ID M7NM00_PNEMU Unreviewed; 1063 AA.
AC M7NM00;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=ISWI chromatin-remodeling complex ATPase ISW2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=PNEG_01885 {ECO:0000313|EMBL:EMR09698.1};
OS Pneumocystis murina (strain B123) (Mouse pneumocystis pneumonia agent)
OS (Pneumocystis carinii f. sp. muris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Pneumocystomycetes; Pneumocystaceae; Pneumocystis.
OX NCBI_TaxID=1069680 {ECO:0000313|EMBL:EMR09698.1, ECO:0000313|Proteomes:UP000011958};
RN [1] {ECO:0000313|Proteomes:UP000011958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B123 {ECO:0000313|Proteomes:UP000011958};
RX PubMed=26899007; DOI=10.1038/ncomms10740;
RA Ma L., Chen Z., Huang D.W., Kutty G., Ishihara M., Wang H., Abouelleil A.,
RA Bishop L., Davey E., Deng R., Deng X., Fan L., Fantoni G., Fitzgerald M.,
RA Gogineni E., Goldberg J.M., Handley G., Hu X., Huber C., Jiao X., Jones K.,
RA Levin J.Z., Liu Y., Macdonald P., Melnikov A., Raley C., Sassi M.,
RA Sherman B.T., Song X., Sykes S., Tran B., Walsh L., Xia Y., Yang J.,
RA Young S., Zeng Q., Zheng X., Stephens R., Nusbaum C., Birren B.W.,
RA Azadi P., Lempicki R.A., Cuomo C.A., Kovacs J.A.;
RT "Genome analysis of three Pneumocystis species reveals adaptation
RT mechanisms to life exclusively in mammalian hosts.";
RL Nat. Commun. 7:10740-10740(2016).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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:EMR09698.1}.
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DR EMBL; AFWA02000009; EMR09698.1; -; Genomic_DNA.
DR RefSeq; XP_007873859.1; XM_007875668.1.
DR AlphaFoldDB; M7NM00; -.
DR STRING; 1069680.M7NM00; -.
DR GeneID; 19895579; -.
DR VEuPathDB; FungiDB:PNEG_01885; -.
DR eggNOG; KOG0385; Eukaryota.
DR HOGENOM; CLU_000315_0_2_1; -.
DR OMA; VHDYQFF; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000011958; Unassembled WGS sequence.
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};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000011958}.
FT DOMAIN 166..331
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 462..613
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 822..874
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 101..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 998..1063
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1063 AA; 124409 MW; 1C2C1BD08789E86E CRC64;
MSKNSKNNSI SDLSEEFDEQ KIKSEDELLE EEKLNQKNYR TIINMERQRE FVEKHAKLNE
AKAVDSTKRL SFLLGQTELF RHFINLQTGA NTDSKEIINK LSDEKPKKEM NSKDHRHRKT
EQEEDAELLQ ENDPNQESQT IFTESPPYIV GGKMRDYQVQ GLNWLISLYE NGINGILADE
MGLGKTLQTI SFLGYLRFLK DIRGPHLVAA PKSTLDNWSR EFSRWIPEIN VFVFQAPKDE
RAGLINERLL TNNFDVCITS YETILREKMH FKKFAWEYII VDEAHRIKNE ESMLSKIIRL
LNSRNRLLIT GTPLQNNLHE LWALLNFLLP DIFADSQVFD RWFESQNGDS DTVVKQLHKV
LRPFLLRRVK SDVERTLKPK KETNLYVGLS EMQVKWYQKI LEKDIDAVNG AIGRKEGKTR
LLNIVMQLRK CCNHPYLFDG AEPGPPYTTD EHIVTNSGKM VMLDKLLKWS KAQDSRVLIF
SQMGRVLDIL EDYCYLRGYK YCRIDGQTSH EDRIVAIDDF NAPGSDKFLF LLTTRAGGLG
INLTTADVVV IYDSDWNPQA DLQAMDRAHR IGQTKQVYVF RFVTDNTVEE KVLERAAQKL
RLDQLVIQQG RAQLQNKNSA SKEELITMIQ HGAEDVFKQR EGGTMTEDDI EEIMKKGEKR
TAELNKRYES LGIDDLQKFS TDSAYEWNGE DYTKKRSTDG TGIKWIYPSK RERTQQSYSL
DQYYKGVLKT GGRTHGPPKA PRPPKQINIQ DHQFFPQRLI DLQDRETAYF RKELGYKVPL
AEGTPEDLEE REAVRDLEQR EIDNAVPLTE EEQLEKEKLL LHGFGDWQRR DFYHFIQACA
KHGRNSFKAL AQEIESKTLA QIKEYSKVFW ERYSEIDGYE RYIGQIEAGE GRIQKQDRQT
KLLHEKISQY RAPLQQLKII YNQNKGKSYT EEEDRFLLVK LNEYGLGTED VYERLREEIR
ISPLFRFDWF FKSRTALELQ RRCATLLTSV KRELEMNEEK TDWKRDRSDD NDDDDDDDDL
PRKKTRTGVK DKRARSRLKN KHVSEGNHSY ISTTRISRSR SKK
//