FAN1_PSEAE
ID FAN1_PSEAE Reviewed; 559 AA.
AC Q9I2N0;
DT 04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Fanconi-associated nuclease 1 homolog {ECO:0000305};
DE Short=PaFAN1 {ECO:0000303|PubMed:25319828};
DE Short=pFAN1 {ECO:0000303|PubMed:24981866};
DE EC=3.1.4.1 {ECO:0000269|PubMed:24981866, ECO:0000269|PubMed:25319828};
GN Name=fan1 {ECO:0000303|PubMed:25319828};
GN OrderedLocusNames=PA1865 {ECO:0000312|EMBL:AAG05254.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION.
RX PubMed=24981866; DOI=10.1016/j.celrep.2014.06.001;
RA Pennell S., Declais A.C., Li J., Haire L.F., Berg W., Saldanha J.W.,
RA Taylor I.A., Rouse J., Lilley D.M., Smerdon S.J.;
RT "FAN1 activity on asymmetric repair intermediates is mediated by an
RT atypical monomeric virus-type replication-repair nuclease domain.";
RL Cell Rep. 8:84-93(2014).
RN [3] {ECO:0007744|PDB:4R89, ECO:0007744|PDB:4R8A}
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) IN COMPLEX WITH MANGANESE AND DNA,
RP CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF 65-ARG--ARG-69; TRP-184;
RP 191-VAL-LEU-192; 191-VAL--ILE-197; TRP-253; LEU-421; ASP-507; GLU-522;
RP LYS-524 AND GLN-534.
RX PubMed=25319828; DOI=10.1101/gad.248492.114;
RA Gwon G.H., Kim Y., Liu Y., Watson A.T., Jo A., Etheridge T.J., Yuan F.,
RA Zhang Y., Kim Y., Carr A.M., Cho Y.;
RT "Crystal structure of a Fanconi anemia-associated nuclease homolog bound to
RT 5' flap DNA: basis of interstrand cross-link repair by FAN1.";
RL Genes Dev. 28:2276-2290(2014).
CC -!- FUNCTION: Nuclease required for the repair of DNA interstrand cross-
CC links (ICL). Acts as a 5'-3' exonuclease that anchors at a cut end of
CC DNA and cleaves DNA successively at every third nucleotide, allowing to
CC excise an ICL from one strand through flanking incisions. Also has
CC endonuclease activity toward 5'-flaps (PubMed:25319828).
CC {ECO:0000250|UniProtKB:Q9Y2M0, ECO:0000269|PubMed:24981866,
CC ECO:0000269|PubMed:25319828}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolytically removes 5'-nucleotides successively from the
CC 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.;
CC EC=3.1.4.1; Evidence={ECO:0000269|PubMed:24981866,
CC ECO:0000269|PubMed:25319828};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:25319828};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25319828};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000269|PubMed:25319828};
CC -!- SIMILARITY: Belongs to the FAN1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG05254.1; -; Genomic_DNA.
DR PIR; D83413; D83413.
DR RefSeq; NP_250556.1; NC_002516.2.
DR RefSeq; WP_003113615.1; NZ_QZGE01000003.1.
DR PDB; 4R89; X-ray; 4.00 A; A/E=1-559.
DR PDB; 4R8A; X-ray; 3.20 A; A/F=1-559.
DR PDB; 5Y7G; X-ray; 3.40 A; A/B/C=1-559.
DR PDB; 5Y7Q; X-ray; 2.70 A; A=1-559.
DR PDB; 5Z6W; X-ray; 3.20 A; A=1-559.
DR PDBsum; 4R89; -.
DR PDBsum; 4R8A; -.
DR PDBsum; 5Y7G; -.
DR PDBsum; 5Y7Q; -.
DR PDBsum; 5Z6W; -.
DR AlphaFoldDB; Q9I2N0; -.
DR SMR; Q9I2N0; -.
DR STRING; 287.DR97_11; -.
DR PaxDb; Q9I2N0; -.
DR EnsemblBacteria; AAG05254; AAG05254; PA1865.
DR GeneID; 877940; -.
DR KEGG; pae:PA1865; -.
DR PATRIC; fig|208964.12.peg.1941; -.
DR PseudoCAP; PA1865; -.
DR HOGENOM; CLU_036183_0_0_6; -.
DR InParanoid; Q9I2N0; -.
DR OMA; QDNQIRW; -.
