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Database: UniProt
Entry: A0A0M9A876_9HYME
LinkDB: A0A0M9A876_9HYME
Original site: A0A0M9A876_9HYME 
ID   A0A0M9A876_9HYME        Unreviewed;      1634 AA.
AC   A0A0M9A876;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=PDZ and LIM domain protein Zasp {ECO:0000313|EMBL:KOX77913.1};
GN   ORFNames=WN51_05799 {ECO:0000313|EMBL:KOX77913.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX77913.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX77913.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX77913.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX77913.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the paxillin family.
CC       {ECO:0000256|ARBA:ARBA00005813}.
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DR   EMBL; KQ435727; KOX77913.1; -; Genomic_DNA.
DR   STRING; 166423.A0A0M9A876; -.
DR   OrthoDB; 370973at2759; -.
DR   Proteomes; UP000053105; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd08368; LIM; 1.
DR   CDD; cd09455; LIM1_Enigma_like_1; 1.
DR   CDD; cd09461; LIM3_Enigma_like_1; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 4.
DR   InterPro; IPR031847; PDLI1-4/Zasp-like_mid.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR006643; Zasp-like_motif.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24214; PDZ AND LIM DOMAIN PROTEIN ZASP; 1.
DR   PANTHER; PTHR24214:SF38; PDZ AND LIM DOMAIN PROTEIN ZASP; 1.
DR   Pfam; PF15936; DUF4749; 1.
DR   Pfam; PF00412; LIM; 4.
DR   Pfam; PF00595; PDZ; 1.
DR   SMART; SM00132; LIM; 4.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00735; ZM; 1.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 5.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 1.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   LIM domain {ECO:0000256|ARBA:ARBA00023038, ECO:0000256|PROSITE-
KW   ProRule:PRU00125}; Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00125};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00125}.
FT   DOMAIN          6..88
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          338..398
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          1519..1578
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   DOMAIN          1579..1634
FT                   /note="LIM zinc-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50023"
FT   REGION          212..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          288..339
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          492..556
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          683..702
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          784..803
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          854..1021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1051..1214
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1277..1351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        247..266
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        311..339
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        502..556
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..908
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        924..979
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        993..1021
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1051..1071
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1103..1120
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1277..1302
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1309..1351
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1634 AA;  181049 MW;  03DD9D99274257F2 CRC64;
     MAQLINVKLS RFDGSPWGFR LQGGKDFGTP LVVQKVNTGS PAEAAGLKAG DAVIRVNNTE
     VYNLRHKDAQ DVIVRAGNNF ELTVQRGGGT WKPHVTPISS SLPSPSPTGG LGNIAPVTKT
     SLAANKKDGP HIGSGHNFSP KPFLNGTGDG SIKSIVNKQY NSPVGIYSEE TIAETLSAQA
     EVLAGGVLGV NFKKNEKNYN AENSEVFKMV QEADKEPKTP EPAEPTAQSG VITPSSPALA
     GLRPVSAPET KQQQPSTPQS SLPPGQNICA ECERLIVTEF YSSVSHAVGG RATSPRSPTP
     LFHALHGNPA FNSNEYPSSK RPAQRQESSS SSPVSSGVRC SNCDRVIVGV FVRIKDKNLH
     VECFKCSTCG TSLKNVVGYY NINNKLYCDI HAKLVARQNA PAGLVPITIP PGGKAPASTI
     SAALANAPLS PPLSNHTSSP QPFSAYNRSS PDYGSPNSQL SSPNRNGCIT NGNCHWESKT
     FTSTITIQTG CTEPTRLGTS PVDPPSFRSV QAPTSNNLIG PKPFGGSSTV SSPPLLNSGN
     STLPRPQSQT VTENSTETYE KSYYYEIVEN TKTDHRPSSV KSKSLAWPPP KPIEDITYPT
     ASPLYIDPNP ALDRRSRQAV KEKKACIEAC EKALTRGQRR GESTDREVEK VTRQCYRFEG
     DPMDRVSCPG PVYRKVELVE TTSRQSKTEV PSRASSAESV RRSLTPTRIV QPVPKPWTAT
     VTTGSNIYEQ SYAGVEPPKV CKKFHQKEIC QKERICERNQ PFHEEHRMYR SEFCRREQTI
     SQKPPLPTQQ VTKQEETREE TTEIDKQVID LRSADEDEDS DGIKGEHDFI TEMSEEDIDG
     MHVKTKMTLE KTVEPSLVRP STPAVKESRE ETTAEETVEE TLEREEEVCM RRTATKVEKE
     ETEEKTVVES AEVVTSAVDV QQLVEKAKQE EEERKREEEE EEKRKQEEAE RKRREEEERW
     RKRREEEERR RQEEEEQSRH VTFEEEEEEV EEVREQPLGR TVVREERVTE AESDTPGRTK
     LIKETYEEIT EEVLVQERVK RKCIEDERKK SLREQVEVHK SLRDQQAPKD RRVCSKYPPA
     QEIMESNKKR VQFMKQTDTG PKPIPHSALQ NSTPKEWKSE MVNALTTAPD RPFTPLMATR
     RGAVESHTYE PNRTPTPTPG RKSPAYGPPE RPSCYVRAQA PRIREDPPST KRSSIHFPTK
     KTVSYKVDED TDDGHRHAEY AASKTVDFDE KRTDDPGKEP TDAVHAAYQE KRYMTSEETS
     EEKMSVTRRS LEVTEDFERC EKRVPTRPLP ERTEKPREKP PKGVCAIGRT SPSQPSLPCP
     LSSQTGTSSP QPIYSSSTEV RHVSYGTPSS KPCPDTGVTV LPCKAQSDQG TKAGVVVVPC
     EGPNICCQKS GVCIVPTPDR SGVCVSPCFG GTCGQPSGTG VGGLGGAGSK SGTFAGSSAP
     KRGRGILNQA SGPGSRLPLC AHCNSYVRGP FITALGQIWC PDHFVCVNTQ CRRPLQDIGF
     VEEKGQLYCE YCFERFIAPS CNKCNNKIKG DCLNAIGKHF HPECFKCTYC GKLFGNSPFF
     LEEGLPYCEA DWNELFTTKC FACGFPVEAG DRWVEALNNN YHSQCFNCTM CKKNLEGQSF
     YAKGGRPFCK NHAR
//
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