ID A0A0H1B3G5_9EURO Unreviewed; 2157 AA.
AC A0A0H1B3G5;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=EMPG_10949 {ECO:0000313|EMBL:KLJ05552.1};
OS Blastomyces silverae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ05552.1, ECO:0000313|Proteomes:UP000053573};
RN [1] {ECO:0000313|Proteomes:UP000053573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA Clay O.K., Klein B.S., Cuomo C.A.;
RT "The dynamic genome and transcriptome of the human fungal pathogen
RT Blastomyces and close relative Emmonsia.";
RL PLoS Genet. 11:E1005493-E1005493(2015).
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:KLJ05552.1}.
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DR EMBL; LDEV01003588; KLJ05552.1; -; Genomic_DNA.
DR STRING; 2060906.A0A0H1B3G5; -.
DR OrthoDB; 103295at2759; -.
DR Proteomes; UP000053573; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd16449; RING-HC; 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; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001525; C5_MeTfrase.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
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:SF26; FAMILY HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_2G09120)-RELATED; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00145; DNA_methylase; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053573};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1885..1928
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 1969..2128
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 28..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2157 AA; 242501 MW; 784C32DDE9C9F211 CRC64;
MAKQEKALLY LLETAQAFIM DEDLTDSSVE GRSVDSNVDT DTCTSPNTDL ETDTSVSEDA
GSDDANISGE DDLRSLINLP PEILRGKYSS LPGKKPKPGL NFNLPPISKI EDIFDDISIN
AEKNGFSDFL DHIGSRDLRV ATMCSGTEAP LLALEMVMDS FKKIFGKTFS MDHLFSAEID
PFKQSYIQRN FSPDIIFRDV NELIADEATT AFGSLRKVPS NLDLLVVGFS CVDFSNMNIH
RKTLDEMGES GHTFYGVLRY TQRCRPPLVI LENVCGAPWG HIKNAFKEME YHAYHIKLDT
KNYYLPQTRE RGYMLCIDQT RLETPLPADP KSSTFAKMMK NFERPASSPV TQFLLKNEDP
RLQDAINDIS TNPIKDRQAV DWTRYKARHL RYRMREGLGN KRPLTRWQDN GTCQMPDFYW
HAWSRAQTER VWDTLDVNYL RSIVRGFDIN FKSRIIDLSQ GLDRELDQRA SGISGCLTPR
GQHFVTSRGG PLLGIEALAL QGIPIDRLLL SNDSQRDLND LAGNAMSSTV VGAAIMSALI
IGHQALASGT TFQRNSKKEE RGTPQIADNG TIEVAPIQLG DEIALSTHEI LEVGKRSSRM
CICEGQLLTK RTDMLTCVKC GLTACRSCGR NPSHVYSPVP RDELNARLCP IDFETQLKKK
LPMRLQVNGL SLALYRALWE SNMSVDIMKA WEDFSRILLP ALGDELRFQG VTRQRSWTIT
YKGSLSVLKF VCSPGRLQWF LYLTPPKDEP SNSPLRQILR CPIAFMTPSG ENILKGIWHI
KSPISSYFDI DIAGSGNLLP SIGSRAGLKH SHFAGAKVWS QINISSTDAA VENLEFDIRG
EYELLQGCGA ASGSLHKKMV PGCGPPVYFF LDPTEIGPTE FDSWVFALDH GRLDIGEPRI
TVAEMHPNWD SCTIAKEPKS VRCWFKKTAS DDAISLGVYP SPPPIYQTPT PQAIVRNIGS
KCLGSYVPML ISSVPASGAE LAWEPGTWRV SNLMESPTVL RKLAWLLQWA SSVDQFSEWN
SICLDGEEYS KKCGICAPRK PRLIWALDDK DRIYAYEDPE DAAVYEQSIK KRPATFLGFT
RLSHDSVLQI KLCLNVITLT HQARGKLAKW DEVSLQWRLC IDNVGFLRQR LPTLKEKNNK
ADTESTQPPG FKFFNLRPEQ LRSLTWMREQ EDIAQPFQEE EVVEAMLPAV NWRAEAKATV
KHLVRGGILG DDVGYGKTAI TLGLIDSQFS NDSKNVPTSV KGAIPIKATL IVAPHHLMDQ
WSREITKFLG KKYNILEIKS IASLRSLTIR RFETADIVLL STSVVRGASY YDRMELFAAS
PAVPKGDGRI FDEWLNDTMA AVRDHVDLLT TEGPEVVLQN MIRKRTNLKN SGIYSKFQPS
RRLKGQKFQD HLLKLKEQMR KIAGDGVAAD KIDSHSEPRL NNTPAKLRKT KRKIMEDYKE
DECTAKVPQS KKRKVKSNLA TEGLSNESDK TFQLLNCNGD WKRMRSPLIH MFEYSRIVID
EFTYSKDRNY SSVLAIPARS KWILSGTPPL NGFADVKSFS PFLGITLGVD DEEGRETENE
RLRSIQRDQT DAEQFQPFVT RHSAAWHRRR HNVAQGFLDQ FMRKNIPGID EIPWTEHICP
VILAPRERAA YLELFMQLMS QNLKLRRNGR GLYDSAAMSR NDAILGNSSG PEEALIKCSS
YFVPLERIMG KQLIDKTKSV ITDDTTTSSS ASSIFESDDG RSSMTCETDA TSVCSGEENP
LFARDTQFYA LALDIIEKLR HAFWLQSKLE TTTHFDTLIK HLERNGAGDL GVTSCFRNAI
TAARTAYTPE DGRYYYLTAQ EKKQTPSDIR IEYPTTQSEF ISDLNACTDS LRRLLEEALV
RVRAASLFVV VRSLQERQLE DVFACSSCFR RLACPTSLTI LGECGHAFCE SCIEIAKVEE
ACRLPACSGG AESFRMIKYS DISISNKDID KDTDNNANDE KWQGYGGTKL LELIRLVQDT
DRIAEDEQVL LFTQFPDLME AASAVLRKAN IPHLMVPATD RMASSKIAQF QTGTEKVKSK
VLILHLGDVS ASGLNLQNAN HVIFFHPLFA KSQYDYNSGM AQAIGRSRRY GQQKHVHIYH
FLALKTIEVN IFEQRRRERL VKREGGFLSV SSGDVLLPTD ESGWRGSSLD GSNAADI
//
