ID W2XHB6_PHYPR Unreviewed; 2039 AA.
AC W2XHB6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Fanconi anemia group M protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=F441_04568 {ECO:0000313|EMBL:ETP22046.1};
OS Phytophthora parasitica CJ01A1.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317063 {ECO:0000313|EMBL:ETP22046.1, ECO:0000313|Proteomes:UP000018958};
RN [1] {ECO:0000313|EMBL:ETP22046.1, ECO:0000313|Proteomes:UP000018958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ01A1 {ECO:0000313|EMBL:ETP22046.1,
RC ECO:0000313|Proteomes:UP000018958};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ01A1.";
RL Submitted (NOV-2013) 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:ETP22046.1}.
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DR EMBL; ANIX01001014; ETP22046.1; -; Genomic_DNA.
DR EnsemblProtists; ETP22046; ETP22046; F441_04568.
DR Proteomes; UP000018958; Unassembled WGS sequence.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd18033; DEXDc_FANCM; 1.
DR CDD; cd15571; ePHD; 1.
DR CDD; cd12091; FANCM_ID; 1.
DR CDD; cd15492; PHD_BRPF_JADE_like; 1.
DR Gene3D; 1.20.1320.20; hef helicase domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR InterPro; IPR034732; EPHD.
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 InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001876; Znf_RanBP2.
DR InterPro; IPR036443; Znf_RanBP2_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; PF13831; PHD_2; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR Pfam; PF00641; zf-RanBP; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00547; ZnF_RBZ; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF90209; Ran binding protein zinc finger-like; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS01358; ZF_RANBP2_1; 1.
DR PROSITE; PS50199; ZF_RANBP2_2; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00322}.
FT DOMAIN 43..72
FT /note="RanBP2-type"
FT /evidence="ECO:0000259|PROSITE:PS50199"
FT DOMAIN 221..389
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 557..725
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1222..1272
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1283..1403
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 100..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1146..1169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1181..1215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1407..1444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1462..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1546..1568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1631..1662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1677..1734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1753..1805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 957..973
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1000..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1077..1091
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1197..1213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1407..1438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1662
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1725
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1757..1804
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2039 AA; 225537 MW; E19E242F001C5D0E CRC64;
MEEDEWDDAL LSEIAALETR HLQTRGQQNQ TQNPSTVAAT TSLSGVWSCR SCTLQNEASR
TTCQVCSTPR GQVYQATASA LVRKAVHVQA RLSFDATSAP VAVPPSQLQR QQEEGGRSEP
SPFTVRDREQ PIRSSQQTTL SSTASAPGLV LTSRRSEHAT AKSPASSALE IPRHAAGEDP
QARNRYLDIA ARSNFPQIDY EAAQHFVYPT NYSIRDYQLT IAEKALYHNT LVSLPTGLGK
TLVAAVVMYN FYRWFPTGKI VFMAPTKPLV AQQIKACHEI MGIPLSDTAE LQGNVPPTMR
RVLWNSRRVF FCTPQSLQND LRRGVCAAEK FVCIVVDEAH RATGNYAYCC VVQEIEAKTH
FFRVLALSAT PGAKFDVIQD VVTNLRISHI ESRSADDSDV KKYTHARQEE VIVCRLGAQI
MEIKTQFLKL FMPIIQRLLR GNIIQNSDPE KLSSWYVLQA REKFRKSPNY ASNRSAESDL
ALLVSLLHAK SLLTGHGLSS FRDQIVNWIE ERKKGKMSWS KREMLQSSEF QALEASLAVT
DDSNSSSNTN SHPKLVKLRE VLLEHFQRHA AGGSSTRAIV FTQYRASVSE IVALLRPLAP
LLNVQPFIGQ GASGKAKENK GQSQKVQQEI VRRFRLGEFN VLVATCIAEE GLDIGEVDLI
VSFDALTSPV RMIQRMGRTG RKRVGRVIIL VTEGDEQKKL ARSASAAKTV SRALTTFKSR
FTYSKCPRMI PTGITPQLRE LEMKIPTFHA SQVGGKTASV ALDPNLWQLS DAERAVALMK
YFPPNFASSS RNKLFPVVAN RAHLLRRQPR SLVRKGVGYS ARSLMLQSLV RKIHDVEEIL
EIDSDDDEKR EGKSIASGAE QQSKSSKKHR RLRVSTDNAE TDSEIGSPWR QPSTPIELDG
DSKYDESFAA MNESINSFDM HFSPQFVDSA TQLAAVEEDS QPKECSKRRQ EGSDTPTAKK
QKTSSAVVES PKKTATSRSE EESEAQTEAV ARAFGDQNDK KFQMSATLSL TLTSDSPRPS
QSVCKSVQQA TETAQSFGEV PRHLSTRQLQ FDEEVDDKPL DPAKPADHSP PKPASETPEQ
PEKHEMSEVE EHSAFSFALL PPEKSAETSK TDTKEGSEDE DQAEEASAFS FALLPSLTGA
GVASIKASPQ PVEDGTDGDE ADETLKEKPT AKNELLRTNT VDLTEKEDHS TPRETVDTLS
KHPTGNKDVT HLTTPSQQKE DDECCSVCLE SESYDDDPIV FCDGCNVAVH QFCYGIRVVP
KDKWFCDVCT ETRAGVNEAK PNQPRCQLCP HRGGAYKRTT CGQWIHVQCF LWIPEFRVEQ
GDNDMLVLGE LNRLDPDRKT LDCSLCHSTK GNGIIQCAHK RCLTAFHVSC AAFAHYRMDQ
LDPPKDEDSG CGTLFLAYCP LHRNSTAPIT LPEQKTPPPS KTRSSKPSLS SPSHLLASPS
SAEAKKKFKT FRRLKRKYDA SQSQMFSQGA KVSPVATSPW QQKRIRRSKR RRETSRVLAA
AYIEDTADVR GARGDDDNED DYGDDYKDAA DDSFINDSSQ LLYSQSVVSP EELGTNTSKK
KRKKSSPDMR AIYARSLFES QSSPLLLRRG GRHLGALPSN GIIRACLDEL HNGPKDVDTP
SPRPCLRSRV SEMEEATTLS APISASATVT ESDGDDSATE AEASPSFNLL GALQTVQEEE
SGAADSEASP SFNLLGTGST TSTGSATSRP QRWTSSDAKL PTEPINQTQD RDEVHMKIEA
NRLKALKKLE ERRQAKLQGQ AQPQPQPSNN QTSGSTPAAR STNGPVTPTR DAPRSTSTID
LTSPKLAKPV SVQPKWIVFV SSAFASATSF PVFLSAKHTD CTVSIAESME ADSLLSVRTA
VLFLTGQQLH EMALASPAQS VVKSRRVGML LAMHKKLIIA VVHDGGDPPE VQRLRQFPNA
TVIVQPRVET LCTQLHQISQ QELAEGYELP SPSQCRREFN GGVVRALDAD FASRLKFFRL
IPPLSLGSAL SLSFRFKNFP ASQVPVLKFN EMHWRRMLPW ISETTAEQIR EYVQQNVRH
//
