ID A0A0C1R4E4_9CYAN Unreviewed; 926 AA.
AC A0A0C1R4E4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Insulinase family protein {ECO:0000313|EMBL:KAF3886617.1};
DE SubName: Full=Peptidase M16 {ECO:0000313|EMBL:KIE10628.1};
GN ORFNames=DA73_0219120 {ECO:0000313|EMBL:KIE10628.1}, DA73_0400014880
GN {ECO:0000313|EMBL:KAF3886617.1};
OS Tolypothrix bouteillei VB521301.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Tolypothrichaceae;
OC Tolypothrix.
OX NCBI_TaxID=1479485 {ECO:0000313|EMBL:KIE10628.1};
RN [1] {ECO:0000313|EMBL:KIE10628.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KIE10628.1};
RX PubMed=25700407;
RA Chandrababunaidu M.M., Singh D., Sen D., Bhan S., Das S., Gupta A.,
RA Adhikary S.P., Tripathy S.;
RT "Draft Genome Sequence of Tolypothrix boutellei Strain VB521301.";
RL Genome Announc. 3:e00001-15(2015).
RN [2] {ECO:0000313|EMBL:KAF3886617.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VB521301 {ECO:0000313|EMBL:KAF3886617.1};
RA Sarangi A.N., Mukherjee M., Ghosh S., Singh D., Das A., Kant S., Prusty A.,
RA Tripathy S.;
RT "Improved Assembly of Tolypothrix boutellei genome.";
RL Submitted (NOV-2019) 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:KIE10628.1}.
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DR EMBL; JHEG04000001; KAF3886617.1; -; Genomic_DNA.
DR EMBL; JHEG02000048; KIE10628.1; -; Genomic_DNA.
DR RefSeq; WP_038074846.1; NZ_JHEG04000001.1.
DR AlphaFoldDB; A0A0C1R4E4; -.
DR STRING; 1479485.DA73_0219120; -.
DR OrthoDB; 9811314at2; -.
DR Proteomes; UP000029738; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; 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; 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.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000029738}.
FT DOMAIN 60..205
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 212..398
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 529..637
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 677..856
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT REGION 253..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 926 AA; 100668 MW; AD2CB5941B4761CE CRC64;
MSFLAKIRPS ILILSILILS GMLWVRDFSV AALQPEVTPV AGLSLTQGVR KTVLENGLTV
LTKEVHTAPV VSVQVWYRVG SRNEQAGENG ISHQLEHLMF KGTTDRPVQF GRLLSALGSQ
FNAFTSYDET AYFSTVQQDK LDALLTLEAD RMESALIQAD QLTSEKRVVI SELQGYENSP
GYRLSRAVMR AAFPKRAYGL PVGGTKADVE QFTLEQVRNY YQTYYSPDNA TLVVTGDFDT
QAVLKSIQQS FGKLPKRGQG ETGTRGHREL VPSSPRPISP SSRSPIVLKE PGSAALLQAV
YPLPDANHPD VAAIDVMDAI LTGGRSSRLY QALVESGLAS SVSASPAELL EPGWYEINVT
AVPGQQLSKI SQVLQQSLTE LQQKQVASDE LNRAKTQLQA SFVLNNQDIT SLATQLGYSQ
TVSGDYLYIK RYLEAIGKVS AADVQRAAKT YLNPAQQTIG FFEPTVRDAK SGEKSASSGR
TVENFSPGKP VDPAELAKYL PAAKATRVST KQPLPEQFIF KNGLQVLLLP DRSVPTVNLS
GQILAGSVFD TDRKAGLANL VAANLMNGTQ TKDALTLAKT LEDRGASLGF QANREGVSIS
GNGLSANLSI LLDTLADVVQ NANFPNAQLE LSRQRSLTSL KVQLDDPRGL GRRVFQQAIY
PENHPFHSFP TEQSLKSITR DDLVRFYQEH YRPDTMTVAL VGDFEPSQVK VLLKKAFGEW
KAEGNPPALN LASVSLPQNT TQLNPVIPGK AEDVTYIGYN SISRKDPRYY TALVLNEILG
GDTLSSRLGT EVRDRQGLTY GIYSVFAAGI NPGPFLIQMQ TAPGDTRKAI ASTVALLKQL
RDQGITEAEL NAAKRSITNS YPVELANPSN VADVILGNAI YGLSPAEIRE YPKRIEAVTI
AQVQQVIQEL IHPDKLVIVT AGPGAQ
//