TF212_SCHPO
ID TF212_SCHPO Reviewed; 1333 AA.
AC P0CT41; Q05654; Q96TJ6;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2013, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Transposon Tf2-12 polyprotein;
DE AltName: Full=Retrotransposable element Tf2 155 kDa protein;
GN Name=Tf2-12; Synonyms=Tf2-43; ORFNames=SPCC1020.14;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP NOMENCLATURE.
RX PubMed=12952871; DOI=10.1101/gr.1191603;
RA Bowen N.J., Jordan I.K., Epstein J.A., Wood V., Levin H.L.;
RT "Retrotransposons and their recognition of pol II promoters: a
RT comprehensive survey of the transposable elements from the complete genome
RT sequence of Schizosaccharomyces pombe.";
RL Genome Res. 13:1984-1997(2003).
CC -!- PTM: Processing of the polyproteins proceeds by an ordered pathway,
CC called maturation. It involves the initial cleavage of a 27 kDa capsid
CC protein (CA) from the N-terminus of the polyprotein, followed by the
CC cleavage of a 56 kDa integrase (IN) from the C-terminus. This leaves a
CC 72 kDa protease-reverse transcriptase fusion protein (PR-RT), which
CC does not seem to be processed further (By similarity). {ECO:0000250}.
CC -!- MISCELLANEOUS: Retrotransposons are mobile genetic entities that are
CC able to replicate via an RNA intermediate and a reverse transcription
CC step. In contrast to retroviruses, retrotransposons are non-infectious,
CC lack an envelope and remain intracellular. Tf2 retrotransposons belong
CC to the gypsy-like elements (metaviridae).
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DR EMBL; CU329672; CAB60245.1; -; Genomic_DNA.
DR PIR; T38401; T38401.
DR RefSeq; NP_001018276.1; NM_001019831.1.
DR RefSeq; NP_587955.1; NM_001022946.1.
DR RefSeq; NP_593984.1; NM_001019410.2.
DR RefSeq; NP_594409.1; NM_001019840.1.
DR AlphaFoldDB; P0CT41; -.
DR SMR; P0CT41; -.
DR STRING; 4896.SPAC27E2.08.1; -.
DR MEROPS; A02.051; -.
DR PaxDb; P0CT41; -.
DR EnsemblFungi; SPAC27E2.08.1; SPAC27E2.08.1:pep; SPAC27E2.08.
DR EnsemblFungi; SPAC2E1P3.03c.1; SPAC2E1P3.03c.1:pep; SPAC2E1P3.03c.
DR EnsemblFungi; SPAPB15E9.03c.1; SPAPB15E9.03c.1:pep; SPAPB15E9.03c.
DR EnsemblFungi; SPCC1020.14.1; SPCC1020.14.1:pep; SPCC1020.14.
DR GeneID; 2538755; -.
DR GeneID; 2541833; -.
DR GeneID; 2541991; -.
DR GeneID; 3361422; -.
DR KEGG; spo:SPAC27E2.08; -.
DR KEGG; spo:SPAC2E1P3.03c; -.
DR KEGG; spo:SPAPB15E9.03c; -.
DR KEGG; spo:SPCC1020.14; -.
DR PomBase; SPCC1020.14; Tf2-12.
DR VEuPathDB; FungiDB:SPAC27E2.08; -.
DR VEuPathDB; FungiDB:SPAC2E1P3.03c; -.
DR VEuPathDB; FungiDB:SPAPB15E9.03c; -.
DR VEuPathDB; FungiDB:SPCC1020.14; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_000384_4_0_1; -.
DR OMA; NCISDER; -.
DR PRO; PR:P0CT41; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005634; C:nucleus; IEA:UniProt.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; NAS:PomBase.
DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.70.10; -; 1.
DR Gene3D; 3.30.420.10; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
DR InterPro; IPR024648; Pept_A2E_retrotransp.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR041577; RT_RNaseH_2.
DR Pfam; PF17921; Integrase_H2C2; 1.
