ID   A0A095A0Q9_SCHHA        Unreviewed;       971 AA.
AC   A0A095A0Q9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   08-NOV-2023, entry version 34.
DE   SubName: Full=Band 4.1-like protein 3 {ECO:0000313|EMBL:KGB40342.1};
GN   ORFNames=MS3_08806 {ECO:0000313|EMBL:KGB40342.1};
OS   Schistosoma haematobium (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6185 {ECO:0000313|EMBL:KGB40342.1};
RN   [1] {ECO:0000313|EMBL:KGB40342.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22246508; DOI=10.1038/ng.1065;
RA   Young N.D., Jex A.R., Li B., Liu S., Yang L., Xiong Z., Li Y.,
RA   Cantacessi C., Hall R.S., Xu X., Chen F., Wu X., Zerlotini A., Oliveira G.,
RA   Hofmann A., Zhang G., Fang X., Kang Y., Campbell B.E., Loukas A.,
RA   Ranganathan S., Rollinson D., Rinaldi G., Brindley P.J., Yang H., Wang J.,
RA   Wang J., Gasser R.B.;
RT   "Whole-genome sequence of Schistosoma haematobium.";
RL   Nat. Genet. 44:221-225(2012).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; KL251437; KGB40342.1; -; Genomic_DNA.
DR   RefSeq; XP_012800100.1; XM_012944646.1.
DR   AlphaFoldDB; A0A095A0Q9; -.
DR   STRING; 6185.A0A095A0Q9; -.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR   CDD; cd14473; FERM_B-lobe; 1.
DR   CDD; cd01765; FERM_F0_F1; 1.
DR   CDD; cd12873; SPRY_DDX1; 2.
DR   Gene3D; 1.20.80.10; -; 1.
DR   Gene3D; 2.60.120.920; -; 2.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR019749; Band_41_domain.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000798; Ez/rad/moesin-like.
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; IPR003877; SPRY_dom.
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; PF09380; FERM_C; 1.
DR   Pfam; PF00373; FERM_M; 1.
DR   Pfam; PF09379; FERM_N; 1.
DR   Pfam; PF00622; SPRY; 2.
DR   PRINTS; PR00935; BAND41.
DR   PRINTS; PR00661; ERMFAMILY.
DR   SMART; SM00295; B41; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SMART; SM00449; SPRY; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF47031; Second domain of FERM; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   PROSITE; PS50188; B302_SPRY; 2.
DR   PROSITE; PS00660; FERM_1; 1.
DR   PROSITE; PS00661; FERM_2; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   4: Predicted;
FT   DOMAIN          120..403
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          532..721
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   DOMAIN          729..921
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
FT   REGION          83..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          435..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        83..107
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   971 AA;  107931 MW;  423B09985060E7C4 CRC64;
     MEPPAMSTFL SDNETVGEST NLLHLEGHSW SQLQDGTIEI TDRLPKKEYY MSLRRFNSTG
     PNSGTAHRLG SISSGSAAGL ANGSSGLLGG NSPSPRPGGS TLRGSSHPSV VDFKPSGKIV
     DCTVVMLDGT TREFRLDKAA YGQQLFDAVC THLGLLEVEF FGITYYDSTN NWFWLQTDQK
     IAKQIGKNEW QFEFQVKFYP CDIDSIKEDI TRYYLCLQVR QDIVSGQLPC SFVTYCILGS
     YIVQSEAGDH DPTQHIGIKY IQDHPFAPHM LQTPEMLGRI VELHKLHRGK TPEEADRLFL
     NNARKLALYG VDLHKVKTSQ GQDITLGVYY GGILLYRNRI RLMRISWPRI ISLSHRGRNF
     IIARRPGDDS LDRNMTFKCI SPTLAKRLYN VCVDHHNFFR LRGSSRPKKP SLFPSFATRK
     YHYPGTTVNS SSIDATVGVG GHNQTSRPLS KFRPMPAHPS ETVDHMNGAV ASQYQYQPAM
     VSGDPACMDP TYFCNQNVIN GLPIPNAHGV QRYYQPSSND VTGLMNGHHP NSNNNHINNM
     PTMITRISFV PEHWRITGAD CTAGLGIDAR GLDVASTRGA GWQGCRANKG VKAPGAYYYE
     AACLEEGLIR VGWSTNDANL ELGADNYGFG YGSDAVGSAG MNGTGRVMHR NTGHDYGIMV
     HQGDVIGCLL DLDKGSISWS CNGKIFQRAF TIPDQLRGEA FLPAASLKDS RILFNFGEEQ
     PLEFPPDGSF IPVAQSADDS QVSNRNPGWR MNQYDATNAL DVAPDGSQVQ SHFNQGWQGC
     RSNHGIRGLG RFYFEVTPIE STGLWRVGWS TDDGNLIVGT DQYGFGYGAD NEGFGLNGQQ
     GKRIHCDEIE NYGEAFSKDD VIGCFLDTIE HTIKWSKNGL EFGDAYRIPS ELLHSKNLTA
     LYPTVSLLNS TLELNFGDKP FKYYPGPDWT PVCCAPPECT KRSRRKGPEV SQIYILTTQY
     VYIHHKHREM K
//