ID A0A1P9WTL5_9BACT Unreviewed; 938 AA.
AC A0A1P9WTL5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Pseudouridine synthase {ECO:0000313|EMBL:AQG78712.1};
GN ORFNames=AWR27_04800 {ECO:0000313|EMBL:AQG78712.1};
OS Spirosoma montaniterrae.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Spirosoma.
OX NCBI_TaxID=1178516 {ECO:0000313|EMBL:AQG78712.1, ECO:0000313|Proteomes:UP000187941};
RN [1] {ECO:0000313|EMBL:AQG78712.1, ECO:0000313|Proteomes:UP000187941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY10 {ECO:0000313|EMBL:AQG78712.1,
RC ECO:0000313|Proteomes:UP000187941};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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DR EMBL; CP014263; AQG78712.1; -; Genomic_DNA.
DR RefSeq; WP_077130153.1; NZ_CP014263.1.
DR AlphaFoldDB; A0A1P9WTL5; -.
DR STRING; 1178516.AWR27_04800; -.
DR KEGG; smon:AWR27_04800; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000187941; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 1.
DR Pfam; PF00675; Peptidase_M16; 2.
DR Pfam; PF05193; Peptidase_M16_C; 2.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000187941};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..938
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012727058"
FT DOMAIN 59..205
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 215..390
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 544..638
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 669..848
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
SQ SEQUENCE 938 AA; 104950 MW; A4CEDD791078AE01 CRC64;
MNQVNKSVRK HLLVASLLAG SLSLSFAQNQ PAAVTMPEGV SRVTSVEGIT EYKLKNGLRV
LLFPDPSKPT ITVNITYMVG SRHEGLGETG MAHLLEHMVF KGSTKHPNIP QELTEHGSRP
NGTTWYDRTN YFETFSATDE NLKWALDLES DRMVNSFIKK EDLQTEFTVV RNEFEMGENS
PQYVLMERIL SGAFLWHNYG KSTIGSKEDI ERVPIDNLKA FYQKYYQPDN AILLVAGKFD
EAKTLALVDQ YFSPIPKPSR VLTQPYTVEP TQDGERSVTL RRVGDTQGVG VAYHTPAAAH
PDYAVMDVLI DVLTNEPSGR LYKALVEGKK AAFTYGWAPS VHDPGFAYFY AEVRKENSLD
SARNTMLTTL DAVSTKVPTN EEVERAKTKL LSDIDLMFKN PDRVGLQMSE WMGAGDWRLV
YLYRDRIRTV TPADVQRVAQ AYLKPSNRTV GVFIPEQKPD RAEIPATPDV AALVTNYKGE
KAVAAGESFD VSPANIDART KRGNLPNGLK YAFLSKSTRG NSVNATIRLR LGDEKSLTNK
MTVASMAASM IERGTKTRSY QQIRDEFDKL KAKVYAYPSG QELNVQIETT KENLPAVLKV
VTDYLRNPTF PESEFTKLKE ERLAQIESQK QEPQAIAFNV AERLINPYPK GHVWYTMTFD
EEIEALKNVK LDEVKQFYKD FYGAQSTVVS IVGDFNEAPV LQTLKTDLGG WKAARPYARV
PLQLAAVTPK IESIQTNDKA NAMLVTGMKL PMRDDDPDFP ALYTANFILG GGFLNSRLAV
RIRQKEGVSY GVGSYLQPDD NDKVTTFGSY AIYNPENSER LEKAYKEEIE KMVNEGVSDA
ELKAAKSAVL QNRQVSRSQD NTLARKWSQY LTKADRSFAF DADFDKKVEA LTPEQVNAAL
KKYIDYNKLV IVKAGDFEKA AKKLTEKAPA AQVGGSKN
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