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Database: UniProt
Entry: A0A0K9NMV9_ZOSMR
LinkDB: A0A0K9NMV9_ZOSMR
Original site: A0A0K9NMV9_ZOSMR 
ID   A0A0K9NMV9_ZOSMR        Unreviewed;      1303 AA.
AC   A0A0K9NMV9;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Fanconi anemia group M protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ZOSMA_80G00400 {ECO:0000313|EMBL:KMZ57948.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ57948.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(2016).
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       FANCM sub-subfamily. {ECO:0000256|ARBA:ARBA00009889}.
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:KMZ57948.1}.
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DR   EMBL; LFYR01001997; KMZ57948.1; -; Genomic_DNA.
DR   STRING; 29655.A0A0K9NMV9; -.
DR   OrthoDB; 12149at2759; -.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central.
DR   GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR   GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR   CDD; cd18033; DEXDc_FANCM; 1.
DR   CDD; cd12091; FANCM_ID; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR039686; FANCM/Mph1-like_ID.
DR   InterPro; IPR044749; FANCM_DEXDc.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR14025; FANCONI ANEMIA GROUP M FANCM FAMILY MEMBER; 1.
DR   PANTHER; PTHR14025:SF20; FANCONI ANEMIA GROUP M PROTEIN; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036987}.
FT   DOMAIN          154..322
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          434..596
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          905..930
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1079..1118
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1137..1165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1095
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1303 AA;  146722 MW;  7E271676586BC25E CRC64;
     MPSPSSHFVP IPPSIVIDDD DDDFDWDAAI REIDSTCANV ASASGCENAA STIPSGKTER
     PSVGSFRQAT LDCFVKKIAK TYDGTSFGRN QVDDHTHHDG IFDDSDIHAQ NGAHLNHLHT
     TTTARGQNVA IDLEAAKTWV YPSNVSHRDY QFSITEKALY SNTMVVLPTG LGKTLIAAVV
     MYNYFRWFPE GKIVFTAPSR PLVMQQIEAC HKIVGMPQEL TIDMTGNTNP RNRIELWKEK
     RVFFVTPQVL EKDIQTGICL TKKLVCLVID EAHRASGNYS YCVVLRELIA ASVDLRILAL
     TATPGTRKEN VQNVIDNLCI STLEYRDENN HDVSKYINDR KSELIKVPMD KGANEILSLF
     IQIIKQYVIS LNSKGVLPPR DCTVMTPSEW VNIKTIFGNE VSTKFGSAEK AKIMSDIGMM
     ISLSYIRQLL LGYGIRLAYV MLEEKLKGPL AKLCHNELIC KTRDLMSKYL SHGAPYPKLS
     KLMELLKDHF GNKLLKGQSQ KTQQAVLQKF RSGEYNVIVS TSIGEEGLDI IEVDLVICFD
     ANISSLRMTQ RMGRTGRKNS HELNGHLRKQ ATGRAIKKKM FNGGVNSFDF HLSPRMVPHC
     CKPKLHIVEF LVGEFIHFGR KTKATPMGRS LLSGILSTEE NDTISKYFHH PNEDDWKPSL
     IAFPHFQTFP SRIHRVGHSM KTVHMFINAM EYLQMSPSSK PNVVLPVEAA KKLISEDSDI
     RLKGVYDFPE QTSCFEPLSL SNPDAVFENY KLEFASQKAG HQFLFETNFV SVNTLGEVVI
     ASFPTLPFID VSDIRSDLSH DHRTKPTYLY EASMFHYNKK TLIPRDALIL SKLSDSRYTD
     SEDVFACQPY IYKEKSKEET YPKEEILHQT PLSTQEMLVS KDNLQMSKVS NSILPACESA
     SARNHFDSSP KFSSKHGHSD SETNHSFSSS INHDHENCEL LTDHHSINSH IRSNLGNDTF
     HGQLNTEEKY DSDYALDDKT NAQVNTNITF NNQVIDGSPG DWLMKLESPK TVQVAPKFKR
     LRKYNDTVQK LPFTDFERNA SETNINLHHI AEDGFCQKRR GLDKKMTLVK SFIEEEADVS
     ADVDVSEDED DDKDEKGEFN NSFIDDRSNP SEASAHEENS IDMMAFYRRS LLTQSPLETP
     SYPISSSHEE ITSTRSEKTD PCLPDEINNS ILISRDEMNH SAKPTSGYST ERITSFELVG
     EAIEAQDDWS VIGSKKRKLF HQCPETGLVA KMQPRDLFQS NNSTTSSVPT HTSTDLSCDD
     DFFENIDLDA LEAQAIELLK NKPKANELPA CNPVSFPSFD LGL
//
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