ID A0A7J7WJA0_MYOMY Unreviewed; 692 AA.
AC A0A7J7WJA0;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE SubName: Full=SP110 nuclear body protein {ECO:0000313|EMBL:KAF6337484.1};
GN ORFNames=mMyoMyo1_018163 {ECO:0000313|EMBL:KAF6337484.1};
OS Myotis myotis (Greater mouse-eared bat) (Vespertilio myotis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yangochiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=51298 {ECO:0000313|EMBL:KAF6337484.1, ECO:0000313|Proteomes:UP000527355};
RN [1] {ECO:0000313|EMBL:KAF6337484.1, ECO:0000313|Proteomes:UP000527355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMyoMyo1 {ECO:0000313|EMBL:KAF6337484.1};
RC TISSUE=Flight muscle {ECO:0000313|EMBL:KAF6337484.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
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:KAF6337484.1}.
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DR EMBL; JABWUV010000008; KAF6337484.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J7WJA0; -.
DR VEuPathDB; HostDB:GeneID_118661409; -.
DR Proteomes; UP000527355; Unassembled WGS sequence.
DR GO; GO:0031981; C:nuclear lumen; IEA:UniProtKB-ARBA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:TreeGrafter.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd15626; PHD_SP110_140; 1.
DR FunFam; 1.20.920.10:FF:000028; Nuclear autoantigen Sp-100; 1.
DR FunFam; 3.30.40.10:FF:000294; Nuclear autoantigen Sp-100; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.10.390.10; SAND domain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR004865; HSR_dom.
DR InterPro; IPR010919; SAND-like_dom_sf.
DR InterPro; IPR000770; SAND_dom.
DR InterPro; IPR043563; Sp110/Sp140/Sp140L-like.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
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; PTHR46386; NUCLEAR BODY PROTEIN SP140; 1.
DR PANTHER; PTHR46386:SF7; SP110 NUCLEAR BODY PROTEIN; 1.
DR Pfam; PF03172; HSR; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF01342; SAND; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00258; SAND; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF63763; SAND domain-like; 1.
DR PROSITE; PS51414; HSR; 1.
DR PROSITE; PS50864; SAND; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000527355};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 1..108
FT /note="HSR"
FT /evidence="ECO:0000259|PROSITE:PS51414"
FT DOMAIN 418..499
FT /note="SAND"
FT /evidence="ECO:0000259|PROSITE:PS50864"
FT DOMAIN 513..559
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 125..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..295
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..420
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 692 AA; 78548 MW; FA245421EAB30EBB CRC64;
MFNITQDLKE TLRQHFIFQK LEISYAICKP FPFLEGLRDK SFISEKMYME SMEACRNMVP
VSKVVYNILT KMEEPFNLSF LEMLFSQINL REYPNLVAIQ RSFRNVFASC GGWRGATVTV
FEVPTNSRGR SPHQNLPPLP APQRPPLRCP TPVPRFNQPS AIPQHSNKIL DKPPHSAGPA
KTLPRVIQEG RTTPANLTSH INDEEDSQQV PSTPPATVQV SSDHPTPQVK DKEDTQEMPQ
APSAPEPVIR NDSPEPNEPV EPQEAASTPL IKKGKKRKRS MWSVPKKRQQ KKRLSKGTAS
PGHRIQEKLQ MVDQVTQGKD DSTRNSKVVI RTQKARTECA QTSGPEGTTS PVPQMVDQAT
QKKNNSTGNS RVMTRSQKAR TECAQTSGPE EKKRKKDVCS SSTISGQKNI PQKEKPKDDT
VDFQSPTLPV TCGGEMGILH KEKMEKGSSE KCIQNEEGVW FTPREFEIKG RGTKSKDWKR
NVRCKGQTLQ QLMEKGLLYC PSRISLKREW ENSNECEVCC GEGQLLCCDA CPRAFHEDCH
IPPMEAKRSP WSCTFCRMKE SSGSQQYLRG SEVLTRQMGP EEQLKCEFLL LKAYCHPQSA
FFAKIPRNIR DYAEPFKEAM WLDLVKERLT EKVYTVEWFV RDIRLIFHNH KTFYKASALG
QIGLDLEAKF EKDLKEVLIF HGASENSLQA PP
//
