ID Q2GN40_CHAGB Unreviewed; 2241 AA.
AC Q2GN40;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN ORFNames=CHGG_10614 {ECO:0000313|EMBL:EAQ84210.1};
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:EAQ84210.1, 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; CH408035; EAQ84210.1; -; Genomic_DNA.
DR RefSeq; XP_001228541.1; XM_001228540.1.
DR GeneID; 4396809; -.
DR VEuPathDB; FungiDB:CHGG_10614; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_000879_0_0_1; -.
DR InParanoid; Q2GN40; -.
DR OrthoDB; 2530607at2759; -.
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:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IEA:UniProt.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00024; CD_CSD; 1.
DR CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR CDD; cd01647; RT_LTR; 1.
DR Gene3D; 1.10.340.70; -; 1.
DR Gene3D; 2.40.50.40; -; 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; IPR023780; Chromo_domain.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
DR InterPro; IPR001995; Peptidase_A2_cat.
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; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR37984:SF7; INTEGRASE CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR37984; PROTEIN CBG26694; 1.
DR Pfam; PF00385; Chromo; 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 SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
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:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 622..649
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 769..854
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 1807..1964
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 2114..2173
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2079..2113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2164..2241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2201..2216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2225..2241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2241 AA; 253170 MW; 84517663A6E14353 CRC64;
MSHGGGGPSG NRADGDNNSV PGNYPEHPSY PDIEQPEMEE ATRHQSAYRR SQIRNLHRTA
AEAPPATSAF GDTPARSRAN TAIRAGSDSG SDSIILRGSD GNDYKLGNNK TSVRYLHRQI
SAQEARTDAL VDRMTATVVE AMDKSFRAFE GKFEKRLQRL ENGPQQRDAA PRGEQSGFAI
PPEGVRLGAH DNLDQPSPPE NFYRQMASGS RPPMPAATPS RSAPQEPYRH RDRHPGGPPP
DREHLRGARE GTCDSILSQP SRNPDKIKRE EIGIFNPDYP DPDDLGIVQD GKNLIFTDVY
SFVDRIATFT ESLGEEASRQ ILGHFQAILG GSAILWWTNE LMAARRIELR SAGLLAILDE
LIVRFGPDAA NATKSFYDCK LYLRDVAADE QALQQFVQKK LRWARSIRML GPDHSNWSSA
MMMIWSHMEF EIQQCLPRPD EFASLSDYMK KIEKSRIIVN SAALKYYPHL VKKSSNKTSL
KSLDKVEDRP RSSRSSDRRE QSRSSRREER YRDDEYRPRD RYRDNRRRDR DGNRDQRKDY
DRRDKERDDR GKRDEKDRKH RDDRYRKDDR DRDRKRDHDR VHFAEIDDDS GSDADHSDAS
SSVSYPSDSE VDIACLVFDA NRTCRKCHKE FDDKTELRHH VKTCEVKGPL RSQRNCQANL
QNPARRTCGH CGELAGSRNA LFKHLKHCQG AKSGTFDRPA DPGIDEAGAA RIAREPAPDD
TSEAPEDLGE INFVKEAPTL GDDKPLEGPL GNFTYLRVNA RTSPKKGDVE VCFDPGAGRS
IVGRNFLRNL DYTIEKREGK VSGIGGGILK LKEWATFSLY LPGVENGKKT LFKFTRGAWV
IDKLLPNLLL GNDFMDPYRA NIDYDTKIVH LRAIDFAVPF SIRVHSVPCV RRVKTTRAIT
LLPDQEAMIP VNYKPLPKGR SFLFNAEHDA AFHAVITAKT PKVVAVKNTS RGTITIPKRY
PVGKIDENHD SGFLACSWNT AFKTMAVGAT LMSMAKPTTI SDIEPANFAL QNTNSLPVSA
EFDFDKRTAA VAEHDLGLRA PDAPTVENYN GTSSTPVSDY VYQLTRDVTV DLPINDQTSE
QPDLPVVPEK QSTLGIRMVD NLPEIVTKEG VHIFAENSQL AARFAELVRR LPRLWEDTGL
IKLPPEQLMR VPLVEGWQNQ RVSSCSYPLS RRDRQLLDEI FDGLHKQGKM IWATRATPFA
HPVFVVWRTV KGVTKGRVVI DLRGLNRVSV PDNYPLPLQA EIIGSLRGKR YITAIDATAF
FYQFGLHPPH RDRFTLISPR GLEQPTVCLM GYRNSPAHVQ RIMDQLLKPH AEYARAFIDD
IVIFSNDAED HLKHLERIFR LFHDKNVAIA PTKSFIGYPS VELLGFRVDS LGLTTTAQRV
EAFRNLAFPK TLKALEQWIG ATGFLRHLIP YYAQLLEPLQ KRKTALLAQG RENGQLVSGN
QGKRANYCAK TTFEPSEAER LSFDSIQKVI CAENPSILYH FDPDKPLFLQ VDGCLERGCG
VMVFHVQDGY EWKPGSVIPS KQVQPVMFLS RCLTKAELRY GPSEQEVACL VWAVKKLRTM
IHSSRHPVNV LTDHSSTRGI VEQTRLDTSS TDRSNRRLIT ASVYLSEYDL KVFHLPGRLN
FVPDALSRLT AVQDKPEREE GEVILDNVMF AWAEAQMDDS LKNEFIAAYH EDSKYSAIIK
DLISGEPAEG SGEFFRPGLP FVLTGGLLYN IRPDGLRSIC IPHKMVKTVL SMVHDQKHHF
GIDRMLYDLR GVSMVNKTRQ VRKFAQHCPQ CNVVSTDRQP PIGTLQPIRP ADTLPMRVIG
IDFIVGLPTV PSEGSPWQLK GKVSFDSLLT VSCKSSKRTL LIPGHTTYTA QQWGQVLMRQ
LFLSDWGVPS AIISDRDRKF TSEFWQGMWE SLGTKLLMTA AYHPQSDGLA ERKNQTVEIA
MRFFVFERPE ANWTDLITPL QWNLNSSYSA PIQSSPHEQL FGFKLPGPFE ALAIPPSVES
DIPSMRESLR EDARLAMDFA AARAKRRYDA NRRDIEFREG DKVYLRLHKG YHLPGNPPRK
LSQQRTGPFE VVRRVGRLAY ELKFPENMGI HPVISIAHLS PTPPGNDPFD RHPVPPGPVE
DSQASTDSAP GEDYEVEVIL RHRVTRRKYE YLIKWKGWGH EHNVWKTEYE LRHTPRLLKE
YWQRQGGQPA LPGDDATEPR RKRGRPRKNV APAEEAPAAN REPEVPPKDG RRRSRRLVPT
GTMPTPASEE ATPASTTAAP Q
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