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Database: UniProt
Entry: A0A0L8I5P4_OCTBM
LinkDB: A0A0L8I5P4_OCTBM
Original site: A0A0L8I5P4_OCTBM 
ID   A0A0L8I5P4_OCTBM        Unreviewed;      1110 AA.
AC   A0A0L8I5P4;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 5 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=OCBIM_22035363mg {ECO:0000313|EMBL:KOF96360.1};
OS   Octopus bimaculoides (California two-spotted octopus).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX   NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF96360.1};
RN   [1] {ECO:0000313|EMBL:KOF96360.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF96360.1};
RC   TISSUE=Gonad {ECO:0000313|EMBL:KOF96360.1};
RA   Tran T., Druce J.;
RT   "MeaNS - Measles Nucleotide Surveillance Program.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC       {ECO:0000256|ARBA:ARBA00009687}.
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DR   EMBL; KQ416583; KOF96360.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0L8I5P4; -.
DR   EnsemblMetazoa; Ocbimv22035362m; Ocbimv22035362m.p; Ocbimv22035363m.g.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR   CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR   CDD; cd00167; SANT; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   Gene3D; 1.20.5.1190; iswi atpase; 1.
DR   Gene3D; 1.10.1040.30; ISWI, HAND domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR044754; Isw1/2_DEXHc.
DR   InterPro; IPR015194; ISWI_HAND-dom.
DR   InterPro; IPR036306; ISWI_HAND-dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR015195; SLIDE.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR   PANTHER; PTHR45623:SF49; ISW-1; 1.
DR   Pfam; PF09110; HAND; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF09111; SLIDE; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51293; SANT; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          246..411
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          541..692
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          896..948
FT                   /note="SANT"
FT                   /evidence="ECO:0000259|PROSITE:PS51293"
FT   REGION          1..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1071..1110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..68
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        143..207
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1071..1104
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1110 AA;  129172 MW;  146D16D9FE53B972 CRC64;
     MSESDQENIP QEENMEEGED DVEAEAEDSE AEEEEEEEAP AEEEDDEEEE EDEAEEQGDD
     DDENESDPEY LADGVKPVKA LLLKQPPKKN GQDAEAYEEH IQADRSNRFD FLLKQTELFA
     HFMSTGGQGG KGPSSPLKMK PGRPRLKKND EKSKLVAIGD EKKPKTDAVK SDAPEEDEKK
     PTTGDVKTDD PADDHRHRRT EQEEDEELLI ESKKSVNVEI RFEKSPSYVH NGELRDYQIR
     GLNWMISLYE HGINGILADE MGLGKTLQTI ALLGYMKHYR NIHSPHLVIV PKSTLANWEN
     EFLRWVPSIR AVCLIGDQNQ RATFIRDVLM PGEWDVCITS YEMVIREKAV FKKFNWRYLV
     IDEAHRIKNE KSKLSEIVRE FKSTNRLLLT GTPLQNNLHE LWALLNFLLP DVFNSSEDFD
     AWFNTNNCFG DTQLVDRLHA VLRPFLLRRI KSDVEKRLLP KKETKIFIGL SKMQREWYTR
     ILMKDIDVVN GAGKSDKMRL LNILMQLRKC CNHPYLFDGA EPGPPYTTDK HLVDNCGKMV
     ILDKLLPKLQ AQGSRVLVFS QMTRMLDILE DYCIWKQYNY CRLDGQTPHE DRQVSINDFN
     APNSLKFLFM LSTRAGGLGI NLATADIVIL FDSDWNPQVD LQAQDRAHRI GQTKQVRVFR
     LITENTVEER IVERAEMKLR LDNIVIQQGR LLDQNTNKLG KEEVLQMIRH GANHVFASKD
     SEITDEDIDA ILAKGEKRTL EIQNKMETLG EGTLKTFSLD THESVYKFEG EDYREKQKIG
     PLGSWIEPPK RERKANYAVD AYFREALRVS EPKAPKAPRP PKQPNVQDFQ FFPPRLFELL
     DKEIYFYRKS IGYKVPKNPD YGADAERIRR EEQKRIDEAY PLNDAEISEK EELLKQGFTN
     WSKRDFNQFI KANEKYGRDD IENIAHEVEG KTPEEVVEYS TLFWERCNEL QDIERIMAQI
     ERGEAKIQRR ISIKKALDVK MNRYRAPFHQ LRIQYGTNKG KNYTEEEDRF LVCMLHKLGF
     DKENVYDELR TSVRQAPQFR FDWFIKSRTA MELQRRCNTL ITLIERENLE LEEKEKQEKK
     RRGPKPGTPK GQKRKADGTP DGRGRPKKKK
//
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