ID Q2GZH8_CHAGB Unreviewed; 1784 AA.
AC Q2GZH8;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Reverse transcriptase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CHGG_05068 {ECO:0000313|EMBL:EAQ88449.1};
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:EAQ88449.1, 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; CH408032; EAQ88449.1; -; Genomic_DNA.
DR RefSeq; XP_001224282.1; XM_001224281.1.
DR GeneID; 4392297; -.
DR VEuPathDB; FungiDB:CHGG_05068; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_000384_38_3_1; -.
DR InParanoid; Q2GZH8; -.
DR OMA; DFREMES; -.
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; 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; 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; 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; 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 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 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 287..300
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 874..1053
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1438..1614
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1702..1760
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 538..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 699..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1157..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1253..1289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1734..1784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 418..473
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 227..252
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..731
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 732..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1747..1775
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1784 AA; 205361 MW; AD16A4D0ED67CF1D CRC64;
MSNPARPTPD SDDEEVDNND LKQELEGVKA LIEGISKQLD DVANAAKVET AFNDLAAKVH
QLRTKEASPR RGQDHLKVAK PPKFDGTKRE ELQGFLTQLR SYFRFNPFNE EADKVLFAAT
YLEGRALEWS ELTQRDYLEL IEDERKKETN KIFEAFVDFE DAITQVFGIF DKRSQAESKL
TKLRQQKRFY DGLKDDVKDE LIKEERDALT LDAYMARAIA IDNRQYERRQ ERTGKKDAVY
PKANDKKKRQ PQSTSHGTHS GPMDIGAAQA QWAGRKGGAK DKSGITCYNC DKKGHVKRNC
HSKKEWRPVP GKEAVTIDQA TVGKKVRIQE VAAASYTQDD LEVDIEQALK REDELTGSDS
DNSELGNEYA LITSDDEGKV APPRHIQQAA QDWGTTLTQQ ADGEWTTHTG DGKVRPSLFF
LQQRILEQRQ RIEELVREKE ELKQLLQARN DQYERLRTEL DSIKEGVREL TSTHEDIGRH
IDGIGRETQA MREAQERAWT DHAPWDRPTE HAEECGDGVH YPEQEYTWAE VPGTALKQTA
SSTQTKNWKS MQKGGSNSTS RLPEGDRGDR EWLNPRKFSG SKNTKRSMPQ AKAAQHRKNW
RRRKPCNDLP ADEYEAAAVR STKPDNRLWI AARWGRIKGK EYIVKGPFDT QWARRETEPL
DMEVAGKTTQ VVFDIVDMGP EKDMILGRPW HEDYDPDISW KGDGHLRPRE PREHPTDLMK
ERAEQEPRMS RGSERTPSTG PPQETASAET RTLESGRSGT RQQKQTREAR TIAVVSVDEH
GKLKHEAWVN RKEAAGIELP AQEIKIPEAS FIESGNKFAY YEAFTAKHLA GLPDHGPWDH
EIKLKEGAQL KFFKVYHTNE KQDAELRSYL EKNLEIGHIR PSTSPAGYPV LFVPKKDGKL
RMCVDYRQLN NERVKNRYPL PLIARLRDQL SGAQYYTRLD LPTAYAHIRI KEGDEWKTAF
RTPYGHYEYL VMPFGLTNAP ATFQAAIDHA IRHCLDKFAV CYLDDILIYS KTLEEHKEHV
RQVLDALHEH KLSVNKDKSE FHVKKTVFLG YEISPGWVKI EPEKLEAVRT WPTPTNATEV
RGFIGFANFV RMFIKNFGDI ARPLHELTKK GTTFQWKQEH ERAFQRMRDA ITADPVLMLP
DPSKLFEVEG NLARETRTAS CTQLRSSPRN SRDQDSTTRS TTKNCSQSSK HFRNGGHTSA
AQHNEVQVHT GHKNLRYFTT TKVLNGRQTR WAEFLSEFNF TIHYKKGSEN ARADALSRRA
DHHDNTSEAS PPLLHQQTDG SPRHASQPTE DYEIAALQQQ LEDPEARPLQ PFVECCAVFR
ERRLERDFQG IITDDERDKW REEPESKIAG LRLEGTRLWY HDKAYIRPSD QKELIQKIHG
SRPGGHMGIS KTIAKVKQNY DFPGIKQATK EILAECDLCG RSKSRPHKPY GLLQPLPVAE
RPWSSVTMDF ITKPPTLKDS ATGTKYDSIL TVVDRLTKWS YFLPYKEPWS AEQLVDVIYR
NVTSVHGWPG EWITDRDTKS ASKFWQALMT KLGTRSKLST AYHPQTDGQT ERLNQIVEQY
LRVPRRSRHS SRITATKQTC DKGPTFRYPE RAVKADRMSS LHAMLKEELE FVRTRMKKFY
DRNRLEGPRL EEGGKVYLIS RNLRTKRPSR KLDFRKIGPF KIDKKISENN YALALPSTMR
LRTNVFHISL LEPAPKNARL DKDVEEVLDS RITEGQLEYL VKWLDFGPED NSWQPATNLN
CPEKPQEFHQ RNPDRPEGTP RRGRPQRGDS PRSSRTPRRS RRKN
//
