ID A1DL19_NEOFI Unreviewed; 2076 AA.
AC A1DL19;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=tRNA-splicing endonuclease, putative {ECO:0000313|EMBL:EAW15490.1};
GN ORFNames=NFIA_048270 {ECO:0000313|EMBL:EAW15490.1};
OS Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=331117 {ECO:0000313|EMBL:EAW15490.1, ECO:0000313|Proteomes:UP000006702};
RN [1] {ECO:0000313|Proteomes:UP000006702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 /
RC NRRL 181 / WB 181 {ECO:0000313|Proteomes:UP000006702};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027698; EAW15490.1; -; Genomic_DNA.
DR RefSeq; XP_001257387.1; XM_001257386.1.
DR STRING; 331117.A1DL19; -.
DR EnsemblFungi; EAW15490; EAW15490; NFIA_048270.
DR GeneID; 4583901; -.
DR KEGG; nfi:NFIA_048270; -.
DR VEuPathDB; FungiDB:NFIA_048270; -.
DR eggNOG; KOG1801; Eukaryota.
DR HOGENOM; CLU_000459_2_0_1; -.
DR OMA; PWHQSEL; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000006702; Unassembled WGS sequence.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
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 Endonuclease {ECO:0000313|EMBL:EAW15490.1};
KW Hydrolase {ECO:0000313|EMBL:EAW15490.1};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Nuclease {ECO:0000313|EMBL:EAW15490.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006702};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 1924..1937
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1941..1957
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1009..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1827..1891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1973..2076
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1476..1503
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1840..1873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1973..1993
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2008..2038
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2039..2055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2076 AA; 232681 MW; F6A9000BFBBD3C20 CRC64;
MDFMDIVGEL RALPDNVHIL CPRQHDDDHG RYDDPNEIDD TGKSAAELVA EANSRREKFL
SCMRILAYNQ EGVEELQTWI WRKLDDALEK CDLCIKQYYT GKIWLMEQLK ENYDDEDIEK
FARMLDDWDV KRITKNLAMA TAKLKEVPPQ EIGLHVLDRA SLLSIFESLS CEAMLRNDAL
LQEHFDEPFR LIQTKRSLKV SDYVPAVTRF LFDSKQSRSF WAIHSWMRYS RPPTALEFDW
AIKEGLLDML KTASQQPPQI AVIQRLWRGM QLVVKRLDKD QITHHLRALE IDPCRLSVEH
LGIQSPGLRF LLNTIQIFLE KAPGDFWDAM QTISPQAIIE LVFYNPQLEA FLMQISEGEP
YEKSALKDML SWVDPFMSSL KGAHQPSACR SLVYQLLDRL QNPRFPDLAR YHCFHVGLAS
LLQTLRSFTD NESSRGSVAR IVLSETMGVV SANIETILKP PKFAVEQRRQ EEISSLCMDV
IRNTLALECQ SLKSDYEVIL RQNSLQHGVS TYSAPIWDAV VRNLHEDNLA LSTSALLGIL
PLVGLETFPT KGESSPEKTH FNLIYGHLTR LSCQIIERLA DFEPEHLNEL FKSQDTSSAL
ISALFAADLD TYQAAVDLIK NMSGQSARRD AISHLLQSFF ITTMYGLSWS FRRISNMKTF
ASAPRMLHTG TDIIDILCDS QTGMLRTRKL ADRREILSLQ KLWEYLWQAL STIFDETEAW
HLRGNDKAVM LEFCRDTIQF ADLLFDQYGV FLSAVVDADP SQEASARENL LKSPTTTMSA
MVKWLRLKDE YLATTLVGLV AKLLRRLGEL SVTTVKDDAL SFIEGVAVKS TIKTILTLRE
KAELVRALEA YYKKPVVTAS TASLKKQSMI TAFAKPAEVS ATPSPAKTTS EDEFDEDNVP
DDVLMQLSRS VELNKERLVA EARRRADKAA KALPAIPKPS AAPLKPNVTV QSFREKREKE
KEAKRKRDLA ELARLKKNLP ARGVGEQTAE QGSGLSGIGV KGKVHTTTEE SMMVSSGSES
ESESDDELDK ELFGPKARSK PDAIKAYEES KKLSLKQQGP VKKIKQVRSA KDMRARLAPD
LSSLHRTILA WDFFANGDLP PNSGRTDYSL VSNTFRDPIE YQKTFEPLLI LEAWQGFNST
KEEGTFRPFE IKVATRLSVD SFVEVSTVLP SLEVKDLGLG EADIVLLSKS SRPTSDSSAP
HCFARVAGIN KKRGTVEISY RVNPGTSFIN SLGPGVTIWG AKITSLTPLE REYGALMALQ
YYDLCEEVIK AKPSPILHYS DASLKPIADN YNVNPAQAKA IKSALDNDAF TLIQGPPGSG
KTKTIVALVG ALLSNVLGDQ GVTISRPMGV ANPRVPVRTT TSKKLLVCAP SNAAVDELVM
RFKEGVKTIH GRHEKLNVIR LGRSDAINTN VLDVTLDELV NARLSQNPRK DSGQRDLQTI
YMEHKAADTA FKETRAKIDQ CRAQGLPVPE ELEREFDLLK KKKTQLSQEI DTARDKNHSA
ARDADLNRRR IQQEIINGAH VICATLSGSG HEMFQNLSIE FETVVIDEAA QSIELSALIP
LKYGCSKCIL VGDPKQLPPT VLSKVASKFQ YEQSLFVRMQ ANHPRDVHLL DTQYRMHPEI
SVYPSAAFYD GKLKDGPNMA KLRARPWHQS ELLGPYRFFD VQGLHQNTTK GHSLINLAEL
RVAMQLYERL ISDFRDYDFS GKIGIITPYK GQLRELKTQF AARYGNSIFN MVDFNTTDAF
QGRESEVIIF SCVRASNKGI GFLADIRRMN VGLTRAKSSL WVLGNSQSLM QGEFWNGLIK
DARRRNVYTD GDILDILQRP QFTGYKDIDM MDADSPNPTV SLKAAGSEPV SRPTSASLER
PTSESSISAS VSRRGTPIEP PPDLPSGGPN GLDDTRTCGY CGSFAHMTHN CDNIDAKEAS
RGTCYRCGRS GHTRMVCTAE RCLQCGEFGH DAQRCQSARE LPKKEKIRIA REEHQHAQMK
KQRTERQRQK QLGGHDPKVP VLQVSSDPPP REDKKPEKRR PDQSNAPGKR KRTGSESPDT
SKVSKPRSSD SVPNPPKGSR RKIDANVPTN AAVSLD
//
