ID A0A024Q919_9BACI Unreviewed; 1994 AA.
AC A0A024Q919;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=LTD domain-containing protein {ECO:0000259|PROSITE:PS51841};
DE Flags: Precursor;
GN ORFNames=BN990_01062 {ECO:0000313|EMBL:CDQ38787.1};
OS Virgibacillus massiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=1462526 {ECO:0000313|EMBL:CDQ38787.1, ECO:0000313|Proteomes:UP000028875};
RN [1] {ECO:0000313|EMBL:CDQ38787.1, ECO:0000313|Proteomes:UP000028875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vm-5 {ECO:0000313|EMBL:CDQ38787.1,
RC ECO:0000313|Proteomes:UP000028875};
RA Urmite Genomes U.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000028875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Vm-5 {ECO:0000313|Proteomes:UP000028875};
RA Khelaifia S., Croce O., Lagier J.C., Raoult D.;
RT "Draft genome sequence of Virgibacillus massiliensis Vm-5.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:CDQ38787.1}.
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DR EMBL; CCDP010000001; CDQ38787.1; -; Genomic_DNA.
DR RefSeq; WP_051739027.1; NZ_CCDP010000001.1.
DR STRING; 1462526.BN990_01062; -.
DR eggNOG; COG1409; Bacteria.
DR OrthoDB; 9772095at2; -.
DR Proteomes; UP000028875; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR001322; Lamin_tail_dom.
DR InterPro; IPR036415; Lamin_tail_dom_sf.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR PANTHER; PTHR43143; METALLOPHOSPHOESTERASE, CALCINEURIN SUPERFAMILY; 1.
DR PANTHER; PTHR43143:SF5; SECRETED PROTEIN-RELATED; 1.
DR Pfam; PF00932; LTD; 1.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF74853; Lamin A/C globular tail domain; 2.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS51841; LTD; 3.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000028875};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..32
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 33..1994
FT /note="LTD domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001532555"
FT TRANSMEM 1964..1987
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..287
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT DOMAIN 461..607
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT DOMAIN 749..897
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT REGION 40..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1887..1955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1894..1939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1940..1955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1994 AA; 224917 MW; FD9B9D0C713FB16A CRC64;
MKKRKLHSLL AVIAATMLFV TSLLQSTSIA YASVSNPIEK VENEEQTDQG ENKTADAKEE
QTMEELKDQK ELPLEIEHEP PSQVGYNQDQ YIQATVPNAT TVQLVYQATK YAQPIRVDMK
RSKNDTFTET IPGSVLWSDS VDYWIEAKNN QEEKTSTVYS LPIKKQADDV SLSTSSLLIT
EVNLREQPFI ELYNNTNQQL KLNDYTLSLG DKKLDIPEST VASGKTIVLW LSEANKNRND
FNQLYETNLT DDQLIMLEYK DLPTQDIKLQ LVHNQKKEDV STVSYSDSDT AASQLYYYHE
GEMKSGGLTK QAAPINLLPG QVPENVIEIK EPTSPENQTE GTSKNKQEKA EQQQALYDNA
DKGKNESTQP IQHEPITSAT DTNDLTITAT APNTNQLTLH YRTGEGMTVQ ELVFTKATDS
NVYTVTIPKE QLWSPTFSYR IVAEAEDGTT ISYPETNDIQ VTIEQTNKAD PQTIPPLLIT
EITPDTANIN GADAYEFIEV YNNSNQPIQM SDYQIIYRYP TETADQHWDI TNDQLIEPQD
SFIIWIKNDG NQKQTVADFN THYGLTMPES HVAKLDSAGM ANGSERTLIV ADKYENEIIA
ASYNQVTDDT NADQGIVYTY PAENDRMVKA GIGEGMTPLT IIDGQAPEEP VVINDTSTPV
IESPTFTVTK EQIIFNVTVT SEQEIIGTNL AILQSEDTQY QTWSLQASED DSQTYTVTIP
REEIWRETIQ FYVEASNQSG DTKTDVEDYT FSQQPIDYQE VPPLLMTEIT PDTTNLNGAD
GYEFIEVYNN STESINFKDY SIRYRYPNTS ASNDLVWGPE EGKDIMIPSG ESIVFWVINH
GNTDKQAADF NAHFQTNLVD GDNLFKIYNN GMANGSERTL LIATKTGEEL SYASYNDLVD
SDDTVANKGI FYRYPIDGSL QSTKISAGEW DATPGETLAA QVPPKRINLP ADREEPIIKN
TTTKKKITSE EPVTLSAAIT DNIGIKSAAV YYRTDEKKDF RKVNLEKQAD NHYQHIVYEP
ELIGKQTLEY YFVASDGRNQ LTAPANYIEI ENPFSQEGLR LNLEDNQLLS GEKVIKATAD
TYNNETQLFI DDRQITDTFE AMETEAYFAF DVKETNIYFK NGVTMGDEIL EVFDDTYTDF
TTLTVPVSAE RLQQGENTIS IRAGNKVSPF DETSEENRDD FMIKNIRLVL KDGTTIYDPA
YSDPSKAYSI GDSPRKDAIY DFNFNLEEEQ FTSTAYVFDT TSVEDGKHEV KTSYQDKTIT
TAIITDNTSP TLIPSINEGK TYKGEFTIDA EAKDATSEVT SITATLDGEY ISLPYETSSA
LLKPGSHELV YQATDKANNV AKKKVSFSVT EEHPLMPDWL SDNAHTTSAN LSVTVKDPTN
DIMDVNFHEA FQYTAEDENI TISQNAVSTE PPIGYLPDGE DRLTKEQRNQ LQALDGNELS
TESKQKFPYH RFDVRVDKQV DKNDEIEIVW NGSSLEGRKV TMYAWNYETS KWAPLVSTIA
GKEAFQLIGS VKGLDYVQDQ KVSVIVQDQI ANPGEDFSFV WMADTQYYSE SYPYIYDKQV
DWIANNRDTL NIEYVFHSGD LVNVYDDFEQ WDVADRSMRV LDDAGIPYGV VAGNHDVYNK
SRNYENYYQF FGADRFENND YYGGSFQNNR GHYDLISANG MDFIMVHLGW GIEEEGIEWL
NEVLQAHPNR KAILNVHEYL LATGSRSPTG DELFEKVVVP NENVFAVLCG HYHNAQTLID
EIDDNRDGIS DRTVYQMLAD YQGGPEGGQG YLRILNFNME NNQIDVQTYS PHLDDYNYYN
PEEYPGKDTF SLDYDMAAQT KKVATDYLEV NVYTDTLIDR VENVPSGEKA SVAWQNLDPD
HEYFWYVEAT DKYGGTTRSD IWSFLTEDGE IVNPGDNDDN KEEDGNESEN KDGDGDGNPS
VEKPKAGSEQ DKTDKNQDDS SPLIENTSNN PGNGSSLPDT ATSIYNYLLI GALFLLAGLS
IWLIYYYRRR HILT
//
