ID A0A177QM75_9PLAN Unreviewed; 1828 AA.
AC A0A177QM75;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Serine protease {ECO:0008006|Google:ProtNLM};
GN ORFNames=AYO44_07530 {ECO:0000313|EMBL:OAI48274.1};
OS Planctomycetaceae bacterium SCGC AG-212-F19.
OC Bacteria; Planctomycetota; Planctomycetia; Planctomycetales;
OC Planctomycetaceae.
OX NCBI_TaxID=1799658 {ECO:0000313|EMBL:OAI48274.1, ECO:0000313|Proteomes:UP000186541};
RN [1] {ECO:0000313|Proteomes:UP000186541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCGC AG-212-F19 {ECO:0000313|Proteomes:UP000186541};
RA Choi J., Stepanauskas R., Howe A.;
RL Submitted (FEB-2016) 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:OAI48274.1}.
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DR EMBL; LSTD01000247; OAI48274.1; -; Genomic_DNA.
DR Proteomes; UP000186541; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR CDD; cd00091; NUC; 1.
DR Gene3D; 3.40.570.10; Extracellular Endonuclease, subunit A; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001604; DNA/RNA_non-sp_Endonuclease.
DR InterPro; IPR044929; DNA/RNA_non-sp_Endonuclease_sf.
DR InterPro; IPR020821; Extracellular_endonuc_su_A.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR040255; Non-specific_endonuclease.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13966:SF5; ENDONUCLEASE G, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13966; ENDONUCLEASE RELATED; 1.
DR Pfam; PF01223; Endonuclease_NS; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR SMART; SM00892; Endonuclease_NS; 1.
DR SMART; SM00477; NUC; 1.
DR SUPFAM; SSF54060; His-Me finger endonucleases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR640255-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000186541}.
FT DOMAIN 1590..1802
FT /note="DNA/RNA non-specific endonuclease"
FT /evidence="ECO:0000259|SMART:SM00892"
FT DOMAIN 1591..1802
FT /note="Extracellular Endonuclease subunit A"
FT /evidence="ECO:0000259|SMART:SM00477"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..949
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1079..1099
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1445..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1454..1468
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1653
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR640255-1"
FT BINDING 1690
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR640255-2"
SQ SEQUENCE 1828 AA; 200096 MW; 74494EC4EB9DD856 CRC64;
MSAEKPGPAT FYDEVDFQQR LSRTRGRSTA PSGPDLQPWR SAAAVLVAFD PAKLNPLGPS
AKEGSGLSLL PELVAATGLR PPLDGKWTLP TQQRKAELRR LGTQQKIAAA LAANPERPAV
PLQRMFDRVI DGTALPRLAD LKRDDLAALL VVIDWLDGIP ITPQLPALNE VRATLENRQD
LDRLQRLVGD FFTGRKEELA QLHAHLFSTD PSILVISGTG GAGKSALLAK SLLQLSEETQ
DPTCWVRVDI ADSNVIPKDP VTLLTQAALQ LGRRDSLLQR VVSSFVGEAE SRRRSRDYAG
LEAVSSRPED ELAWAMGRFN EVIKRYRTPG RSQDVFAFCV DSFEEAQLLG GPVAGPVLEM
LARLATSTGS RVIVCGRAAP PGSFLFMPLE SAADPKAAVR LEILPLADLP ATDAVILLER
FIHQEKPDVL IDREKLQHVV EVIGGNPLSL KLAGQLINTK DFDALDDPRT LQELKAEAAQ
ARLYSRILAH IDDVEVQRLA IPGLVVRLID KDVIRQVLAE PCGLGDVDDA RASELLEKLA
REITLVERLP DGVLRHRADI RRVMLAGIPD EMRDQVNEIH RKAVAYWGAR TDSQARGEEL
YHMLRLGMDR EALENRWSPK MAAELQGALF GALEELPPGS PGRVWLAEKL GVTLSESERA
TIAIEEQESQ AERAATQFLA HGDAGQALAV LENQKPFTPG SRLFALLARV LFRIGRTDDA
LAMTAEGIQS ALPNDAELAD LLLLRAYLLE SQGRENEALD ALKQAETERT TRLAQLRIKV
RRSRLLRKLN RDDPAIRTEI IRLAESLVSE IVQHPALLRE VAAEIGDANP TLLGQALERF
GPEILDGMTS EAQEEMLLAI GAYSKEELTT FSGISRIKLL ELVRTNLDQL IHGTDDRSRK
ASRLFVEALR RSVNEVLQRN YLAPPASSPT PGPTTSPTQG PSPVTSLTDD SRKKLVDVLV
QVPAETLRKV AQFNLDFDLE RLGGTIPFPE LTARLIDTAE SNGLLEPFFQ GLLANVSTET
AALLSDILNN NQTLRQPDLV TQTEMMKGPT MAPRTPSPSV SGMMTHYKRI AAARASGRTG
GFESLGAPES VPERTKSTEE ELKRIVKDYL GNDPQLLDVA KKIVTDGGEA LRRLEANDAD
ALQSHPEFIS GLEAIVRTDG SRPSFLIRNG DVDRNSSPIG SWADLLDRSA DRLRGAIACV
GRIDIPGTSA GFMGTGFLIQ ENLILTNRHV LQVSAQLVNG TWKFTDGAAI DFGHEFRARD
SINRRKLKRV VFCGDKTIDF NTIDHSKLDL ALIELEPATP ASRPSMVLPL KLAANWAAPG
TKIITIGYPG SPPTMLYPPT LLEQLFHATF GYKRIAPGEL ITSELGVQPW TLTHDATTLG
GNSGSIVLVA DQEQWAAGLH YGGRGIEPRE NWGHVLASVL NATDGTSPKS LQDILRENGV
RFLDGAGAPA ARPTAPSPQQ PSPTAARPPD TEPATSEEVT PQTEPKSPAA VPGCTLHFTV
PLHISVSIGA PTVARAGPSP TVSAIPSAAA GFALEKVEID TDYSDREGYD PQFLGGGNRR
VSLPKLTPAM VQDAATNLEA TDGAKRYELP YHHYSVVLNS KRRLAFFTAV NIDGTLEKNL
GKREKDRWIR DHRVESNLQI GDEWYEKPFD RGHLVRRLDP AWGRSAKIAK TANDDTFHFT
NCSPQHSRFN QGKNLWQGLE NYLLDTANKE DRRINVFTGP IFTNDDPVYD HVQVPKRFWK
VAAFVRTDGS MGAAGFIVSQ EELLAAMGLE ATAEQVARTF QERVSVIERL TKLDFGSLRT
VDTLPGAGLL EGVEATRVEL TSFEQIKL
//
