ID A0A0R3RTT1_9BILA Unreviewed; 1405 AA.
AC A0A0R3RTT1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_03023, ECO:0000256|HAMAP-Rule:MF_03038};
DE Includes:
DE RecName: Full=Katanin p60 ATPase-containing subunit A1 {ECO:0000256|HAMAP-Rule:MF_03023};
DE Short=Katanin p60 subunit A1 {ECO:0000256|HAMAP-Rule:MF_03023};
DE EC=5.6.1.1 {ECO:0000256|HAMAP-Rule:MF_03023};
DE AltName: Full=p60 katanin {ECO:0000256|HAMAP-Rule:MF_03023};
DE Includes:
DE RecName: Full=Cytosolic Fe-S cluster assembly factor NUBP1 homolog {ECO:0000256|HAMAP-Rule:MF_03038};
GN Name=KATNA1 {ECO:0000256|HAMAP-Rule:MF_03023};
OS Elaeophora elaphi.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Elaeophora.
OX NCBI_TaxID=1147741 {ECO:0000313|Proteomes:UP000050640, ECO:0000313|WBParaSite:EEL_0000540001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:EEL_0000540001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
CC -!- FUNCTION: Catalytic subunit of a complex which severs microtubules in
CC an ATP-dependent manner. Microtubule severing may promote rapid
CC reorganization of cellular microtubule arrays and the release of
CC microtubules from the centrosome following nucleation.
CC {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- FUNCTION: Component of the cytosolic iron-sulfur (Fe/S) protein
CC assembly (CIA) machinery. Required for maturation of extramitochondrial
CC Fe-S proteins. The NUBP1-NUBP2 heterotetramer forms a Fe-S scaffold
CC complex, mediating the de novo assembly of an Fe-S cluster and its
CC transfer to target apoproteins. {ECO:0000256|HAMAP-Rule:MF_03038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1)
CC alpha/beta tubulin heterodimers.; EC=5.6.1.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03023};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03038};
CC Note=Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable
CC clusters in the N-termini of NUBP1 and two labile, bridging clusters
CC between subunits of the NUBP1-NUBP2 heterotetramer. {ECO:0000256|HAMAP-
CC Rule:MF_03038};
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by microtubules,
CC which promote homooligomerization. ATP-dependent microtubule severing
CC is stimulated by interaction with KATNB1. {ECO:0000256|HAMAP-
CC Rule:MF_03023}.
CC -!- SUBUNIT: Can homooligomerize into hexameric rings, which may be
CC promoted by interaction with microtubules. Interacts with KATNB1, which
CC may serve as a targeting subunit. {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- SUBUNIT: Heterotetramer of 2 NUBP1 and 2 NUBP2 chains.
CC {ECO:0000256|HAMAP-Rule:MF_03038}.
CC -!- SUBCELLULAR LOCATION: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
CC Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome {ECO:0000256|HAMAP-
CC Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle pole
CC {ECO:0000256|HAMAP-Rule:MF_03023}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000256|HAMAP-Rule:MF_03023}. Note=Predominantly cytoplasmic. Also
CC localized to the interphase centrosome and the mitotic spindle poles.
CC Enhanced recruitment to the mitotic spindle poles requires microtubules
CC and interaction with KATNB1. {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. Katanin p60 subunit A1
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_03023}.
CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family.
CC NUBP1/NBP35 subfamily. {ECO:0000256|HAMAP-Rule:MF_03038}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467,
CC ECO:0000256|RuleBase:RU003694}.
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DR STRING; 1147741.A0A0R3RTT1; -.
DR WBParaSite; EEL_0000540001-mRNA-1; EEL_0000540001-mRNA-1; EEL_0000540001.
DR Proteomes; UP000050640; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008568; F:microtubule severing ATPase activity; IEA:UniProtKB-EC.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProt.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0051013; P:microtubule severing; IEA:UniProtKB-UniRule.
DR CDD; cd22325; ERCC1_C-like; 1.
DR CDD; cd00834; KAS_I_II; 1.
DR CDD; cd02037; Mrp_NBP35; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 3.40.50.10130; -; 1.
DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_03023; Katanin_p60_A1; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR HAMAP; MF_03038; NUBP1; 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; IPR000794; Beta-ketoacyl_synthase.
DR InterPro; IPR047260; ERCC1-like_central_dom.
DR InterPro; IPR028596; KATNA1.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR000808; Mrp-like_CS.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR028601; NUBP1/Nbp35.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR033756; YlxH/NBP35.
DR NCBIfam; TIGR00597; rad10; 1.
DR PANTHER; PTHR23074; AAA DOMAIN-CONTAINING; 1.
