ID A0A089ICS5_9BACL Unreviewed; 1447 AA.
AC A0A089ICS5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Phosphohydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=H70737_04165 {ECO:0000313|EMBL:AIQ22121.1};
OS Paenibacillus sp. FSL H7-0737.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1536775 {ECO:0000313|EMBL:AIQ22121.1, ECO:0000313|Proteomes:UP000029519};
RN [1] {ECO:0000313|EMBL:AIQ22121.1, ECO:0000313|Proteomes:UP000029519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL H7-0737 {ECO:0000313|EMBL:AIQ22121.1,
RC ECO:0000313|Proteomes:UP000029519};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009279; AIQ22121.1; -; Genomic_DNA.
DR KEGG; paej:H70737_04165; -.
DR eggNOG; COG1409; Bacteria.
DR eggNOG; COG3211; Bacteria.
DR eggNOG; COG5184; Bacteria.
DR eggNOG; COG5297; Bacteria.
DR HOGENOM; CLU_252190_0_0_9; -.
DR Proteomes; UP000029519; Chromosome.
DR GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 3.60.21.10; -; 2.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.40.380; Purple acid phosphatase-like, N-terminal; 2.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR029052; Metallo-depent_PP-like.
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; PF00041; fn3; 1.
DR Pfam; PF00149; Metallophos; 2.
DR Pfam; PF16656; Pur_ac_phosph_N; 2.
DR Pfam; PF00395; SLH; 3.
DR SMART; SM00060; FN3; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 2.
DR SUPFAM; SSF49363; Purple acid phosphatase, N-terminal domain; 2.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS51272; SLH; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000029519};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 661..763
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1266..1329
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1330..1390
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT DOMAIN 1392..1447
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
FT REGION 1186..1272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1196..1212
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1246..1262
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1447 AA; 156605 MW; 1C56F3B841B79F79 CRC64;
MMNRLFKQAV SMTLAFVMVL GITFTGIPAY AEDSNGDAGL LQLQSLEPVT LLAGNSTWKY
LDHGTDQGTV WRSVYDDSTW ASGQAPLGYK DSGSGVSSKQ FGALNTNISY GSNKSMKYRT
SYFRTNVTVN KEEIAKSDKI LGNFAFDDGA VLYLNGKEIY REAMPAGEIN FQTKSSTNLS
DPNEYTKVDL TEVVKANLKD GSNELSAEVH QSSDGSSDLY WDMNLIAYPV VEPVDPGVGK
PESIALTFNG NPQTSMGFNW YAPESVTGTK LEVVEASKLV DGQFPVGAQT YEGTSVTTSV
YMTKADKSAK KPVVLTSHKV IADHLQPGTE YAYRAGDGQA DNWSDIGTFT TESSSNQAFK
FLYTTDSQGT TEGDFDIWNH TLQEGLAKFP TSEFILNSGD LVDNGDIEEQ WGWFFNKPKD
ILANIPLVPL VGNHESKSYS NYTTHFNLPN VSNTGAKPDG SVYSFDYGSA HFMVINTEYY
GASSSLENNE IYKKQVEWLR SEAAKSDQKW KVVLLHKSPY SVASHTNDTD VLYYRANLTK
VFDELGIDMV IGGHDHTYTR SYQMYNNQPL TDIKPDKNGV VTDPKGTLYL ITNAAGNKKY
NVAAGPFPFA AKYEQPGKEM FTGMTVTNNE FSYEAYTTTT GGSTDLYDKY SIHKSDVAVK
PVQNAKATVA DGGKITLTWD APASGAPVSG YRIYEQNDLV SANWTVSVPN TEGQTSYSYT
VENTNPNQTY QFVIKAVSDR TNSEAKIASS DSIKKVTVTF NGDPVSAKGF TWYTALKSAG
SDLQVVENTG VTPDFTKAAE FTGRSAVSRN SKDELVHKAE ASGLKADTKY YFRVGDKALG
LWSAVGTFET AAKTGAFTFI DLADTQAKTE DEAILSGETM AKALTTFPNA EFVAINGDIV
DTGTNESQWN WLLGHSQETL LNTTIVPVAG NHEDKANAFY EHYNIKEAAG SPTETGAYYS
YDYSNAHFVV LNTNENSDEY ANFSKAQLDW MKADVKAAKA AGAKWIIVAM HKGPYTTSNH
ATDKDIMGAN GERAKVAPMM AELGIDLVLQ GHDHIYARTK PIKADGTAAD TVKIKESFNG
QTVEYTVNPD GTIYLIPATA GAKVYYKNMK KELGNAYYNL FEVANENTAA KYGADPSDAT
RPMRGQVQTF VGITVDAGKL TAVSYEIDQN VNEAKPYVLE EFGIVKGDEN GGVTPTPTPT
PTPTPTPTTE PTTAPTTAPT TAPTTAPTTA PTTAPTTKPT ATPTPTVAPT ATPAPTTAPS
PTATPVSKPS LTDTSNHWAA AVIEKAVAAG FVSGYPDDTF RPNQKVNRVE FITLLARALQ
LPENGDTSSF KDSAKIPAWA KSFVAQAVSL QIISGYDDGT FRPTQELTRT ELAVMVVRAL
GITVDPKATL TFNDAKDVPA WAVPYIAAAA KSGLVNGIGQ NKFAPNQKAT RAEAVTIILA
LLEKGQK
//
