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Database: UniProt
Entry: Q2H3F3_CHAGB
LinkDB: Q2H3F3_CHAGB
Original site: Q2H3F3_CHAGB 
ID   Q2H3F3_CHAGB            Unreviewed;      2106 AA.
AC   Q2H3F3;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE            EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN   ORFNames=CHGG_06812 {ECO:0000313|EMBL:EAQ90193.1};
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:EAQ90193.1, 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; CH408031; EAQ90193.1; -; Genomic_DNA.
DR   RefSeq; XP_001222907.1; XM_001222906.1.
DR   GeneID; 4391390; -.
DR   VEuPathDB; FungiDB:CHGG_06812; -.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_000384_38_3_1; -.
DR   InParanoid; Q2H3F3; -.
DR   OrthoDB; 2734036at2759; -.
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; 1.20.5.340; -; 1.
DR   Gene3D; 2.40.50.40; -; 1.
DR   Gene3D; 3.10.20.370; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
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   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 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; IPR005162; Retrotrans_gag_dom.
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:SF437; RIBONUCLEASE H; 1.
DR   PANTHER; PTHR24559; TRANSPOSON TY3-I GAG-POL POLYPROTEIN; 1.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   Pfam; PF03732; Retrotrans_gag; 1.
DR   Pfam; PF17917; RT_RNaseH; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF50630; Acid proteases; 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          291..306
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          1061..1240
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          1602..1767
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   DOMAIN          1902..1927
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   REGION          354..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          715..738
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          869..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1417..1452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1935..2057
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2079..2106
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          15..77
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          439..473
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        354..373
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        715..736
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        869..889
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..913
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        918..932
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1417..1433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1434..1449
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1935..1950
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1977..1991
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2016..2030
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2106 AA;  240966 MW;  8B287FCA60AE335E CRC64;
     MAAETPTPAQ MQSAIEEIAA RVATTETNLA ATETNLAATE TKLAATETKL AATETKLAAA
     EGQLATARAE LTQAKAGEGD PAKNKVKLEQ PEKYGGDREA LPGWITAMRN YIDHNSHQFI
     TEASKTRYAA TRLKDTALRW FSGTLENYLG GGNHKAFTQK VFENYSEFEH EIQKVFGDKN
     EKLHAQERLS KLRQTKSAMA YAAVFRQDCM KAEINDEGLK KMFYDGLKEE VKDELYQKDE
     VDTLDEYIAL AIRIDERQAP LLATHAGPMD VDAIQKAGKK NNARDKSGIT CYNCGKKGHC
     KRDCQSKKEW KPVPGKEAAT IDEIKKGVRF QEVAAASYTQ EDLEVDIDQA LEREDELTDS
     DEAEPSDSDS DDLIPEDDVR RILEMDNEYA LVISDDEGEV APPGYVLRMA QHWGLTLVQQ
     TDGHWRTRNN ADESEGPNLV FLQNRVRELR ERITRLEDEK QVLERTLEER NKLYGKLRAE
     FDLIGQGVRE LNNTNRTLGQ HIDTIGEVAQ NMLKDAGQPS LDHTSWDGPS LDISEIHMDK
     VCFPHYAYRE AQEQRESQGL DSQDWDDYWS RHQYLSRGKP TSDLETAGLR GVNGRFQLME
     GDHPRMNPRR RDHVHLPRFQ CVAHECRYHF QTKFQSNHWP VRPQNERGNP VPTTWVYDHG
     DAPAALLWKV DMIPDGRLRF SPKNAWPEGC NNPRWTNHCG QADCLVHADA KLEEHARSQA
     QRNRPRPTRA QRRENRQPVE PQMMQWLQEH KTIDAASQGA DRDALMLWIP ARWKKYEALA
     LVDPGAQMDL ISPSFVNQLR IPWRIKKQSL IVRGPFDTQW VRRETEPLDI EVAGKTTQVV
     FDIVDMGPTK DMILGRPWHR IYDPDISWKG DGHLRPREQR EHPTSLMGER AEQEPRQSSG
     SERTPSTGPP QEAASAEERT LESGRSGTRQ QKQTREARTI AVVSVDEHGK LKHETWVNRK
     EAASIELPAQ EIKILEASFI ESGNKFAYYG GTPKSATTGR VPDEYKGHPA FTAKHLTGLP
     DHGPWDHEIK LNEGAQLKFF KVYHTNEKQD AELRSYLEKN LEIGHIRPST SPAGYPVLFV
     PKKDGKLRVC VDYRQLNNET VKNRYPLPLI SRLRDQLSGA QHFTRLDLPT AYAHIRIKEG
     DEWKTAFRTP YGHYEYLVMP FGLTNAPATF QAAIDHATRH CLDKFAVCYL DEIVIYSKTL
     EEHKEHVRQV LDALHEHKLS VNKYKSEFHV KRTVFLGFIG FANFVRMFIK SFGDIARPLH
     ELTKKDATFQ WKQEHEQAFQ QIRDAIIADP VLMLPDPSKP FEVEADASDF AIGGQLGQRD
     KDGKLYPVAF FSKKLEGPRL NYPIHDKELL AIIEAFQEWR PYLSGTTHEV QVYTDHKNLR
     HFTTTKVLNG RQTRWAEFLS EFNFTIHYKK GSENARADAL SRRADHHDDT SEVSPPLLHQ
     QTDGSLRHAS QPTEDCEIAA LQQQPEDPEA RPLQQFVECC AVFREQRLER DFQGIIADDE
     RDAWQEEPES KIAGLRLEGT RLWYHDKAYV RPSDQKELIR RIHESKLGGH MGISKKIAKV
     KQNYDFPGIK QATEEVLAGC DLCRRSKPGR HKPYGLLQPL PVAERPWSSV TMDFITKLPT
     SKDPVTGVKY DSILTMVDRL TKWSYFLPYK ESWSAEQLAD VIYRNVTSVH GWPEEWITDR
     DTKFASKFWQ ALMTKLGTKS KLSTAYHPQT DGQTERLNQV VEQYLRLYVN FQQDDWVELL
     PTAQLAYNTT VTETTKVTPF FANYGYEADL RQGPDVSVPR AAVKADKMNS LHTMLKEELE
     LVRTRMKKFY DRNRLEGPRL EEGGKVYLIS RNLRTKRPSR KLDFRKIGPF KIDKKISENN
     YALALPSTMR LRTNVLHVSL LEPAPKNARL DKGVEAEDEE LWDVEEILDS RITKGRVEYL
     VKWLGISTGG IRIDQERHRR PVEPGKKIDG RGTNSRVSGK ARGREGRTQT PGPRRGQEGE
     HSQRPKRTTA RQQPHDAPVP AIPRPLDQTS DVLDPPKIGV DDEDGQPAQG RHQGPDRPRV
     APCPTDASAE SNVGRRSCRN QMSHKRCCAL WRTQYKRRYQ KARDSQEDPY PCNQGPEQLH
     GNTHCS
//
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