ID A0A452GW18_9SAUR Unreviewed; 1974 AA.
AC A0A452GW18;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Uncharacterized protein {ECO:0000313|Ensembl:ENSGAGP00000006248.1};
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:ENSGAGP00000006248.1, 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:ENSGAGP00000006248.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: May modify the assembly dynamics of microtubules, such that
CC microtubules are slightly longer, but more dynamic.
CC {ECO:0000256|ARBA:ARBA00003210}.
CC -!- SIMILARITY: Belongs to the WD repeat EMAP family.
CC {ECO:0000256|ARBA:ARBA00006489}.
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DR STRING; 38772.ENSGAGP00000006248; -.
DR Ensembl; ENSGAGT00000007261.1; ENSGAGP00000006248.1; ENSGAGG00000005024.1.
DR Proteomes; UP000291020; Unassembled WGS sequence.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 6.
DR InterPro; IPR024977; Apc4-like_WD40_dom.
DR InterPro; IPR005108; HELP.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR13720:SF16; ECHINODERM MICROTUBULE-ASSOCIATED PROTEIN-LIKE 5; 1.
DR PANTHER; PTHR13720; WD-40 REPEAT PROTEIN; 1.
DR Pfam; PF12894; ANAPC4_WD40; 2.
DR Pfam; PF03451; HELP; 3.
DR Pfam; PF00400; WD40; 11.
DR SMART; SM00320; WD40; 28.
DR SUPFAM; SSF50998; Quinoprotein alcohol dehydrogenase-like; 2.
DR SUPFAM; SSF50978; WD40 repeat-like; 4.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 6.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000291020};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 4..48
FT /note="HELP"
FT /evidence="ECO:0000259|Pfam:PF03451"
FT REPEAT 250..265
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 330..354
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 381..461
FT /note="Anaphase-promoting complex subunit 4-like WD40"
FT /evidence="ECO:0000259|Pfam:PF12894"
FT REPEAT 404..435
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 663..715
FT /note="HELP"
FT /evidence="ECO:0000259|Pfam:PF03451"
FT REPEAT 899..929
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1234..1266
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1344..1407
FT /note="HELP"
FT /evidence="ECO:0000259|Pfam:PF03451"
FT REPEAT 1702..1736
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1746..1826
FT /note="Anaphase-promoting complex subunit 4-like WD40"
FT /evidence="ECO:0000259|Pfam:PF12894"
FT REGION 610..633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1275..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..632
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1974 AA; 219952 MW; 0D7EC2A4A78E9AC9 CRC64;
MADQNAPNSH LRLEWVYGYR GHQCRNNLYY TAAKEIVYFV AGVGVVYSPR EHRQKFYLGH
QDDIISLALH PEQVLVATGQ VGKEPYICVW DSYTVQTISI LKDVHTHGIA CLAFDLDGQR
LVSVGLDSKN TICVWDWRRG KMLSMAPGHT DRIFDISWDL YQPNKLVSCG VKHIKFWSLC
GNSLTPKRGV FGKTGDLQTI LCLACARDEV THSGALNGDI YVWKGINLIR TIQGAHAAGI
FSMNACEEGF ATGGRDGCVR LWDLNFKPIT VIDLRETDQG YKGLSVRSVC WRGDHILVGT
QDSEIFEIVV HERNKPFLIM QGHCEGELWA LAVHPTKPLA MTGSDDRSVR IWSLIDHALI
ARCNMEEPIR CAAVSTDGIH LALGMKDGSF TVLRVRDMTE VVHIKDRKEA IHELKYSPDG
TFLAAGSNDS SVDIYGVIQR YKKVGECVGS LSFITHMDWS SDSKYLQTND GSGKRLFYKM
PSGKEVTNKE ELKGIQWASW TCVYGLEVNG IWPKYSDIND INSVDGNFNG QVLVTADDYG
IVKLFRYPCL RKGAKFKKYL GHSAHVTNVR WSHDHQWVVS IGGADHSVFQ WKFIPERKLK
DAIHIAPQES LVDSNSDESD SDQSDVPELD SEIEQETQIT YRRQVYKEDL PQLKEQCKEK
RKSAASKRRE RAPGNSIRLH FVHGYRGYDC RSNLFYTQTG EIVYHVAAVG VVYNRQQNTQ
RFYLGHDDDI LCLAIHPLKD YVATGQVGRD SSIHIWDTET IKPLSVLKGY HQYGVCAVDF
SADGKRLASV GIDDNHTVVL WDWKKGEKLS AVRGSKDKIF VVKINPYMPD KLITAGIKHM
KFWRRAGGGL IGRKGCIGAM GRTDTMMCAV YGWTEEMAFS GTSTGDVCIW RDLFLIKTIK
AHDGPVFSMH ALEKGFVTGG KDGVVALWDD TFERCLKTYA IKRAALAPGS KGLLLEDNPS
IRAISLGHGH ILVGTKNGEI LEVDKSGPIT LLVQGHMEGE VWGLATHPHL PICATVSDDK
TLRIWDLSPS HCMLAVRKLK KGGRCCCFSP DGKALAVGLN DGSFLMVNAD TLEDLVSFHH
RKDVISEIRF SPGSGKYLAV ASCDSFVDIY NVMSSKRVGI CKGASSYITH MDWDIRGKLL
QVNTGAKEQL FFEAPRGKRQ TIPSLEVEKI GWASWTSVLG SCCEGIWPII GEVTDVTASC
LTSDSKVLAT GDDFGFVKLF RFPAKGKFGK FKRYVAHSTH VTNVRWTHED SLLVTVGGAD
TSLMLWTYEM EGHRESRQCD SEESDLDSEE DGGYDSDVTR ENEINYTIKA LSTNIRPMFG
IKPHLQQKEP SLDERHGVVR PPVSRALPQP EKLQTNNVGK KKRPIEDLVL ELVFGYRGKD
CRNNVHYLND GADIIYHTAS VGILYNVATG SQSFYQEHND DILCLTVNQH PKFTNLVATG
QVGDSADMSA TAPSIHVWDA MNKQTLSVLR CYHSKGVCSV SFSATGKLLL SVGLDPEHTI
TIWKWQEGAK IASRTGHNQR IFVAEFRPDS DTQFVSVGVK HVRFWTLAGR ALLSKKGLLS
SIEDARMQTM LSVAFGANNL TFTGTISGDV CVWKDHVLVR IVAKAHNGPV FTMYTTLRDG
LIVTGGKERP SKEGGAVKLW DQELKRCRAF RLETGQMTDC VRSVCRGKGK ILVGTRNAEI
MEVGEKNAAC NILINGHMDG PIWGLATHPS RDFFLSAAED GTVRLWDIAE KKMLNKVSLG
HAARTVSYSP EGDMVAIGMK NGEFIILLVT SLKIWGKKRD RSSAIQDIRF SPDSRYLAVG
TSENAVDFYD LTLGPTLNRV SYCKDIPSFV IQMDFSADSR FLQVSTGSYK RQVYEVPSGR
QLMDQAVIDR ITWATWTSIL GDEVVGIWSR HAEKADVNCA CVSHSGISLV TGDDFGMVKL
FDFPCPEKFA KHKRFLGHSA HLTNIRFTSG DKYVVSAGGD DCSLFIWKCV HMLH
//
