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
//