ID A0A653BUG6_CALMS Unreviewed; 2631 AA.
AC A0A653BUG6;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=FERM domain-containing protein {ECO:0000259|PROSITE:PS50057};
GN ORFNames=CALMAC_LOCUS3657 {ECO:0000313|EMBL:VEN38936.1};
OS Callosobruchus maculatus (Southern cowpea weevil) (Pulse bruchid).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Coleoptera; Polyphaga; Cucujiformia;
OC Chrysomeloidea; Chrysomelidae; Bruchinae; Bruchini; Callosobruchus.
OX NCBI_TaxID=64391 {ECO:0000313|EMBL:VEN38936.1, ECO:0000313|Proteomes:UP000410492};
RN [1] {ECO:0000313|EMBL:VEN38936.1, ECO:0000313|Proteomes:UP000410492}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sayadi A.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000256|ARBA:ARBA00004536}.
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DR EMBL; CAACVG010005098; VEN38936.1; -; Genomic_DNA.
DR Proteomes; UP000410492; Unassembled WGS sequence.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0009887; P:animal organ morphogenesis; IEA:UniProt.
DR GO; GO:0030182; P:neuron differentiation; IEA:UniProt.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13184; FERM_C_4_1_family; 1.
DR CDD; cd01765; FERM_F0_F1; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR008379; Band_4.1_C.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014847; FA.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23280; 4.1 G PROTEIN; 1.
DR PANTHER; PTHR23280:SF21; PROTEIN 4.1 HOMOLOG; 1.
DR Pfam; PF05902; 4_1_CTD; 1.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF47031; Second domain of FERM; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000410492}.
FT DOMAIN 29..309
FT /note="FERM"
FT /evidence="ECO:0000259|PROSITE:PS50057"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..880
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1056..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2106..2142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2412..2498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..356
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..499
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..876
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2107..2138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2412..2480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2631 AA; 287644 MW; 80D2CD6D05584452 CRC64;
MPEDKKMAID GDHNNSKAAA NKGAGGGTAL AQVTMLDGSV LDIAIDRKAK GRELLDRVCE
AVNLIEKDYF GLTYADRHDP RNWLDLEKRI SKFMKEPWKM NFEVKFYPPD PAQLQEDITR
YHLCLQIRND ILSNRLPCSF VTHALLGSYL VQSELGDYDP DTMGKNYLKD FKFAPNQTAD
LEEKVMELHR THKGQNPAEA ELHYLENAKK LAMYGVDLHP AKDSEGVDIM LGVCASGLLV
