ID H0ZC52_TAEGU Unreviewed; 689 AA.
AC H0ZC52;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Fidgetin-like protein 1 {ECO:0000256|ARBA:ARBA00035694};
GN Name=FIGNL1 {ECO:0000313|Ensembl:ENSTGUP00000008161.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000008161.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000008161.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000008161.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001836};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region
CC {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR STRING; 59729.ENSTGUP00000008161; -.
DR Ensembl; ENSTGUT00000008246.2; ENSTGUP00000008161.2; ENSTGUG00000007929.2.
DR Ensembl; ENSTGUT00000027596.1; ENSTGUP00000018866.1; ENSTGUG00000007929.2.
DR GeneTree; ENSGT00940000161552; -.
DR HOGENOM; CLU_000688_21_10_1; -.
DR OMA; YSDKWES; -.
DR OrthoDB; 276256at2759; -.
DR TreeFam; TF105013; -.
DR Proteomes; UP000007754; Chromosome 2.
DR GO; GO:0000228; C:nuclear chromosome; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR GO; GO:0007140; P:male meiotic nuclear division; IEA:Ensembl.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0033687; P:osteoblast proliferation; IEA:Ensembl.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0010569; P:regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
DR CDD; cd19525; RecA-like_Figl-1; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR047858; FIGNL1_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015415; Spast_Vps4_C.
DR PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23074:SF75; DYNEIN REGULATORY COMPLEX PROTEIN 11-RELATED; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003651};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003651};
KW Reference proteome {ECO:0000313|Proteomes:UP000007754}.
FT DOMAIN 448..584
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 137..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 689 AA; 74441 MW; BE03947C14CE9088 CRC64;
MEAPNPSAVH LSDWQESYFA VTSGTCTPGQ KADGYRAKIL RIQYAWANSE ISQVCAANLF
KEYAEKYSAI IDSGNAETGL NNYAENILTL AKCQQSDSDK WQSALTTDNV FELKCVRERM
QAGKIFQSSQ MAQTDARVQA DKGVSASAAP APPKLDVFGS TRETELTAGS AKCASQGPDL
LGHPSSSKSL QSSVPSVTRT SDTLPAASAA LSKQVLPGFQ ATPLFGSKEA TNSSSLKTPG
NCCDGQNSSL FSQSGVPAWS ANSGKRKAFY GLADEGSTAI PSLAPCQASI STETNGFSGQ
RNRNEESSAP GFKTAKEQLW MDQQMKSQNQ RAPVSSYGGV KKSLGAGRSR GPFSKFVPPV
PKQDGSENGG AQCKPRVGES TDPLLPVDER LKNIEPKMVE LIMHEIMDHG PPVSWDDIAG
VEFAKATIKE IVVWPMLRPD IFTGLRGPPK GILLFGPPGT GKTLIGKCIA CQSGATFFSI
SASSLTSKWV GEGEKMVRAL FAVARCQQPA VIFIDEIDSL LSQRGEGEHE SSRRIKTEFL
VQLDGATTSS EDRILVVGAT NRPQEIDEAA RRRLVKRLYI PLPEASARKQ IVTRLMAKEH
CSLNEEEIKL IVQKSDGFSG ADMTQLCREA SLGPIRSLQS MDIATITPEQ VRPISFLDFE
SALRTVRPSV SPKDLELYET WNQTFGCGR
//
