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Database: UniProt
Entry: A0A2U4AFD2_TURTR
LinkDB: A0A2U4AFD2_TURTR
Original site: A0A2U4AFD2_TURTR 
ID   A0A2U4AFD2_TURTR        Unreviewed;      2020 AA.
AC   A0A2U4AFD2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Fanconi anemia group M protein isoform X3 {ECO:0000313|RefSeq:XP_019779519.1};
GN   Name=FANCM {ECO:0000313|RefSeq:XP_019779519.1};
OS   Tursiops truncatus (Atlantic bottle-nosed dolphin) (Delphinus truncatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Delphinidae; Tursiops.
OX   NCBI_TaxID=9739 {ECO:0000313|Proteomes:UP000245320, ECO:0000313|RefSeq:XP_019779519.1};
RN   [1] {ECO:0000313|RefSeq:XP_019779519.1}
RP   IDENTIFICATION.
RC   TISSUE=Spleen {ECO:0000313|RefSeq:XP_019779519.1};
RG   RefSeq;
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   RefSeq; XP_019779519.1; XM_019923960.2.
DR   GeneID; 101335644; -.
DR   OrthoDB; 12149at2759; -.
DR   Proteomes; UP000245320; Chromosome 2.
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:0004518; F:nuclease activity; IEA:InterPro.
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   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:UP000245320}.
FT   DOMAIN          107..275
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          461..636
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          866..887
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1299..1318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1423..1468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1489..1511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1645..1709
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        866..885
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1299..1316
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1431..1449
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1489..1510
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1656..1709
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2020 AA;  228438 MW;  EFE7502E8D66D637 CRC64;
     MSRRQRTLFQ TWGSRVSRST GAPSCSSGTE RPQSPGISGA SFPAAAQAAE AAEAAEAQPE
     SDDDVLLVAV YEAERQLSLE NGGFCTSAGA LWIYPTNCPV RDYQLHIART ALFCNTLVCL
     PTGLGKTFIA AVVMYNFYRW FPSGKIVFMA PTKPLVTQQI EACYRVMGIP QSHMAEMTGC
     TQAFTRKEIW GSKRVHFLTP QVMVNDLSRG ACPAAEIKCL VIDEAHKALG NYAYCQVVRE
     LVKYTNHFRI LALSATPGSD IKAVQQVITN LLIGQIEIRS EDSPDILPYS HERRVEKLVV
     PLGEELGAIQ KAYIQILEAL ASSLIRRNVL MRRDIPNLTK YQIILARDQF RKNPSPNIVG
     LQQGIIEGEF AICISLYHGY ELLQQMGMRS LYFFLCGIMD GTKGMTRAKK ELSRNEDFMK
     LYNHLECMFA HTRSTSASGI SAIKKGDEDK KFCYSHPKLK KLEEIVVEHF KSWNAQKTSD
     KKCDETRVMI FSSFRDSVQE IAEMLLQHQP IIRVMTFVGH ASGKSMKGFT QKEQLEVVKQ
     FRSGGYNTLV STCVGEEGLD IGEVDLIICF DAQKSPIRLV QRMGRTGRKR QGRIVVILAE
     GREERTYNQS QCNKRSIYKA ISGNRQVLHF YQGSPRMVPD GINPHLHKMF ITHGVYEPDK
     PSRNLQRKSS IFSYRKGMRQ SNSKNDWFLS EEEFKLWNRR YRLRDTDEIK EITLPQVQFL
     SLQNEENRPT QEPTTGIHQL SLSEWRLWQD HPLPTYQVDH SDRCHHFVNI MQMIEGMRHE
     EGECSYELEI KSYLQTEDVS STSSAPRNEY NPFANGIFTS NKKSSFTKNI NQGKSLSITE
     SDEECAEIFK QIRIKPTEIA SLKRKASKEL KKDQPKKEHK EVVMGPLDTD GSSTAKNIFQ
     VDLLNDKRVS DTDEVAATCA ISENVGNRSC GLLADCQFTN KSTSSFTGKF LDSGYNSFSD
     EKSLSSSLFF PFEDELYIAR TDDKFYNCHS LTKEVLANVE RFLSHSPPPL SALSNLEYEI
     SKGSALENLL FVPYTECLQN DKSTCLMSHS TINSQQNLEL SSLKFITHPS EKSCLYGTIN
     DKISAEPSFC YYNKVHKDIK NEHLVSNHHI QINTGPPKYF VEEKNHDVDN SGLPILHTDQ
     DESLLLFEDV NTECNDVNLP PLNSKCKSLC VSDKTALSEM ALGSQFLISD ELLLGNNSEP
     QDQIIGDTNS WKSHEDLRGV HEEKLKNDEY GFDCSKDLFS VTFDLGFCSP DTDDEILEHA
     SDTNKNKILD DLSGGCLDIK EINDANYVSN QAVISRDHVD SSTSETITNP SSEDKRSPTF
     ACFPMNATKN KEFMSPGYSQ FSLPVREKVM STPLSQSNTA NLFSKKRIEM ARKSDSNKGK
     INLQSFKETL NSTFDDLGLS IEKANSREQI NLHQSCHSAK VLDEQLTSSE SEDDEIFRRK
     SKKTKGNVLE SPENQKNSEV DSPLHAVKKR RVPPNRLVAR KFLDDEAELS QEDAECVSSD
     ENDESENEQD SSLLDFLNDE TQLSQAINDS EMRAIYMKSV RSPLMNNRYK MVHKKHNNIN
     IFSQIPEQDE TYLEDSFCVD EEESCKSQSS EEVCVDFNLI TEDCFASRSK KYKTRRAVKL
     KQMKMRQNCA SSKKKLCRII LPDDSSEEEN DVNDKQESST VINPSAVTKS EQQNHCLNLV
     PSGSSLQSRD HSNPVVNQSP NQRQQTPLNL KVTVSDVSDF KPQSRTKIEP TSSSFTTVDS
     QKDCRKFPIQ LKDTSALEDS GTSVAYCSNS RPRLAGTHAS LRLPQEGQRT CILVDSREIT
     SGSEVISSLR AVHGLQVEVC PLNGCDYIVS NRMVVERRSQ SEMLNSTNKN KLIEQIQYLQ
     SMFERICVIV EKDREKTGDT SRMFRRTKSY DSLLTTLTGA GIRILFSSCQ EETADLLKEL
     SLVEQRKNVG IHVSTVVNSN KCEALQFYLS IPNISYIAAL NMCHQFSSVK KMTNSSPQEI
     SMYAQVTHQK AEEIYRYIHY IFDMQMLPND LNKGSFKSDA
//
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