ID A0A0H1BNI2_9EURO Unreviewed; 1274 AA.
AC A0A0H1BNI2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Helicase C-terminal domain-containing protein {ECO:0000259|PROSITE:PS51194};
GN ORFNames=EMPG_12310 {ECO:0000313|EMBL:KLJ12678.1};
OS Blastomyces silverae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ12678.1, 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 -!- 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:KLJ12678.1}.
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DR EMBL; LDEV01000750; KLJ12678.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H1BNI2; -.
DR STRING; 2060906.A0A0H1BNI2; -.
DR OrthoDB; 101644at2759; -.
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 CDD; cd18008; DEXDc_SHPRH-like; 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 InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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 PANTHER; PTHR45626:SF52; SNF2-RELATED DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 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 PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
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:UP000053573}.
FT DOMAIN 929..1084
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1126..1181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 867..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1274 AA; 141884 MW; 510C41ACABAE5F72 CRC64;
MSFSGIDAVL PTNGLPQDSP LAQQLQSAIA DILPDELATP SSSSSTQSRA TSPSAPSVTS
SFGSSPPTPH RPVTDLTLEK ENLLGDLNHF IPVGILQRYD ELDNNHQPSV IDQGSVSPYP
SAALSQLEQN NWIRTSICRN KKFPGWSAIR IYVLPDDIGR KHIHRSSGVL RGCLKVVMSK
VDTSAAAWEG NFDPYAQPVA RSAEVESLFY IFNTLESPTP DIDKVSDPHA RAAIEEVLWK
EGDYVDGSDE DIGVIGLKTP LYTYQRRSAA YMIQRESEPA QMLDPRLQVL HGPTGQPYYY
DKEEGSILHE KRLYSEACGG ILAETMGYGK TLICLAVILA TRGHFPRIPI TCMEGLHPVR
EKTASLLEMA AATAGRFSLP WKSYFERLEA SGMHFEKCIS ACESNRGSYA MPRPPQRYKS
REVAVKLTPT KLRLCSGTLI VVPPNLVDHW LSEIDKHTQG LKVLVLRDSR RSTPPPEKLL
EYDILLFSKS RFEKEAGGGG GGGRSAGFAT EPQKDSPLKR LHWLRIIVDE GHNFAAKGAR
TTAVHALSQL HVERRWVVSG TPSRGLYGIE VALASQESAE GGCEKQGDAS SILQARKVPT
NVMEEELKNI DKLRSIVVDF LALKPWSNSR AEDPANWAKY IKPVGLDGNR RTSPSLRSTL
QSLVVRHRAE DVNRDLTLPK LHNKVTYLEP TFYDKMSLNL FIFTLTVNTI TSERTGEDYM
FHPKNRKLLA VLINNLRQAG FWAGFEKNEV QKTVDLAREY LGKNSHRIDA GDKRRLSEAI
IVTEKAINCR SWDALSKFTE LGVFLDEFPD HARAEWAIDD NNGHSEPLLL GISQARHAQK
FVASHLCAFD PSEGIAGAGI RARSQMKERG NVPDKKSNDT LVHRPKPEGI EISPSKKSFS
LGRVKRLSPE SPLNKTKLVA TASAKLTYLL DKVLEFQEQE KIIIFYEGNN TAFYIGEGLE
ILGVQFRIYA NTLNTKTRSA YLSLFNKTET VRVLLMDLRQ ASHGLHIACA SRVFIVNPIW
DPNIESQAIK RAHRISQTKP VYVETLVLKG TLEDRMLRRR KQMTNAELRH AEKDPLDDQT
MSSIIQNEEV IPIPETDASE RPAYLKIPVG FFDRHTLPIP DDYQEVGQVS PVSLPPPPSA
PAPVKVATPT KKRKPPNDLP WIESDVQASS NSSPNIRKQR RLNGRLETIN GIIMEAPRTR
TPPSRRDSVP RVTLHTNEGP SPANNTHDFP VSYDGPSDTV EDLPLSEEDP EAHLFENLSP
FGAGFFRTGN SFLN
//