YRDRLRINRF AWPKILKISY KRHNFYIKIR PGEFEQFEST IGFKLANHRA AKKLWKTCVE
HHTFFRLMSP ETNQKSSLFP KLGSKFRYSG RTHYETKKTP IERPAPHFER SLTGKRLTSR
SMDPLGGIRA EESYNEANKR HTMPHPPDHI PDIDNTSPAK TKSPKERKDK ERKPIGGVAV
LPAGGLFSKK DKKEKDKENR DTNAPEQNGI DDSQTHSIAE DDKSPKKEKS KSPAFLFGSK
REKSPKDKKE KEKLATKESE KGGPPVGSPQ LPGYTREYDY EPTDEQVTPR RQQGFSYENQ
GSPTTPKSSP ENQQSPSSKR ATATAFNYAP GDAEKLKKPF KDPKADTAAF LAGEQYLHQA
PPEATQLPAS AAGIKKTRPV TLFVITGTRD PKTGYIDTST GFADKCIGQQ NVETGLIESK
YGLIDPSNGT VIITDPSNGQ KEVVQGYINP QTKQIVITSG SVIDPKTGKK SNTLGQIITV
AEQQPKPGSK LALPPKKRII KITVTTAKKD PKSGRVEAEK GTTETLEAIL EPAKGLIETK
YGIIDLIHTK YIVKDPKSGK SEVFPIEVDD NLGHIIVKQG VIDPKTSKID NSLGQLIKIS
EQGDCVVPVT AVTAKKDRNT GQLDPSRAHK ETTNGKLDPK SGLIVTKYGS VDVNRKTITN
RDPKTGKVDE FPIQFDANEN VIVLNGAIDP RTGSRADDIS QILQIESEID PEVSVFSTCG
KMDKKGFDPK TVSPPEKSAG MFDPDTNKVY TKYGVLDLVR ETLTFIDPKS GKAETKHGLR
DHNTGELIFK GVVNPKTGKA DKDFGRTIKI NVDHQQADPT ARSVPTSAKD IKKVASPVAP
AKTPSDTSSI KPGDKNKVVK LLVITARRDP KTNHLDLENG HVDQSAGILH PTGEIDSKYG
FIDPKKGTVT ITDPATGKQE TVQGQIDPTT GQIQILTGPI IDPRTGKKDT TMGQVITIST
YGPSKDAAPV KTLLPSHPIP KKRVVKILVI TSKKDPTTGR IDTEKGTVEK LTATVDPVSG
IIESKYGKID PQNKKAITKD RTGKTNVTPV KLDESTGQIY INDNVVDVRT GKVDPNLSQV
VNIVDPQHPA VVITTITTTK DPQTGAIDIA KGRQETTNGK IIPETGEIVT KIGTINLKFM
RLSTRDPKTG HLQERAIQVD KDDNIIIPVV DPKTGKVDPN MVQIVQVGSE VDPEIQIRTF
VGKVDNKRNT IDSKNATPDT TPGLYDPDRN KIYTKYGHLD PVTETLTVFD PKTGKPEVRQ
GHIESNTGEL IFKGGFVNPK TGKIDKDLGR AVSVHITEPT IDPVTSQQPC EKELQKTAQI
VTPEKKPKQS ISPVKSTSPV KATTPVKEII TGILHPIAKH RIVKIMVITG KKDPKSGAVD
VENGQVEHLS GIVDPKHGLI ETKYGQLDPT TGTLLAKDTS TGKTELIQGK VDGTTGQIIV
NGGPVIDPKT GKMDSSLGQV FSVVGLKQVQ DPTAAPTPKK RIIKITVITT KIDPKTGKMD
AEKGHVEQST ALLNPETGLI ESKYGLIDPK SGKVIINDPK SGKVDAKSAQ VNETNGQILL
VGATDPKTGK AESSLGQIIS IAGQNDSIID ITTITAKKDP KTGSVDLNNG QMDNSKAKKV
SATGDIETKY GIINIKKMLL TTKDPKTGKI ENRTIQLDAE GNILVTTGVK DPKTDTVNPD
LCQVIKLGAE VEPEVQIVTF IGKLDTKKNI IDTKNVVPEV SNGLYNPSTH KIDTKYGQID
PIKGTLTCMD PKTGRAEVKQ GTVDPTTGQL IFKGGYINSK TGKPDPHFAR LVAVLISNPE
INEKGEIVPR DAKNIKVDPK TNQVWAFDHH DPISNEDVYS TGHVDPVTGY VVTVYGRIDP
KTGTISKISK VDPSSTKVDP QTQQVFTKTS QTDESGAPIY SASEIDPKTG QIYTKYGKID
PKTGKLVIIK VYLITQNDPT GKVKEIDPKD CQFDEKTGRI INVTTHTVYI YSMVDPKTGK
IVQVDPNDPV VKSANTKVTQ VLTLSGEIDP VTGKIHTEWG HIDPQTGDID PDTARTDPVT
GKLILNYAQI DASHFTDLKD TKVKVKTYMK GEQDSGESSD DDLNEYASEN LSDIAKLNIP
KGKKVTTSTP VIVKTTTKQI VTKDKDGLTQ NIEERVEDGR TGEVKVSTQI NKADAPKDSP
FVTARAVTTR TAMTHEDLET NAKTQQLEEK TVARSTTKSA TRQEQRTVTQ EVKTTSTVVS
GDQLGRRDSL SSTSSGDSGT PIDPPDDPNH PYYNSPIYKD DIPAEGIVQT ESVIYRGDPT
VVHSTTNVPV VATESRKVNL TSDDGSYSAT GEIVSSQTIS SKTRTVETIT YKTERDGVVE
TRVEQKITIQ SDGDPIDHDR ALAEAIQEAT AMNPDMTVEK IEIQQQTSQP Q
//