ID A0A0N1H679_9EURO Unreviewed; 959 AA.
AC A0A0N1H679;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3-like 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AB675_9171 {ECO:0000313|EMBL:KPI41493.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI41493.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI41493.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI41493.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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:KPI41493.1}.
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DR EMBL; LFJN01000009; KPI41493.1; -; Genomic_DNA.
DR RefSeq; XP_018001456.1; XM_018149682.1.
DR AlphaFoldDB; A0A0N1H679; -.
DR STRING; 1664694.A0A0N1H679; -.
DR GeneID; 28741562; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000038010; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.30.70.2330; -; 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 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; IPR014905; HIRAN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR45626:SF11; FAMILY HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G06590)-RELATED; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF13923; zf-C3HC4_2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00910; HIRAN; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 393..569
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 726..764
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 797..940
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 959 AA; 107245 MW; 9F8DA44E470CB386 CRC64;
MPTGVGRQPK RKLSDVIDLT AFSSDEEFPS SSSKKAKTNN NSTVTTGPGG HQYLTPPSSS
AVRSSQHGYN GRSSSFNVYS SQPSYSNQHS QRERDSWLGS TQEQEDDVSR EIDLTADDDD
DVYENYQLYG ILNTKIVGCR YYDGRATVGE YVKVRREPGN TYDRNAFRID NCVGDQIGHI
GRQVAAKLAA LFDSKELLIE GALTGPKTVF ECPIGLKLFG TSDPVAQADL KQKMQDLKLP
VNELARTERE RKQQEKDRIA REKAAKSMMK GGGQVVDHEG PNKYANISTL PSGSQPALTM
ESVLSNTAMF NPRDVQDAVN KFVAGEATLE KMTPAKQPSE MATRLLPYQL QGLQWMLQKE
SPKLPEKDAD EPVQLWKRSH GLYTNIATNF SLTKAPALAR GGILADDMGL GKTIQIISLI
MADPHKEGRP TLIVAPLSVM SNWRQQAELH VTADQRPRLL TYHGQDNRWL SPAQFAEYDI
VVTTYATMSQ ELFPSGKDKA VKTPSQKGLF SLKWRRIVLD EGHNIRNPKT KMSIAACTLD
ATSRWTLTGT PIINTLKDLY AQVKFLHISG GLDELEVFNT LLVRPLKRND PNARILLQAL
MATLCLRRMK DFKFIDLKLP GINFHQYPVK LLTHEQERYD AFKHEAKGLL EAAKAKKGDS
NTMTNLLEVL LRLRQTCNHW KMCGEARLKQ VMELVEENKA VDVTNIANRK ALQDLLQVRI
DSQEECPVCY DTMRSPVITA CSHAYCQQCI ERVIEVQHKC PMCRADLPTI ESLVAPAANF
GEADEEIEID ADSTSSKIEA LIKVLKAAQN ENGAKCVVFS QWTSFLDLVQ TQLIKHDLRF
SDTALEMLNT DNSCRIMLAS LSVCSVGLNL VAANTVVLCD SWWAPAIEDQ AVDRVHRLGQ
QRPCKCIRLV AEDTIEQEVI EIQTKKRKLA SMAFGEKDGQ RSRKEQRANT LNDIARLLA
//
