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Database: UniProt
Entry: A0A2T5LRM9_9EURO
LinkDB: A0A2T5LRM9_9EURO
Original site: A0A2T5LRM9_9EURO 
ID   A0A2T5LRM9_9EURO        Unreviewed;      2137 AA.
AC   A0A2T5LRM9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN   ORFNames=P175DRAFT_0442009 {ECO:0000313|EMBL:PTU18943.1};
OS   Aspergillus ochraceoroseus IBT 24754.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=1392256 {ECO:0000313|EMBL:PTU18943.1, ECO:0000313|Proteomes:UP000244073};
RN   [1] {ECO:0000313|EMBL:PTU18943.1, ECO:0000313|Proteomes:UP000244073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 24754 {ECO:0000313|EMBL:PTU18943.1,
RC   ECO:0000313|Proteomes:UP000244073};
RX   PubMed=29317534; DOI=10.1073/pnas.1715954115;
RA   Kaerboelling I., Vesth T.C., Frisvad J.C., Nybo J.L., Theobald S., Kuo A.,
RA   Bowyer P., Matsuda Y., Mondo S., Lyhne E.K., Kogle M.E., Clum A.,
RA   Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA   LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA   Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R.;
RT   "Linking secondary metabolites to gene clusters through genome sequencing
RT   of six diverse Aspergillus species.";
RL   Proc. Natl. Acad. Sci. U.S.A. 115:E753-E761(2018).
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:PTU18943.1}.
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DR   EMBL; MSFN02000007; PTU18943.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:P175DRAFT_0442009; -.
DR   OrthoDB; 170190at2759; -.
DR   Proteomes; UP000244073; Unassembled WGS sequence.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd18042; DEXXQc_SETX; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR024481; Helicase_Sen1_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10887:SF525; HELICASE SENATAXIN-RELATED; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF12726; SEN1_N; 1.
DR   SMART; SM00343; ZnF_C2HC; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50158; ZF_CCHC; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          1921..1934
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          1938..1954
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          930..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1846..1886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1963..2137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1473..1500
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        949..973
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1846..1872
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1963..1990
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2008..2043
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2087..2111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2137 AA;  238745 MW;  095DB93E4ED8E6C9 CRC64;
     MEFMDIVAEL QALPNDVHIL CPRQHDDDHA RYDDETEVDE SGKSVAELVL EANTRREKFL
     SCMRILAFNQ EEVEELQNWI WRKIDDALEK CDLCIKQYYM GKIWLMDQLK ENYDEEDIEK
     FSRMLDEWDI KRITKNLTTA TTKLREVPAE QIGLHVLDRA SLLSIFETLS CDAMLRNDSL
     LKEYFDEPFQ LIQTKRTLKV SDYIPAVSRF LFDPNQSRSF WAIHSWMRYP RPPTTAEFDW
     AIKEGLLAAL RTASQQPIQV AVIQRLWRGM QIVVKRLDKD QITHNLRALE IDPCRLSVDH
     LAIQSPGLRF TLNTIQTFLE KAPGDFWDAM QTISPQAIVE VVFYNPQVDA FLTQATDGEP
     YEKSAMKDIL SWVSPFMSSL KGAHQPTACR SLVYQLLDRL QDARFPNLAR YHCFHVGLVS
     LLHTLRSFTD HEASRGSVAR VVLSETLGVV SEHINKILKP PQFAVEQGRQ REIKSLCMDV
     IRNTLALECQ SLKSDYEVIL RQNSLQHGVS TYSSTIWDAV VQHLHEDDLA LSTSALLGIL
     PLVGLEKFPT KGESSPEKTH FNSIYGHLTH LSCQIIERLA DFKPDHLDEL FKSQDTGSAL
     ISALFAADHN TYQAAVDLIK NVSGQSARRD AISHLLESFF TTTMYGLSWS FRRISNMKTF
     ASAPRMLHTG TDIVDILCDS QTGMLRTRKL ADRREILSLQ KLWEYLWQAL TTIFDETESW
     HLRGNDKAVM LEFCRDSIQF ADLLFSQYGV FLSAVVDADP NQESSARENF IKPPTATMSG
     MVKWLRLKDE YLATTLVGLV AKILRRLGEL SVTTVKEDAL NFIEGVAVKS TIKTIITPRE
     KAELVRALEA YYKKPVVTAS TASLKKQSMI TAFAKPAEPS ASPSPSRTAD EFEEADLSDD
     VLLQLSRSVE LNKERLAAEA KKKAERAAKA LPVIPKPAPA PPKSNLSVQA FREKRERERE
     AKKKRDLAEL ARLKRGAPPH GVAEQTAHQG SAIAGIGIKG KDHTPAESMM VSSGSESESE
     SEDELDKELF GPKTGSKPDA VKAYEESKRM SLRQQGPVKK IKQVRSAKDM RARLAPDLSS
     LHRTILAWDF FAAGDLPPNS GRTDYSLVSN TFRDPIEYQR TFEPLLILEA WQGFRSSKEE
     GSFKPFEVKV ATRLSVDSFV EVSTVMPALE VKDYGLGEAD IVLLSKGNSP ATDSSAPHCL
     ARVSGINKKK GTVEVSYRVN PGIPFINSLG PGATIWGAKI TSLTPLEREY GALMALQYYD
     LCEEVIKAKP SPILNYSDAS LKLVADNYNV NPAQAKAIKS ALDNDAFTLI QGPPGSGKTK
     TIVALVGALL SGVLGEQGVS ISRPSATSST RGPARTTTSK KLLVCAPSNA AVDELVMRFK
     DGVKTITGRH EKLSVIRLGR TDAINTNVLD VTLDELVNAR LNRTSRREGG EVDLQKIYME
     HKAADTAFKE TRSKIDQCRA QGLPVPLELE REFDLLKKKK TQLSQQIDNA RDKNHSAARD
     ADLNRRRIQQ EIIDGAHVIC ATLSGSGHEM FQNLSIEFET VVIDEAAQSI ELSALIPLKY
     GCSKCILVGD PKQLPPTVLS KVASKFQYEQ SLFVRMQANH PRDVHLLDTQ YRMHPEISVF
     PSTAFYDGKL QDGPNMARLR ARPWHQSELL TPYRFFDVQG MHQSATKGHS LINIAELKVA
     MQLYERLVTD FRDYNFSGKI GIITPYKGQL RELKNHFAAK YGNAIFSMID FNTTDAFQGR
     ESEVIIFSCV RASNKGIGFL SDIRRMNVGL TRAKSSLWVL GNSQSLIQGE FWNSLIKDAR
     RRNVYTEGEI LKVLQKPQFT GYKNIDMVDA DASESAVPSR AASAASISRP SSASLDNLPS
     QSPFSATASA KGTPPASLPD GPSGGPNGLD ETRMCGYCGS FTHMTHNCDN EEVKEMAKGT
     CYRCGEPGHT RFACAAERCT ECGQFGHASN SCRSTKVLPK HEKNRIAREE YNHARNQKQR
     TEKQRLKQLG GHDPKVPVIQ VTTEQPANDN RKSERPRPDH AAGSSKRKRT DSPVADASKS
     ARPRKFEQGA PPTGPKNQRH KIDANIPSNT ENLVKPSRDG PAYTPLSGKP LSSTPSGPDP
     TRQAPRQPQQ RPSNGTRPPP PMRKRKEVDP FIRPKRR
//
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