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Database: UniProt
Entry: A0A0F4Z202_TALEM
LinkDB: A0A0F4Z202_TALEM
Original site: A0A0F4Z202_TALEM 
ID   A0A0F4Z202_TALEM        Unreviewed;      1484 AA.
AC   A0A0F4Z202;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   03-MAY-2023, entry version 33.
DE   SubName: Full=tRNA-splicing endonuclease {ECO:0000313|EMBL:KKA23893.1};
GN   ORFNames=T310_2077 {ECO:0000313|EMBL:KKA23893.1};
OS   Rasamsonia emersonii CBS 393.64.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX   NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA23893.1, ECO:0000313|Proteomes:UP000053958};
RN   [1] {ECO:0000313|EMBL:KKA23893.1, ECO:0000313|Proteomes:UP000053958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA23893.1,
RC   ECO:0000313|Proteomes:UP000053958};
RA   Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA   Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKA23893.1}.
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DR   EMBL; LASV01000083; KKA23893.1; -; Genomic_DNA.
DR   RefSeq; XP_013330505.1; XM_013475051.1.
DR   STRING; 1408163.A0A0F4Z202; -.
DR   GeneID; 25314428; -.
DR   OrthoDB; 170190at2759; -.
DR   Proteomes; UP000053958; 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:SF495; 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; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Endonuclease {ECO:0000313|EMBL:KKA23893.1};
KW   Hydrolase {ECO:0000313|EMBL:KKA23893.1};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Nuclease {ECO:0000313|EMBL:KKA23893.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          1294..1310
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          233..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          286..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          345..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1193..1241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1328..1442
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1463..1484
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          834..861
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        308..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        383..411
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1213..1227
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1328..1348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1427..1442
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1484 AA;  163954 MW;  0558AC1B7BB81A42 CRC64;
     MYGFSWSFRR ISNMKTFASA PRMIHTGTDI VDILCDTQSG MLRTRKLADR REALALQKLW
     EYQWQALTTI FDETESWHRR GNERSVMLEF CRDTIQFADL LFAQYGVFAS AVVDADPALE
     ASARENLLKS PTATMSGMVK WLRLKDEYLA TTLVGLVSKL LRRLGELNVT TVSQDALDYI
     DGVAVKSTIK TILTPREKAE LVGALEAYYK KPVVTASTAA LKKQSTITAF AKPVDTSGAS
     TPSRATSEDD FDDSGVPDED LLQLSRSVEL NKARLAAQAQ KKAEAAAKAP LALPKPSKAS
     AVSTASIESF REKREKEKEA KRKRDLAELA RLKKNIPVHG VAEQTAGQGS GVNGIGVKGK
     DHTPVDSMMV SSGSESESQS EDELDKELFG KRVTSKPDAV REYEESKRRS LKHQGPVKKV
     KQWRSARDMR ARLAPDLSSL HQRILSWDFF ASGDLPPNAE RTDYTLVSST FRDPIEYQRT
     FEPLLILEAW QGFQSAKEDG TFKPFEITVA SRLSVDSFVE VSTSMKIPDM KEFGLGEADL
     VLLSKSKDPL NDSAAPHCLA RVSGINKKKS SVEVSYRVVP GTPVVPLLAP AVTLWGARIT
     SLTPLEREYG ALMALQYYDL CEEIIKAKPS PILNYTEANL KPIIDNYNVN PAQAKAIKSA
     LDNDAFTLIQ GPPGSGKTKT IVALVGALLS NSFSNQGPGV AISRPGENKA PNQAARTTTS
     KKLLVCAPSN AAVDELVMRF KEGVKTLQGK HEKLSVIRLG RSDAINTNVL DVTLDELVNA
     RLNQTSRKDS GERDLQKIYE EHKAADTAFK EVRSKLDRCR AQGQPVPPEL EREFDLLKKK
     RSQLSQEIDN ARDRNHAAAR DADLTRRRIQ QEIIDGAHVI CATLSGSGHE MFQNLSIEFE
     TVVIDEAAQS IELSALIPLK YGCSKCILVG DPKQLPPTVL SKVASRFQYE QSLFVRMQKN
     HPDDVHLLDI QYRMHPEISR FPSIAFYDSR LQDGPNMAKL RNRPWHESEL LSPYRFFDVQ
     GLHQSAPKGH SLVNMAELNV AMQLYERLVT DFQGYDFTGK VGIITPYKGQ LKELKSRFAA
     KYGNSIFTAV EFNTTDAFQG RESEVIIFSC VRASNKGIGF LADIRRMNVG LTRAKSSLWV
     LGNSQSLVQG EFWEKLIIDA KERNVYTDGD ILQMLRRPQF TGYRNVEMVD ADLDVPMESP
     PGPSMEPSAG PASVGRPSSN ELESVSARNT PAPLPEGPSG GFNGLDETKT CGICGSFEHF
     THNCDNTEAK EASRGICHRC GIAGHSKVNC TTERCIQCGE FGHTAQQCTS TVLLSKEKKN
     KIAKEEYRHK RLQQERREQQ KQRQLAEHDP KVPVVQVSTK SPPPSTKSPP PSTKRKLESN
     EPAPAPKIAK RKVDTRTPQP PSDLVKPSRD GPSFQTIAHD DKAAAGSGTT PDTSNNSNKV
     RQSFSSISRG AIWALIQCLG STTTATSRRA EAHQRGASAN AYAP
//
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