DR PhylomeDB; Q9I2N0; -.
DR BioCyc; PAER208964:G1FZ6-1904-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IDA:UniProtKB.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IDA:UniProtKB.
DR GO; GO:0070336; F:flap-structured DNA binding; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR GO; GO:0036297; P:interstrand cross-link repair; IEA:InterPro.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR033315; Fan1-like.
DR InterPro; IPR040603; FAN1_SAP.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR014883; VRR_NUC.
DR PANTHER; PTHR15749; PTHR15749; 2.
DR Pfam; PF18081; FANC_SAP; 1.
DR Pfam; PF08774; VRR_NUC; 1.
DR SMART; SM00990; VRR_NUC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; Endonuclease; Exonuclease; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Nuclease; Reference proteome.
FT CHAIN 1..559
FT /note="Fanconi-associated nuclease 1 homolog"
FT /id="PRO_0000431957"
FT DOMAIN 443..555
FT /note="VRR-NUC"
FT /evidence="ECO:0000255"
FT BINDING 386
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25319828,
FT ECO:0007744|PDB:4R89"
FT BINDING 507
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25319828,
FT ECO:0007744|PDB:4R89"
FT BINDING 507
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:25319828,
FT ECO:0007744|PDB:4R89"
FT BINDING 522
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25319828,
FT ECO:0007744|PDB:4R89"
FT BINDING 523
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:25319828,
FT ECO:0007744|PDB:4R89"
FT MUTAGEN 65..69
FT /note="RMVMR->AAAAA: Impaired ability to incise a 5' flap
FT structure."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 184
FT /note="W->A: No effect on nuclease activity."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 191..197
FT /note="VLADLGI->AAADAGA: Decreased nuclease activity."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 191..192
FT /note="VL->RR: Decreased nuclease activity."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 253
FT /note="W->P: Weak nuclease activity."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 421
FT /note="L->R: Strongly decreased nuclease activity."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 507
FT /note="D->A: Loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 522
FT /note="E->A: Loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 524
FT /note="K->A: Loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:25319828"
FT MUTAGEN 534
FT /note="Q->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:25319828"
FT HELIX 21..36
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 43..54
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 57..68
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT STRAND 69..75
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 76..79
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 87..96
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 117..123
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 135..142
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT STRAND 181..184
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 188..194
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 215..232
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 237..243
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 252..271
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 304..316
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 321..337
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT STRAND 353..359
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT STRAND 362..364
FT /evidence="ECO:0007829|PDB:4R8A"
FT HELIX 367..375
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT STRAND 380..384
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 388..397
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 419..422
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 426..429
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 431..439
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 446..457
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT TURN 467..469
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 472..481
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 484..496
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT STRAND 507..512
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT TURN 513..516
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT STRAND 517..524
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT HELIX 532..543
FT /evidence="ECO:0007829|PDB:5Y7Q"
FT STRAND 548..556
FT /evidence="ECO:0007829|PDB:5Y7Q"
SQ SEQUENCE 559 AA; 64528 MW; 6917F74369356B67 CRC64;
MHEQYQAPLP VNSPALPEPF YYLHNFRAVL AWIGERYADL LDDQERAFIA AFAELPEASQ
ALLVRMVMRK GTLFREGKLA YAEIGDTRAA VQPLLALGWV DAQPTLELAQ LFGLLKKDEL
SQLFRDHLGR ANLRKDALLE RLQPLFPEAR RLAEWQADFA EPVYELRCMA LCDRLRLMYF
GNLWQDWSEF VLADLGIYRY ESVEFSADSR GFRLRADVDA YLHLFDCRQR FDLGEPLEEL
LAGLPGEPYA NPWLEGRRVK LLFQFAQHCE KQRDFDLAQR LYRQSSHPGA RLRAIRSLER
GERFAEAHAL AREASCAPES DAERQGLARL LPRLQGKLGL PRQARAAAPE IDRLDLCLAF
PSEPCSVEWA VREHLEEPGC AVHYVENGLI NSLFGLLCWE AIFAAIPGAF FHPFHSAPAD
LHSADFRQRR AALFEACLGR LEDGSYRDAI RCRYRDKFGL QSPFVYWELL GEELLEQALD
CLPAAHLRAW FERLLEDIPG NRAGLPDLIQ FWPAQRRYRM VEVKGPGDRL QDNQLRWLQF
CREREMPVAV CYVRWHVDD
