ID A0A3M2TDR7_9EURO Unreviewed; 2050 AA.
AC A0A3M2TDR7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Helicase C-terminal domain-containing protein {ECO:0000259|PROSITE:PS51194};
GN ORFNames=PHISP_01213 {ECO:0000313|EMBL:RMJ27945.1};
OS Aspergillus sp. HF37.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1960876 {ECO:0000313|EMBL:RMJ27945.1, ECO:0000313|Proteomes:UP000272442};
RN [1] {ECO:0000313|EMBL:RMJ27945.1, ECO:0000313|Proteomes:UP000272442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF37 {ECO:0000313|EMBL:RMJ27945.1,
RC ECO:0000313|Proteomes:UP000272442};
RA Tafer H., Lopandic K.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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:RMJ27945.1}.
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DR EMBL; RAQS01000030; RMJ27945.1; -; Genomic_DNA.
DR STRING; 1960876.A0A3M2TDR7; -.
DR Proteomes; UP000272442; 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:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 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 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
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:UP000272442};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1872..2037
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1351..1389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1692..1747
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1365..1384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1693..1720
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2050 AA; 229363 MW; C29F718A657B4ABF CRC64;
MPPKRKKTPS LPVSQSQIPK KPRLDTHLPS PSPTPTEEDA AIPERVDSRH LFGGPGSRAK
LALDLPPMHS LDDIYASMIS HAMANGLGGF LGHMDRPLRV ATVCSGTESP LLALEMVQRC
MRDRYSQPFD FEHLFSAEIV PFKQAYIERN FKPPLLFRDV AQLKDGVAQT AYGSLRKVPR
DMDILIAGFS CVDFSALNCK RKKLDENGES GGTFMGIINY ARSYRPRMVV LENVKSCPWD
EVAAYWQGLG YLATHVAADT KDFYIPQTRV RGYMFCIDET ALAGSGLDGS AIMDHWRDTF
TSFKRRASSP AGMFLLDTDD RRLEQIESDM ALRINATNPR VAADWTKYQN RHRGYREDNK
LGDKRPVSKS GGHATCQMPD FAWHVWARAS VERIWDTLDI NFLRKLQAGY DMNYKERYLD
LSQGVEREID SRPYGIIGCI TPCGIPFVTT RGGPLSGRES LSLQGLPIDR LLLTRETQRE
LQDLAGNAMS STVVGAAVLS ALMTGYKTLR RGASPVSLKE NEDTTQIVPM DKYDLVQNDM
CLDTAGEDID IAQLQAHAAQ TARYCTCERQ SRVKPNILAC TLCGHTACSD CAWNPTHSFK
LASDLPRSQP VDFVGTLKRI LPTRLVFSGL SESDFDILKA EPTPFDPDTW AAFLRSVMQT
VGDELRFSDI KRSEVWTVVY SGRFSVLKLV LGAAASTWLL FAKPPDSEPV SSLSRVILGK
PIARMIPASD SILSGDWEIC APLSAKREMT IHGTGARVTS YEHACGLKMA EHRASKVWSD
LVVDGSEKSV KDLDADIRGI YTRLPYCGMA NATLHKKPAT QDSPAVYLFL DPSKYGSPEG
DMFVFSFEHT RIPGYEPRLS IAQVSHTWRS SEASYQPEPV SVYHRKWIKA RSAVLQPYAS
DAHISCRSLK PGTCISIGDE GCHHANVTIL SLSAPATAIE ALWQEGPWEA ADPAHAASLE
SQISWIVQRA AGFSDFQDWT EVEYFGPLTE SNAPCAVCAP PKPRILWTRG PKGIKGYEHP
QDAAVYERLS KSKPSPFLVF RRVDENGVGD LRVTLNIQTL LHRAYDKLVG SRVDNSASFR
WRLVPNAYDS KTLLPKFALT GNQTDQQARP PRFRIELRPE QQRSLFWMMS QEDDNRPFEQ
EETEEVFLPL TTWRAEGRVT VHKQVGGGVL ADEVGYGKTA IVLALIAAKY DVDKPGTPGS
DLIPSKATLI IVPEVVISQW RSEIAKFMDI RREDVLVLPD VKTLTKTKVR AVRDARIILV
PSSLLSSQSY YQKMNDFTGM PEVPARPGRN FDHWFKDAQG SLRDHVQVLM NDGPLDLLDA
IHTRREEVHN NHTDCTYEPS KRFRGQQYAK AQSRKLNMVD ESSTGSEEPA EKVTTDRKSK
PSGSRTNGKL EFNIANANPA QDFGDVQITL LHAFSFARLV MDEFTYADQD RLAPLFALQA
HSKWILSGTP PLNDFADVNT IAPFFGLHLG VADDELSPGS KRPKHELGVE NFQSFKEPHS
GAWHLNRHSI AQRFLGRFAR RNVAEINEIP FTEHVVLVDQ SPAETVLYLE LHMRLMAQKD
QYRRIGKIKH SNDRLQKLKE IINASKTPRE ALIKRGSCLV LQGSWTNRLE ITLESLIALR
RAEIDGLQEL FQEKLRLANW IYFHQELRDK RYQNFIADVF QNQFGNEVLD TDVFQAIKES
LFGSQDTAAL DDWTRHSSSR EADNRNIESA EHQQDESGQR DPDTFEEDSE SETSSDENDI
PKNPETLADF ECANRKTVGG MRSVLRKWVR QAGALRFPES VRLVQLSTDV PGCNACESQP
DVLASISVLG SCGHVLCRDC TSVTMHSEEC AVDGCTASVK EFEVIKGQEI GRWNGAAVPK
GLGQCSKYGG SKMDKLVEVI QGTPQEDKVL LFIQFPDLVE VACMALEVAG IKHQRVTASK
HALFRQDEKL IAELNQHKVL ILNLGTDTAA GLNLQHANHV IFLAPMLCDT QYNYESSMCQ
AIGRARRYGQ SKHVHVYHLL AKRTIDVSIY QGDRILIERD GQGMLVTPGE ASVDELKGCQ
GPVFEEYQKE
//
