ID A0A091V6B1_NIPNI Unreviewed; 1295 AA.
AC A0A091V6B1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Peroxisomal ATPase PEX1 {ECO:0000256|ARBA:ARBA00034532};
DE AltName: Full=Peroxin-1 {ECO:0000256|ARBA:ARBA00032509};
GN ORFNames=Y956_11288 {ECO:0000313|EMBL:KFQ98339.1};
OS Nipponia nippon (Crested ibis) (Ibis nippon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Pelecaniformes; Threskiornithidae;
OC Nipponia.
OX NCBI_TaxID=128390 {ECO:0000313|EMBL:KFQ98339.1, ECO:0000313|Proteomes:UP000053283};
RN [1] {ECO:0000313|EMBL:KFQ98339.1, ECO:0000313|Proteomes:UP000053283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_Y956 {ECO:0000313|EMBL:KFQ98339.1};
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; KL410701; KFQ98339.1; -; Genomic_DNA.
DR STRING; 128390.A0A091V6B1; -.
DR eggNOG; KOG0735; Eukaryota.
DR Proteomes; UP000053283; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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 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:UP000053283};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 601..751
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 884..1020
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1175..1197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1276..1295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1295 AA; 143602 MW; B37EEA3A23AF6F35 CRC64;
MWGSGNPGGG GAGAAAVTVV LSGTRDCFLH LPPLLASHLR LQQGQAVKVS CGHQPIFLSW
MEIRHRGHQG ENIAEINRQL AEKLGITDGE QVFLEPCSHV SSCQQVEVEP LSTDDWEILE
LHASSLEKHL LDQIRIVFPK AIFPVWVEQH THVYIKIGTL MPAAPYGRLE PCTELLILPK
TREREENITS TPSTESDILL KSFVKNNMEQ EETVKDPFAK QPYLKPGVLE QSKADANVTF
GSNVLPNIWN FIGSIFSHTS EQKQKTLCDK DEMSTFKDKL LNLIHMDSIF RVCQSQPPSV
QNASATHAFL KCNAIHVFPW NLEFIDLDPN PVVSYGKINE LLSPRQRHQE AKQNLPFEKQ
KHLTSTQDKN HSNSNSSQAS SEGSVVQIVW NGFEDLKSVI EYGHSGEALH VGRVWIPDDM
RKKLRIEIHS TVRIKSIESI PTIPVSLRLQ PKQNLHKDIH EDDVKSAFSS WLQDSSTDDL
PWIMTSTDSI HLSVKEGMEE FFLSVVHPTH TEENKSENIF MLSPSLLQKT NIQVLLHPLT
TKADGDSQPP MCDTDRNLPY HKLNDLGGVD KLGTSSFEHI SHSLLGRPLS QKLAAIAVGL
RSGGVLLTGG KGSGKSTLAK AICKEAFDRL DAHVEVIDCK ALRGKRLVNI RKNVEEAFLE
AAWRQPSILL MDDLDHIVGV PSTPEHENSP ETIQSNRLAY VLKDLIKEVI SMGSLIALIA
TSQSEHSLHP SLVSAQGTHI FQCFKCIRPP DQKQRCEMLY SIIKKKLNSD IKTFSDLDLQ
CIAKETEGFV ARDFTMLVDR AIHACVSNQN AFQNGGELNL STMDFQKALK DFTPLALTNV
NLHKPKDIGW DRIGGLKDVK QILMDTIMLP AKYPELFANL PIRQRSGVLL YGAPGTGKTL
LAGVVARESG MNFISIKGPE LLSKYIGASE QAVRDIFNRA QAAKPCIVFF DEFDSIAPRR
GHDNTGVTDR VVNQLLTQLD GVEGLQGVYV LAATSRPDLI DPALLRPGRL DKCLYCPPPD
QNSRYEILKA LSHSLSLAND VDFQDLAAKT ERFTGADLKA LLYNAQLEAI HTNLGSGLTQ
DFGSSSDSDF SLSSMVFLNH SSGSDDSAID GEAGLEQSLI SLDMSDLLPE DPRSNMYRLY
FGSSYESELG NGTPSELSSL CLSGPNSITH DFTSVTQRDT ASSQPSMLRT ASQEDSLENN
QEQQMEHLRT EISAIKANYR SKNGEDSTLN QSVLAKNTLI ITQSHLMTAL EGIRPSISQD
DWKNFTELYD NFQNPKKRKG QVGSTFRPGQ KMTLA
//