ID A0A2A2L6H1_9BILA Unreviewed; 1250 AA.
AC A0A2A2L6H1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=cGMP-dependent protein kinase interacting domain-containing protein {ECO:0000259|Pfam:PF15898};
GN ORFNames=WR25_19070 {ECO:0000313|EMBL:PAV81753.1};
OS Diploscapter pachys.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Diploscapter.
OX NCBI_TaxID=2018661 {ECO:0000313|EMBL:PAV81753.1, ECO:0000313|Proteomes:UP000218231};
RN [1] {ECO:0000313|EMBL:PAV81753.1, ECO:0000313|Proteomes:UP000218231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF1309 {ECO:0000313|EMBL:PAV81753.1};
RA Fradin H., Zegar C., Gutwein M., Lucas J., Kovtun M., Corcoran D.,
RA Baugh L.R., Kiontke K., Gunsalus K., Fitch D.H., Piano F.;
RT "Genome architecture and evolution of a unichromosomal asexual nematode.";
RL Curr. Biol. 0:0-0(2017).
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:PAV81753.1}.
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DR EMBL; LIAE01007129; PAV81753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2L6H1; -.
DR Proteomes; UP000218231; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0019901; F:protein kinase binding; IEA:InterPro.
DR CDD; cd21930; IPD_PPP1R12; 1.
DR Gene3D; 6.10.140.390; -; 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; IPR011010; DNA_brk_join_enz.
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 SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56349; DNA breaking-rejoining enzymes; 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:UP000218231}.
FT REPEAT 50..82
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 83..115
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 176..208
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 209..241
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 921..1010
FT /note="cGMP-dependent protein kinase interacting"
FT /evidence="ECO:0000259|Pfam:PF15898"
FT REGION 312..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..532
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 566..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..912
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 969..1025
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 327..343
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..426
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..696
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..847
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..912
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1250 AA; 136022 MW; 5E3410610F6BAFC8 CRC64;
MNNESCRPKK QARVQFQDSD VFLSACMSGD EEEVEQLLSN GADINTCTVD GLTALHQSVI
DSKPEMVRFL CEHGADVNAQ DNEGWTPLHA ASCCGNVGIV KYLCEHGADL AIINSDKELA
IDLADDEKCK EFLEQDYKKK GINLDDCRDE ELTIMMRDAE KWLKQGRYED RIHDKTGAHA
MHVAAAKGYT QLLELLIKAG GDVAAKDNDG WTPLMAAAHW AEKDSCKILI EHGASIHTVN
HLGQNVIAVA DKDIAEYLEE LEATAEKKRN SPAVGPSASI LHDKNIRVAH EEHTINQTLE
HKRDLQHKDA ASENEILHKL PRLETTGRIG STETSSSVKS NGSPPDALIR EEKNSPDASR
SSEEREMSVA SGSSGSGSGS YISGSGSQTG SSLYSSSQRS SSYTSESQTE PSNHSSSIHS
SDQNVSATVT VPRLHQQAPN SWINRGVQLV TRSSSSSSTS RSGQRSEGSP LIQSSPSNTS
LSATYTINTG SKNLPVQSGA VSYGGNVNGS STKSVVHEQS SRNLLPSSST LSMVTPTSSS
ALPWASLYRS GSSPNTNTAG IQRMLSGSST SSFTPSIQST QSQPQTPLQI SRISAFRPLV
KSQVTSSVPS EFPKSFQPQH LQPHQMRPWV SSGINESEAE RRNNSRLQRQ HRRSTQGVTK
EQLEEASRIM NQERQNMGSS ETSASRTLTS SVGTSHRAAG MPIRLASQER DSADEIDGRA
GGSHRNQNGN GTSSGNVDTT MTLTLTNTPA PNHTSSTANM KRRSQAMISG PLARSNRRGT
GPVLPEDVQA AVSASSSTSR PTSGAYSTVQ STGKTPVFTV PSLPISGGST KYSGNGSDNG
NGSPKSQSVP PPSSPQTITP TAAGLRGAVL STAVNSPRNA ATTTRPSSGI GSTSYGTSSN
NNAIPDSMNS QHLRLNETNL NYKALWEKER LEKDRMRREL DDFRRDRLRN GASSASSSTT
KTVSNLSNLS LDENERRALE RRIAELEIQL KKQDEVTTEN ERLKVENEAL SLGQVRQENQ
RLKEENAALI SYLNLTISFN FKGKLNCPVN KTCKLPGPVF KALETLSMQA GPEKPLFGYT
KTTLRHAAKN LENIVYELAG DENRDLPFSW KYLRKLYAAQ MFVNNYLILK SADPGKLLTP
EDVLSILNDV SKELSHTMKI PKQEVCSPTL TLRNYIDGLA VVELCAKEKI STQEVWFKDK
ILKIKKKTYK FQVLDVLEKK LTFSHLGKGL EKAINAGYAE YTKNAHIYFG
//