DR PANTHER; PTHR23074:SF19; KATANIN P60 ATPASE-CONTAINING SUBUNIT A1; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF10609; ParA; 1.
DR Pfam; PF03834; Rad10; 1.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00825; PKS_KS; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF52980; Restriction endonuclease-like; 1.
DR SUPFAM; SSF47781; RuvA domain 2-like; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS01215; MRP; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_03038};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03023}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_03023};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_03023};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03023};
KW Cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03023};
KW Iron {ECO:0000256|HAMAP-Rule:MF_03038};
KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_03038};
KW Isomerase {ECO:0000256|HAMAP-Rule:MF_03023};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03038}; Microtubule {ECO:0000256|HAMAP-Rule:MF_03023};
KW Mitosis {ECO:0000256|HAMAP-Rule:MF_03023};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03023}; Transferase {ECO:0000256|RuleBase:RU003694}.
FT DOMAIN 1004..1401
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT REGION 84..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258..265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03023"
FT BINDING 733
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT BINDING 747
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT BINDING 750
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT BINDING 756
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT BINDING 787..794
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT BINDING 961
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
FT BINDING 964
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="ligand shared with heterodimeric partner"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03038"
SQ SEQUENCE 1405 AA; 154073 MW; 580BD91C62C09DB1 CRC64;
MEWEISESYR AAKEAAQRRK YDQSALFLRT ALSLVERRLN GISTDDPNRD QLVKVKSVLK
LNVERMNGIA DVVSQMRQMI GVTTSSSPVD APPSDPDVWP LPPLTKKTSA ISSPKSINKK
QTSSRIDTKT KKGSSGKSPC ASAGCRSITK RTNSLGRTSM NELSEVTTKE EGDSNSNVGV
LSYSEKGEKV FDDKGFDKEL VEIIERDIMQ KRPDVHWDDI AGLDEAKKLL KEAVILPSVM
PNFFKGIRRP WRGVCMVGPP GTGKTMLAKA VATESQTTFF CVSSATLTSK YRGDSEKLVQ
LLFKMASPAR FYAPSTIFID EIDSLCSRRG VDSEHEASRR VKSELLTQMD GCSPDVSRVL
VLAATNFPWD LDEALRRRLE KRIYIPLPDK TNRFQLLKLA LAEVSINNEV NLEAVADSLD
GYSGADITNV CREAAMMSMR VRIANLTAEE IKALTQEEVD LPITSSDFSQ AIQNTSPSVS
YSDVQNANIA KMEVACSSQS RATLLNSKLV INRKRQGGNP VLKYIRNVPF EWADIKADFE
AGKEMGILYL SLKWHKLHPN YIETRINSDG GGYAVKVLLV LVNVEPRHIL RELNLFCYRT
GWTLMLCYSA EEAAEYLENL YISKNKNEQS AVNAVQERKR KRLCLPDDDS ELYQAIKFLT
VIRSLTISDA QRLIATFGSI RKIANADIDR LLLCPGLEVG FFYLATIFLK VLPDLFRLSK
TMNDIPENAN EDCPGATSAD AGKAASCASC PNQALCISGE IRKPDEDLSA IADRLKNVKH
KILILSGKGG VGKSAVATNL ARALAENDKV QVGLLDVDIC GPSQARMLGV EQESVHESGN
GWCPIVVKDN LIVMSIAFLL QNRTEAVIWR GARKNALIKQ FLKDVDWGSL DYLLIDTPPG
TSDEHISTVQ FLLQAGSADG AIVVTTPQEI SLLDVRKEIN FCRKTKINVL GVIENMSSFI
CPCCSKASQL FPRSTGGAET MCNELSVPLL ASLPFDSHMA ECLMKRVVIT GIGIVSPFGV
GKRLLFDNLL ANNVALRYDE KFKIIVGRIA ECGKHGLDLS SWTARELKQM SRVLRVISWS
WIPGSVLAIV AAEEAVRDAG LKECHMEETG VNVGMGIADL EVIYEVGKQI AEGKGRRVTP
FFIPRILTNM PAGHVSIKFG MRGPQLSSCT ACATGLHSVG DSATFIRMGR AKRMLAGATE
ACINTIAITG FSQMRALATT CSRPFDKRRD GFVLSEGAAI LILEEIEEAL KRKANIYAEI
LGYGVAGDAY HLTTPSEDSI GAFLSMKRCV ADSCINPEQI TYVNAHATST VLGDHFESRA
IARLFPGHIG HTLAAAGAIE TAITAMCVEE GKLVGNVRLE ESDIKENLRF LKQSESWNEG
RVALVNSFGF GGSHATLCLS AVENS
//
