ID A0A452GKH3_9SAUR Unreviewed; 2007 AA.
AC A0A452GKH3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=WW domain-containing protein {ECO:0000259|PROSITE:PS50020};
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:ENSGAGP00000002133.1, 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:ENSGAGP00000002133.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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DR Ensembl; ENSGAGT00000002430.1; ENSGAGP00000002133.1; ENSGAGG00000001670.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
DR GO; GO:0043227; C:membrane-bounded organelle; IEA:UniProt.
DR CDD; cd00201; WW; 1.
DR Gene3D; 3.30.1470.10; Photosystem I PsaD, reaction center subunit II; 1.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR18902:SF27; CENTROSOMAL PROTEIN OF 164 KDA; 1.
DR PANTHER; PTHR18902; NUCLEAR MITOTIC APPARATUS PROTEIN 1-RELATED; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000291020}.
FT DOMAIN 58..91
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 105..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 630..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 845..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1041..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1093..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1683..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1139..1627
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 175..194
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 578..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 633..660
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1071
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1684..1701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2007 AA; 225712 MW; A111157F2A3F8380 CRC64;
MDMAGPAIRI GDQLILEEDY DETYIPSEQE IQEFAREIGI DPGNEPELMW LAREGIVAPL
PPEWKPCQDI TGDIYYFNFS NGQSTWDHPC DEHYRELVIQ EREKLSAHGS IKKKDKKKKK
DKKEKKEKKE REPVKHAAEM QPEPGILPSS SFYRMSSPIL SSECASPDLD QHSQMRIEGF
LKKGKRKPSE RPPETSDSNK QFAGPSPNKL QPLFTAKSCR THQILADVEK ILGRMPSFSR
SDVDHQQGQD RSPKIGDKPC LGFSDSESEG LDVVRTKPIS YVARKSCSQD LENGRSVLDS
CEVLEDKGML FDEEKLSDNW KQEEMTGGSV CQPDDGLSVR ERSTGPGGDK ERGPGFSQAD
ENEAFLTPSA PDHTFYSRKC EMILFDASPL EDLSLMEEGD VHCPQRELRA HSRAVESRRK
RKLQDQALSQ ATKFCKSSEV VGKHERESSK QAEFVESEGA GLQAAPQKDL LDSHLAVPEV
TADTLPYTRG VEAYAHAGAD ISASEPVSLS AAQHKDKEKA NGLGPEPDNS LTSNSADHFA
SQILGEIDNF SWDLQSSRES DRPTDLLAAA AKGSLPTHPF TGTLQTPPRS SANGKSQSDC
NSEDEKFYQH VQENDQVPSQ EHSCVSFNMK LNRSRDAPEK NNEGRQEETG EGEQKTEPVP
RGLEVDVFTE GLQVSPGWLY QTAECQESSR LCQQVEGELT QSGKVTEDYC KLKLCEGAGS
NESPGSLLAP IQVPPGSLAP LRGVMDGPAS AFHGLLSTNV EISGVPSPLL REGTLPLQTL
KSTGCTKSLL GSMHEEKASL NLLALDEEEE EESENQSPRG TARLLKNLHM DISALGGGFE
YEESLKMSHA EESQTFPLDS DGVRPPAPDK LLNRDADSSL CGLNKEESSG KPLGNELLEK
EDTDVEDTVS VAYEQSGTLG ERTAEGTHVV SSQGHPVAAS PDVRAAETDQ MESVAVTVDA
VSVSEKIVNG MREEAADLET DSKLDAGKES EASEHVKELQ VSDCSDHELL HLTDFGFQSR
ISEQVLDMDI LSAALDSPKV EAQGLREEEK DQSEASLEEE QSKRPKAAES ERNQRPFSAC
KMAEEKCLSL ENASQEETAA LEQKEGSLDS PKEEEPAAPH QAQLGEEIKQ VVSLNWPSAE
SLNEIARKQE QELEQEKERL LQAKEERVRR FQEELRQEEE EEAQVLHQQK EKSLWSLKEE
LAKASEEEEL RMREEEVEKL SKLRSQISSE TKTEKEKIRA EQEAALQKLR EEWESLQKVE
RERLEERKKR VLEMLKVEVE EAQQREAAEL EQEKQRVLNE LKERLERKRK EAAEVLEKQF
AAELQELKST AEEKHQKVVS SLRKQIAEAQ RSEEAQLREE LERAEQKVQQ KMYQVAEFER
ELSELMKEKR QEVERDHDRK MERMKEEHKE VLARIQEQYE EEERKQRTKK LEELKGELER
LRQLHDGELK ALQKQLDEQL SDLRQSHKVK ERKLQELEME LEIQATDAKA RCAQLNHQEE
AMRKKRQQLL DEEKQTELQR NEAALAAQLR LEESRKEHAD LVESIRQLRR TLEELQDQKA
ELESQVDLLQ TRSQRLQRRI SELEAAVQSK QETLKELVAE DSMASPRREA ELHLEDLRET
LQAHSSREPA SLTSHSNEDS DLQLDNVRHF ISAEGVSIKN AKEFLVRQTR SMRKRHTALK
AAKQQWRHNM QQAQDAVQDP DSSQLLEDVR RNLEEESAQL DKMKSAMQKG QVLLKKKEEK
LSQLESSLLE ELSDEDTLKG AACKKVVTFD LSDSEETHSL SSTDVPQHKF DLKPDVQFPQ
LDKIQHLTST LQHITAELNG VLSTLGSLNQ RQPPLFAPVQ VPMTALPSDG VPLSMYTSLA
RAQAAGPIMP PAGIPLVNQW AWSTGLNSSP SSTAGQSVDD ILAEKWHKYF PGGFPSLSGS
PAPLDSNLGY LPAGEQIGLF QRSQLQGPET DSTSVQGMID ANKKWLENFK KDSKVPLFPR
TQKPFASSPG LVQLGLDENN QIKVYHC
//
