ID A0A151M0E8_ALLMI Unreviewed; 2762 AA.
AC A0A151M0E8;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=WD repeat, SAM and U-box domain-containing protein 1 {ECO:0000256|ARBA:ARBA00020894};
GN ORFNames=Y1Q_0011587 {ECO:0000313|EMBL:KYO17960.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO17960.1};
RN [1] {ECO:0000313|EMBL:KYO17960.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO17960.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
CC -!- SIMILARITY: Belongs to the WAL family. {ECO:0000256|ARBA:ARBA00007444}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO17960.1}.
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DR EMBL; AKHW03006853; KYO17960.1; -; Genomic_DNA.
DR STRING; 8496.A0A151M0E8; -.
DR eggNOG; KOG1245; Eukaryota.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd05503; Bromo_BAZ2A_B_like; 1.
DR CDD; cd01397; HAT_MBD; 1.
DR CDD; cd15630; PHD_BAZ2B; 1.
DR CDD; cd16655; RING-Ubox_WDSUB1-like; 1.
DR CDD; cd09505; SAM_WDSUB1; 1.
DR CDD; cd00200; WD40; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR037374; BAZ2A/B_Bromo.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR018359; Bromodomain_CS.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR016177; DNA-bd_dom_sf.
DR InterPro; IPR001739; Methyl_CpG_DNA-bd.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR003613; Ubox_domain.
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 InterPro; IPR028941; WHIM2_dom.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45915:SF1; BROMODOMAIN ADJACENT TO ZINC FINGER DOMAIN PROTEIN 2B; 1.
DR PANTHER; PTHR45915; TRANSCRIPTION INTERMEDIARY FACTOR; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF01429; MBD; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF07647; SAM_2; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF00400; WD40; 7.
DR Pfam; PF15613; WSD; 2.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00391; MBD; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00504; Ubox; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF54171; DNA-binding domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00633; BROMODOMAIN_1; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS50982; MBD; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 2.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 4.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 792..863
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 1146..1211
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 2032..2082
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2178..2248
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REPEAT 2331..2372
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 2374..2415
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 2516..2557
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 2558..2592
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 2613..2677
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 2684..2758
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT REGION 47..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 247..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 510..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 576..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 893..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1080..1102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1328..1402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..1590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1633..1667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1731..1762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1910..1930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2095..2142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..336
