ID A0A3B4E967_PYGNA Unreviewed; 1758 AA.
AC A0A3B4E967;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Calmodulin binding transcription activator 1 {ECO:0000313|Ensembl:ENSPNAP00000033112.1};
GN Name=CAMTA1 {ECO:0000313|Ensembl:ENSPNAP00000033112.1};
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:ENSPNAP00000033112.1, ECO:0000313|Proteomes:UP000261440};
RN [1] {ECO:0000313|Ensembl:ENSPNAP00000033112.1}
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 Ensembl; ENSPNAT00000023689.1; ENSPNAP00000033112.1; ENSPNAG00000021547.1.
DR GeneTree; ENSGT00940000155203; -.
DR OMA; GCANYSA; -.
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 InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23335:SF11; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR 1; 1.
DR PANTHER; PTHR23335; CALMODULIN-BINDING TRANSCRIPTION ACTIVATOR CAMTA; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF03859; CG-1; 1.
DR Pfam; PF01833; TIG; 1.
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; PS51437; CG_1; 1.
DR PROSITE; PS50096; IQ; 2.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043};
KW Transcription {ECO:0000256|ARBA:ARBA00023163}.
FT DOMAIN 14..139
FT /note="CG-1"
FT /evidence="ECO:0000259|PROSITE:PS51437"
FT REGION 235..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..630
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1257..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1370..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1257..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1758 AA; 189595 MW; 7FE7995DAF4D708F CRC64;
MVRLETAQER EWQNRSGFYA GPRVTFHLQE IAAYLITFEK HEEWLTTSPK TRPQNGSMIL
YNRKKVKYRK DGYCWKKRKD GKTTREDHMK LKVQGVECLY GCYVHSSIIP TFHRRCYWLL
QNPDIVLVHY LNVPAIEDCG KPCGPILCSI NTDKKEWAKW TKEELIGQLK PMFHGIKWTC
SNGNSSSGFS VEQLVQQILD SHQTKPPPRT HNCLCTGTLG AGSSVHHKCN SAKHRIISPK
VDPRSGGYGS GHSELQNSDV SEGKTEHSHG SSKAGTGAAG GGGTAREKRN GKVHKPVLLH
QNSTEVSSTN QVEVPDTTQN SPVSISSGLN SDPDMADSPV VTGMGHVASV MSGLSQSVFM
SEVTGDPVYS MSPTGGPNAH IMGPDATSHG LVLAVTSESH KFAFPGSGGT DTGGPGTTDG
LSMLSAAGVS EELVLSSSLD SGSIKLPETT MNFDPDCFLN NPKQGQTYGG NGLKQENGSS
AVASTNGLQH SPPMSDSNFG FSATLIKNIK TEDTSFEQQL AKESGYQVGA VVSCSVSSGS
GTQNSLTLTP ANSLLPSGGG LSPSTTLEQM DFSAIDSKPD FSSNTSVGYE QAMNNAHLAH
QSHSPSFFLQ EAPQSAQNQQ GRPNSGQKSH LLEHNSHDRA FMGMQVVKTD SPGSNGHLHH
HHGHQNQHRP NCNGSSPVEQ SSGQNGSLQL LQYPGGFPSL GPEHEDVVSH DQSGNAGPVQ
AGGAETRADG LLKAGDHLQV CARSNAEGGS EHYLQPNSEN GTAGDESVAL SNGNSGESTN
SSGQQQLQPL LQGAGLVQGL YNTVGSHQAS SGGGSGMEIS LDHFDISFGN QFSDLINDFI
SVDGGATAVG PGGTLYTHQL VAPPGSDGQQ APGSSQQQGQ EDGANRAAGY SSSELCLQPC
CSPQSLGGAA AGTGGSGEAG SLSYMHVAEV VSAAVAQGTL GMLQATGRLF MVTDYSPEWS
YPEGGVKVLI TGPWQEASSH YSCLFDQISV PASLIQPGVL RCYCPAHDTG LVTLQVAVSN
QIISNSVVFE YKARALPSLP SSQHDWLSLD DNQFRMSILE RLEQMERRMA EMAGQQQQSN
GAAGGTGAGP GGGGAGAGGG GNGGNGSNSQ SQCVSAQGQA GSSFESRVVV VCEKMMNRAC
WAKSKHLIHS KTFRGMTLLH LAAGQGYATL IKTLIKWRTK HADSIDLELE VDPLNVDHFS
CTPLMWACAL GHLEAAVVLY KWDRRALAIP DSLGRLPLSI ARSRGHTKLA ECLEQLQREE
QQQPPSSRMA FSPNSDAPSS DSWMVTWASD SVVNPSGQKS GGVTTTSTNP SNLTPDLRRP
RSEPSSYYIS ECQRDLPAAK KHKPNPEVAQ TRPDKAVSVP LSLEHQQLSR LSASTGTHPA
DPTSPERSVA AEGTETSGVS QAKLGSFRAG GHKWGSREVY RKVPGGIGGS SIGKEKLASR
LRQRAEPLSM LTMADREMVD TELLSYKEDL ENQDCLSHME DLQANMMSLA EHIIEATPEH
IKRENFAEVE SVPLDSSGLS STMSWLATYL GDVEQLPSII HLRSLYSEPL TPKPSMSPGG
SPLHDGPFEK ATLPSPADWS EFLSASNSKV ERELSQLTLS DPEQRELYEA ARLVQTAFRK
YKGRPLREQQ EVAAAVIQRC YRKYKQYALY KKMTQAAILI QSKFRSYHEQ KKFQQSRRAA
VLIQQYYRSY REFRRLRPHR RSPASALVQH KLRSSLLTKR QDQAARKIMR FLRRCRHRVS
ELRKAKEHES IQKSPLTM
//
