ID A0A069DLN1_9BACL Unreviewed; 2211 AA.
AC A0A069DLN1;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=SLH domain-containing protein {ECO:0000259|PROSITE:PS51272};
GN ORFNames=TCA2_5861 {ECO:0000313|EMBL:GAK43365.1};
OS Paenibacillus sp. TCA20.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1499968 {ECO:0000313|EMBL:GAK43365.1, ECO:0000313|Proteomes:UP000028160};
RN [1] {ECO:0000313|EMBL:GAK43365.1, ECO:0000313|Proteomes:UP000028160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCA20 {ECO:0000313|EMBL:GAK43365.1,
RC ECO:0000313|Proteomes:UP000028160};
RA Fujinami S., Takeda-Yano K., Onodera T., Satoh K., Sano M., Takahashi Y.,
RA Narumi I., Ito M.;
RT "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain TCA20,
RT Isolated from a Hot Spring Containing a High Concentration of Calcium
RT Ions.";
RL Genome Announc. 2:e00866-14(2014).
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:GAK43365.1}.
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DR EMBL; BBIW01000024; GAK43365.1; -; Genomic_DNA.
DR eggNOG; COG1409; Bacteria.
DR eggNOG; COG4632; Bacteria.
DR eggNOG; COG5492; Bacteria.
DR OrthoDB; 9809781at2; -.
DR Proteomes; UP000028160; Unassembled WGS sequence.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 2.60.40.1080; -; 4.
DR Gene3D; 2.60.40.680; -; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.60.120.430; Galactose-binding lectin; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 1.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR018711; NAGPA.
DR InterPro; IPR008963; Purple_acid_Pase-like_N.
DR InterPro; IPR015914; Purple_acid_Pase_N.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR45867:SF3; ACID PHOSPHATASE TYPE 7; 1.
DR PANTHER; PTHR45867; PURPLE ACID PHOSPHATASE; 1.
DR Pfam; PF00149; Metallophos; 1.
DR Pfam; PF09992; NAGPA; 1.
DR Pfam; PF16656; Pur_ac_phosph_N; 1.
DR Pfam; PF00395; SLH; 3.
DR SMART; SM00635; BID_2; 4.
DR SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 3.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 1.
DR PROSITE; PS51272; SLH; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000028160};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 2029..2092
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2093..2151
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 2153..2211
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 1793..1838
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1797..1838
