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Database: UniProt
Entry: M7NM00_PNEMU
LinkDB: M7NM00_PNEMU
Original site: M7NM00_PNEMU 
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
//
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