ID V9G0B8_PHYPR Unreviewed; 1621 AA.
AC V9G0B8;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 13-SEP-2023, entry version 45.
DE RecName: Full=ATPase family AAA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=F443_00495 {ECO:0000313|EMBL:ETI57159.1};
OS Phytophthora parasitica P1569.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI57159.1, ECO:0000313|Proteomes:UP000018721};
RN [1] {ECO:0000313|EMBL:ETI57159.1, ECO:0000313|Proteomes:UP000018721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1569 {ECO:0000313|EMBL:ETI57159.1,
RC ECO:0000313|Proteomes:UP000018721};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica P1569.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914}.
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:ETI57159.1}.
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DR EMBL; ANIZ01000081; ETI57159.1; -; Genomic_DNA.
DR EnsemblProtists; ETI57159; ETI57159; F443_00495.
DR OrthoDB; 2783776at2759; -.
DR Proteomes; UP000018721; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR045199; ATAD2-like.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR23069; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23069:SF0; TAT-BINDING HOMOLOG 7; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF47370; Bromodomain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 3: Inferred from homology;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117, ECO:0000256|PROSITE-
KW ProRule:PRU00035}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000018721};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 788..839
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1092..1162
FT /note="Bromo"
FT /evidence="ECO:0000259|PROSITE:PS50014"
FT REGION 1..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1513..1549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..93
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..113
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..172
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..238
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..255
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..370
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1514..1528
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1621 AA; 183718 MW; 1B1EDA7007900C09 CRC64;
MEDDESEDVD TDELEESKEE DEEEETTKRA STELDITSPP PSTGHEEVSS ASPESSTRYS
LRTRPKPKRI DESIYNDVFP TAHSTYAEST PESQVPSKKR RRRRNRSRRS KRQKRRVEQE
EDEEDDDEEE EQDEETQYED GMSMQEINRK IKAQERQERE QQRRERSTRY SLRSRESLTM
SDASVVSPPQ TESRGRTTRR SQVAENHVEE EEQEEDADNE SQSENDAISD DGQDEDDAEE
PASSTRYHLR QRRQVATDET SIATRSRTKT RVAPMFEPED TSRRYSLRDR SKTHRADAEE
DTAASPETSA YAEYQKRQAT RASRRSSTTG SGSNRRLFLP DMDSSPPPRR RRSRGRNKYS
RGRRNRHRRS LSSSSSGSSS SSDMYMDDDD SDGGMRTTSP WRSSKSSRKS GSSRADITPV
EVDRSITWDS VGGLKSHIEA LKEMVMLPLL YPEFYSKYSV SPPSGVLFYG PPGTGKTLLA
RALANSCSFY GEGEQPSGSI QATSPAQKKK KQRPRRHVTF YMRKGADCLS KWVGEAERQL
RLLFEEAKRN QPSIIFFDEI DGLAPVRSAK QDQIHASIVS TLLALMDGMD SRGRVVVIGA
TNRLDAIDPA LRRPGRFDRE LGFKLPSVDE RKSMLAIHSK HWKPPLSNRF LTELAEQTVG
YCGADIKALC AEAALCSLRR VYPQVYASQD KLLINLDKVV VARGDFVKAA KKITPASHRA
ISSFASPLPR AVKGLLQTQL MQVLRDVARH FPLFPLDKAA IDDAVTTNSE EDEEEEEDDV
DIYAVTSHDD CDVCHGNEGE LLCCDACPGA FHRACLSEMA TSTEEDTGGL WFCLDCRTSS
SAAMQRAIQR GKKKRVHSIA SLHLPRHSGF PRVLIAGKAG MGQQYIGPAL LHSLEGLTHF
SLDYPSLVAD SNSHFPEEAL IQRLSEAQKC LPCVIYLPHV ELWWKNTNES MHLTLKMMLM
DLQVRANLPI LFLACTAPSC DEKTLPEDLL ALFKEDPSVS LTSVVMEMDA PSEEARLTHF
DQVFSSFATP PAVQKKKRFK HEKLAVLPLA PLPPAPSKME LSPEEQKKRR ERDFHFLREL
RIFLSQVLHY CYSQRLYTPF YVPVDPVAVP NYYLIVKRPM DLSTMRDKLN DEEYTCFEQF
MDDIQLIVRN ANVFNPKRSR TRHIAHAAGT MKDNILSYAH RFRIRQGYDL FAKCREVTKR
LRAHPTMYGE YGQRFLKTGR NTRKNSVRAA EKPGVRTSAR LRGVKAPEIS LDAAISRATE
STNVISNGVK EERTEVQCGN KSKEEVPKLQ SAQQWFDEEE EEKKSDEEAS TDDKSDDKTN
EDTGEEMEEE VYEEGDRIFV SSRTHPGINR EGGAAVVQSR NKDGTYNVKY ILGGSEKSVS
CKYVRRLTDD AVMESVKTQR SVANDADGVA SVRLIQDEEK MDETDYFDEL LWPLLKEEGW
TRDDNFDIIE ASGKESGLAV QRVVFTPGKT RDGETVMLNS VVEALKYINE DPELSLKLFG
NRYAERMMTE EALGEEASSD EETVEMEEAS AAENNVAVAE GNNDEPMPEA EEEVQETPEF
IYDEARMTAV LTKLVEKTAN WSVDKLRDEL LMLNKLAYPF RNSFDRTELM TLIEAHVATL
L
//
