ID A0A0F7ZJ33_9HYPO Unreviewed; 1543 AA.
AC A0A0F7ZJ33;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Reverse transcriptase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HIM_11410 {ECO:0000313|EMBL:KJZ69210.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ69210.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ69210.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ69210.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(2014).
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DR EMBL; KQ030747; KJZ69210.1; -; Genomic_DNA.
DR OrthoDB; 2623044at2759; -.
DR Proteomes; UP000054481; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd01650; RT_nLTR_like; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR InterPro; IPR004875; DDE_SF_endonuclease_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR33481; REVERSE TRANSCRIPTASE; 1.
DR PANTHER; PTHR33481:SF1; REVERSE TRANSCRIPTASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF03184; DDE_1; 1.
DR Pfam; PF14529; Exo_endo_phos_2; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF56219; DNase I-like; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000054481};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 163..178
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 637..896
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT REGION 541..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1034
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1047..1243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..986
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1034
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1085..1099
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1148..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1234
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1543 AA; 173455 MW; CD6EDEAB725E2AED CRC64;
MEPSRSHWSP PTGSIRQAIE SEVRAKEGQA TWRCAAVVRS SRNTEQVKII CRDEIELQRV
KEGAQNTAVT GARVMRDQLY PVKVDNVNRT AILDGEGNIQ QGAAEALGAE NNVTIETGKA
YGSMVVYVTK NDAKKLLDGK YFDLAGESAC TNPFEPRKGP MQCYNCQEIG HKAFRCKKPQ
MCGSILQLNV RKREPVQQSL MNDEDLRDYG VLAVSEPHAR KIDGKVVTSP MMHSNWTRIL
PTYTRDAPWP TRSMLWVRND VEVEQIPVPS ADLTAAVLRL PERGVLVVSV YVEGKSTEAL
KTTTGLLHDL IRQFRHDSGT RTDVVLAGDF NSHDLLWGGD EISDRRQGEA EPIIDLMNEH
GLRSLLPRGM KTWQDRDQES TIDLILTTSE LADEMNYDAK ALFKNAPWSL IKARVKDDLR
PLPWAVDVQT QTDQLTRVVL EAVHELTPRA RPSPYAKRWW TKNLTRLRRV YTFWRNLART
QRRAGQLQPD LERRAKEAAK EYHDTIRSQR KAHWNDFLAD DVNLWGAAKY LKLGEDTMGD
KVPPLRRRNG SSTKDKAEQT DELLSTFCPP LPTRIEDEGV RSQRKAVRMP DLTLEEFEEK
IMAAKPWKAP GEDELPTVVW RQLWPVVQYR VFALFKASLR DGIVPRQWRS AKIIPLRKSD
KEDYTAWRSI SLLSTLGKIL EAVVAERISY AVETHGLLPA NHFGARKRRS AEQALLFLQE
QIYRAWRNRK VLSLISFDVR GAYNGVCKDR LLDRMKARGI PADLIKWIDA FCTGRTASVV
VNGYVSEQRE LPQAGLPQGS PLSPILFLFF NADLVQRRIK AGSGSIAFVD DYSAWVTGPT
AEANRAVIQS IINDALEWWE ARSGATFEAD KTTVIHFTRV ARRDSDMSIL IIGEEVKPRE
RTHGEGGCQR AQRCHVPEKI ENAVAKGSET TVRSDSRAGH GLRLQCLDAC SPRKTSGMDE
QSTDDWDADH HGRVSYGRDG GGRSRSKHSN GRGTTHTGYD ETLHQSSNST DNTPSGSHEE
QSKQALRITN SKDFSAAEVR QTEWKLYTRN NDNNAQLADE RHSGNGRRGV QPGPRPPRQC
SCQLFRDSRT DRRTESVHSG TGSDGDGADV QTGQPSLSRS DGCDEQPLSP GSDQATSEAI
RPVHYSPNLR TRRSTGETWQ FGKTQVGTSQ TRRVHVGNSR QGSSAECNPG SIHRGRTILP
SKVHHASFGA RPTTAWTASG RDRKTREAHR QGVAGKTHPK KKSKGNKRLL ILDGFSSHHT
YPFIEYCRRN GIVLFSVPPH LTHLLQPLDV VVFQPLKHYH AKAVDLAVRD GCTDITKVEF
LDFIQDVRKK IFRHQTIISA FRKTGIVPFN QEVVLAVMRA RKNRTPSPEL DSALQSSPFD
TPVTLGQMHK TASHLEDCLI AAEDCNDGSI LLENDFLVSM GQFIRGAISN STELIQTKRD
LGRTRLAEKT RQLRRAMKNT PLQSGGVLTV AQGRQMAARK GEIEFQRAQR KVEASRARYD
NALKRWYSEA AKKARAMRMA RQLGEMLVYS GPHGCKAIRR VGK
//
