ID Q1ZRL3_PHOAS Unreviewed; 457 AA.
AC Q1ZRL3;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=MBL fold hydrolase {ECO:0008006|Google:ProtNLM};
GN ORFNames=VAS14_06323 {ECO:0000313|EMBL:EAS65314.1};
OS Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS CCUG 15956)).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS65314.1, ECO:0000313|Proteomes:UP000001603};
RN [1] {ECO:0000313|EMBL:EAS65314.1, ECO:0000313|Proteomes:UP000001603}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14 {ECO:0000313|EMBL:EAS65314.1,
RC ECO:0000313|Proteomes:UP000001603};
RX PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA Robb F.T., Kjelleberg S., Cavicchioli R.;
RT "The genomic basis of trophic strategy in marine bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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:EAS65314.1}.
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; AAOJ01000002; EAS65314.1; -; Genomic_DNA.
DR RefSeq; WP_005369143.1; NZ_CH902600.1.
DR AlphaFoldDB; Q1ZRL3; -.
DR eggNOG; COG1236; Bacteria.
DR HOGENOM; CLU_009673_5_0_6; -.
DR OrthoDB; 9803916at2; -.
DR Proteomes; UP000001603; Unassembled WGS sequence.
DR CDD; cd16295; TTHA0252-CPSF-like_MBL-fold; 1.
DR Gene3D; 3.40.50.10890; -; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR022712; Beta_Casp.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR011108; RMMBL.
DR PANTHER; PTHR11203; CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR FAMILY MEMBER; 1.
DR PANTHER; PTHR11203:SF37; INTEGRATOR COMPLEX SUBUNIT 11; 1.
DR Pfam; PF10996; Beta-Casp; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR Pfam; PF07521; RMMBL; 1.
DR SMART; SM01027; Beta-Casp; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
PE 4: Predicted;
FT DOMAIN 13..220
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
FT DOMAIN 236..376
FT /note="Beta-Casp"
FT /evidence="ECO:0000259|SMART:SM01027"
SQ SEQUENCE 457 AA; 50397 MW; B9ADA3320AD56387 CRC64;
MDIIHHGAKT GVTGSCHELV IGNSSLLVDC GLFQGAENKN NKFDIEFDVK RIEALLITHS
HIDHIGRIPW LLAAGFTGPI YATEATAALL PLMLEDGLKI QLGFNSQQCK QFTQLIQQKI
RPVPYDCWAK VVLLNGDSVS IRFRQAGHIL GSAYIEVELP DQNIVVFSGD LGPCNTPLLT
DPVSPDKVDV LVIESTYGDK ALHDIQQREA HLRKIIEHSL QDGGAILIPA FSVGRTQELL
FDIENILADV LTGSSHDNSY RRWKSLPVIL DSPLALKVTE QYRHFQELWS KEAKDRRYMG
RHPLSFEQCI TIETHQDHIE LVNRLKHSGE PAIIVAASGM CAGGRIVNYL EALLSDSRTD
VIFAGYQAEG TLGRVLCNGD EVVEIHDQVI DVKANIYKMS GYSAHAAQDD LVKFVAGINE
GPAVIRVVHG DITAQTQLAK CLQDCKPEAH VIIAANE
//