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Database: UniProt
Entry: A0A178E5K2_9PLEO
LinkDB: A0A178E5K2_9PLEO
Original site: A0A178E5K2_9PLEO 
ID   A0A178E5K2_9PLEO        Unreviewed;       974 AA.
AC   A0A178E5K2;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OAL50965.1};
GN   ORFNames=IQ07DRAFT_630931 {ECO:0000313|EMBL:OAL50965.1};
OS   Pyrenochaeta sp. DS3sAY3a.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC   Pyrenochaeta.
OX   NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL50965.1, ECO:0000313|Proteomes:UP000077535};
RN   [1] {ECO:0000313|EMBL:OAL50965.1, ECO:0000313|Proteomes:UP000077535}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL50965.1,
RC   ECO:0000313|Proteomes:UP000077535};
RG   DOE Joint Genome Institute;
RA   Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA   Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT   "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT   ascomycete fungi.";
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; KV441643; OAL50965.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A178E5K2; -.
DR   STRING; 765867.A0A178E5K2; -.
DR   InParanoid; A0A178E5K2; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000077535; 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:SF11; FAMILY HELICASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G06590)-RELATED; 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   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
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:UP000077535}.
FT   DOMAIN          400..595
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          823..974
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          124..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..143
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   974 AA;  111460 MW;  581A911812800379 CRC64;
     MRIEQRQLRH IPKALLTCQP PLFHIIHPTD LPQALDDTIM ALKHLLNDDS LEADFGSFSC
     ERDFDFSHEA IPHLQQQSWG EYAGEVFGTQ SSSEDLENTF SMYESLQSTQ SQIEQWIADP
     AIIPPEAAPE EPEKETREEP QEEPDICYGT LYGIRVQLCG DMTELLRRLS MSNKSPIPGH
     VQVKLVKLET GFSIVFEDLT AIGAVNAQLE KALKKIEEHQ YSLNFDVFAP INLLKDTIGR
     VSKEKEAVVR VQITVYGPSS AAQGVGKELS SHKLYLQQAE YIKEGTKYDN PHVLVLPSFQ
     HSTTQIQVAT EETQVEKTTT EVLKNTITDV FSSLTRSHDL RGVEADERLI TPLLLHQKKA
     LDFMMQRENG PIPEKYQLWK ATEVDGVPGH RHSVTQGIIH REPIETGGGI LADEMGMGKS
     LSVLALILRT LDAAHQWAME HRETTTEESR AWRIRERSRA TLIVASSDLM INQWFEELDL
     HFDDHTRKAL TKIKYHGQNR DKHHGQNGIT VPNKLCDADI VITTYHTLAS DISHVNDIEW
     YRIVLDEAHI IRRQATKFYR TCSGIDARSR WCLTGTPIQN RLDDIGSLFA FLKIAPFHNL
     SNFRKFISVP FDEGFKRRKL AIQRFTTLFD SLCLRSKKEE LEKHLPDQLS RVRSIELSSE
     ERTQYDHTND IMFRAVRNQN GEVDTRSTLG MFQVQLQLRI ICNHGTWQQP FSWTRRKLYL
     QDEREALETS LEKDGEKNCF ICKQSMPIYN TGSTFRHFEG NCHVICSQCL EQSLPSSQET
     LPTKCPVCYP LWKQFEGTPQ NRPTALEDTY FRAEGQSSKM EALMRDVLTD LSTTKSIIFT
     CWTRTLDLLE IYLQRASLTA HNYQRIDGES TTSKREKIIH EFANSPHLRI LIMTTGTGAV
     GLNLAMANRV FIVEPQWNPS VENQAIARAS RLGQQQPVLV TRYVVNQTVE TNMQWLKAKK
     EEAANIVETQ DQKQ
//
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