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Database: UniProt
Entry: A0A2B4S901_STYPI
LinkDB: A0A2B4S901_STYPI
Original site: A0A2B4S901_STYPI 
ID   A0A2B4S901_STYPI        Unreviewed;      1534 AA.
AC   A0A2B4S901;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Alcohol dehydrogenase class-3 {ECO:0000313|EMBL:PFX27144.1};
GN   ORFNames=AWC38_SpisGene8171 {ECO:0000313|EMBL:PFX27144.1};
OS   Stylophora pistillata (Smooth cauliflower coral).
OC   Eukaryota; Metazoa; Cnidaria; Anthozoa; Hexacorallia; Scleractinia;
OC   Astrocoeniina; Pocilloporidae; Stylophora.
OX   NCBI_TaxID=50429 {ECO:0000313|EMBL:PFX27144.1, ECO:0000313|Proteomes:UP000225706};
RN   [1] {ECO:0000313|Proteomes:UP000225706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Voolstra C.R., Li Y., Liew Y.J., Baumgarten S., Zoccola D., Flot J.-F.,
RA   Tambutte S., Allemand D., Aranda M.;
RT   "Comparative analysis of the genomes of Stylophora pistillata and Acropora
RT   digitifera provides evidence for extensive differences between species of
RT   corals.";
RL   bioRxiv 0:0-0(2017).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU361277};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU361277}.
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:PFX27144.1}.
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DR   EMBL; LSMT01000110; PFX27144.1; -; Genomic_DNA.
DR   STRING; 50429.A0A2B4S901; -.
DR   EnsemblMetazoa; XM_022932383.1; XP_022788118.1; LOC111328033.
DR   Proteomes; UP000225706; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   GO; GO:0044281; P:small molecule metabolic process; IEA:UniProt.
DR   CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR   CDD; cd01647; RT_LTR; 1.
DR   Gene3D; 1.10.340.70; -; 1.
DR   Gene3D; 3.10.20.370; -; 1.
DR   Gene3D; 3.30.70.270; -; 1.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR041588; Integrase_H2C2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR048270; PNMA_C.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR041577; RT_RNaseH_2.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR43880; ALCOHOL DEHYDROGENASE; 1.
DR   PANTHER; PTHR43880:SF12; ALCOHOL DEHYDROGENASE CLASS-3; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   Pfam; PF14893; PNMA; 1.
DR   Pfam; PF17919; RT_RNaseH_2; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF50129; GroES-like; 2.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|RuleBase:RU361277};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000225706};
KW   Zinc {ECO:0000256|RuleBase:RU361277};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          403..417
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          1140..1249
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          901..922
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1534 AA;  171808 MW;  1B13BA7B633EF792 CRC64;
     MSETEGKSLS CLAAVAWEPI KPLVIETIEV APPKAKEVRI KILATGVCHT DSYTLGGHDS
     EGMFPCVLGH EGGGIVESVG EGVTRVEPGD HVIPLYIPQC GECKFCQSPK TNLCSTIRTT
     QGKGVMPEGT SRLSCKGQTL YHFMGTSTFS EYTVVAEISI AKTEDDQPVE DVIEEVKTTF
     EVREMTPAER VDFIMSHLEG PAKEEVQMYS KKDRSNPDFL LHILTQAFGE KRSSSQLLKL
     FYERKQKESE KLRAYSYSLN ELLKNGTKAD PKAVPDPEKT LRDQFVDNVR DPFVRKELKK
     FIRERDPSFL DLREEALCWS EEEERPQRIM PRTPLSQEVS TAAPESSQCH ASSTTTPMDK
     VLDALLKQQN SLEELTSSIR DLKQPRTQHP AKEWSGQRSN VVCFKCNRNG HIARNCRTKD
     NLAVRGGPPQ ANGLVIPYIG YLELDVEALG VMIPRRGILV VESPASQEAR TNSISVRGFA
     KVAGKSQIRV PAGSVSVVRI NGWQGPQTRN TAVLVEPLNG HVPGNLVIIS TLIHVNNGQL
     HVRVANVTDE DVWLQPHTRI GVLLEVKDVE DTKNNIDFKR VSINEAMVFV RESTTENKQE
     QPSVCPTDLS DVKCTHEQPN KLENLFQKHA SIFTKDENDL GYTETVKHKI PTIDQVPVAQ
     PYRRIPPNQF QEAKDHIRKL LDNRIIQESD SAYPPPIVLV RKKDGSLRLC VDYRRLNAKT
     IRDQFPLPRI EESIDAIGNA KLFSTMDMAS GFNQRWNSEC QTAFDALKTK LTRAPVLGFA
     DYNKPFIVET DASHVGLGAV LSQDQDGQRK VIAYASRRLR PSEKKNPRNY SSMKLELLAL
     KWAVTEKFRT YLLGSKFEVF TDNNPLKYLQ TTAKLGALQQ PWAAQLALFD FTINYRSGRS
     NANTDALSRQ PHGPVPDETE ESREDELLHI ESILTMETPA PPDLSHAIVT TPIPIEVRRM
     AVHEPDLNLS TVNLTSDENK KLLRDNTVIA TTSFPTHTKK ELINMQKADP TIKEFMKFWE
     KGTKPTLDER RRLSHQCVTL LRQWNRITRD QGLIYRVVQD PKLGELKQLL LPASLREKVI
     TSLHDDTGHQ GLERNLQLIG ERCYWPKMYS DVENWIKNCE RCTLAKMPNP RIQPPMGSLV
     ATKPLEILAI DFTVLEPATD GRENVLVMTD VFTKFTCAVP TRDQKATTTA KVLVKEWFFK
     YGIPLRVHSD QGRNFESEVI TGLCRLNGIK KTRTAPYHPQ GNAQFHFLMF GWGARLPIDL
     LLGEDENVDE NHADCLTEHQ ARLRDAYQRA GEHLKQQAEK RHEQHCDREY DIPIQKGQLV
     ADNAPLEKVC LLGCGISTGY GAALNTAKVE PGSTTAIWGL GAVGLAVAMG CKAAGASRII
     GIDLNPNKFA IAKKFGCTEF VNPKDHNKSI QQVLIEMTDG GLDYTFECVG NVGTMRAALE
     SCHKGWGTSV IVGVAGAGQE ISTRPFQLVT GRTWKGTAFG GWKSCESVPK LVDEYMAGKL
     KVDEFITHTL PLDKINEAFD LMHDGKSIRA IINF
//
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