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2211 AA; 238971 MW; AF1010A688945B4F CRC64;
MIRWYRRSGQ AFLAFLLALF FMLQPLGSVY AALSEAPDTA FGRVLDVRKT ELAPGADYTW
YDMEIERGLE KMHFVEFNPD SPQLDLRAGT KGGYVYGMEG VSEMAEHTDA PGNRVIAGIN
GDFYDLSGYG TGVPNGLFVD QGRILNSGSS SFAFGLKEDG TSVYGKPKLT MSVTIDGTQT
NLTSINRYRE NNHLTLYTPD FYTSTKTNAS GTEVVLQVQE GDVKSGQTMK LKVLEVRANQ
GDAPIAEGNV VLSASGTKLP VVSSLAAGDE LTASFELDGE WQDASMVISG QGPLVKDGVV
QTGVGPEGVH PRTAIGTKAD GSIVLFEIDG RAPGFSEGVT TEELAKILAD IGVVNAMNLD
GGGSSTFVAR MPGTSDVQML NRGSDGGERA TGNGLLLVNT APEGAASRLA VTPGEERILA
GSSYEYNAAA VDQTGHPAEH EGAVTWSVSP DLGTISEDGV LTAGQNAVAG QVSASAGGLE
GTAEVEVVDQ ITELEFLDDI KTYNTGVNEK LTVTALRDGQ VIQSSNDVFE WRVEGDIGTI
DDNGVFHSTN EGGQSGIIFV SYKGIETSME VNVGVPPVVL EEFESIDSYK ASGAAYNSVK
VDLNTDPDYV RSGDGSIKLS YDFVGMTGTS GAYVSANSKA ENIQIPGYPQ KIGMWVYGDG
QKHWLRAQVR DGNNAAFAID FTGADYGVDW TGWKYVEANI PAGKTTPLTM DLPVRYMETN
NNKKTAGAIY IDQIRAVYGP LDEDHEPPVI TDVTPSEDTA VTTGTPVIHA HAADAGWDVE
VHPGTTLIDP SKIRMYIDGE QVAHTLYPPE GRISYTPGLP LEDGYHTVKL AVRDLSGNQT
IKEWNFTVDT GAPKFRYTTP EQVYAGHTYT VDISADQVDL LTGGHLELGF DTAFVKDISV
VKGDKLAESQ ITRSVDAETG VARMQFSGLE SASLTDEDII AQISYTVNGT ASGSNAIAFR
SSELDMVGSN EPKSYRGASL KSEIKHELLL QWDENIAQNY VTTFTVTDEN GQPVEGAKLF
ADGAEVGDGT LVTDASGQLR TGQLTEAMKS YDVQAIKDRQ HSLVSEFTTS SLAGTETPYN
ITVGMGEDPT ISRSFNWHTH PSVNETVVEI AEEEGFAGFN QPDVIRLSGD SSLFNTLDIG
TIRVHKASAD VLKPGTAYVY RVGDGTEHYS EQGSFTTAPD TGDYTKFLVF GDSQAADLAG
FELWGRTMDA AIAEQPDAEF MVHVGDMVDN GFKEKEWNWW FSQVQEELMN LTAVTLVGNH
EVTGTKKNGD FLAHFNHPQN GSQNQKGTNY SFDYKNMHIS VLNSEYEIEE QKAWLEADLE
NTDKQWKLVF FHRGPYASIY DTENVRTAWT PVFDKYNVDL VMNGHDHIYL RTYPLYNHEI
VGEREGTTYI IPGATGPKFY ERTERYFQDV VVDEDIQMYS SVEVDGDTLT VTTKTVDGKL
VDKAVLENPM YTVEAPTSEI QVGEELQLSV NGMLPEDMEW SVTELSEEQA KEGLEGLVEV
SESGVVKAIK SGDVVIRATS KSSPNRFGDI KLHITDAEAP VAIELKGKPW LKPGETDTTV
VEAVYASGER MPITEGVQYQ SADPAIAEVD ELGVVTALTE GMVKITAKYG GLTDDYDLQV
IEEQLEPELA YIQFSGPEQL QVGETSATVT QAVYTDNSLH PLTEGVQYTS SEETVAAIDS
EGTITALREG VTVISAVYGE FSNAFTLTVL DEEQPAVDLE RIELTGIPSR LEVNDTAKAL
VNGYYSDGTV SEITEGVKFS SSNDNVASID ANGLIRTHRK GETVITAVYG EESASQALRV
EPSSDTTGPD EDNSESGNGS NEDNGSNNGN GEEEASNTPG QLIVSEEDLN ALGSEEQIQF
SMGSNSFTEL VMPGKAAELA EGKSITVQAN NIRLVIPSEV LRKFADLASD EQLADSTIVL
RAKAADEAEV SSWLSQAEDR YGANLQIGGA YDLTLSLEPS NGKVITLNEF EVEEPIVISL
PIPEGANPAL TGIYYGESDG SVTYMGGTVR NGWVTAELNH FSFYAAMEYN KSFTDLPVGH
WAESAVKQLA ARQIVEGTTT ERFEPNRTVT RAEFATMLAR LLNLEGEAQA EFTDITSDQW
FANEVGLAAD AGIVQGYTDG SFAPAQRITR QEMAAMIIRA YTFKTGEKPE AGDAEYTDLA
DSPQWAVQAI MVANKLGVVN GFSADEFRPF GVGTRAESAQ MMFNLANIMN P
//
