ID K1Y3H3_MARBU Unreviewed; 1612 AA.
AC K1Y3H3;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Reverse transcriptase {ECO:0008006|Google:ProtNLM};
GN ORFNames=MBM_01656 {ECO:0000313|EMBL:EKD19704.1};
OS Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Drepanopezizaceae; Drepanopeziza.
OX NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD19704.1, ECO:0000313|Proteomes:UP000006753};
RN [1] {ECO:0000313|EMBL:EKD19704.1, ECO:0000313|Proteomes:UP000006753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB_m1 {ECO:0000313|EMBL:EKD19704.1,
RC ECO:0000313|Proteomes:UP000006753};
RX PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA Huang M.-R., Wu R., Zhou Y.;
RT "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT evolution.";
RL BMC Genomics 13:382-382(2012).
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DR EMBL; JH921430; EKD19704.1; -; Genomic_DNA.
DR RefSeq; XP_007289545.1; XM_007289483.1.
DR GeneID; 18757591; -.
DR KEGG; mbe:MBM_01656; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_003446_0_0_1; -.
DR InParanoid; K1Y3H3; -.
DR OMA; NDILMEH; -.
DR OrthoDB; 1775554at2759; -.
DR Proteomes; UP000006753; Unassembled WGS sequence.
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; 2.40.50.40; -; 1.
DR Gene3D; 3.30.70.270; -; 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; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR041577; RT_RNaseH_2.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR37984:SF7; INTEGRASE CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR37984; PROTEIN CBG26694; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00078; RVT_1; 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 Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000006753};
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 480..495
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 867..1048
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1276..1466
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1516..1574
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 114..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..134
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1612 AA; 182662 MW; DDA0B86715F6848D CRC64;
MPRSTAFLIT ARKLHAFITT GHSIAVRVLA LPGTLENVAE HIESYSTLWP PSKAPNPSLD
FNIEWTEGRN FMKALDAWIK IAVLQDTDSD HAPSSSASDS QLDPEAAVFV TQQRVLPQPP
VSPITPPATR APATSPPAAP RASRRLTISG QFPDSSVIEP SLIPDQEMSA PPPAFTAAQQ
EVINKAILAA VAQALAMQAQ QPQPAVQPAT LAADLQPTPE YFLPVLDSSV PIVEHSKVKW
PRSQFSDHRG NVEYDAWKMD MKLFLEEYSG NFITGTSQVK AYFKCTSSEA KSMILEHMSL
DFADSCTCAA DVLRLLDHRF FDHNRVQSAR KAYYQLTMSG SMSYNDFRSK FTAHAITSKI
SRARWFEDMC EKISPALKTH LMIEKYKMQS SYERLDEYLA IVDRESRNIK SEEAAIARRY
ASYASSSSAN VSFTSGARTS GTRGILKKET WRPTSLSPRA TSPAPSPFGS RSTSPSSIIC
FGCKKPGHMQ RECPDLKLDK KIAEMTIDSY YGVGHNLWKE LRFDFRSLIG GPQFLVPIEL
ARNGFFIKTT AHIDSGANIF GAIKTSLASQ LSSRFGNKFV TLPHPIVPTG YNGALGDPIT
YVILLTLTID RRRINFPFLV TNLGSTDVLI GRKFIAHYDI GQRFGAKPQL YWPSDMLVIP
YFGPRIFLDL SHTATKLSHQ ADASRRDQFE VDRSQPSTKE RTWLTFDEHD SRHTTSISLI
SASLMRATLR RFRENYRAAK QAGTPPPDEF VFLASVHDIQ REQDRRDIDS ADEETIQIAS
MNGVNPAQAL SVKYAVNDAK VDLELPFEYA EFKDLFSKKA SDVLAVRRPK VDHKIVLATE
NTLITKLLRR LTDEQLSEVK QYVQDHLHKG FIEPSNAPYS ALILFIKKKD GSIRLCVDYR
RLNSITQKDL YPLPLINEMI ARISRATIFI KIDIQQAFHR IRISSESKEL TTFRTRYSTY
KYKVLPFGLT NRPATFQRFI NDILMEHLDD FCSAYLDDIL IYSTNELEHT EHIKKIMRIL
NDHGLQADIK KSCKEAWEKL KVALQNALIL CHYDPYKQTR LETDSSDGVI AGVLSQLQED
GFYYPIGFFS KTMIDAELNY LIHDKELLAI FHDSITIVNS IPLFTHRTAD TVPQVVLAPV
EEAPPHLLIP GDILLDEDPS DHTNMIAYDI DGYDIIDRVL RANETSPLLQ DLRDGIDTDI
DYELRSGKLY FQGRLVVPLE PLELRTALIR HVYDQPCVAH AGIIKTRQLL ELRYIANCKC
ARMKAKRDKT PGLLVPLPIP ARTNQHLTMD FTELPLDEEG YDFGLVIVDR LSKRSITIPC
HKNITAKGLA DLFFVYWVRY FGMPDSIVSD RGPQFVSTFW LSNGYEARFS FDLINPDPPS
SATERLNREE AIQVATRAQH AIEFAQSSIA VQQEKMKRLA DLRRRPADWT VGDEVWIDTR
NWKMDRPSRK LLDKWYGPVE VLAKVGESWK VQLPEGWKIH PVFHSHSLRK YTGNPLPGQV
REPPAPIQLL PEQDEWEIEE ILGSKVSYNT LYYQIKWTGA DDDLNWYPCS DAMTGLHMLR
RFHLAHPQAK GPPRALPLWL QAYNEGRDDY SELEDNRPMT ATARTQFFEG GG
//