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Database: UniProt
Entry: A0A016WA59_9BILA
LinkDB: A0A016WA59_9BILA
Original site: A0A016WA59_9BILA 
ID   A0A016WA59_9BILA        Unreviewed;      2308 AA.
AC   A0A016WA59;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Reverse transcriptase domain-containing protein {ECO:0000259|PROSITE:PS50878};
GN   Name=Acey_s0960.g3219 {ECO:0000313|EMBL:EYC35908.1};
GN   ORFNames=Y032_0960g3219 {ECO:0000313|EMBL:EYC35908.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC35908.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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:EYC35908.1}.
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DR   EMBL; JARK01000560; EYC35908.1; -; Genomic_DNA.
DR   STRING; 53326.A0A016WA59; -.
DR   Proteomes; UP000024635; Unassembled WGS sequence.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09601; M1_APN-Q_like; 2.
DR   CDD; cd01650; RT_nLTR_like; 1.
DR   Gene3D; 1.25.50.20; -; 1.
DR   Gene3D; 2.60.40.1910; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 3.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 2.
DR   InterPro; IPR045357; Aminopeptidase_N-like_N.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR   InterPro; IPR024571; ERAP1-like_C_dom.
DR   InterPro; IPR034016; M1_APN-typ.
DR   InterPro; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR000477; RT_dom.
DR   PANTHER; PTHR11533:SF293; AMINOPEPTIDASE-2-RELATED; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR   Pfam; PF11838; ERAP1_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 2.
DR   Pfam; PF17900; Peptidase_M1_N; 2.
DR   Pfam; PF00078; RVT_1; 1.
DR   PRINTS; PR00756; ALADIPTASE.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF56219; DNase I-like; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 2.
DR   PROSITE; PS50878; RT_POL; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR634016-3};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000024635};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT   DOMAIN          354..608
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   ACT_SITE        1078
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT   BINDING         1077
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   BINDING         1081
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT   SITE            1138
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ   SEQUENCE   2308 AA;  262582 MW;  2B078E79D39E4FC6 CRC64;
     MDLEKFYRQE HTFYKVIVGD FNTKIGPRRT PEELQIGTHG LQWNEQGERL SEFIMTTKTI
     HGNSQFQKPT SLRWTWESPG GEYHNEIDHI IVNRRFCLTD VGVVPKFYTG SDHRLLRARF
