ID E4V4A8_ARTGP Unreviewed; 1868 AA.
AC E4V4A8;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN ORFNames=MGYG_09171 {ECO:0000313|EMBL:EFR04832.1};
OS Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS gypseum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN [1] {ECO:0000313|Proteomes:UP000002669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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DR EMBL; DS989828; EFR04832.1; -; Genomic_DNA.
DR RefSeq; XP_003170595.1; XM_003170547.1.
DR STRING; 535722.E4V4A8; -.
DR GeneID; 10025836; -.
DR VEuPathDB; FungiDB:MGYG_09171; -.
DR eggNOG; KOG0017; Eukaryota.
DR HOGENOM; CLU_000384_38_1_1; -.
DR InParanoid; E4V4A8; -.
DR OMA; DFREMES; -.
DR OrthoDB; 2150499at2759; -.
DR Proteomes; UP000002669; 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; 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; 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; PF00385; Chromo; 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; SM00298; CHROMO; 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 Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000002669};
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 294..309
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 889..1069
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1439..1604
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1743..1802
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 254..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 365..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..816
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1789..1868
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 8..58
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 314..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..455
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..816
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1789..1836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1868 AA; 219438 MW; 16741EE1364D6DDD CRC64;
MSTASGHTTN SNHILAQLKQ QIDALEKKVN DQDCEDDIEQ CETQIKGMSD EIRALKARTG
DTRASVKIRT PDTFKGERHK LEHFLSECDI YLATKAGLTE VEKVIFTGSY LRDTAATWFK
PILEDWINTQ GRPKVYAEVL GSYPNFKTVI RQFFGDTDRK RTLERKLASL RQTRDAAQFA
AQLQQLCQEL EIHDDDRKMA IFEQGLKPET QYETIKMGPY TNYSKMVEMA VRLDNQLYNL
RNLRQGKATF WKGTNQRSTS KRDNYGPMPM ELDATTKKPY DKEKNMRCRR QKLCFYCEKP
GHQMKDCKKK QGDTGKSLNA TTTSRTSSQQ DTHHQNAKRY LCATARTYLQ VPDQNSDSDY
EANYQRMESQ WSKSDEQIAH GDKPTLQRQN ATLGQEWRYL ERHRRERSQR DTLPTDQEHD
LTTGSNQGIM TPERTDSEED TESEDDQEIP ESEQEDHEWE NALPRIEEEP RIKDSLKECM
NDLGEEHWTV CEQKGICFVH NMKKQREVSD PAHPCHDEYD WDCHCEYHIF KETWKYGRRL
HHDNCLQCPG CRNNKDIHWR YCKDNECLVH DKYQGWIDGK SISITDEENI TPHEHLEIRY
WKKERKVKVL YQGHMAEFTS NTTTRYWLDT TRLLRVQLQL QKQQRELAAR MQQEASLESS
SSEESSSSED EWNETCESIE QIQEQQTHDQ DTQTITEGRQ TLKGRPSLAA IVGNHLVIVA
KLAGKYAQAL VDSGATGNFI DSRYVKESGI ATRKKEEPYQ LNGLNGEWAN IVNEETTDKD
QGQILGMAPQ VETGTTKTAS DRSTKEEQRT VHREQDATEL DKLRQQIPQE YHDMIEVFRE
REPSESLPEH QAWDHEIPLK EGMEPTHKPT YRLTGTELEE LRQYIDKNLE KGYIRESTSP
AGYPIIFVPK KDGSLRLCVD YRQLNDITIK NRYPLPLIDE IQDRLKGTTW FTALDIREAY
YRIRIKEGEE WKTAFRTRFG LYEYQVMPFG LTNAPATFQA FINNVLREYL DIFVIVYLDD
ILIFTKEDRR DHTEKVRLVL QRLQEYNLHL KASKCEFYRQ AVKFLGHIIS TIGIQMDPDK
TKAIEEWPTP TSVKEVQQFH GLANYYRQYI HRFSALAKPL TDLFRKGKDF IWGSKEESAF
KELKEKFRQG DMRLHFDPNK EAYVDTDASD CAIGARLQQK DEDGKLRLIA CYARTMTPAE
QNYDIHDKEL LAIVVAFKRW KQELQGTKHR VTVISDHQNL TYFTTTKELT RRQSRWYTET
LAYYNFRIQH CKGTENAFAD ALSRRPDLMT KRREHRAILR LDPDASDMVL DTQALRATRI
VTSDADTLEA EVQKYSERDP LVGRLSGSSE HYRQENGLLL YQGLIYIPKE VRQRVLKESH
DNLSAGHFGI EKTMERITRS YYWPGMWKDI RRYIRECDTC QRNKDNRHAP YGLLQPIPHK
DAPWKSIAMD FITKLPKSKE PRTGIQYDTI MTITDRLTKY TYFIPFVEKT TAPDTAYILL
RQVFANHGLP DEIISDRDTR FMSKFWMTLT ERMGIEQKAS TAYHPQTDGQ SERMNQTVEQ
YLRCYINHEQ NNWVELLPMA QLAYNGAKAA STGITPFFAN YGREPETIKI PRKAKTHARE
AEISAEKLRL LHENMKRDSE FLSYRMSNYY DKQRMEAPTF ERGEKVFLLR RNIKTLRPND
KLDHRKIGPF KILEKTGQVN YKLQLPEHMK IHPVFHVSLI EKAPQNAKPY EPEIQQENQE
QEYEVERILD EKRINGKIHY LVKWKGYDDS ENTYEPMRNL QNATQAIEKY HQRRDSQEEP
REKDHEKRRS PKRPRHADDS TKTSGQRRRS SCEDKRNNFY WKNPSQGTES KKRSSYHKRT
LPRNHIGQ
//
