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
//