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Database: UniProt
Entry: A0A452I5D2_9SAUR
LinkDB: A0A452I5D2_9SAUR
Original site: A0A452I5D2_9SAUR 
ID   A0A452I5D2_9SAUR        Unreviewed;      1251 AA.
AC   A0A452I5D2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000022730.1};
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:ENSGAGP00000022730.1, 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:ENSGAGP00000022730.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A452I5D2; -.
DR   Ensembl; ENSGAGT00000025891.1; ENSGAGP00000022730.1; ENSGAGG00000016661.1.
DR   Proteomes; UP000291020; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   CDD; cd01274; PTB_Anks; 1.
DR   CDD; cd09499; SAM_AIDA1AB-like_repeat1; 1.
DR   CDD; cd09500; SAM_AIDA1AB-like_repeat2; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 2.
DR   InterPro; IPR033635; ANKS1/Caskin.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR041880; SAM_ANKS1_repeat1.
DR   InterPro; IPR041882; SAM_ANKS1_repeat2.
DR   PANTHER; PTHR24174; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR24174:SF3; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1B; 1.
DR   Pfam; PF12796; Ank_2; 3.
DR   Pfam; PF00640; PID; 1.
DR   Pfam; PF00536; SAM_1; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM00454; SAM; 2.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 2.
DR   PROSITE; PS50297; ANK_REP_REGION; 5.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
DR   PROSITE; PS01179; PID; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 2.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   REPEAT          58..90
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          91..123
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          127..159
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          193..225
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          225..257
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          808..871
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          879..938
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          1054..1183
FT                   /note="PID"
FT                   /evidence="ECO:0000259|PROSITE:PS01179"
FT   REGION          382..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          491..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          582..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..772
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          939..991
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1188..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        582..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        632..657
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        732..771
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        955..982
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1251 AA;  138446 MW;  006B9C44E51ADAF6 CRC64;
     MGKDQELLEA ARTGNVALVE KLLSGRKGGI LGSGSGAIPL SSLLSIWRGP NINCADSSGY
     TALHHAALNG HKDIVLKLLQ YEASTNVADN KGYFPIHLAA WKGDVDIVKI LIHHGPSHSR
     VNEQNNENET ALHCAAQYGH SEVVAVLLEE LTDPTIRNNK LETPLDLAAL YGRLQVVKMI
     INAYPNLMSC NTRKHTPLHL AARNGHKAVV QVLLEAGMDV SCQTEKGSAL HEASLFGKVD
     IVRILLETGI DANIKDSLGR TVLDILKEHP SQQSLQIATL LQDYIKTGNA TILDEPTQEC
     LVTEHQSCIL SPEVSPSQTT KSEAVTGELS KLLDEIKLCQ EKEYSFEDLC HTISDHYLDN
     FSKISEEEFM SNGIQTKLIR PSSTNLSTGE EEEEDARENS CGPAGLWEAL TPCKGCRNLG
     FPILAQESYQ KKRSYTLEVV PSASLDAHSS ENENNLCDFM DIAVTKKPCS LEIARVPSSR
     TDNVPQVAIT APGTGNHRNS STGPTPDCSP PSPDTALKNI VKVIRPQPKQ RTSIVSSLEF
     HRLNHSHDYF EINSSIGYAS FTSSPSISPA NFSIGSIEEN ELSENLSQQE TSTENKLPKG
     HPAEQFAGLL HGSSPACDPP ENPLQLYGKA NHCSDPQESS LNKNTVQQRQ LQQENNPDAP
     AKKKKPQVVN RTIFHTKINP LENHTLVGTK TRIGEQWIIT TGGFVERACT LGRIRSLPKT
     LLEMHLSKNV SKSDSNLISY PPNGKKSGSN WSEPTQSQQN SKGNSERTPS FTSEWEEIDK
     IMSSIDAGIN TGLEEMNDDT AGLRCPVQTV GQWLENIGLP QYENHLLANG FDNVQFMGSN
     VMEDQDLLEI GILNSGHRQR ILQAIQLLPK MKQIGNDGYN PTSVAEWLES IELGDYTKSF
     LINGYTSMEL VKKIWESELV NVLKINLVGH RKRVLASLGD RLHEDPPQKP PRSITLREPS
     GNHTPPQLSP SLSQSTYTTG GSLDVPHIIM QGDARRRRNE NYFEDIPRSK LERQMAQTGD
     WGEPSITLRP PNEATASTPV QYWQHHPEKL IFQSCDYKAF YLGSMLVKEL RGTESTQDAC
     AKMRKSTEQM KKVPTIVLSV SYKGVKFIDA TNKNIIAEHE IRNISCAAQD PEDLSTFAYI
     TKDLKTNHHY CHVFTAFDVN LAYEIILTLG QAFEVAYQLA LQARKGGHSS TLPESFENKP
     TKPIPKPRVS IRKSVQIDPS EQKTLANLPW IVEPGQEAKR GINTKYETTI F
//
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