ID A0A151M0B9_ALLMI Unreviewed; 2693 AA.
AC A0A151M0B9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=WD repeat, SAM and U-box domain-containing protein 1 {ECO:0000256|ARBA:ARBA00020894};
GN ORFNames=Y1Q_0011587 {ECO:0000313|EMBL:KYO17961.1};
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:KYO17961.1};
RN [1] {ECO:0000313|EMBL:KYO17961.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO17961.1};
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:KYO17961.1}.
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DR EMBL; AKHW03006853; KYO17961.1; -; Genomic_DNA.
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..867
FT /note="MBD"
FT /evidence="ECO:0000259|PROSITE:PS50982"
FT DOMAIN 1112..1177
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1963..2013
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 2109..2179
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REPEAT 2262..2303
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 2305..2346
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 2447..2488
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 2489..2523
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 2544..2608
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 2615..2689
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..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1537..1556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1599..1633
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1697..1728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1877..1897
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2026..2090
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 859..889
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1345
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1599..1618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1697..1723
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2026..2075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2693 AA; 299244 MW; D7975DF2A13C2CB3 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
KGMQWCLLKE EEVLPRIRAM EGRRGRPPNP DRQHAREESR MRRRKGRPPN VGSAEFLDNS
DAKLLRKLQA QEIARQAAQI KLLRKLQKQE QARAAKEAKK QQVIFMIIFQ ISKYMRVIIQ
EKIKRIQQIR MEKELRAQQI LEAKKKKKEE AANAKLLEAE KRIKEKEMRR QQAVLLKHQE
LERHRLDMER ERRRQHMMLM KAMEARKKAE EKERLKQEKR DEKRLNKERK LEQRRLELEM
AKELKKPNED MCLADQKPLP ELHRIPGLVL CGSTFSDCLM VVQFLRNFGK VLGFDVNMDV
PSLSVLQEGL LNIGDSMGEV QDLLVRLVSA AVCDPGVVTG YKAKTILGEH LLNVGINRDN
VSEILQIFME AHCGQTELTE SLKTKAFQAH TPAQKASVLA FLVNELACSK SVVSEIDKNI
DYMSNLRRDK WMVEGKLRKL RIIHAKKTGK RDAVVGGDIG EEQHSLETPT PGRKRRRKGG
DSDYDDDDDD DSDDQADEDE EDEEDKDEKK GKKAEVCEDE DDGDQTASVE ELEKQIEKLT
KQQSQYRKKL FEASHSLRSM MFGQDRYRRR YWILPQCGGI FVEGMESGEG LEEIAKEKEK
LKNAESIHIK EEMFETSEEK LNCLSTTHCE QKEDLKEKDN TNLFLQKPGS FSKLSKLLEV
AKMPPESDIL SQKPNGSAAN GCMLSYPNNS KNSLCSLQPT VSQSGTEKSD PSNLFNPIAS
GSGKFYNSPL VPNDQLLKTL TEKSRQWFSL LPRIPCDDTS VTNTDTPAAS STLTPHSHPP
SKSPSPVPSS LISSASAQSS IGLNPFALSP LQQMKTGLPI MGLQFCGWPT GVLTSNVPFS
SPLPSLGSGL GLSEGNANSF LTPSVPTSKS ESPVPQTEKA ASAPSTAVEV AKPVDYPSPK
PIPEEMQYGW WRITDPEDLK ALLKVLHLRG IREKALQKQI QKHMDYITLA CIKNKDVAII
EINENEENQV TRDVVENWSI EEQAMEMDLA ILQQVEDLER RVASASLQVK GWICPEPASE
REDLVYYEHK SITKLHKKHD GESAGGEEAS TSALERKSDN PLDIAVTRLA DLERNIERRM
EEDIAPGLRV WRRALSEARS AAQVALCIQQ LQKSIAWEKS IMKVYCQICR KGDNEELLLL
CDGCDKGCHT YCHRPKITTI PDGDWFCPAC IAKASGQTLK IKKLQIKGKK SNEQKRGRKL
SLTGDTEDED SAATSSSLKR GKTDPKKRKM DENISVNQLK QESFTPIKKP KRDESKDLAL
CSMILSELET HEDAWPFLLP VNLKLVPGYK KVIKKPMDFS TIRDKLSSGQ YPNLEAFSLD
VRLVFDNCET FNEDDSDIGR AGHNMRKYFE KKWTEIFKSP EPVENILFIA DNMMKLIYTL
ADHSDDVNYC ALSSSCLATC SMDKTIRLYS LNNFSELSYS PLRGHTYAVH CCCFSSSGNI
LASCSTDGTT VLWDTQNGQR LAVLEQPSDS PVRVCQFSPD STYLVSGAAD GTVVLWNVES
LRLYRSGSVK DGSLVACAFA PNGNFFVTGS SCGDLTIWDD KMRCLYNEKA HDLGVTCCDF
SSLPVSDGEQ GSRYFRMASC GQDNQIKLWL FSFADYLGAE LKYKCTLSGH SAPVLACAFS
YDGQMLVSGS VDKSVIIHET KTGNILHTLT RHTRYVTTCA FAPDALLLAT GSMDKTVNVW
QFDPDQHFAG SGLEDKPKMS VENWSEEEVS AWLCAQGLKD LVECFKTNNI DGKELLSLTK
ESLTSDLKIE SLGLRSKVIR KIEELSIKMD SVSVGIPDEF LCPITRELMK DPIIASDGYS
YEKEAMENWI SNKRRSSPMT NLPLQSLVLT PNRTLKMAIS RWLETQQKYN ETT
//
