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Database: UniProt
Entry: A0A091PSL1_LEPDC
LinkDB: A0A091PSL1_LEPDC
Original site: A0A091PSL1_LEPDC 
ID   A0A091PSL1_LEPDC        Unreviewed;      1250 AA.
AC   A0A091PSL1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Peroxisomal ATPase PEX1 {ECO:0000256|ARBA:ARBA00034532};
DE   AltName: Full=Peroxin-1 {ECO:0000256|ARBA:ARBA00032509};
DE   Flags: Fragment;
GN   ORFNames=N330_04327 {ECO:0000313|EMBL:KFQ10243.1};
OS   Leptosomus discolor (Madagascar cuckoo roller) (Cuculus discolor).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Coraciiformes; Leptosomidae; Leptosomus.
OX   NCBI_TaxID=188344 {ECO:0000313|EMBL:KFQ10243.1, ECO:0000313|Proteomes:UP000053001};
RN   [1] {ECO:0000313|EMBL:KFQ10243.1, ECO:0000313|Proteomes:UP000053001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N330 {ECO:0000313|EMBL:KFQ10243.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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:ARBA00034440};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000256|ARBA:ARBA00034440};
CC   -!- SIMILARITY: Belongs to the AAA ATPase family.
CC       {ECO:0000256|ARBA:ARBA00006914}.
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DR   EMBL; KK677680; KFQ10243.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091PSL1; -.
DR   PhylomeDB; A0A091PSL1; -.
DR   Proteomes; UP000053001; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0007031; P:peroxisome organization; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd19526; RecA-like_PEX1_r2; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 3.10.330.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR029067; CDC48_domain_2-like_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR015343; PEX1-N-lobe.
DR   InterPro; IPR015342; PEX1-N_C-lobe.
DR   PANTHER; PTHR23077; AAA-FAMILY ATPASE; 1.
DR   PANTHER; PTHR23077:SF12; PEROXISOME BIOGENESIS FACTOR 1; 1.
DR   Pfam; PF00004; AAA; 2.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF09262; PEX-1N; 1.
DR   Pfam; PF09263; PEX-2N; 1.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF50692; ADC-like; 1.
DR   SUPFAM; SSF54585; Cdc48 domain 2-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053001};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          558..708
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          840..976
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          304..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1132..1154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1229..1250
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..323
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFQ10243.1"
FT   NON_TER         1250
FT                   /evidence="ECO:0000313|EMBL:KFQ10243.1"
SQ   SEQUENCE   1250 AA;  138878 MW;  06A350FEB47D3AA8 CRC64;
     GQAVKVSCGH QPMFLSWMEI RHRGHQGENI AEMNRQLAEK LGITDGEQVF LEPCSHVSSC
     QQVEVEPLSA DDWEILELHA SSLEKHLLDQ IRIVFPKAVF PVWIEQHTHV YIKIGTLMPA
     ACYGRLEPCT ELLILPKTRE LEENITSMPS TESDILLKSF VKNKMEQEET VKDPFAKQPY
     LKPGVLEHSK TDANMTFGSN VLPNIWNFIG SVFCHTSEQK QKTLSDKDGM STFKDKLLNL
     IHMDSIFRVC QSQPPSVQNA STTHAFLKCN AIHVFPWNLE FIDMNPNPVV SYGKINELLS
     PRRRHQEAKE NLPFEKQKHL TSTQDKNHSN SNSSQASSEG SVVQIVWNGF EDLKSVMEYG
     HSGEALHVGR VWIPDGLRKK LHIKIHSTVR IKSVESIPKI PVSLTLQPTQ NLHKDIHEDD
     VKSAFSSWLQ DFTSDDLPWI MTSTDYIHLS VKEGMEEFVL SAVHPVHIEA NTSENIFILS
     PSLLQKTNMQ VLLHPLTRKA DNDSQPPMCD TDRNLPYYKL NDLGGVDKLG TSSFEHISHS
     LLGRPLSQKL AAVAVGLRSG GVLLTGGKGS GKSTLAKAIC KEAFDRLDAH VEVIDCKALR
     GKRLANIRKN VEEAFLEAAW RQPSILLMDD LDHIVGVPPT PEHENSPETV QSNRLAYVLK
     DLIKEVISMG SLIALIATSQ SEHSLHPSLV SAQGTHIFQC FKCIRSPDQK QRCEMLYSII
     KKKLNADIKK SSGLDLQCIA KETEGFVARD FTMLVDRAIH ACVSNQNAFQ NGELNLSTMD
     FQKALKGFTP LALRNVKLHK PKDIGWDRIG GLKDVKQILM DTIMLPAKYP ELFANLPIRQ
     RSGVLLYGAP GTGKTMLAGV VARESGMNFI SIKGPELLSK YIGASEQAVR DIFNRAQAAK
     PCIVFFDEFD SVAPRRGHDN TGVTDRVVNQ LLTQLDGVEG LQGVYVLAAT SRPDLIDPAL
     LRPGRLDKCL YCPPPDQNSR CEILEALSHS LSFANDVDFQ DLAAKTEQFT GADLKALLYN
     AQLEAIRTNL GSGLTQDFGC SSDSDFSLSS MVFLNHSSGS DDSAIDGEAG LEQSLISLDM
     SDLLPEDPRS NMYRLYFGSS YESELGNGTP SELSSLCLSG PNSITHDFTS VTQRDTASAQ
     PSVLRTASPE DSLENNQEQQ IEHLRTEINA IKANYRSKNG DSTFNQSVLA KNTLIITQSH
     LMTALDGIRP SISQGDWKNF TELYDNFQNP KKRKGQVGST FRPGQKITLA
//
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