ID A3LMU7_PICST Unreviewed; 867 AA.
AC A3LMU7;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 2.
DT 24-JAN-2024, entry version 103.
DE SubName: Full=Mitochondrial respiratory chain complexes assembly protein RCA1 (TAT-binding homolog 12) {ECO:0000313|EMBL:ABN64747.2};
GN Name=RCA1 {ECO:0000313|EMBL:ABN64747.2};
GN ORFNames=PICST_34770 {ECO:0000313|EMBL:ABN64747.2};
OS Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS Y-11545) (Yeast) (Pichia stipitis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX NCBI_TaxID=322104 {ECO:0000313|EMBL:ABN64747.2, ECO:0000313|Proteomes:UP000002258};
RN [1] {ECO:0000313|EMBL:ABN64747.2, ECO:0000313|Proteomes:UP000002258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545
RC {ECO:0000313|Proteomes:UP000002258};
RX PubMed=17334359; DOI=10.1038/nbt1290;
RA Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.S.,
RA Passoth V., Richardson P.M.;
RT "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT yeast Pichia stipitis.";
RL Nat. Biotechnol. 25:319-326(2007).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC family. {ECO:0000256|ARBA:ARBA00010550}.
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DR EMBL; CP000496; ABN64747.2; -; Genomic_DNA.
DR RefSeq; XP_001382776.2; XM_001382739.1.
DR AlphaFoldDB; A3LMU7; -.
DR STRING; 322104.A3LMU7; -.
DR MEROPS; M41.003; -.
DR GeneID; 4837507; -.
DR KEGG; pic:PICST_34770; -.
DR eggNOG; KOG0731; Eukaryota.
DR HOGENOM; CLU_000688_23_0_1; -.
DR InParanoid; A3LMU7; -.
DR OMA; ARQKGNF; -.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000002258; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.1690.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR HAMAP; MF_01458; FtsH; 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; IPR005936; FtsH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR PANTHER; PTHR43655:SF14; MITOCHONDRIAL RESPIRATORY CHAIN COMPLEXES ASSEMBLY PROTEIN YTA12; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 1.
DR Pfam; PF01434; Peptidase_M41; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002258};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 226..244
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 422..562
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 163..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 867 AA; 97715 MW; 6F55999A57E413E1 CRC64;
MLNAFLDQCH IYNSNNRSRL TPDQIIDEID TMFKNLHPDL TPLTKKEVLF YFHIYYSLSN
NVVFLDELDF QNVQVTKYLK GYVSMSPTTN KEELIEELAK SSETAPEVVS SWFNIFDTLS
STPFADSNTR YTNPLCPYEY ARYQSFTNEL RTMQEKLKQV YGGSTTKDSK NESVFGNFSF
QTNSDNNKGK DSKTNSSKDN KDGKDNKNNK KNIDIEINFN SSPMRFFQVG VLIGLLSYIV
YNLTQSSNNE ISFQQFTTDF LSKNLVDKVV VVNNRIAVVE LNENGRAQYP HHEGNFYFNI
GAIESFEKNL RSVQEDYNVA DSMRVPVIYT NEGSTTKMLV NFLPTVLFLG AIYYMTKKAT
GMGGMGGPLG FGKSTAKKFN QDTDIKIRFR DVAGMAEAKE EVMEFVKFLQ NPEKYERLGA
KIPRGAILSG PPGTGKTLLA RATAGEAGVP FYSVSGSEFV EMFVGVGASR VRDLFKTARE
NAPSIVFVDE IDAIGKQRSK GNASGANDER ETTLNQLLVE MDGFDTSDHV VVLAGTNRAD
ILDRALLRPG RFDRHISIDN PELQGRKEIF QVHLRKIKLK KDIDDDLPGR LAALTPGFSG
ADIANVCNEA ALIGARYNAD SVTLRHFELA IERVIGGIEK KSKLLNAEEQ RIVAYHEAGH
AVCGWYLKYA HPLLKVSIIP RGQGALGYAQ YLPPDQFLLS TLQLYDRMIM TLGGRVSEEL
HFSSVTSGAH DDFKKVTNIA QSMVLRFGMS KKVGMVNYAD TQSQDNLTKP FSDETSKTID
EEVQRIVGEC HKRCKELLIE KSKEVELVAE ELLKKEFITR EDMIRLLGKR PFPETNDAFD
KYLEKKPAFK NEKPADEKKD DEKEEEK
//
