ID M0PHX1_9EURY Unreviewed; 316 AA.
AC M0PHX1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=AN1-type Zinc finger protein {ECO:0000313|EMBL:EMA69676.1};
GN ORFNames=C461_02066 {ECO:0000313|EMBL:EMA69676.1};
OS Halorubrum aidingense JCM 13560.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Halorubrum.
OX NCBI_TaxID=1230454 {ECO:0000313|EMBL:EMA69676.1, ECO:0000313|Proteomes:UP000011575};
RN [1] {ECO:0000313|EMBL:EMA69676.1, ECO:0000313|Proteomes:UP000011575}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13560 {ECO:0000313|EMBL:EMA69676.1,
RC ECO:0000313|Proteomes:UP000011575};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the peptidase S54 family.
CC {ECO:0000256|ARBA:ARBA00009045}.
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:EMA69676.1}.
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DR EMBL; AOJI01000013; EMA69676.1; -; Genomic_DNA.
DR RefSeq; WP_007998201.1; NZ_AOJI01000013.1.
DR AlphaFoldDB; M0PHX1; -.
DR STRING; 1230454.C461_02066; -.
DR PATRIC; fig|1230454.4.peg.426; -.
DR OrthoDB; 26567at2157; -.
DR Proteomes; UP000011575; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 4.10.1110.10; AN1-like Zinc finger; 1.
DR Gene3D; 1.20.1540.10; Rhomboid-like; 1.
DR InterPro; IPR035896; AN1-like_Znf.
DR InterPro; IPR022764; Peptidase_S54_rhomboid_dom.
DR InterPro; IPR035952; Rhomboid-like_sf.
DR InterPro; IPR000058; Znf_AN1.
DR PANTHER; PTHR43731:SF14; RHOMBOID DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43731; RHOMBOID PROTEASE; 1.
DR Pfam; PF01694; Rhomboid; 1.
DR Pfam; PF01428; zf-AN1; 1.
DR SMART; SM00154; ZnF_AN1; 1.
DR SUPFAM; SSF118310; AN1-like Zinc finger; 1.
DR SUPFAM; SSF144091; Rhomboid-like; 1.
DR PROSITE; PS51039; ZF_AN1; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 175..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..253
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 259..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..44
FT /note="AN1-type"
FT /evidence="ECO:0000259|PROSITE:PS51039"
FT REGION 290..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 316 AA; 33113 MW; 764785CC58080F5B CRC64;
MATCDVCGEY ENLPYQCNRC GKTFCATHRL PENHDCPGLT EWNDPGGVFD SSFDGGANAG
ASATDAGVAG RVKQRVQRET STGGLVSYFR GNATYVLLAA MWVTFLAQWA VTLLFGDAVH
SQIFVLRSDA LGRVWTWVTS VLSHSRVSLF HIIGNSIVIL FFGPLVERAV GSKRFVGFFF
ASGILAGLGH VLFAIATGAP TTGVLGASGA GFAILGVLTV WRPNMQVLLF FVIPMKIKYL
TWGIALVSAV LVIQTGTGGV GGIAHLAHLI GFAIGLAFGK RNENLARSAR GPGGIQMGGA
RGPGGPRGPG GPGGRF
//