ID A0A452IY93_9SAUR Unreviewed; 1016 AA.
AC A0A452IY93;
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:ENSGAGP00000033050.1};
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:ENSGAGP00000033050.1, 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:ENSGAGP00000033050.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR AlphaFoldDB; A0A452IY93; -.
DR Ensembl; ENSGAGT00000037470.1; ENSGAGP00000033050.1; ENSGAGG00000023577.1.
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; 1.
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:SF4; ANKYRIN REPEAT AND SAM DOMAIN-CONTAINING PROTEIN 1A; 1.
DR PANTHER; PTHR24174; ANKYRIN REPEAT AND STERILE ALPHA MOTIF DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF00640; PID; 1.
DR Pfam; PF00536; SAM_1; 2.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 3.
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; 2.
DR PROSITE; PS50088; ANK_REPEAT; 3.
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 5..37
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 38..70
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 70..102
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 575..638
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 646..705
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 818..949
FT /note="PID"
FT /evidence="ECO:0000259|PROSITE:PS01179"
FT REGION 129..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 951..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..746
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..788
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 111178 MW; 3EF08492CE6702B4 CRC64;
MRNNKFETPL DLAALYGRLE VVKMLLNAHP NLLSCNTKKH TPLHLAARNG HKAVVHVLLD
AGMDSNYQTE KGSALHEAAL FGKTDVVQIL LAAGIDVNIK DNRGLTALDI VRELPSQKSQ
QIAALIEDHT TEKKSRKAAE KAPPTPVIPA TEPAVRIPQG DVEKAVTELI IDLEMNPEEE
CPYEALYNAT SCHSLDSLAS GRSSDRDSVN KEAETTGLKA AAIRPRERPP PPAKPPPDEE
EEPVEKKLGR SASCEASVVQ RKSRGGAAEE EEEHPYELLL TAETKKPLAV DRKTKGESPS
SGAVSSNQLQ AKPRKGTSSQ DGQWPLNRQG SSDLSSSHSE QHPNPEACMT ETSTDHRRSS
GSRSQDSADS QDIQVPEQFS GLLHGSSPVC EINEDPFRLI SVAKGGTEVT GHSPAMQLEG
ADLPVSGSVR TSSPEQNLKV IYATVQPKNV QQAEPETAVT PQALQHPGGA EEEGDRGGAG
GRAHLGGKPK AELKLSRSLS KSDSDLLTCS PTEDDAMGSR SESLSNCSTG KKRLEKSPSF
ASEWDEIEKI MSSIGEGIDF SQEQQRISGS RMLEQSVGEW LESVGLQQYE SKLLLNGFDD
VRFLGCNVME DQDLREIGIS DPQHRRKLLQ AARPLPKVKS LGCDGNSQPS VPAWLDSLGL
QDYIQSFLSS GYSSIDTVKN LWELEIVNVL KVNLLGHRKR IIASLADRPY EEPPQKPPRF
SQLRCQDLMS QTSSPLSQTD SYTGRSADPL LPSGDSGKRQ CDSGRDAASH PRADRYKAQE
EHRESRLTLR PPSLAAPYAP VQNWQHQPEK LIFESCGYEA NYLGSMLIKD LRGTESTQDA
CAKMRKSTEH MKKIPTIILS ITYKGVKFID ASNKNVIAEH EIRNISCAAQ DPEDLCTFAY
ITKDLQTSHH YCHVFSTVDV NLTYEIILTL GQAFEVAYQL ALQAQKSKPT GASAAETIET
KSSKPVPKPR VGVRKSALEP SEVDQDSQSH ASVSWVVEPK QDSKRTLSTK YETTIF
//
