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Database: UniProt
Entry: Q2HHR9_CHAGB
LinkDB: Q2HHR9_CHAGB
Original site: Q2HHR9_CHAGB 
ID   Q2HHR9_CHAGB            Unreviewed;      1967 AA.
AC   Q2HHR9;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 88.
DE   RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE            EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN   ORFNames=CHGG_00235 {ECO:0000313|EMBL:EAQ92000.1};
OS   Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS   NRRL 1970) (Soil fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=306901 {ECO:0000313|EMBL:EAQ92000.1, ECO:0000313|Proteomes:UP000001056};
RN   [1] {ECO:0000313|Proteomes:UP000001056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970
RC   {ECO:0000313|Proteomes:UP000001056};
RX   PubMed=25720678; DOI=10.1128/genomeA.00021-15;
RA   Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT   "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL   Genome Announc. 3:E0002115-E0002115(2015).
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DR   EMBL; CH408029; EAQ92000.1; -; Genomic_DNA.
DR   RefSeq; XP_001219456.1; XM_001219455.1.
DR   GeneID; 4386591; -.
DR   VEuPathDB; FungiDB:CHGG_00235; -.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_000384_38_3_1; -.
DR   InParanoid; Q2HHR9; -.
DR   OMA; HRTHASG; -.
DR   OrthoDB; 1837738at2759; -.
DR   Proteomes; UP000001056; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   CDD; cd00024; CD_CSD; 1.
DR   CDD; cd00303; retropepsin_like; 1.
DR   CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR   CDD; cd01647; RT_LTR; 1.
DR   Gene3D; 1.10.340.70; -; 1.
DR   Gene3D; 2.30.30.850; -; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR041588; Integrase_H2C2.
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; IPR041373; RT_RNaseH.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR24559:SF425; RT_RNASEH DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24559; TRANSPOSON TY3-I GAG-POL POLYPROTEIN; 1.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   Pfam; PF17917; RT_RNaseH; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   SMART; SM00298; CHROMO; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF54160; Chromo domain-like; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50013; CHROMO_2; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50878; RT_POL; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001056};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transposable element {ECO:0000256|ARBA:ARBA00022464};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          364..379
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          958..1138
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          1538..1700
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   DOMAIN          1862..1920
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   REGION          110..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          378..411
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          433..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..780
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1909..1967
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          64..105
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1730..1757
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        433..450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1967 AA;  222458 MW;  A333CC8E44CF9659 CRC64;
     MGDIIAKLDG NAFPSLKNFF QSLRAEVTGS EATAGLIDTM QRDATGREFL KIIDNVVGTQ
     NSRYNNLQAN ADSLQATVNN GAAELAQYKE ALTKARAERD TWEKAAGRIR AGSGDTPVDR
     DGSMPHPTPF TGDEMDTAKR TSQFRTWQTR IMGRWVSRPQ EFSTEGKKII YASALLEGSA
     AAGVFKGVEK VTASPDNSDD WPWKTATDFM NHLARKYATM DLAANAENKL RSLSQKDQFA
     AFTDFLTEYT NLTDVCDWDD TARVRGFRER LSRRMRDALN MQINTPERHD FEGWVTMAQK
     LAINMEGEDH LRKAVSGDNS NQNRNHNNGG KARDADAMDL DQMRVKMAKI PEEEKLRRVN
     DGLCFNCGKA GHQARLCRSP TNTGRNGRGG ARGGGQRGGY HDRYGNQGQP QAYYGSQQGD
     NGNQFGGAYQ QPWGLSGPGN NPNTNNGAYH GNHRGAPARR GGMHDGYRGD YRGGYKPQVR
     FMDVQNPGRV VGEVDPEGSW GGDGQPATGI VLAGADDRLV ISAIGQKNSI TLSSYLLVNG
     RAIPCVSLVD SGCTGLAFLD FKFAVRHHIP LTKLRERKPL FLADGALSSW IEWKTEVGLV
     VGDHRERLQF YITTLAEDNP VILGLPWLSK HNPAVDWKNL SLTFGEDCRG RCLPLQMAGL
     TAPTNTKKQF HARVEDAEDE GEPGEHIEVS IGQRSAEQRT ARSRRRRDWR HRQQLARHRD
     AAEARGGPRW TLAPPHARAR LIPNQPSHTP QQARKAAGRR VSPVRQGRPP LVTATPPRTG
     RIDGKDIKLL NAPNFALFCR QKGVTAMRIT FGELEEAMRA APDTELPNLS DSFFKNLLHR
     GGKADDYKAQ LPTDFHDFID EVWRDGPTMR RITEEDARKF FDKSDKPSLT ADEIKARLPP
     EYRDLFEAFL PQEADTLPPH RSYDHKIELV PGSKPPFSRN RPLSPMELRV VKRWLDDNLV
     KGFIRPSKSS SASPLLLAQK PGGGVRICVD YRGVNNISMK SRYPIPLIKE TLDSICKARV
     FTKLDVIAAF NRVRIAEGHE WLTAFITRFG LYESLVTPFG LQGAPATFQH YINDVLYDLL
     DDCATAYLDD ILIYSRSKDD HVKQVRKVLK RLIDAGLQID IEKCEFHTVK TKYLGLIITP
     GGIEMDPEKV SAIESWLPPT TRRQLQRFLG FANFYRRFIK NFSGVAKPLH DLTKKTADWD
     WTDRCQAAFE RLKHCFASAP ALRIYDWEKP AVVETDASDW SAGGTLLQEA DDGELHPVAY
     FSAKHSAQEC NYDIYDKELL AIIKALEEWR PELEGTGQRF DIITDHKNLQ TFATTKQLSP
     RHMRWSEFLS RFNFRIVYRP GAANARPDAL SRKPEHMPQG VADDRLRNRK RPLIDPDSFD
     PLTFDERESL FGMKILQLDV SRHIDDLLTE MYTNSRPLQA VMGALTDPGA RAWPRQLKQQ
     LRVPYAECRA VAGKAYFRDR LIIDPEDTDM HLQLIHRTHA SGPGGHPGRT KTLDLMNRKY
     WWPGMSVAVR SYCNACLLCD KTKTPRSLPT GFLKPLPVPM APWRDISVDY ITPLPPCKRR
     EQDFHHVAVV VDRLTKMRHF IPTATLEVEE LADRFIERIY SLHGVPETII SDRGTQFVSA
     FWRTLSARLG VALKPSSAFH PQTNGQTERI NAELEQYLRL FCDWAQDDWV DWLPLAEFAG
     NNTTSETTGV SPFFANYGFH PRMGVEPAQP CPPNITEAQR REFFRASEIA ERFKAILEKA
     TALSKQAQDR YEESANRRRS DAPIYHVGDR VMLNMKNYKT GRPTQKLEPR WEGPFQVTKA
     SSHAVTLRLP ANMKIFTTFH VSMVRPYRGK GIPGQEQTDD DVTANRGRVV TRTDDGDDVV
     EWRFEDILDY GKADNGRWQY LVKWEGHDTP TWQPATDLRG CDDAIWKFHD AHPNHPRPPV
     WVKKRGHDEE GRGSRQRHRD GYGDDDRGRN EGGQPRRQSP RNKTEVT
//
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