ID A0A2T2YGP8_9BACT Unreviewed; 965 AA.
AC A0A2T2YGP8;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PSR54679.1};
GN ORFNames=AHMF7605_14765 {ECO:0000313|EMBL:PSR54679.1};
OS Adhaeribacter arboris.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Adhaeribacter.
OX NCBI_TaxID=2072846 {ECO:0000313|EMBL:PSR54679.1, ECO:0000313|Proteomes:UP000240357};
RN [1] {ECO:0000313|EMBL:PSR54679.1, ECO:0000313|Proteomes:UP000240357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMF7605 {ECO:0000313|EMBL:PSR54679.1,
RC ECO:0000313|Proteomes:UP000240357};
RA Kang H., Kang J., Cha I., Kim H., Joh K.;
RT "Adhaeribacter sp. HMF7605 Genome sequencing and assembly.";
RL Submitted (MAR-2018) 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:PSR54679.1}.
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DR EMBL; PYFT01000001; PSR54679.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T2YGP8; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000240357; Unassembled WGS sequence.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd09603; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR008969; CarboxyPept-like_regulatory.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF13715; CarbopepD_reg_2; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..965
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015773944"
FT DOMAIN 467..639
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 731..880
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 965 AA; 111316 MW; BCE54EE5C3417CAF CRC64;
MKKIYYPSVL ILIFFLHQTF STYAQETTLT LSGSIVNGET NAPIPFASVG IGQSGIGTSS
NQEGKFTIKI PASQQQDTLR VTYVGYSVFR QAILNIKNQP LLIQLKPASI TLTEVVINGK
RKTALDILHE AIAAIPVNYD TTSVQLTAFY REDVKLEDYP ISYSESVLEV RKPPYHTLTE
QEQVKIIKGR KKPYDHSRLR LHGYLDMPNG AHRLLRDDFV KYQLGGGEFS FVGKHHMKAY
EYKLRGIVPE GDRQVYVIQL IPRKNARKAH VAGNLYIDVN TLAFTKAEWI MTQRGIDFDN
NRNFLLKQLS YKVAKLSHKL TYLKETTTYS NYNNKWYLKD KHRHYEMRVN SKSRGIENKL
WTANTDITIT NIGAKNIPPF TEGDIYQSEA SISGLINNDN DPNFWENYNI VEPAADSVFM
KMPEVKSLEK PVNNAPIKVS NRATGFTRAD TLRGKLTPQR SYDVTFYHLD VAVNIPNKSI
SGSNKIRFRV TDPLNKMQVD LYANMTIHSV KYRGQELSYT REFDAVFIQL PETLPSNSQH
EIEITYSGAP QVPNFNISMH GGFLWEQDRN GNPWVQVVCQ GSGASLWWPN KDHLSDEPDS
MRLSVTVPSN LTEISNGRLL RKVPLANNQT RYDWYVSYPI NNYNVTLNIG QYKHLQDTYV
TNDTLTLDYY AKPEHLDKAR WLFNQVKPML ATLEKHYGKY PFPRDGFTLL ESLHPMEHQS
AVTFGKLPDG ELDSVNTMKL VWHEVSHEWW GNNVSCKDLA DMWLHEAFAT YTEGLFFKTQ
FGEDTELGYA QSLQERAVNK EPIIGEYDVN HIFYNTEDMY SKGALMLRTF RNVLANDNLW
FSILRGIQQE FKYQTVTSAD IIRYINQQTQ RDYSYFFNQY LKHPAIPTLQ IKFGQQGQTL
VLHYKWNTDV ADFKMPIKVT KLPGKYSFIY PTTAWQTLRL PNVSPEDFEV DQNRFYVNVT
QEDFD
//
