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Database: UniProt
Entry: M3IZZ4_CANMX
LinkDB: M3IZZ4_CANMX
Original site: M3IZZ4_CANMX 
ID   M3IZZ4_CANMX            Unreviewed;      1498 AA.
AC   M3IZZ4;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Pol {ECO:0000313|EMBL:EMG45183.1};
DE   Flags: Fragment;
GN   ORFNames=G210_5239 {ECO:0000313|EMBL:EMG45183.1};
OS   Candida maltosa (strain Xu316) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG45183.1, ECO:0000313|Proteomes:UP000011777};
RN   [1] {ECO:0000313|EMBL:EMG45183.1, ECO:0000313|Proteomes:UP000011777}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA   Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT   "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT   for xylitol and ethanol production.";
RL   Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Integrase (IN) targets the VLP to the nucleus, where a
CC       subparticle preintegration complex (PIC) containing at least integrase
CC       and the newly synthesized dsDNA copy of the retrotransposon must
CC       transit the nuclear membrane. Once in the nucleus, integrase performs
CC       the integration of the dsDNA into the host genome.
CC       {ECO:0000256|ARBA:ARBA00025615}.
CC   -!- FUNCTION: Reverse transcriptase/ribonuclease H (RT) is a
CC       multifunctional enzyme that catalyzes the conversion of the retro-
CC       elements RNA genome into dsDNA within the VLP. The enzyme displays a
CC       DNA polymerase activity that can copy either DNA or RNA templates, and
CC       a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-
CC       DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA
CC       primers. The conversion leads to a linear dsDNA copy of the
CC       retrotransposon that includes long terminal repeats (LTRs) at both
CC       ends. {ECO:0000256|ARBA:ARBA00025590}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000077};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EMG45183.1}.
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DR   EMBL; AOGT01002940; EMG45183.1; -; Genomic_DNA.
DR   STRING; 1245528.M3IZZ4; -.
DR   eggNOG; KOG0017; Eukaryota.
DR   HOGENOM; CLU_238940_0_0_1; -.
DR   OrthoDB; 1997758at2759; -.
DR   Proteomes; UP000011777; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR   CDD; cd01647; RT_LTR; 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; 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   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   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011777};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transposable element {ECO:0000256|ARBA:ARBA00022464}.
FT   DOMAIN          678..854
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          1241..1414
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          390..469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          85..155
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:EMG45183.1"
SQ   SEQUENCE   1498 AA;  170944 MW;  A701FA5B24C14497 CRC64;
     MPPNKNNPKT EPTTGNQSNP DEFRANVLQA FEHPSMVEYL TRIIQQAIRP AIQEAEADTV
     NYVASVEEQS KQEILDDVHQ ITQDIANKEM NLESREKALE AKEEELEAKT ATLEQVEKQF
     QQETMQFAAS KNAEMAQMQE QIAVLTQQLN DVQATQANQP NQVVTVQRPV RLERDVNFLI
     KTYMPSFIIL PEKAPQLAAG VINQSPRYVP ELIINGSDDL GKLSKLSSLE RHFSGTNVPY
     IRWGELIAPY LNFDLKTAYL NAERVRPGGG KLTWREVVEL IAASGNLVLE DMAKIERFCN
     LQPKPDQLVK DYLNEAEARS QDFSNFSNKH ILVRSRVYHC LGTYFRHIIQ SYDLILCNKL
     EDFFKELHSI FSNLRFPSVL SGDQSAVNVS QIGSQSTGPP VRNQFQYRSS NNNSSFNQNS
     NNFNRWNSSN PPSNNTNYNN GNNNYHNGNN NYHNGNSNYN NGNNNNRFKG NQWRRRKIFR
     NFSKNGRVTR RINVIRFEND DGDEFEFAED CLEQFPDAKI DQLQHSITAT TASNIQHSIH
     QSAEVLLPPP FSIPISFLIL PHLQQIIIGK PTLRTWNYAL SDDTETITIN NQVIEIESVA
     TVPFNSIKLD LESLRQKLRD EIFHQYTELF DTTPRSAAQR IFQYDLITTS EVPIRCRAYP
     AGPEEKKAIE AFITEKLKAG VLVENVKDPW YCPIFAVRQK DLYRIVNDLR KLNAVTVLDV
     AYLSTFKDLM VMLAKSRYYT VFDLKSAFHQ IGLTPRSIQK MGIISHLGIH NFTSLPFGAK
     CAPYILAKFL QGIFGSMENL FIYMDDILIM TSTLESHIQL VHKVCHLLNS NHLQANIKKV
     QLLQEQITFL GYQISHDKIQ PTADKLKAIQ SWSLPETTTE IRSFVNFVNY FHLLIPNVSR
     LTSKLTALTA GEGKRIPINH TEESRAAFET LKHQLINIPY VHHYDPSQPV HILVDTSDQA
     VGAIITQQRM VDGQDILVPI CYVSYSLNEV QRRYSSMEKE SLGMLIVIRK YEYLLGTQAN
     IYSDHQSLSI LQSRTVKPPL RISRFLDVLG CYSPLVYYLP GKNNFLADIL SRHQTKNIND
     QVDEASLLGD EVVPIENIRS SSINSIALDN LNESNLQQIK DHLMSIPPPV VNHVNEDPDD
     ESPIVNEFSD TLPVSYFAVL EDRLFVTLNN NKVVPVVSRE EFLDEATKIH QSFHASIRVI
     NYIAIQKIWH PDHLLLCTEV VRNCNTCTIH GSFREIAREL VSLEPTTAFH RWAFDYTHAG
     AESHGYRNIL VAVEYVTSLT YAIAVKNADT KSFLSLLTLI IQAHDVPKQI ITDNGSPFVS
     EDAKKFLQEW KITPTTASNY HPMSNGKVEK TNHLLKNIIK GLTNKTWQDW YTLLPKAVNI
     LNNTPSMFGK SPYFLAYGKD ATINSPIEIH DLEDISVIPT IASSDTSEES VNQLNMIQDD
     VNLRLHDLDL LMQDREEHNN LKKRRDAMRN LLLEPYGTPA VYSKGQWVYR QKTEKKET
//
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