ID G3QZQ3_GORGO Unreviewed; 2048 AA.
AC G3QZQ3;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=FA complementation group M {ECO:0000313|Ensembl:ENSGGOP00000008369.2};
GN Name=FANCM {ECO:0000313|Ensembl:ENSGGOP00000008369.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000008369.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000008369.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000008369.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000008369.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC FANCM sub-subfamily. {ECO:0000256|ARBA:ARBA00009889}.
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DR EMBL; CABD030091031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030091032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030091033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004055167.1; XM_004055119.2.
DR STRING; 9593.ENSGGOP00000008369; -.
DR Ensembl; ENSGGOT00000008600.3; ENSGGOP00000008369.2; ENSGGOG00000008546.3.
DR GeneID; 101153685; -.
DR KEGG; ggo:101153685; -.
DR CTD; 57697; -.
DR eggNOG; KOG0354; Eukaryota.
DR eggNOG; KOG0442; Eukaryota.
DR GeneTree; ENSGT00940000156480; -.
DR HOGENOM; CLU_000801_0_0_1; -.
DR InParanoid; G3QZQ3; -.
DR OMA; MQMLPND; -.
DR OrthoDB; 12149at2759; -.
DR TreeFam; TF324610; -.
DR Proteomes; UP000001519; Chromosome 14.
DR Bgee; ENSGGOG00000008546; Expressed in testis and 4 other cell types or tissues.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0071821; C:FANCM-MHF complex; IEA:Ensembl.
DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:0003682; F:chromatin binding; IEA:Ensembl.
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:0004518; F:nuclease activity; IEA:InterPro.
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 GO; GO:1902527; P:positive regulation of protein monoubiquitination; IEA:Ensembl.
DR GO; GO:0031297; P:replication fork processing; IEA:Ensembl.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; IEA:Ensembl.
DR CDD; cd18033; DEXDc_FANCM; 1.
DR CDD; cd12091; FANCM_ID; 1.
DR CDD; cd18801; SF2_C_FANCM_Hef; 1.
DR CDD; cd20077; XPF_nuclease_FANCM; 1.
DR Gene3D; 3.40.50.10130; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 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 InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR006166; ERCC4_domain.
DR InterPro; IPR031879; FANCM-MHF-bd.
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 InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR047418; XPF_nuclease_FANCM.
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; PF02732; ERCC4; 1.
DR Pfam; PF16783; FANCM-MHF_bd; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00891; ERCC4; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 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:UP000001519}.
FT DOMAIN 98..266
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 452..627
