ID A0A077ZF11_TRITR Unreviewed; 1114 AA.
AC A0A077ZF11;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN ORFNames=TTRE_0000728001 {ECO:0000313|EMBL:CDW58951.1};
OS Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichuridae; Trichuris.
OX NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW58951.1};
RN [1] {ECO:0000313|EMBL:CDW58951.1}
RP NUCLEOTIDE SEQUENCE.
RA Aslett M.;
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDW58951.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT "The whipworm genome and dual-species transcriptomics of an intimate host-
RT pathogen interaction.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HG806462; CDW58951.1; -; Genomic_DNA.
DR STRING; 36087.A0A077ZF11; -.
DR GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0019899; F:enzyme binding; IEA:UniProt.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00303; retropepsin_like; 1.
DR CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR Gene3D; 1.10.340.70; -; 1.
DR Gene3D; 3.10.20.370; -; 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; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
DR InterPro; IPR001995; Peptidase_A2_cat.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR041373; RT_RNaseH.
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; PF13975; gag-asp_proteas; 1.
DR Pfam; PF17921; Integrase_H2C2; 1.
DR Pfam; PF17917; RT_RNaseH; 1.
DR Pfam; PF00665; rve; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 2.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50175; ASP_PROT_RETROV; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Protease {ECO:0000313|EMBL:CDW58951.1};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 263..279
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 346..425
FT /note="Peptidase A2"
FT /evidence="ECO:0000259|PROSITE:PS50175"
FT DOMAIN 1031..1114
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT COILED 212..239
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1114 AA; 125278 MW; 62027D7EA6685301 CRC64;
MEPPSRPVVV PQTYDSEGSW QNWRTAFEQC SILNRWTEQD KLQWLAVSLT GDAAWAFGQL
TAEQRESYDS CITGLTTLLV PPNVEQLNVT LFRTRRKTKE EDWFTFAREL SKLAARAYPA
FAPGVRDALS LERFLTELGP EEWASTVRRA NPSSLMDAVR MAIQQEATEQ AYRGKATHSA
RIHVGEVEEV AAAISRGVLP ERRGGSPPIY QRAGSLDEVR ALRNEVDELK RMMQEMSLQL
SPLAVGLHGR QSTEGPRAVG RARCFSCGRR GHLRKDCPRM QAAERCPDRY TKPWNKSLDA
YPVVNARRNS NAACADTVKM AYAKESGGAN TGACLCVPVK VRTKFIRMLV DTGAGRTLLR
SDEFRRIGGQ WELSPCKVCL LSAGGTALDV MGSVLLPLQV GDKTFAMEVI VVDKLQFAGL
LGVDFLKLHG FVVDLARGTL NCSEQKLKIP LQSAGRASGN GAWSVSPGKS ASTSERMLQR
LIESTGAPLT VSQQGKLRGM LSKFCNAFAA SEVDFGRTSI LKHDIITDSN RPVRHPLRRL
SPLERNEVSQ LIQRMLDNKI IEPSNSPWAA GIVPVRKKDG SIXXXXXXXX XXXXXXXXXX
XXXXXXXXXX XXXXXXXEHI EHLAQVLSRL QEAGLKVNSR KCKLFCKEVC YLGHIVSERG
IEPDPSLTEK MRTYPVPKCL TEVQRFLGLA SYYRKFIKNF AAIAKPLHQL TEKRKPFEWS
LECAEAFHKL RAALLSHPVL QLPDFSVPFI LDTDASDTAI GAVLSQTDVQ GREHPVAFAS
RTLTRAERRY CVTRREMLAV ITFVEQFRPY LQQKFKLRTD HGSLQWLRNF KNPDGQWARW
QQKLQQYDFV IEHRAGSRHA NVDTLSRIPC KQCGRSGTEG TSQPVNVVVL DGLEDMRKAQ
LEDEDVGPVL KAKEAGMAEH ELSRQRRSNA KNLLMLNWHR LAVRNGILVR KWFCADYSGF
RWQVVVPKRM ISRVLKQAHE GATAGHLGME KTTERIRERF YWPGYRTDIK GYVGTCYECN
TRNGPLPKGK APLHPLRATR RWQRIAIDIL GPLVTSETGN RYILVVMDYF SKFAEAFPIP
NQETKTVTAV LVNEFICRYG VPEAIHTDQG AQFE
//
