ID A0A2J7QEE0_9NEOP Unreviewed; 919 AA.
AC A0A2J7QEE0;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=cGMP-dependent protein kinase interacting domain-containing protein {ECO:0000259|Pfam:PF15898};
GN ORFNames=B7P43_G12695 {ECO:0000313|EMBL:PNF26954.1};
OS Cryptotermes secundus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Polyneoptera; Dictyoptera; Blattodea; Blattoidea; Termitoidae;
OC Kalotermitidae; Cryptotermitinae; Cryptotermes.
OX NCBI_TaxID=105785 {ECO:0000313|EMBL:PNF26954.1, ECO:0000313|Proteomes:UP000235965};
RN [1] {ECO:0000313|EMBL:PNF26954.1, ECO:0000313|Proteomes:UP000235965}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole body {ECO:0000313|EMBL:PNF26954.1};
RA Harrison M.C., Jongepier E., Robertson H.M., Arning N., Bitard-Feildel T.,
RA Chao H., Childers C.P., Dinh H., Doddapaneni H., Dugan S., Gowin J.,
RA Greiner C., Han Y., Hu H., Hughes D.S.T., Huylmans A.-K., Kemena C.,
RA Kremer L.P.M., Lee S.L., Lopez-Ezquerra A., Mallet L., Monroy-Kuhn J.M.,
RA Moser A., Murali S.C., Muzny D.M., Otani S., Piulachs M.-D., Poelchau M.,
RA Qu J., Schaub F., Wada-Katsumata A., Worley K.C., Xie Q., Ylla G.,
RA Poulsen M., Gibbs R.A., Schal C., Richards S., Belles X., Korb J.,
RA Bornberg-Bauer E.;
RT "Hemimetabolous genomes reveal molecular basis of termite eusociality.";
RL Submitted (DEC-2017) 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:PNF26954.1}.
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DR EMBL; NEVH01015312; PNF26954.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J7QEE0; -.
DR Proteomes; UP000235965; Unassembled WGS sequence.
DR GO; GO:0019208; F:phosphatase regulator activity; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd21930; IPD_PPP1R12; 1.
DR Gene3D; 6.10.140.390; -; 1.
DR Gene3D; 6.10.250.1820; -; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR017401; MYPT1/MYPT2/Mbs85.
DR InterPro; IPR031775; PRKG1_interact.
DR PANTHER; PTHR24179:SF21; MYOSIN BINDING SUBUNIT, ISOFORM O; 1.
DR PANTHER; PTHR24179; PROTEIN PHOSPHATASE 1 REGULATORY SUBUNIT 12; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF15898; PRKG1_interact; 1.
DR PIRSF; PIRSF038141; PP1_12ABC_vert; 2.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 4.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000235965}.
FT REPEAT 76..108
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 109..141
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 202..234
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 235..267
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 823..919
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 308..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 574..626
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 825..913
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 316..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..597
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..626
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..705
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..732
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..784
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 786..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 919 AA; 102193 MW; 4750B8541488DF79 CRC64;
MSNETRSNSA LFKRAEQLKR WEESETNREA AVPNNKSRKV QFSAGCVFLA ACAAGDKEEV
LRLLEKGADI DTANVDGLTA LHQACIDDNL EMVEFLVENG ADVNRGDNEG WTPLHATASC
GFISIAKYLI EHGGNVAAVN NDAELPLDIA ESDEMEDMLQ QNINAQGIDC DEARNEEERM
MLEDAKEWLN NGGIEETPHP KTGATALHIA AAKGYIKVMS VLLQGGANLN SQDFDGWTPL
HAAAHWGQKE ACEMLVEEFC DMDMKNYVGQ TAYDVADSEM FKLLEELKKK QVTAQKDRGD
INSILQKKGA SIPKRRSSIT RMSVTDKSNL INKDTSSERQ LLDQSITEEG SNKVKKVELE
IETESEKEAS IPPPEIEVEK KNRANKDEPS KIPTVPEVSK TVPNATPNSP SKTPGETEDI
NLPTWKRPGS FRSRGVDGRL DQPPNKSLSL RIGEKDYVSH RATTPTGADS RNIADTPEVV
LRRTQSFEAD EKFYRRYMEL QARIKAGSCP TLHSSPVSAL PTRSASLREK HLPRRGTNDE
AKITSCPSQE VPTTTTAATT TVTTTTAAIV TTTVTSSPAK TTATSPTTTS PLPTSQIRRS
FVPPVRDEES ETQRKAHAKR VRETRRSTQG VTLEEIKVAE QLVKKKNQQQ LHQATQQLSN
HEQFMLEDAR NRNTVSENTS PYVRRLTGGT NTAVRPSSAP VENNIADATL TIPLRRQTKP
PDDKEQDKEN DIRNAQATQA VIQRRRRPKR RSTGVVHVDM DEINPDRQES PSRGDGDEIM
KANNDESGGD LSSHSSRLSS VASSRGDISA NVAKDGSENG EVDYKKLYEE SLVENERLRE
KLKKTEEDLN DRKSQLDKLS VATAKNSLTE MEKRERRAME RKLSEMEEEL KLLEQFKSEN
QRLKDENGAL IRVISKLSK
//
