ID F4W9T4_ACREC Unreviewed; 735 AA.
AC F4W9T4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Coagulation factor IX {ECO:0000313|EMBL:EGI69070.1};
DE Flags: Fragment;
GN ORFNames=G5I_02242 {ECO:0000313|EMBL:EGI69070.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI69070.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR EMBL; GL888033; EGI69070.1; -; Genomic_DNA.
DR AlphaFoldDB; F4W9T4; -.
DR STRING; 103372.F4W9T4; -.
DR EnsemblMetazoa; XM_011070771.1; XP_011069073.1; LOC105154953.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; F4W9T4; -.
DR Proteomes; UP000007755; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00033; CCP; 1.
DR CDD; cd00112; LDLa; 4.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 4.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF00057; Ldl_recept_a; 4.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00032; CCP; 2.
DR SMART; SM00192; LDLa; 4.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 4.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 4.
DR PROSITE; PS50923; SUSHI; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Reference proteome {ECO:0000313|Proteomes:UP000007755};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT DOMAIN 239..287
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 454..715
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 175..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..218
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 3..21
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 39..51
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 46..64
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 98..110
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 105..123
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 139..151
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 146..164
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGI69070.1"
SQ SEQUENCE 735 AA; 81651 MW; A4E25BCA797FF154 CRC64;
FRCYNGDCIA GDLLCDGTPH CRDLSDETET ECTKPEILCH RYAFRCNYGA CVNGDSVCNG
VQDCIDNSDE TQPQCAKNIT NNQTGRPTSR PISRPNRCTT NQVACDNGEC IHKDNMCNGI
QDCADGSDET SEKCRSIYCP PTAFRCSYGA CINGDLRCNG VIECVDRSDE DSRCSETTGW
PSPLPTVRPT TETTRWPVPT PTPTRWPVPT PTPTNACRAP PQPQNGRWKL HRSQCSGGQE
CNVPEGTELG LGSHLIYSCN SGYKLRGPTD VSCSFEGKWL NIPVCTEIRC KALTTASIEA
RCTYDDEWIS CESPVPPRTK AVLECQNSYR PETNLLTGQR KNVRCNANGQ WEPEPMRCIP
GPLMINIYIN NTKFTFHTTF DRNATFIEVL DDRIIIYTNA NNPNYPNINI RVSKSNNNIV
TDEPWACCYV AMISPIKIFV VVCGTLPPDV TPTVVGGVRP NITEFPWHAT MYRDVPGESK
KFFCGASIIQ PNLLITAAHC VYDEINRQPI NARSIYILTG NIFRDYDYPF HNPTLVKKNQ
VKHVYIVRNY LGLIGNYLWD IAVLELDRPF VLSTWLVPVC IDTLSDRSVL EAGSYGKVAG
FGRTALGESS AILQALTVPV IPLSQCRSAS QNANTEQFIT NDKFCAGYTN GSSVCDGDSG
GGLVFKTNSL WYLRGIVSVS LGTIQKDGTA YCDNNLYSLY TEISRHISWI QDVITKIEQN
QIHILCSNES QTRCS
//
