ID A0A0V1LK02_9BILA Unreviewed; 1485 AA.
AC A0A0V1LK02;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Mitochondrial chaperone BCS1 {ECO:0000256|ARBA:ARBA00016942};
DE AltName: Full=BCS1-like protein {ECO:0000256|ARBA:ARBA00032816};
GN Name=bcs1l {ECO:0000313|EMBL:KRZ59818.1};
GN ORFNames=T02_6000 {ECO:0000313|EMBL:KRZ59818.1};
OS Trichinella nativa.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6335 {ECO:0000313|EMBL:KRZ59818.1, ECO:0000313|Proteomes:UP000054721};
RN [1] {ECO:0000313|EMBL:KRZ59818.1, ECO:0000313|Proteomes:UP000054721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS10 {ECO:0000313|EMBL:KRZ59818.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Mitochondrion inner membrane
CC {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004434}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family.
CC KE4/Catsup subfamily. {ECO:0000256|ARBA:ARBA00038485}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ59818.1}.
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DR EMBL; JYDW01000036; KRZ59818.1; -; Genomic_DNA.
DR Proteomes; UP000054721; Unassembled WGS sequence.
DR GO; GO:0000813; C:ESCRT I complex; IEA:InterPro.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR CDD; cd19510; RecA-like_BCS1; 1.
DR CDD; cd16654; RING-Ubox_CHIP; 1.
DR Gene3D; 2.100.10.50; -; 1.
DR Gene3D; 6.10.140.2020; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR014851; BCS1_N.
DR InterPro; IPR045202; CHIP_RING-Ubox.
DR InterPro; IPR041312; CHIP_TPR_N.
DR InterPro; IPR023341; MABP.
DR InterPro; IPR018798; MVB12A/B.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR003689; ZIP.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR16950:SF25; ZINC TRANSPORTER SLC39A7; 1.
DR PANTHER; PTHR16950; ZINC TRANSPORTER SLC39A7 HISTIDINE-RICH MEMBRANE PROTEIN KE4; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF08740; BCS1_N; 1.
DR Pfam; PF18391; CHIP_TPR_N; 1.
DR Pfam; PF10240; DUF2464; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13181; TPR_8; 1.
DR Pfam; PF04564; U-box; 1.
DR Pfam; PF02535; Zip; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01024; BCS1_N; 1.
DR SMART; SM00028; TPR; 3.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS00674; AAA; 1.
DR PROSITE; PS51498; MABP; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS51698; U_BOX; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00022792};
KW Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW Reference proteome {ECO:0000313|Proteomes:UP000054721};
KW Signal {ECO:0000256|SAM:SignalP};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1485
FT /note="Mitochondrial chaperone BCS1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006881941"
FT TRANSMEM 184..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 220..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 261..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 385..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 418..443
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 484..517
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 552..585
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 679..753
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT DOMAIN 791..939
FT /note="MABP"
FT /evidence="ECO:0000259|PROSITE:PS51498"
FT REGION 65..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..140
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1485 AA; 167757 MW; 39841338670ACDBD CRC64;
MAVRFCIVAL ISSVFLMNFG VVLNHDSHVH HHHQHQEEAP HFKYTKEAND PQYNRQGVDQ
TVDDHHHHVD HSHSHDHDHD YHDHNHDHDH DHHDHSHSHD HDHHDHGHSH DHDHHDHSHD
HGQGSGHHHH HHHHHAHGHG PHFHFHEEPG IVKYLQIGSL KWIRSIPFFD AALELIPKDP
TTRLWFMAIG STVAVSLAPF LILPFVPLTG GVMNESNENL LKVLLSFASG GLMGDAFLHL
IPHALIARNA ELAEGSHGHD MSVGLNVLYG ITGFLIVEKL ARLLKGDHDH SHNAEEISSD
EEAEESTRKI VSDATEIRED LKIAGYLNLI ADFAHNFTDG LAVGASYLIS DMIGVITTIT
VILHEVPHEI GDFAILIRSG YSKPAAMILQ LITALGAVLG CMVSLYSANS ELLLEAAAAS
WVLPFTAGGF IYIATVSIIP ELLDETSFWQ TAKELAAMFV VVICVSDDVE ASLIRRAVKL
SMSATDFKQQ GNRYFSAHLY DDAIRCYNRA IVLDPDNATY FTNRALCHLN LKRFENAAQD
CRKALEMDRA SVKASFFLGK ALIHLEQFDE AAKVLLRALE LAKSQNMNYG DEITSMYRTA
RRERFRLEEE KRIMQEISLQ TYVVDLILRD KDEQIKKLKG CTDDPSKEEL CEIETAAEER
ITQINNLFSQ VDERRRKRDI PDYLCGKISF ELMRDPVITP SGITYDRKDI MEHLHRVGHF
DPVTRTALTA DQLIPNLSMK EQYKGDTNEN AKRWAPHHRL IKVGQCGKVG VMQNQSRLLM
IIMNGLYLGT DPPITEIIFV ADKSKAPPHY YVISKAEDDT SCEADLWKDS FFNFNRNYRY
LCYSRSENAS QASGMIIADV CLVNEKDKIP TNYAAVEWTY DSREKCLRRK RLCVRRVHRS
VAIDAVCSIV LLAKSKAPPV GYFCAGDIEG FLLCYKFCAM YSRDRNSVVA AGLPYPENSS
LISNLYPRVP QPNPQKTMSS EENYTSSKTS LRTAVLSPLQ SQSGVEGVPF ELHAKLKARF
DLTSALKDLP PLPDSSNYLE AMCDYSSCVI AVRQHCYTWS KMMDYLSSLG SNPYFGAGFG
LFGLGTLAAA LRKGAQLGSM LFYRKCLISM EISSEDKAYS WLLHWINAYA ASETQHVSVE
TIYQQSSGGK VSTRFRFVPG PGDHFIQYKG RWVRLHRDRD KQMVSLQHGS PFETVTLTTV
GRNADFFSRM LDEARTMALE QMQSGTVVYQ AVGHEWRQFG HPRRKRPLQS VILDEGIQEF
LVTDVREFIS TSSWYVDRGI PYRRGYLLYG PPGCGKSSFI TALASELEYG ICMLSLSEQT
LTDDRLQHLL NVAPLETIIL LEDVDAAFIN REEQHPDMRV AYSGLTHVTF SGLLNAVDGV
ASSEARLLFM TTNYINRLDA ALIRPGRVDV KQYVGYCSDY QLKTMFSRFY PNASPVQAVA
FQRKVRDHYP TDSISAAQVQ GYFLMHKYDA ASAIENIDKL LKKQP
//
