ID A0A091MAN2_CARIC Unreviewed; 1035 AA.
AC A0A091MAN2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 32.
DE SubName: Full=Pappalysin-1 {ECO:0000313|EMBL:KFP68576.1};
DE Flags: Fragment;
GN ORFNames=N322_11424 {ECO:0000313|EMBL:KFP68576.1};
OS Cariama cristata (Red-legged seriema).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cariamiformes; Cariamidae; Cariama.
OX NCBI_TaxID=54380 {ECO:0000313|EMBL:KFP68576.1, ECO:0000313|Proteomes:UP000054116};
RN [1] {ECO:0000313|EMBL:KFP68576.1, ECO:0000313|Proteomes:UP000054116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N322 {ECO:0000313|EMBL:KFP68576.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M43B family.
CC {ECO:0000256|ARBA:ARBA00008721}.
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DR EMBL; KK527271; KFP68576.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091MAN2; -.
DR MEROPS; M43.004; -.
DR Proteomes; UP000054116; Unassembled WGS sequence.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR CDD; cd04275; ZnMc_pappalysin_like; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 4.10.470.20; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR011936; Myxo_disulph_rpt.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR043543; PAPPA/PAPPA2.
DR InterPro; IPR008754; Peptidase_M43.
DR NCBIfam; TIGR02232; myxo_disulf_rpt; 1.
DR PANTHER; PTHR46130; LAMGL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46130:SF2; PAPPALYSIN-1; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF05572; Peptidase_M43; 1.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00004; NL; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000054116};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 97..246
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT DOMAIN 381..423
FT /note="LNR"
FT /evidence="ECO:0000259|SMART:SM00004"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP68576.1"
FT NON_TER 1035
FT /evidence="ECO:0000313|EMBL:KFP68576.1"
SQ SEQUENCE 1035 AA; 115721 MW; B1BD49370A4E1FC1 CRC64;
TALASGPECG MDERSRRARR DTRHSRQLRY SAPGTCATRL ARGRRSTAGL EPGHVPRRRQ
QREVKEEEES LTPSRALYFS GQGDQLRLKA DIELPRDAFT LQVWLKAEGG QRSPAVIAGL
YDKCSYTSRD RGWVLGINTV SDQGNRDPRY FFSLKTDRAR KVTTIAAHRS YLPNQWVHLA
ATYDGHLMKL YVNGAQVATS GEQVGSIFSL LTLKCKVLMV GGNALNQNYR GYVEHFSLWR
TARSQKEILL DMGQAIHRQD MPLPQLVLQD SLLNVKNTWS PMKDGSSPQS KFSYHHGYLL
DTSLDPPLCG QTVCDNTDVI ASYNKLPSFR RNKIVRYRVV NLYDDKHQNP TVSQQQIEFQ
HQHLNEAFSR YNITWELEVL EVKNSSLRHR LILANCDISK IGDENCDPEC NHTLTGYDGG
DCRHVRHTLF NKKKQNGVCD MDCNYERYNF DGGECCNPEI TEVTKTCFDP YSPYRAYLDV
NELKNILKLD GSTHLNIFFA NSSEEELAGV ATWPWDKEAL MHLGGIVLNP SFYGIPGHTH
TMIHEIGHSL GLYHVFRGIS EILSCSDPCM ETEPSFETGD LCSDTNPAPK HKLCGDPGPG
NDTCGFHNFL NTPFSNFMSY ADDDCTDSFT PNQVARMHCY LDLVYQSWQP TKKPAPIAIA
PQIVARTSAS VTLEWFPPID GHFFEREVGS ACDLCAEGRV LVQYAFSASS PMPCDPSGHW
SPREAEGHPD VEQPCKSSVR TWSPNSAVNQ HTVPPACPEP QGCYLQLEFH YPLTPESLTV
WVTFVSPDWD SSGAVNDIKL LTISGKNISL GPQNVFCDIP LTIKLDAGQV GEEVYGIQIY
TLDEHLEIDA AMLSSVPYST LCADCKPIQY KVVRDPPFQS GSPVVISNLN RRFVDTELSD
RTTYTYQVVI VSGTEESEPS PALVYISGSG YCGDGIIQID LGEECDDMNK INGDGCSLFC
LQELSFNCID EPSRCYFHDG DGVCEEFEQM TSIKDCGVYT PKGFLDQWAS NVSVSHHSDQ
QCPGWVVIGQ PAATQ
//