ID   A0A317WQL9_9EURO        Unreviewed;       761 AA.
AC   A0A317WQL9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=AP complex subunit beta {ECO:0000256|PIRNR:PIRNR002291};
GN   ORFNames=BO94DRAFT_595628 {ECO:0000313|EMBL:PWY87991.1};
OS   Aspergillus sclerotioniger CBS 115572.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY87991.1, ECO:0000313|Proteomes:UP000246702};
RN   [1] {ECO:0000313|EMBL:PWY87991.1, ECO:0000313|Proteomes:UP000246702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY87991.1,
RC   ECO:0000313|Proteomes:UP000246702};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Adaptins are components of the adaptor complexes which link
CC       clathrin to receptors in coated vesicles. Clathrin-associated protein
CC       complexes are believed to interact with the cytoplasmic tails of
CC       membrane proteins, leading to their selection and concentration.
CC       {ECO:0000256|PIRNR:PIRNR002291}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000256|ARBA:ARBA00006613, ECO:0000256|PIRNR:PIRNR002291}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWY87991.1}.
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DR   EMBL; MSFK01000013; PWY87991.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317WQL9; -.
DR   STRING; 1450535.A0A317WQL9; -.
DR   OrthoDB; 648032at2759; -.
DR   Proteomes; UP000246702; Unassembled WGS sequence.
DR   GO; GO:0030117; C:membrane coat; IEA:InterPro.
DR   GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IEA:InterPro.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR026739; AP_beta.
DR   InterPro; IPR016342; AP_complex_bsu_1_2_4.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   PANTHER; PTHR11134; ADAPTOR COMPLEX SUBUNIT BETA FAMILY MEMBER; 1.
DR   PANTHER; PTHR11134:SF3; AP COMPLEX SUBUNIT BETA; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   PIRSF; PIRSF002291; AP_complex_beta; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|PIRNR:PIRNR002291};
KW   Protein transport {ECO:0000256|PIRNR:PIRNR002291};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246702};
KW   Transport {ECO:0000256|PIRNR:PIRNR002291}.
FT   DOMAIN          26..544
FT                   /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01602"
FT   REGION          655..675
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..761
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        742..761
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  82889 MW;  43AE9F223CD4DD97 CRC64;
     MMFGSSVDNR RKVEAVDKGA FAVPKKGETF ELRAGLVSQY AYERKESIQK TIMAMTLGKD
     VSALFPDVLK NIATSDLEQK KLVYLYLMNY AKSHPDLCIL AVNTFVQDSE DPNPLIRALA
     IRTMGCIRVD KMVDYMEEPL RKTLRDESPY VRKTAAICVA KLFDLNPAMC LENGFLEMLQ
     EMIGDPNPMV VANSVTALSE IYHAAPETQA LKVTSNTLRK LLMALNECTE WGRVTILTTL
     AEYKTSEVTE SEHICERVSP QFQHANPSVV LAAVKVVFLH MRNVNAELAS NYLKKMAPPL
     VTLVSSAPEV QYVALRNIDL LLQKQPDILN KELRVFFCKY NDPPYVKFQK LEIMVRIAND
     RNVDQLLAEL KEYALEVDMD FVRRAVKAIG QVAIKIESAS ERCVNTLLDL INTKVNYVVQ
     EAIVVIKDIF RKYPGYEGII PTLCQCIDEL DEPNARAALI WIVGQYAEKI SNAGDILAGF
     VEGFNEEFSQ TQLQILTAVV KLFLKRPEKA QGLVQKVLQA ATAENDNPDV RDRAYVYWRL
     LSNTSDPNAT KTIVLSDKPP IVTTIQSLPP ALLEQLLGEL STLASVYHKP PEQFVGQGRF
     GADAVQRAAI EEQIQNAREN PLAAAAAAAA VTGSAPPPQA QNNMENLLDI DFDGTAPASA
     QKEPSGGMSG LEGLAGTPVR VESPAVGAPA GSNNLDDLLG VFGDGGATAS ASGSGAPNGG
     GAGTDLMNGF DGLDLSGGSM ASPPPGGSQP KKTNEDIMSL F
//