ID E3PY28_ACESD Unreviewed; 447 AA.
AC E3PY28;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Deoxyribodipyrimidine photo-lyase (DNA photolyase) (Photoreactivating enzyme) {ECO:0000313|EMBL:CBH21343.1};
DE EC=4.1.99.3 {ECO:0000313|EMBL:CBH21343.1};
GN Name=phr {ECO:0000313|EMBL:CBH21343.1};
GN OrderedLocusNames=CLOST_1223 {ECO:0000313|EMBL:CBH21343.1};
OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Acetoanaerobium.
OX NCBI_TaxID=499177 {ECO:0000313|EMBL:CBH21343.1, ECO:0000313|Proteomes:UP000007041};
RN [1] {ECO:0000313|Proteomes:UP000007041}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF
RC {ECO:0000313|Proteomes:UP000007041};
RX PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT its metabolism through its genome sequence.";
RL BMC Genomics 11:555-555(2010).
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DR EMBL; FP565809; CBH21343.1; -; Genomic_DNA.
DR AlphaFoldDB; E3PY28; -.
DR STRING; 1511.CLOST_1223; -.
DR KEGG; cst:CLOST_1223; -.
DR eggNOG; COG0415; Bacteria.
DR HOGENOM; CLU_026342_2_1_9; -.
DR Proteomes; UP000007041; Chromosome.
DR GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.25.40.80; -; 1.
DR Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR InterPro; IPR032673; DNA_photolyase_2_CS.
DR InterPro; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR10211:SF0; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE; 1.
DR PANTHER; PTHR10211; DEOXYRIBODIPYRIMIDINE PHOTOLYASE; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 1.
DR PROSITE; PS01084; DNA_PHOTOLYASES_2_2; 1.
DR PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Lyase {ECO:0000313|EMBL:CBH21343.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007041}.
FT DOMAIN 19..147
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
SQ SEQUENCE 447 AA; 52728 MW; A75DB5B299502A38 CRC64;
MIYDERIKNL NHKKINNGDY VLYWMQASQR SEYNHALEYS IEYSNKLKLP LIVLFIIMED
FPKANFRHFR FMLEGIEDVM NQLKSRKIKM VIRKGEALPI VNELSKNASI LITDFGYLKH
EIIMKSNIAQ QLNCSMLSVE SNVIIPVEVT SNKEEYGAYT IRPKINKIID KYLIELNSRL
VMQSSIDYPI KSEDISDLNS FIDSLKIDKS INESIYKGGS VEAEKYLKDF IENKAQYYSE
LKNHPGMNYS SNLSPYLHFG QISPLYIALK IIKSDIKSKK DFLEELITRR ELAINYIYYN
KNYDSDIEKI LPSWAYDSLI SHQNDLKDYL YSLEELENAK THDEFWNKAQ KEMVITGKMH
GYMRMYWGKK IIEWSLTIND AFSKALYLND RYSIDGRDAN GYAGIAWCYG KHDRPWKERE
IFGKIRYMND KGLIKKFNME KYLDLKL
//
