ID A0A2P5AND7_PARAD Unreviewed; 1399 AA.
AC A0A2P5AND7;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Fanconi anemia group M protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PanWU01x14_315670 {ECO:0000313|EMBL:PON38065.1};
OS Parasponia andersonii (Sponia andersonii).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Cannabaceae; Parasponia.
OX NCBI_TaxID=3476 {ECO:0000313|EMBL:PON38065.1, ECO:0000313|Proteomes:UP000237105};
RN [1] {ECO:0000313|Proteomes:UP000237105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. WU1-14 {ECO:0000313|Proteomes:UP000237105};
RA Van Velzen R., Holmer R., Bu F., Rutten L., Van Zeijl A., Liu W.,
RA Santuari L., Cao Q., Sharma T., Shen D., Roswanjaya Y., Wardhani T.,
RA Kalhor M.S., Jansen J., Van den Hoogen J., Gungor B., Hartog M.,
RA Hontelez J., Verver J., Yang W.-C., Schijlen E., Repin R., Schilthuizen M.,
RA Schranz E., Heidstra R., Miyata K., Fedorova E., Kohlen W., Bisseling T.,
RA Smit S., Geurts R.;
RT "Parallel loss of symbiosis genes in relatives of nitrogen-fixing non-
RT legume Parasponia.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:PON38065.1}.
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DR EMBL; JXTB01000507; PON38065.1; -; Genomic_DNA.
DR STRING; 3476.A0A2P5AND7; -.
DR OrthoDB; 12149at2759; -.
DR Proteomes; UP000237105; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd18033; DEXDc_FANCM; 1.
DR CDD; cd12091; FANCM_ID; 1.
DR CDD; cd18801; SF2_C_FANCM_Hef; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR039686; FANCM/Mph1-like_ID.
DR InterPro; IPR044749; FANCM_DEXDc.
DR InterPro; IPR006935; Helicase/UvrB_N.
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; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000237105};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1176..1197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 128..296
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 461..612
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 31..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1129..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1378..1399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1129..1146
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1212..1268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1276..1292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1379..1393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1399 AA; 155483 MW; 1F54D60E367F2704 CRC64;
MSSIVHIDAD DDDDEFDWDA AVKAIDVAFP NANLPSTSTS APTPLNPSFI APPPNNFDNN
KKRNGSSNSK QSTLDKFVVK PFPRPQPEIP TVFEPGDGKP PNVRIDAEAA KTWIYPVNVP
LRDYQLAITE RALFSNTLVA LPTGLGKTLV AAVVMYNYFR WFPDGKIVFA APSRPLVTQQ
IEACHNIVGI PQEWTTDMTG QINPAKRACL WKSKRVFFVT PQVLEKDIQS GTCLVKYLVC
LVIDEAHRAL GNYSYCVAVR ELMDVPIQLR ILALTATPGS KRQTIQQIID NLHVSTLEYR
NESDHDVGKY VHNRKIELIQ VSMGKDAVEI DDKLLEVIRP YVAKLSEKGV LQHRDHKTLS
PCELLNSREK FRLAPPPNLC QIIIRDMESY YGLLLTLYHI RKLLSSHGIR PAYEMLEDKL
KLGSFARYMS RNEDLFKAKL RMQQSLSHGA PSPKLSKMLE VLLDHFKTYD PENSRVIIFS
NFRGSVRDIM DALVKIGNSV RATQFIGQSS GKASKGQSQK VQQAVLEKFR AGRYNVIVAT
SIGEEGLDIM EVDLVICFDA NVSPLRMIQR MGRTGRKHDG RANSKTVGKH LRNGGINSFN
FHPSPRMVPH IYKPAVDYVR FSIEKFVRSA KKVKDDDSMT TPVFKEKLTD DESNLIAKYF
QLPGGITWKP SLIAFPHFQT FPSRVHKVMH SFKTGLLIDA MQQVQGLSFA SDSKISPIED
EVSLEKGLGV DCDEHENREG LWFIDDSSQH LQGKFLGPEA SPARTIETKE KNSVCDLPHQ
SPDRHSYHFG PDFISVDTIG NVLILSVPLL TFKGVSHPKS KSSPVLLNSL DRVSCHLKNV
GDNEDPSVQD GALEDLIIPQ TSCIKYGCPK CLCSSDALQG KTFDAIEKVP QTPNKKGNFQ
DEYNVKETLD AEIKASLPLP DNYNNDFRDT ELSPRLTNMI KSGVVPESPM DNNGSSNGEE
RDKYIAADPV SPVQLYNGLR SKFLSPGINE AVNTETDACG RNVSVLPVDN AVQTPVQYED
NSASMREYSF ASIVDRSHSP LAGLTNGSCS KDWCLSIGDK SESVKPPHKF KRLRKVRDQG
KSENLQGGED SSFVPRAKLE KLFAQQKSRR GKKKPVNCII RDFIDEEAEV SADDMSDDEE
DDDDQYNNSH DSFIDDRTSP TFMATQSATG RTDMMAIYRS LAALLSLSLP AFIKVLLLMK
MVYRRSLLSQ SPMPRFTSGS ATPSPHSAAP TTRTSETGSS SGKTSLSFRS PLTESANQLL
SSSSKDSKEA KTSQMKIHSS EAVPCTTSNG ETEFGGRKRK LSFFCPSTCS IPSINLEQEF
EYQYEAAGGG GPPPQHGGEY GEMVCDDEFY EGLDLDMVEA QATLLLKQKA ELSQRREVTA
HINPENPSSP SMPSFDLGI
//
