUB1 N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51489"
FT   DOMAIN          787..1100
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          394..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..670
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          266..315
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        396..430
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        579..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        602..616
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        617..670
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1100 AA;  123320 MW;  8FC2003F5370DC66 CRC64;
     MDDPLQIYAF MFDQNIGCAL AALYEEWAGF LERLGHASKA DQIYLEGIKR EAQPIDLLKH
     KHQEFQIRMI RGMSRESLAE TEEGDMEEQR IVLGQLKADR KNRVGTMRTG AIRMSATRSQ
     VGLQSASQSS TQVQRTVQVF QDENQAPSLL QTGEWKTVPC REQTNRENDL VPDIWTKARV
     HQKKGVISCT PAPLTFKVHE DQEMVQPPRA PVLDTYALSS RKVEKPVHLL DPICKSESSN
     VERPAYCKDK IYCGTQEFSF EEIRALRVME RRRQKKLQEE RDLMEKQLAE MRLMRDQMCK
     DMERMKEEAL LLNQRQPTAT HCMQLQLSAQ DNAFHSSSSS SFNTMDFLSS SLMPTRNRQS
     LRLSQISSTV QVGAPSGHAS TQLTPIHDML ASDNLERSCG SGTQFSLHQS HSDGRTPENN
     TSKHSLHSVS PTINTREALQ MVQGMYNATL DCEKMVWTQE DITEATAPVP PVPVEIYDET
     KQNPSTSSIP IFCDQENRLP GLVFSQIKKD GPSLNLANVR KALPEKPMST SSSLIRGGQF
     NTEDFMQEGT ELYNNLTLTL APVGSQDSFS AAARLASTPF GPSTNNSHGL PTFSLDSSKS
     IDPGKENGEM WKGKCHTEEQ QSVSQCPDPH QQQTFLGHRT TAGNNHLSPI TEGSTEGSTE
     ESKSHAASSL GGSRTFFSTL AKTSAGHDNQ GDFLSMTSRD YLNEESTEQH IIDTTAYIPL
     EQYEKAEALL STSVCLDTHN PFDEATTRTL LSSVQPPISC RANYIACHQH VPNFSNCHFI
     NLGEDTYQLA GLIGEGGFAK VYRATNFGNN FDDLSDDEMD SPSCVIKVQK PAAPWEFYIC
     SVVHEQLSKL QIPMDIRPSL QEITHGYFYD DGSCLVSELC PLGSLLTLAN SLKQDKKLLA
     DLEPLAAFLA VQLLNIVHGL HRCNIIHGDI KPDNILLLQL PQVNKGSDID KVFGHQTQVL
     RLVDFGQAID MSLYPPGTTF LAKVKTSGFQ CIEMMTDRPW TFQTDMFGLV GSLHVLIFGQ
     YMKVYSSQGH WYITSSFQRK WKVDLWKKLF YQLLNIPDCD HQPDLLALSH QFQQHFVDNL
     LCDFRPLMAR VTAVCQADSL
//
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