FAN1_DICDI
ID FAN1_DICDI Reviewed; 1087 AA.
AC Q55FW8;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Fanconi-associated nuclease 1 homolog {ECO:0000305};
DE EC=3.1.4.1 {ECO:0000250|UniProtKB:Q9Y2M0};
DE AltName: Full=Protein MTMR15 homolog;
GN Name=mtmr15; ORFNames=DDB_G0267916;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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.
CC {ECO:0000250|UniProtKB:Q9Y2M0}.
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:0000250|UniProtKB:Q9Y2M0};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9I2N0};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9I2N0};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000250|UniProtKB:Q9I2N0};
CC -!- SIMILARITY: Belongs to the FAN1 family. {ECO:0000305}.
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DR EMBL; AAFI02000003; EAL73411.1; -; Genomic_DNA.
DR RefSeq; XP_647415.1; XM_642323.1.
DR AlphaFoldDB; Q55FW8; -.
DR SMR; Q55FW8; -.
DR STRING; 44689.DDB0238616; -.
DR PaxDb; Q55FW8; -.
DR EnsemblProtists; EAL73411; EAL73411; DDB_G0267916.
DR GeneID; 8616222; -.
DR KEGG; ddi:DDB_G0267916; -.
DR dictyBase; DDB_G0267916; mtmr15.
DR eggNOG; KOG2143; Eukaryota.
DR HOGENOM; CLU_285203_0_0_1; -.
DR InParanoid; Q55FW8; -.
DR OMA; FWDIIFD; -.
DR PhylomeDB; Q55FW8; -.
DR PRO; PR:Q55FW8; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008409; F:5'-3' exonuclease activity; IBA:GO_Central.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0070336; F:flap-structured DNA binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004528; F:phosphodiesterase I activity; IEA:UniProtKB-EC.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR Gene3D; 3.40.1350.10; -; 1.
DR InterPro; IPR033315; Fan1-like.
DR InterPro; IPR011856; tRNA_endonuc-like_dom_sf.
DR InterPro; IPR014883; VRR_NUC.
DR PANTHER; PTHR15749; PTHR15749; 1.
DR Pfam; PF08774; VRR_NUC; 1.
DR SMART; SM00990; VRR_NUC; 1.
PE 3: Inferred from homology;
KW Coiled coil; Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease;
KW Reference proteome.
FT CHAIN 1..1087
FT /note="Fanconi-associated nuclease 1 homolog"
FT /id="PRO_0000393272"
FT DOMAIN 961..1083
FT /note="VRR-NUC"
FT REGION 1..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 169..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 816..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 419..490
FT /evidence="ECO:0000255"
FT COILED 830..874
FT /evidence="ECO:0000255"
FT COMPBIAS 24..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..871
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 899
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 1023
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 1023
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 1051
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
FT BINDING 1052
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I2N0"
SQ SEQUENCE 1087 AA; 125767 MW; 2DBE90740A848885 CRC64;
MKSNTKNSVK RKSPPPVNPN KKFPSFEGKQ TSIKDFFFND TTTPPKTPTQ PIRFTQNNNK
ENDKSNNNNN NNNTITPIKK TTTTTTVVVE SFDDSRNTNL IQQFQKASTP SSPQIPNKLP
QQENQQQIPN TQQQQIKQLQ QQQQQQQQES PNNLFKTIKT TTTTETFEEF LLSQPTTPPP
SNTTTTTTTT SSSSPSSSNN ITTIDDKNNL IKNNRYYLND FLIVTETVYK RDKHLFINDE
KDYIEGMIET LDRDSQHLFV RLYNRKGPWF QINELKSSNY QNEIKNIGAA IESLVEYGFL
EYYSSDKHDY NEIANLLKID QLKSIASSFS IPNSSGKETF LKVISGEPFK GQSTLFSPKP
IYKKKVENLV GESIKIVTEV VELWRMIHHL YFYSWSTHDS KSMIVNNIMG IKYPEYTVWK
SKVKKEVQQK EEEVEKEKEE ILQNQLIQVK QESDVIDLTQ NSSGSSNNNN NNNNNNNNNN
NNNNNIKEYD IDLTENESIF PNRESLLKYE NARKLEEKSI NLYESGGDLV ALESILQVCL
DELGRSVSKK VKYSFALKFT VGWVYTRILS WSIDIFEKLR KYQQCIDFLM LLIESPYCRG
KRGYWWQRMI INHKHLHRSD DALLIAERSL KEDPFLRSGD RLAIEKHLIQ LSSPPRRWRI
PAGLIQFSYK LKEPISTTIY REKVSNNQQG YKSKYLFLTP QIKINKIKKI IIKSSQSQNN
QQKVQSSLSS QIQTQIQTQI QTQIQSSQIQ IQSPIQSQSQ SQNQTPIQSQ INNNNNNILA
ISSQKSFDSI LTTTSINNTQ SSSQNIYIDE ETSLEITSDD ELFPPGQSYK IEKENQLQIT
NSVKKEEEQE EEEEEEEEGQ GQEEEEEEEE IIEITHGTVE EVSLEHYSQN GGWEGIHCET
SIFITLYVLY FWDIIFDSNV PHVFQSPFQN SPLDFGSDEF YFTRKEAIDN RIKRLEHSNY
DDLLILLNQS WLHNGCEARG VNWKSTSLEQ LSIISKCLGG KLIAFISRLL TEDFKSFSHG
MPDLLLWKLN NNNDDDIDDK NNNNSSIKFV EVKGTGDRLR DQQRIWIDML ISFGCDVEVC
LVKNKKN
