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Database: UniProt
Entry: A0A0A2L2B9_PENIT
LinkDB: A0A0A2L2B9_PENIT
Original site: A0A0A2L2B9_PENIT 
ID   A0A0A2L2B9_PENIT        Unreviewed;       432 AA.
AC   A0A0A2L2B9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Band 7 protein {ECO:0000313|EMBL:KGO74149.1};
GN   ORFNames=PITC_022070 {ECO:0000313|EMBL:KGO74149.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO74149.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO74149.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO74149.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the band 7/mec-2 family.
CC       {ECO:0000256|ARBA:ARBA00008164}.
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:KGO74149.1}.
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DR   EMBL; JQGA01000706; KGO74149.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2L2B9; -.
DR   STRING; 40296.A0A0A2L2B9; -.
DR   HOGENOM; CLU_024949_1_0_1; -.
DR   OMA; YLQMLPK; -.
DR   OrthoDB; 179673at2759; -.
DR   PhylomeDB; A0A0A2L2B9; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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; IPR032435; STML2-like_C.
DR   InterPro; IPR001972; Stomatin_HflK_fam.
DR   PANTHER; PTHR43327; STOMATIN-LIKE PROTEIN 2, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43327:SF10; STOMATIN-LIKE PROTEIN 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01145; Band_7; 1.
DR   Pfam; PF16200; Band_7_C; 1.
DR   PRINTS; PR00721; STOMATIN.
DR   SMART; SM00244; PHB; 1.
DR   SUPFAM; SSF117892; Band 7/SPFH domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT   DOMAIN          83..241
FT                   /note="Band 7"
FT                   /evidence="ECO:0000259|SMART:SM00244"
FT   REGION          384..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   432 AA;  47103 MW;  955E593F143AA467 CRC64;
     MEGASRQTSR LLRPRGQKLL PQRFTRTSAV STTPLTQTQR RTLSHSLRSL APESLFNSFR
     TGGSYGEGPT SYFSNRQTLP ANTVVRFVPQ QTAWIVERMG KFDRILEPGL AILVPFLDRI
     AYVKSLKEAA IEIPSQNAIT ADNVTLELDG VLYTRVFDAY KASYGVEDAE YAISQLAQTT
     MRSEIGQLTL DHVLKERANL NTNITKAINE AAQEWGVVCL RYEIRDIHAP EAVVAAMHRQ
     VTAERSKRAE ILESEGQRQS AINIAEGRKQ SVILASEALR SEKINHASGE AEAIKLKAEA
     TALGIDAVSR AIEEGGENAH NAVSLSVAEK YVAAWSNLAR EGTAVVVPGN VGDMGGMIAN
     AMAVYGKVSE TQARGLAKKA LGVEGASRSS ERQQNSQIPT FFEEHTEQNT QSTVASQTAD
     EGFETVTGEH KK
//
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