     FFSRKGEKAA KYKKRSPKPT INWDLFTTLA GFWEDTVVDN TDEEYERLIQ HLRDSAKKAE
     GSRTTKRRLS HETLELIRQR GAARAAGNYQ LTSELARRCR EAIKEDLKER RAAVLAEAAE
     AGRSIRNTRR DFANRKTKMT ALRRPDGTIT SSRRVMEKVI YDFYSDLFDS HVHLPPYHLR
     EDGYLIPSVL PSEVRHAIKS VKNRTAPGPD RIRPEHLKNL PTALVNTLAR LFTRYLSECK
     VPSQWKTSRT VLLYKKGDPQ DIGNYRPICL LSVVYKLFTR VILNRIERTL DEGQPCEQAG
     FRKGFSAIDH IHTVTRLVEV SREYEMPLCL TFIDLKKAFD TVETEAVLEA LGNQGVPTQY
     IRIFRELYSN FTTRISPFYD DITIDVRRGV RQGDTVSPKL FTATLEDVMR RLEWDNMGVR
     VDGRLLHHLR FADDIVLITP SISQAERMLA DFDDACGKIG LQLNLTKTMF MRNGWVPDAP
     FSLNGTTISE CSSYVYLGRE VNMMNDLAPE LGRRKRAAWG AYKSIEDVVK RTKNTRLSHL
     FNTTVLPDLT YASETWAVPK QDENAVSVIE RSIERVMLGM TRLTQQLIVD RLQSSMDRVR
     LVDVLLLAVT LLGHFTSALP HHQLFIPGDP RIQDIDRDDG PEDDIPARIP DDISVTEYYI
     KIQPYYPAPG IQLDKGRNMT FDGSVSMSVK IVKPTSEIIL NAANLKIVSI ELTDFLKRPV
     VIKEMRLNNE TEQLSFVLQK RPRVGSVFVL AIKYTGKINP YYDAGLYYTY YEDSEGEVHW
     MVATQLAPFS ARTVFPCMDE PAFKAIFHVE LVYPSSHVAL GNMKETPPVD LGNGWSKVSF
     PPTPVMSTYL VAFSSGPYVS HSVINKDGTL VRSWGWTGQE NFLKFSAETA GECLHQMGLY
     TNIKFPLEKC DHLGLPEFLA GAMENFGLIV YKYQFISFNP DAMTTLDKIG AALVICHEVS
     HQWFGDLVTA ECKDSLLGSF QEAATVRIDR EKALARDGSA YTHPLIAVDG PHFDPITYEK
     GQMLLRMLAD TIDEEVLRSG LQNYLRAHQY STASHWDLWS GLTEVSNDAG VRGWHGPLNV
     TELMEPYALQ SSFPVINVHA GKTGISFSQE RFNDISTQSS SPWNYTWIIP LRTAEYSSPG
     TTIRWLVPDR FEEPLEHSSQ ATNRWHVVSH SSATYGRVVY DENSLHALLQ KIAAVDVPVG
     VKIALIGDEV AMIKRNKSIK QPYSYHRLLD ILATMFNTPS KEDPSSQLVD IALPQMEFFA
     NLLRDSIDAP LIEQLFGLVF GKAYKSEIWD APSSWNADAM KNIFLPYAVR YSIGDASSTA
     QKFFNQIAEN CKSAESNNGS AWCSKVPNDI HRAAYCGAAK YDNNLGANFA RLLFLYNGEV
     KTNPYYYQEY TALLEGMACT ERAPQLKTLI RLLIASPHRP SMIFGWLKTN PKASEALYLY
     LKTKSDSVLR YTGLSYYLDA MVYNWRSERR LRQFNELHKS LLPKLNNKQK DAFAKFEKKI
     RDNIEWSKQH LPSIMRWMYD NLVVVGKAPW RKSLPGIISP ERYDVEITPY IPGSGKYHFS
     KNMTFDGSVK MKFTVTQETS EIVVNAHRMV IDVDSIVVKD SHNSNIEVSA VDIAKDYEHG
     ILKIPLATKI VPGLNYSMSI SYTGFIFDKL HHGVHSNYNF YEFNGKQGWI FSTDFEGGPG
     SRSLMVCCDE PSYKALFHIS VRHPADMTAL SNMFHTGTTV LKEGWAVTRF RETPKMSTHL
     LAICVGHFAS LSAVSETGVL VRAFSWTGME IYADFSLKIM AGAMDYMNDY FNYKFPLSKL
     DVVALPQHAD RGATGKWGLI LGSYKSLIVD KDYADAKTLA NVAITVARAV VQQWFGGLAS
     MEWWSEIFLS NGFAEYFATN GVNHVMPEQR EYLMNYAPFY RTSVGLWDDC RAGVSVPVIS
     EDEGLFTSAV NQKASSLLHT LSNTIWEATF LKGIRTYLTN NAYRSANPEE LWNTLTEACS
     EAGVPDWDGK DLDVSTFMKN WTTKVSFPIV KVSTGRNGLV TYRQESCLGD DTTWYIPIVS
     VSEYNEELNW FVGKDGSSPV WQQPSPLSRV DNVGGNSFVR IYYDKITWKS MLRNMDIAND
     AATQGTLLRD AWFFVSKGNY SWPQFLDLVN VIQWDDSLIK WTTGLEFFEE LYHRFRFHDS
     FPRITIQQAK VGRAGQIGMQ RNPSIQRR
//
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