ID A0A317KZL9_9BACI Unreviewed; 1965 AA.
AC A0A317KZL9;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Metallophosphoesterase {ECO:0000313|EMBL:PWU68454.1};
GN ORFNames=DLJ74_08390 {ECO:0000313|EMBL:PWU68454.1};
OS Gracilibacillus dipsosauri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=178340 {ECO:0000313|EMBL:PWU68454.1, ECO:0000313|Proteomes:UP000245624};
RN [1] {ECO:0000313|EMBL:PWU68454.1, ECO:0000313|Proteomes:UP000245624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD1 {ECO:0000313|EMBL:PWU68454.1,
RC ECO:0000313|Proteomes:UP000245624};
RA Deutch C.E., Yang S.;
RT "Genomic analysis of Gracilibacillus dipsosauri DD1 reveals novel features
RT of a salt-tolerant amylase.";
RL Submitted (MAY-2018) 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:PWU68454.1}.
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DR EMBL; QGTD01000008; PWU68454.1; -; Genomic_DNA.
DR OrthoDB; 9772095at2; -.
DR Proteomes; UP000245624; 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; 2.60.40.1260; Lamin Tail domain; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
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; 3.
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:UP000245624};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..35
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 36..1965
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5016281338"
FT TRANSMEM 1933..1953
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 122..229
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT DOMAIN 427..555
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT DOMAIN 709..871
FT /note="LTD"
FT /evidence="ECO:0000259|PROSITE:PS51841"
FT REGION 39..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1847..1923
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..287
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1847..1862
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1864..1878
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1883..1915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1965 AA; 223233 MW; 5E449EB6719CB8CC CRC64;
MRKRNKKKVA RLFSVFLITC ILFSHVFVHF SVVQASPNQK IEENTDEERS AETSGQQSVE
SKDKQLTRKP NQIHNEEDKS STKEVEESNE ITESATKQEK NIPEIDEKKE KVEKSSIENA
EGTPSIDFQK VPSILITEVM PFSKENDQFA YFEIYNNSNQ AIQLDYYNIS FHSTASSGEK
ILELPPTSLE PGETVVAWNN GGNLSIDDFN HHYGTKLTEE QVISYQAISF SNTNKQTISI
RDNQQEIVSA SFSEEDIQLG KTLTYLYPQE STAMQTSKQQ QKPTPGKLDK QQIPEKPVTV
SASDAPIIKS KPVSEADVNS TITINAIIDD ADSSLQAKLF YRYQGEASYR SVEMSRQESN
NYHAEIPAEE VITGQIEYYI MATNAHHRAV DPTKDTPNVI TVKKIEKEKK QVNTVVEEQK
MINEDFTQYP QLLITEISPN TAGGGTDYFE YFELYNNTNQ TLHLSDYHFI YHYTDSSKNI
MFELPDVDIA SEETLVFWYN NGKNELEAFN EQFSTNLTKE EVIPFNSSSF PGFANGGNRA
LIIKDHKNNE VVYADYLGED NNNDGKVIQY KYPLEEATKM KKHQVLADPT PGMVDEVQVP
SESVEVPEEE IDQEAPMITH KQVKEGQAFS PISIQAEIVD NHTIPSANLY VKKKDSEYIS
LPMSIDPENP SQYTVEIPGN HVDENLTYYI EATDGRNKSK TEEFTIQIDQ EKIDSQALPP
LLVTEVVPDT TNTGSADGYE FIEIYNNTDQ PINLKDYKIQ YRYGTDPESD VIWPSIPDDV
VIPAKETLVF WIINGHNNDQ TVADFNANFS SQLVENQDIV RIESAGMANG STRGLIIASN
TGIEYSIAYY NDTENVDDVV ANKGIVYRYP VDKTNVMEKI SAGELDATPG TVEDYQVPNE
PVQKQQDTIA PEIDNITTIS QVNHTENIDL QVSANDNQEV KTVAVYYRTE DEKEFKEALL
EESEEKGVYQ YRIYAPEIIG KEYVEYYFQA SDGTNSVKSG IETIRVASDL DQSPLRLNVE
NEQILSGKSI IKGTAEKSSS DDLIMKIDEQ VINDTYKAVE HQAYLAFEVS GINTYFQNGV
TIGDEIVHIF DDWMAQWETI TVPIDPTKLQ LGDNTITIRA GNKATPWEGD PGENRDDFNL
RNVRLVMTDG TVLTDPSHPD PSDVLDMGDD GTERIAEHFT FTITDGLANS LAYQWDTTTV
EDGSHRVQIL QNTKLIERKV FVDNTAPIIS PNMEENRSYK GEFEINAEIT DEIAGVDSYQ
AWLDNEEITL PYMTSSGSLA PGEHVLKIKA IDKVGNAKIE EIMFHTVEEN PTEPNNQTDT
QIGDPKLRVK VKDPMGDQLD VGFYQAFQYK PSDKSSVISY QSTAKTEPPA TKKISAQAEL
SDQELKLASE QDGKYLVTDS TTEFPYHRFD VTLDESVNND DQVELVWNGH SLEGRKVSMY
AWNIEKAQWD LIDYQIAGTD DFTLSGYVEV TKYADNHTIH VIIQDEIPAN PNQYDYTFVW
MSDTQYYSES YPHIYDRQTQ WIAENQEKMN IEYVFHSGDL VDEADQEYQW LHADEYMKTL
DDANIPYGVL AGNHDVLQKD NDYTEYYKYF GEDRFMEKPY YGGSYLNNRG HYDLISVNGN
DFIMMYLGWG IDEEGIAWMN EILAQYPDRM AILTFHEYLQ ATGTRHPLGE KLYNEVVIPN
ENVMAVLSGH YHEAQTLIDE IDDDGDGTPD RTVYQMLADY QAGPEGGQGY MRLLHFDSTN
NRIFVNTYSP YMDDYNYYDT DEYPNKDEFM IDLDLTPKEK RVATDSFVVN VYTNSEIGTV
QNVASGDTAE ITWSGLEEGK TYYWYTRITD QYSGSTRSSI WSLIKGRDDV SEGEHDENNQ
DEGTGTGDND QEQPPTKPEV NPIQDEKGNE IDNQDEIEKH SESDKIIRVN KNQDKEPLTS
KQGISLPDTA TNIYNLLLGS MVLLVMGIIL FIWQRQKRQK QKYSN
//
