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Database: UniProt
Entry: A0A1I5ZEV7_9PSEU
LinkDB: A0A1I5ZEV7_9PSEU
Original site: A0A1I5ZEV7_9PSEU 
ID   A0A1I5ZEV7_9PSEU        Unreviewed;       465 AA.
AC   A0A1I5ZEV7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Regulator of protease activity HflC, stomatin/prohibitin superfamily {ECO:0000313|EMBL:SFQ54961.1};
GN   ORFNames=SAMN05421810_109121 {ECO:0000313|EMBL:SFQ54961.1};
OS   Amycolatopsis arida.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=587909 {ECO:0000313|EMBL:SFQ54961.1, ECO:0000313|Proteomes:UP000198727};
RN   [1] {ECO:0000313|Proteomes:UP000198727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.5579 {ECO:0000313|Proteomes:UP000198727};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family.
CC       {ECO:0000256|ARBA:ARBA00008164}.
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DR   EMBL; FOWW01000009; SFQ54961.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I5ZEV7; -.
DR   STRING; 587909.SAMN05421810_109121; -.
DR   Proteomes; UP000198727; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd08829; SPFH_paraslipin; 1.
DR   Gene3D; 3.30.479.30; Band 7 domain; 1.
DR   InterPro; IPR001107; Band_7.
DR   InterPro; IPR036013; Band_7/SPFH_dom_sf.
DR   InterPro; IPR018080; Band_7/stomatin-like_CS.
DR   InterPro; IPR001972; Stomatin_HflK_fam.
DR   PANTHER; PTHR43327:SF63; PROTEIN QMCA; 1.
DR   PANTHER; PTHR43327; STOMATIN-LIKE PROTEIN 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   PRINTS; PR00721; STOMATIN.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
DR   PROSITE; PS01270; BAND_7; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:SFQ54961.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Protease {ECO:0000313|EMBL:SFQ54961.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198727};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          22..180
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
FT   REGION          312..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        318..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..446
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   465 AA;  50298 MW;  2FA1FF94CBBDB65C CRC64;
     MSTAALIVVA IIALFVIVTV AKAIMVVPQA QSAVIERLGR FRTVASPGLN FLVPFLDKVR
     ARIDLREQVV SFPPQPVITQ DNLTVSIDTV VYFQVTDSRA AVYEISNYIV GVEQLTTTTL
     RNLVGGMSLE ETLTSRDQIN GQLRGVLDEA TGRWGIRVAR VELKAIDPPP SIQDSMEKQM
     RADREKRAMI LTAEGQRESA IKTAEGQKQS QILAAEGSKQ AAILAAEAER QSRILRAQGE
     RAARYLQAQG QAKAIEKVFA AIKAARPTPE VLAYQYLQTL PQVAQGDANK VWLVPSDYGK
     ALEGFARSLG APGDDGVFRY EPPKEEQVEK PPLEDEEVAS WFDTSTDPKV AEAVREAEAV
     ARQEVPGPLA PPRTVPPALS SLRGTPSQEE ESQPAAPLPK RSPEPPAPEF QQRPGGDQPP
     QPPQPPQQQA QPPAPPRPPA GPYGGQQGGP YPPQGGPYGG PPRQQ
//
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