ID A0A158PMU5_ANISI Unreviewed; 1193 AA.
AC A0A158PMU5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=CG-1 domain-containing protein {ECO:0000259|PROSITE:PS51437};
GN ORFNames=ASIM_LOCUS9946 {ECO:0000313|EMBL:VDK42081.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001021501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001021501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK42081.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: May interact with calmodulin. {ECO:0000256|ARBA:ARBA00029480}.
CC -!- SIMILARITY: Belongs to the CAMTA family.
CC {ECO:0000256|ARBA:ARBA00008267}.
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DR EMBL; UYRR01030977; VDK42081.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158PMU5; -.
DR WBParaSite; ASIM_0001021501-mRNA-1; ASIM_0001021501-mRNA-1; ASIM_0001021501.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR GO; GO:0051171; P:regulation of nitrogen compound metabolic process; IEA:UniProt.
DR GO; GO:0080090; P:regulation of primary metabolic process; IEA:UniProt.
DR Gene3D; 1.20.5.190; -; 2.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR005559; CG-1_dom.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23335; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR CAMTA; 1.
DR PANTHER; PTHR23335:SF0; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR, ISOFORM F; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF03859; CG-1; 1.
DR Pfam; PF00612; IQ; 2.
DR Pfam; PF01833; TIG; 1.
DR SMART; SM00248; ANK; 2.
DR SMART; SM01076; CG-1; 1.
DR SMART; SM00015; IQ; 3.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS51437; CG_1; 1.
DR PROSITE; PS50096; IQ; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000267096};
KW Transcription {ECO:0000256|ARBA:ARBA00023163}.
FT DOMAIN 12..138
FT /note="CG-1"
FT /evidence="ECO:0000259|PROSITE:PS51437"
FT REPEAT 597..620
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 231..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..973
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1193 AA; 134237 MW; 706BE0D2273D288E CRC64;
MHTQQVINFL PSYDEFNANQ TKWNSNEDVA RILYSAQNHP DWIASETHTF PPSTSQRLFK
RLDGLHFKQD GYEWKRRKEG KLIREDHVKL KVQKLETIAG SYVHSAIVPS FHRRTYWLCD
HPEIVLVHYL NVTGEETRDG QPLHIRIAQS VRSNGLSFNR SQLEQQIRPI LCYSMHPAEI
SSLLANVCAI LNLAHSIPAT VTYQHDSEHQ LNNYVDEYGM EGIELMHLAT DQPTNNNTNT
HSERFQQHSQ NDQHEQPSAH HPHHQLERSN SCGSAFRRGL SSIAMRRQPS AFSDTVDGRF
TGTLLTNYAV ESDASLIANN DKLSATSASI PNAFLNFASC QPETTNTLSK SAVATSEQQS
SSSNLACELR RCGTIAAVQS NSATSQQHNT ASCSTPLIQI ADLSPDRSPL RGGTKVLIVG
GWYLRGHDYT VMFDDQQVPA TLFHAGVLRC FAPPHNAGVV KLEVYCDGLL ISHAVQFEYL
DMSRTGGQSA VLLEISERLR FFHSCMITDR SQCAMRELPE LDTETVALEI WSEMMRYPFD
YNLLTNRSAT MRNDNSLLHL CAMLNFHRLI QSVLQFRSEI SSQYYIRDLD VVSRDAEGRT
PLHLAVLHAN LNSIQILISN CPSSVDVLDD RGETPQDLIF KSQNSHIINS YKQTIDTVRH
QAKASDDRCG QSQESINSTA LWVMTNGETV TDEQRLANTS TITSSSRQTM LQIDMPVWQQ
LPVNHGSDGQ AASKSCSASL LARVQLIYWL GVENGGGDSS IKSLNEYSDI DDSHHDGSSL
SANKLHHCEN LERGGWMDDT LAMDVHIPDS PTTADMWNAL SSSDDATSEG ARARMASLAQ
QIIDALPARI KSFNEAADPN FVDDVGGLSE PSESSGLSIH SRNPFLGNAY VRSSSEWEEL
VTPLDNTTYE FTSPNFMDRA RNEVLIAHDE VGGPLDVLNA SSSSSTFHTL PSESINNPTE
SANDHSSPNT STKDLGEFFN TEGVMGPLER HFRDLRLSDR EQRELYEAAK IIQHAYRQYK
ARISSQKQNE AERNAAVVIQ SYYRRYKQFC YFKKLHKAAV LIQKHFRMHR ALHCAEEQHI
DEPLNDDCIR LTQCNASAHV SSLMTEDQAA LTIQQAYRGH YQRKRQAAAR KIQKFMRQSK
QKLVLYFNTF FNISSRHQCL SELHFTNYEE CDCSQQYTVC DISSYASASS LQS
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