ID A0A199W770_ANACO Unreviewed; 1274 AA.
AC A0A199W770;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Putative SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3-like 3 {ECO:0000313|EMBL:OAY85086.1};
GN ORFNames=ACMD2_15460 {ECO:0000313|EMBL:OAY85086.1};
OS Ananas comosus (Pineapple) (Ananas ananas).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Bromeliaceae;
OC Bromelioideae; Ananas.
OX NCBI_TaxID=4615 {ECO:0000313|EMBL:OAY85086.1, ECO:0000313|Proteomes:UP000092600};
RN [1] {ECO:0000313|EMBL:OAY85086.1, ECO:0000313|Proteomes:UP000092600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. MD2 {ECO:0000313|Proteomes:UP000092600};
RC TISSUE=Leaf {ECO:0000313|EMBL:OAY85086.1};
RX PubMed=27374615; DOI=10.1093/dnares/dsw026;
RA Redwan R.M., Saidin A., Kumar S.V.;
RT "The draft genome of MD-2 pineapple using hybrid error correction of long
RT reads.";
RL DNA Res. 0:0-0(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
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:OAY85086.1}.
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DR EMBL; LSRQ01000131; OAY85086.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A199W770; -.
DR STRING; 4615.A0A199W770; -.
DR Proteomes; UP000092600; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF16; SNF2 DOMAIN-CONTAINING PROTEIN / HELICASE DOMAIN-CONTAINING PROTEIN / ZINC FINGER PROTEIN-LIKE PROTEIN; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000092600};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 552..826
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 980..1016
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1110..1269
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 371..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 715..747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1274 AA; 141993 MW; E214810D19328E26 CRC64;
MPMAESVEDP GGGFFRSDLG DGRSDHNDDN LSISLGDLFA ILDEEPRQSQ PYPAVAAQKS
ICQGKVADPI VNEKVFQPQD DFTADWKDLG EELGCNLRDI DASNCQNLTK FQLLSESEEN
FEPFMINEKS HRVSEHDSSK NSFSFMSNHT PDWLSYPTLE YNMLNSNVAH DTDGAYLLTL
EHANLGNGLY LDGNEERDYK EMTGVKEIES GTKFMPSLLM QNGGTGALPE RDLSGSMTRY
AFVDHEATLP YAFPGEMNTS EATELQCNTS GSCLTLHRES ISDENKNGSK QFISAVYQQP
LLPHVKESLI RINDKRKDQL LHSHNSGRSS EVQLGTQELL DISLSGFPMS FMDASSPSTL
SFEHCEDIHF RSESSTDSSP HLSSRNSTSE NFHTSSLDTT KQFMFDSNVY SNMKKETFSK
NETEDKMLPS SVKQPGIPED TGNVHMDEYD EEEEDDDTDL YIVDNISDPA HPPLPPVHQK
PNLIYQRSAH GEAYYSGFGG MRLKANDERL TFRLILQDLS QPKSEATPPD GLLAVPLLRH
QRIALSWMVQ KECASLHCSG GILADDQGLG KTVSTIALIL TERSPSSRSS TKENLDNYET
LDLDDDDDDD GDVAEVYKTN ITKQPRISTP AKKENLMMVM SRPAAGTLVV CPTSVLRQWA
EELQNKVTSK ANLSFLVYHG SNRTKDPNDL AKYDVVLTTY AIVSMEVPKQ PLVDKDEEEK
VKPDTSTSSV GHIGGKKRKI PGSSVKNPKL EKTMENALFE SAARPLARVG WFRVILDEAQ
SIKNHRTQVA RACWGLRAKR RWCLSGTPIQ NAVDDLYSYF RFLRYDPYAA YKSFCSMIKV
PINRNPTNGY KKLQAVLKTI MLRRTKGTLI DGQPIITLPP KTVTLKKVDF SMEERTFYST
LEAESREQFK VYADAGTVKQ NYVNILLMLL RLRQACDHPL LVKGYDSSSV WRSSLEMAKK
LPMEKQQNLL SCLEHCSAIC TICNDAPEDA VITICGHVFC HQCICEHLTG DDSICPSAGC
KVRLNVASVF SRGTLQSALS GVTGGECCPN DSGSEMTQAG LFYDSSKVRT ALQILQSLPR
AARQDSSMTT KSAKLNDETA EISDGKNFGP IISSDSCVTE KAIVFSQWTG MLDLLEVPLK
DSSIQYRRLD GTMSVAAREK AVKDFNTRPE VSVMIMSLKA ASLGLNMVAA CHVLLLDLWW
NPTTEDQAID RAHRIGQTRP VTVSRLTVKD TVEDRILALQ QRKREMVASA FGEDESGSRQ
TRLTVEDLKY LFMV
//