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 620..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 658..717
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 727..741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 773..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..923
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1341..1357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1358..1379
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1731..1757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2762 AA; 306548 MW; 02DB7F0A2EDD8BA0 CRC64;
MRKETEKGLM FLSSGIENES FLVMQVFLFK LAKKQCHRTD HIYHNMESGE RLTSSASSTT
ATSSPASTTP SVTSAVSKSS LSTGAASLSS AVNTCGHLFR TAGDQPCNLS TVSSAFPMVS
HPVFGLHTAS SGHSEFGGLG TLGTPTALAA HPQLAPFPGT EWWRTTDVHT RTGAAFFPPL
LGIPPLFAPP TQNHDSTSFH SRTTGKNSRS SIEKGVNGSV NGNSTTSVPG ISTSVLSTTT
ASSAGQAKAI TSGGGSHKCH QDQNKNQLLD TRADKIKDKK PRKKAVESSS NSDSDSGSSS
DTSSEGISSS DSDDLEEDEE EEEEDQSGEE TEDDSDSENE AHHKNKNKVL MHSGVTDMKA
DGQKTHEKSQ EKRTHQQIPL MSDSQTHSSF QSQQKQPQVL SQQLPFIFQS SQAKEESVNK
HTSVIQSTGL VPNVKPLSLV NQAKKETYLK LIVPSPDLLK AGNKNTSEES NPLTSDVRSK
REQYKQTFPA AQLKKQQESS KNLKKVITAL SSPKPTSSSP AHPKHTSLEN NHSNPFLTNA
LLGNHQPNGV IQSVIQEAPL ALTTKSKSQP KINENIATSS STSFSSPVNL TTCGKKTSGN
RTPVMPSTSP LLPGPGKEKA VSNNTVTAVK TQHRLHSAKS LVEQFRGTDS DIPSSKDSDD
SNDEDDDDDD DDDDEDEDDD DDDSDDSQSE SDSNSESDTE GSEDEDDEDD KDQDESDTDT
EGEKTPVKLN KTTSSVKSSS INLTAHSTPL NLQVAKTPSS APAALCPESQ SPVFLGTPPS
TLTPSTSKRR RVTDERELRI PLEYGWQRET RIRSFGGRLQ GEVAYYAPCG KKLRQYPEVI
KYLSRNGIMD ISRDNFSFSA KIGVGDFYEA RDGPQGMQWC LLKEEEVLPR IRAMEGRRGR
PPNPDRQHAR EESRMRRRKG RPPNVGSAEF LDNSDAKLLR KLQAQEIARQ AAQIKLLRKL
QKQEQARAAK EAKKQQVIFM IIFQISKYMR VIIQEKIKRI QQIRMEKELR AQQILEAKKK
KKEEAANAKL LEAEKRIKEK EMRRQQAVLL KHQELERHRL DMERERRRQH MMLMKAMEAR
KKAEEKERLK QEKRDEKRLN KERKLEQRRL ELEMAKELKK PNEDMCLADQ KPLPELHRIP
GLVLCGSTFS DCLMVVQFLR NFGKVLGFDV NMDVPSLSVL QEGLLNIGDS MGEVQDLLVR
LVSAAVCDPG VVTGYKAKTI LGEHLLNVGI NRDNVSEILQ IFMEAHCGQT ELTESLKTKA
FQAHTPAQKA SVLAFLVNEL ACSKSVVSEI DKNIDYMSNL RRDKWMVEGK LRKLRIIHAK
KTGKRDAVVG GDIGEEQHSL ETPTPGRKRR RKGGDSDYDD DDDDDSDDQA DEDEEDEEDK
DEKKGKKAEV CEDEDDGDQT ASVEELEKQI EKLTKQQSQY RKKLFEASHS LRSMMFGQDR
YRRRYWILPQ CGGIFVEGME SGEGLEEIAK EKEKLKNAES IHIKEEMFET SEEKLNCLST
THCEQKEDLK EKDNTNLFLQ KPGSFSKLSK LLEVAKMPPE SDILSQKPNG SAANGCMLSY
PNNSKNSLCS LQPTVSQSGT EKSDPSNLFN PIASGSGKFY NSPLVPNDQL LKTLTEKSRQ
WFSLLPRIPC DDTSVTNTDT PAASSTLTPH SHPPSKSPSP VPSSLISSAS AQSSIGLNPF
ALSPLQQMKT GLPIMGLQFC GWPTGVLTSN VPFSSPLPSL GSGLGLSEGN ANSFLTPSVP
TSKSESPVPQ TEKAASAPST AVEVAKPVDY PSPKPIPEEM QYGWWRITDP EDLKALLKVL
HLRGIREKAL QKQIQKHMDY ITLACIKNKD VAIIEINENE ENQVTRDVVE NWSIEEQAME
MDLAILQQVE DLERRVASAS LQVKGWICPE PASEREDLVY YEHKSITKLH KKHDGESAGG
EEASTSALER KSDNPLDIAV TRLADLERNI ERRYLKSPLS TTIQIKLDNV GTVTVPAPAP
SISGDGDGME EDIAPGLRVW RRALSEARSA AQVALCIQQL QKSIAWEKSI MKVYCQICRK
GDNEELLLLC DGCDKGCHTY CHRPKITTIP DGDWFCPACI AKASGQTLKI KKLQIKGKKS
NEQKRGRKLS LTGDTEDEDS AATSSSLKRG KTDPKKRKMD ENISVNQLKQ ESFTPIKKPK
RDESKDLALC SMILSELETH EDAWPFLLPV NLKLVPGYKK VIKKPMDFST IRDKLSSGQY
PNLEAFSLDV RLVFDNCETF NEDDSDIGRA GHNMRKYFEK KWTEIFKSPE PVENILFIAD
NMMKLIYTLA DHSDDVNYCA LSSSCLATCS MDKTIRLYSL NNFSELSYSP LRGHTYAVHC
CCFSSSGNIL ASCSTDGTTV LWDTQNGQRL AVLEQPSDSP VRVCQFSPDS TYLVSGAADG
TVVLWNVESL RLYRSGSVKD GSLVACAFAP NGNFFVTGSS CGDLTIWDDK MRCLYNEKAH
DLGVTCCDFS SLPVSDGEQG SRYFRMASCG QDNQIKLWLF SFADYLGAEL KYKCTLSGHS
APVLACAFSY DGQMLVSGSV DKSVIIHETK TGNILHTLTR HTRYVTTCAF APDALLLATG
SMDKTVNVWQ FDPDQHFAGS GLEDKPKMSV ENWSEEEVSA WLCAQGLKDL VECFKTNNID
GKELLSLTKE SLTSDLKIES LGLRSKVIRK IEELSIKMDS VSVGIPDEFL CPITRELMKD
PIIASDGYSY EKEAMENWIS NKRRSSPMTN LPLQSLVLTP NRTLKMAISR WLETQQKYNE
TT
//