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1518..1540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1668..1735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1751..1809
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1463
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1518..1539
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1668..1683
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1684..1735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1752..1767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1783..1803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2048 AA; 232272 MW; FAA7FE3F00BF5F3B CRC64;
MSGRQRTLFQ TWGSSISRSS GTPGCSSGTE RPQSPGSSKA PLPAAAEAQL ESDDDVLLVA
AYEAERQLCL ENGGFCTSAG ALWIYPTNCP VRDYQLHISR AALFCNTLVC LPTGLGKTFI
AAVVMYNFYR WFPSGKVVFM APTKPLVTQQ IEACYQVMGI PQSHMAEMTG STQAFTRKEI
WCSKRVLFLT PQVMVNDLSR GACPAAEIKC LVIDEAHKAL GNYAYCQVVR ELVKYTNHFR
ILALSATPGS DIKAVQQVIT NLLIGQIELR SEDSPDILAY SHERKVEKLI VPLGEELAAI
QKTYIQILES FAHSLIQRNV LMRRDIPNLT KYQIILARDQ FRKNPSPNIV GIQQGIIEGE
FAICISLYHG YELLQQMGMR SLYFFLCGIM DGTKGMTRSK NELGRNEDFM KLYNYLECMF
ARTRSTSANG ISAIQQGDKN KKFVYSHPKL KKLEEVVIEH FKSWNAENTT EKKRDETRVM
IFSSFRDSVQ EIAEMLSQHQ PIIRVMTFVG HASGKSTKGF TQKEQLEVVK QFRDGGYNTL
VSTCVGEEGL DIGEVDLIIC FDSQKSPIRL VQRMGRTGRK RQGRIVIILS EGREERIYNQ
SQSNKRSIYK AISSNRQVLH FYQRSPRMVP DGINPKLHKM FITHGVYEPE KPSRNLQRKS
SIFSYRDGMR QSGLKKDWFL SEEEFKLWNR LYRLRDSDEI KEITLPQVQF SSLQNEENKP
TQESTTGIHQ LSLSEWRLWQ DHPLPTHQVD HSDRCRHFIG LMQMIEGMRH EEGECSYELE
VESYLQMEDI TSTFIAPRNE SDNLASDTFI THKKSSFIKN INQGSSSSVI ESDEECAEIV
KQTHIKPTKI VSLKKKVSKE IKKDQLKKEN NHGIIDSLDN DRNSTVENIF QEDLPNDKRT
SDTDEIAATC TINENVIKEP CVLLTECQFT NKSTSSLAGN VLDSGYNSFN DEKSVSSNLF
LPFEEELYIV RTDDQFYNCH SLTKEVLANV ERFLSYSPPP LSGLSDLEYE IAKGTALENL
LFLPCAEHLR SDKCTCLLSH SAVNSQQNLE LNSLKCINYP SEKSCLYDIP NDNISDEPSL
CDCDVHKHNQ NEHLVPNNRV QIHRGPAQNL AGENNHDVDN SDLPVLSTDQ DESLLLFEDV
NTEFDDVSLS PLNSKSKSLP VSDKAAISET PLVSQFLISD ELLLDNNSEL QDQITRDANS
FKSRDQRGVQ EEKVKNHEDI FDCSRDLFSV TFDLGFCSPD SDDEILEHTS DSNRPLDDLY
GRYLEIKEIS DANYVSNQAL IPRDHSTNFT SGTLIIPSNE DMQNPNYVHL PLSAAKNEEL
LSPGYSQFSL PVQKKVMSTP LSKSNTLNSF SKIRKEILKT PDSSKEKVNL QRFKEALNST
FDYSEFSLEQ SKSSGPMYLH KSCHSVEDGQ LLTSNESEDD EIFRRKVKRA KGNVLNSPED
QKNSEVDSPL HAVKKRRFPI NRSELSSSDE SENFSKPCSQ LEDFKVCNRS ARRGIKVPKR
QSHLKHVARK FLDDEAELSE EDAEYVSSDE NDESENEQDS SLLDFLNDET QLSQAINDSE
MRAIYMKSLR SPMMNNKYKM IHKTHKNINI FSQIPEQDET YLEDSFCVDE EESCKGQSSE
EEVCVDFNLI TDDCFANSKK YKTRRAVVLK QMMEQNCAHS KKKLSRIILP DDSSEEENNV
NDKRESNIAV SPSTVKKNKQ QDHCLNLVPS GSSLQSKVRS TPRVNPLAKQ SKQTSLNLKD
TISEVSDFKP QNHHEVQSTT PPFTTVDSQK DCRKFPVPQK DGSALEDSST SGASCSKSRP
HLAGTHTSLR LPQEGKGTCI LVGGHEITSG LEVISSLRAI HGLQVEVCPL NGCDYIVSNR
MVVERRSQSE MLNSVNKNKF IEQIQHLQSM FERICVIVEK DREKTGDTSR MFRRTKSYDS
LLTTLIGAGI RILFSSCQEE TADLLKELSL VEQRKNVGIH VPTVVNSNKS EALQFYLSIP
NISYITALNM CHQFSSVKRM ANSSLQEISM YAQVTHQKAE EIYRYIHYVF DIQMLPNDLN
QDRLKSDI
//
