ID A0A452I5F4_9SAUR Unreviewed; 1613 AA.
AC A0A452I5F4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=CG-1 domain-containing protein {ECO:0000259|PROSITE:PS51437};
OS Gopherus agassizii (Agassiz's desert tortoise).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Testudinoidea; Testudinidae; Gopherus.
OX NCBI_TaxID=38772 {ECO:0000313|Ensembl:ENSGAGP00000022792.1, ECO:0000313|Proteomes:UP000291020};
RN [1] {ECO:0000313|Proteomes:UP000291020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=28562605;
RA Tollis M., DeNardo D.F., Cornelius J.A., Dolby G.A., Edwards T.,
RA Henen B.T., Karl A.E., Murphy R.W., Kusumi K.;
RT "The Agassiz's desert tortoise genome provides a resource for the
RT conservation of a threatened species.";
RL PLoS ONE 12:e0177708-e0177708(2017).
RN [2] {ECO:0000313|Ensembl:ENSGAGP00000022792.1}
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; ENSGAGT00000025967.1; ENSGAGP00000022792.1; ENSGAGG00000016711.1.
DR Proteomes; UP000291020; 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; -; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transcription {ECO:0000256|ARBA:ARBA00023163}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..1613
FT /note="CG-1 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019212552"
FT DOMAIN 1..123
FT /note="CG-1"
FT /evidence="ECO:0000259|PROSITE:PS51437"
FT REPEAT 997..1019
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 218..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1139..1179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1199..1226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1613 AA; 178492 MW; 5721B1B257185145 CRC64;
MQVNSFLHIF LFQEIAAYLI TFEKHEEWLT TSPKTRPQNG SMILYNRKKV KYRKDGYCWK
KRKDGKTTRE DHMKLKVQGV ECLYGCYVHS SIIPTFHRRC YWLLQNPDIV LVHYLNVPAI
EDCGKPCGPI LCSINTDKKE WAKWTKEELI GQLKPMFHGI KWTCSNGNSS SGFSVEQLVQ
QILDSHQTKP QPRTHNCLCT GNLGAGSSVH HKCNSAKHRI ISPKVEPRTG GYSTHSEVQN
NDVSEGKNEH SHGKTSSREK RNGKVAKPVL LHQNSTEVSS TNQVEVPDTT QNSPVSISSG
LNSDPDMADS PVVTGVSSMA VASVMGSLSQ SATVFMSEVT SEAVYTMSPT TGPNQHLLSS
DAAAQGLVLA VSSDGHKFAF PTPGSSESLS MLTTNVSDEL VLSTTLDGSR KIPETTMNFD
PDCFLNNPKQ GQTYGGGGLK GDSISTNIRQ SPTTERGFNF SAALTKEIKT EDTSFEQQMS
KEAFSSTSAS NSLSLTTGSG LLPSGGGLSP STTLEQMDFS AIDSNKDYSS SFNQTVQSPH
VHQTPSPSFF LQDASKPLPL EQNTHNNLND TSGSFVNTLG IPNVKTESSQ TTSNCNGTVE
TRIESTSSLQ LMQFQANFQA MTAEAEVPME TSQQAEGNEN LLKSGDLQAC NSEHYMQPEA
NGGIRNGNNL PILQGNMVQG LYPVAHPSLN NSSNMELNLD HFDISFSNQF SDLINDFISV
EGGSNAIYGH QLVSSDSAGL SQPEDGNRAT YNQAEMCIPC CSPQQASMQL SSAENGTSTM
AYMHVAEVVS AAAAQGTLGM LQQSGRLFMV TDYSPEWSYP EGGVKVLITG PWQEASNNYS
CLFDQISVPA SLIQPGVLRC YCPAHDTGLV TLQVAFNNQI ISNSVVFEYK ARALPTLPSS
QHDWLSLDDN QFRMSILERL EQMERRMAEM TGSQQHKQGV GGGGNGSGNG GTQTQCVSGA
GTLGSCFESR VVVVCEKMMS RACWTKSKHL IHSKTFRGMT LLHLAAAQGY ATLIQTLIKW
RTKHADSIDL ELEVDPLNVD HFSCTPLMWA CALGHMDAAI VLYKWDRRAI SIPDSLGRLP
LAIARSRGHV KLAECLEQLQ RDEQVQLGQN PRIHCPSSGE SSTESWVAQW QSEIITSQEP
QKGVTVMSSS NTELRRPRSE PSNYYSSESQ KDYPAPKKHK LNPEYFQARQ EKLLSTALSL
EQPSVRKQSS SSKQSISETI SPSEGIRDYG RELSQHIPEV AGYRGSGGQA GVKWNPKDVY
IGVSAVQVTG SQKGLALGKD IVAHRLRQRE QMNVLMMADR EIVDGELLSF RDSVENEDCL
QHMDDLQVNM MTLAEHIIEA TPDRIKRENF VPMESPLVER TDSAAISTTM SWLASYLADV
DHIPSAAQIR SLYGEPLTPS SNTSLSPVGS PVSEIPFEKP SLPSAADWSE FLSASTSERV
ENEFAQLTLS DHEQRELYEA AKLVQTVFRK YKGRPLREQQ EVAAAVIQRC YRKYKQLTWI
ALKYALYKKM TQAAILIQSK FRSYYEQKKF QQSRRAAVLI QQYYRSYKEC GKRRRQSRAA
AIVQQKLRSS LLTKKQDQAA RKIMRFLRRC RHSPLVDHRL YKRSERIEKG QGT
//
