GenomeNet

Database: UniProt
Entry: A0A3B4C4G4_PYGNA
LinkDB: A0A3B4C4G4_PYGNA
Original site: A0A3B4C4G4_PYGNA 
ID   A0A3B4C4G4_PYGNA        Unreviewed;      1647 AA.
AC   A0A3B4C4G4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Calmodulin-binding transcription activator 1-like {ECO:0000313|Ensembl:ENSPNAP00000005935.1};
GN   Name=CAMTA1 {ECO:0000313|Ensembl:ENSPNAP00000005935.1};
OS   Pygocentrus nattereri (Red-bellied piranha).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Characiformes;
OC   Characoidei; Pygocentrus.
OX   NCBI_TaxID=42514 {ECO:0000313|Ensembl:ENSPNAP00000005935.1, ECO:0000313|Proteomes:UP000261440};
RN   [1] {ECO:0000313|Ensembl:ENSPNAP00000005935.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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   STRING; 42514.ENSPNAP00000005935; -.
DR   Ensembl; ENSPNAT00000004441.1; ENSPNAP00000005935.1; ENSPNAG00000012102.1.
DR   GeneTree; ENSGT00940000155203; -.
DR   OMA; YNSADLC; -.
DR   Proteomes; UP000261440; Unplaced.
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; -; 1.
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   PANTHER; PTHR23335:SF11; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR 1; 1.
DR   PANTHER; PTHR23335; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR CAMTA; 1.
DR   Pfam; PF03859; CG-1; 1.
DR   Pfam; PF00612; IQ; 1.
DR   Pfam; PF01833; TIG; 1.
DR   SMART; SM01076; CG-1; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF81296; E set domains; 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}.
FT   DOMAIN          1..82
FT                   /note="CG-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51437"
FT   REPEAT          1064..1096
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REGION          129..238
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..471
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          501..539
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..588
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          605..698
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          786..806
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          984..1031
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1167..1197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1221..1318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1433..1452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..169
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        199..231
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        504..539
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        570..588
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        653..698
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        786..801
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        986..1002
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1167..1191
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1221..1243
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1269..1301
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1647 AA;  175414 MW;  4D2C9BF68BBB92A0 CRC64;
     MILYNRKKVK YRKDGYCWKK RKDGKTTRED HMKLKVQGVE CLYGCYVHSS IIPTFHRRCY
     WLLQNPDIVL VHYLNVPAIE DCGKPCGPIL CSINTDKKEW AKWTKEELIS QLKPMAGSSL
     HHKCNSAKHR IISPKVDPRS GGAYSSTHSE VQNSDVSEGK TEHTHGGSKN GRAGADGPGG
     SAAREKRNGK VPKPALLHQN SMEVSSTNQV EVPDTTQSSP VSISSGLNSD PDMADSPVVT
     GMSHVASVMS SLSQSATVFM SEVTGDPVYS MSPTGDPNAH LLGPDTASSS LVLAVAADSH
     KFAFPGAVGV GLGDAGSTDG LAMLSAASVS EELVLSSNLD SGSIKLPETT VNFDPDCFLN
     NPKQGQTYGG NGLKTEVSNG SSCSNGGVRC SPPLSDNGFG FNASLVKNIK TEDTSFEQQL
     AKESGYQVGE VVSGAGGLSS SSGSGTSQNS LALTPTGSLL PSGGGLSPST TLEQMDFSAI
     DAKQDYTSTV MSATGYGQAI PSPHLAHQSH SPSFFLQGSP QSTQTQNHQS NGNSAQNSHD
     TAAYMGLSVV KTDSSGTNGH IHHHHAHQGQ HAASSCNGNS PTERNGQGGT LQLLQYQNHF
     PGAAQEHEDV GGLEQSATSE AGDAGGPEKE TEGLLKAGDH LQPCVGNGAD GSGSTEHYLQ
     QSESSNLGPG PGSTGTRANN GALCNGTEGS GAAGSPHQQL QPLLQGAGLV QGLFNTVAAH
     QGLTTSGASG SGSMEINLDH FDVSFGNQFS DLINDFISVE GGSGAAVGAQ GGNALYSHQL
     LAHSGAEGQV SSGTTPQQGA EEGTARGAAG YNSTDLCLQP CCSPQSAQSG AVAGEAGQLA
     YMQVEEVVSA AVAHGTMGML QATGRLFVVT DYSPEWSYPE GGVKVLITGP WQEASSDYSC
     LFDQITVPAS LIQPGVLRCY CPHDTGLVTL QVAASSQIIS NSVVFEYKAR ALPALPTSQH
     DWLSLDNQFR MSILERLEQM ERRMAEMAGQ QQQSSGGSSE SGVAGGGSGG EGRGSADQAQ
     FSPGQGQGQA GSSFESRVVV VCEKMMNRAC WAKSKHLIHS KTFRGMTLLH LAAAQGYATL
     IQTLIKWTKH ADSIDLELEV DPLNVDHFSC TPLMWACALG HMEAAVVLYK WDRRALAIPD
     SLGRLPLATA RSRGHTKLAE CLENLQREEQ QQQQQPGTLT TTPSMPFSPS AEGSATEGWM
     DVWGNESASV GLRGSSISSS ATTLNTLRRP RSEPSSFYNS EGQGDAPLTK KHKPNPESHQ
     ARPGKPSSAP LRLEEHAHKT KACPPKAPRE GTVEKEAGKG EQSQTKLGSA CGGGGRWSAR
     QAVGRRGQFG GLAKERLASR LRLREASGTG TVSELLASQE DLENTGDLQQ MNMMTLAEHI
     IEATPDRIKS ETFVATEPTP LDNVTVNSTM SWLATYLGDA EFLYNKPLAS SAGLGGGHSG
     AKPEPESPLG KLGLPSPADW SAFLNASHSK EERDLTQLAL SDHEQRELYE AARQVQSTFR
     KYKGRPLREQ QELAAAVIQR CYKKYKQLTW IALKYALYKK MTLAAILIQS KFRSYHEQKK
     FQQSRRAAML IQQYYRSYKE LGRPNAHSHS HAAAAAVLVQ HKLSGLLTKR QDQAARKIMR
     FLLRCRHPLM DHRLFKRGER IEKGQGT
//
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