DR Pfam; PF12382; Peptidase_A2_2; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SUPFAM; SSF50630; SSF50630; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00141; ASP_PROTEASE; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW Aspartyl protease; DNA integration; DNA recombination; DNA-binding;
KW DNA-directed DNA polymerase; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nuclease; Nucleotidyltransferase;
KW Protease; Reference proteome; RNA-binding; RNA-directed DNA polymerase;
KW Transferase; Transposable element.
FT CHAIN 1..1333
FT /note="Transposon Tf2-12 polyprotein"
FT /id="PRO_0000424430"
FT DOMAIN 266..342
FT /note="Peptidase A2"
FT DOMAIN 436..615
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT DOMAIN 979..1138
FT /note="Integrase catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT REGION 199..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 271
FT /note="For protease activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10094"
FT BINDING 502
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 566
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 567
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for reverse transcriptase
FT activity"
FT /evidence="ECO:0000250"
FT BINDING 990
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250"
FT BINDING 1050
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for integrase activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1333 AA; 154916 MW; B40D781E29577771 CRC64;
MSYANYRYMK ARAKRWRPEN LDGIQTSDEH LINLFAKILS KHVPEIGKFD PNKDVESYIS
KLDQHFTEYP SLFPNEHTKR QYTLNHLEEL EQQFAERMFS ENGSLTWQEL LRQTGKVQGS
NKGDRLTKTF EGFRNQLDKV QFIRKLMSKA NVDDFHTRLF ILWMLPYSLR KLKERNYWKS
EISEIYDFLE DKRTASYGKT HKRFQPQNKN LGKESLSKKN NTTNSRNLRK TNVSRIEYSS
NKFLNHTRKR YEMVLQAELP DFKCSIPCLI DTGAQANIIT EETVRAHKLP TRPWSKSVIY
GGVYPNKINR KTIKLNISLN GISIKTEFLV VKKFSHPAAI SFTTLYDNNI EISSSKHTLS
QMNKVSNIVK EPELPDIYKE FKDITAETNT EKLPKPIKGL EFEVELTQEN YRLPIRNYPL
PPGKMQAMND EINQGLKSGI IRESKAINAC PVMFVPKKEG TLRMVVDYKP LNKYVKPNIY
PLPLIEQLLA KIQGSTIFTK LDLKSAYHLI RVRKGDEHKL AFRCPRGVFE YLVMPYGIST
APAHFQYFIN TILGEAKESH VVCYMDDILI HSKSESEHVK HVKDVLQKLK NANLIINQAK
CEFHQSQVKF IGYHISEKGF TPCQENIDKV LQWKQPKNRK ELRQFLGSVN YLRKFIPKTS
QLTHPLNNLL KKDVRWKWTP TQTQAIENIK QCLVSPPVLR HFDFSKKILL ETDASDVAVG
AVLSQKHDDD KYYPVGYYSA KMSKAQLNYS VSDKEMLAII KSLKHWRHYL ESTIEPFKIL
TDHRNLIGRI TNESEPENKR LARWQLFLQD FNFEINYRPG SANHIADALS RIVDETEPIP
KDSEDNSINF VNQISITDDF KNQVVTEYTN DTKLLNLLNN EDKRVEENIQ LKDGLLINSK
DQILLPNDTQ LTRTIIKKYH EEGKLIHPGI ELLTNIILRR FTWKGIRKQI QEYVQNCHTC
QINKSRNHKP YGPLQPIPPS ERPWESLSMD FITALPESSG YNALFVVVDR FSKMAILVPC
TKSITAEQTA RMFDQRVIAY FGNPKEIIAD NDHIFTSQTW KDFAHKYNFV MKFSLPYRPQ
TDGQTERTNQ TVEKLLRCVC STHPNTWVDH ISLVQQSYNN AIHSATQMTP FEIVHRYSPA
LSPLELPSFS DKTDENSQET IQVFQTVKEH LNTNNIKMKK YFDMKIQEIE EFQPGDLVMV
KRTKTGFLHK SNKLAPSFAG PFYVLQKSGP NNYELDLPDS IKHMFSSTFH VSHLEKYRHN
SELNYATIDE SDIGTILHIL EHKNREQVLY LNVKYISNLN PSTIMSGWTT LATALQADKA
IVNDYIKNNN LNI
