ID A0A2V1EA37_9PLEO Unreviewed; 741 AA.
AC A0A2V1EA37;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=AP complex subunit beta {ECO:0000256|PIRNR:PIRNR002291};
GN ORFNames=DM02DRAFT_609013 {ECO:0000313|EMBL:PVI07488.1};
OS Periconia macrospinosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI07488.1, ECO:0000313|Proteomes:UP000244855};
RN [1] {ECO:0000313|EMBL:PVI07488.1, ECO:0000313|Proteomes:UP000244855}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE2036 {ECO:0000313|EMBL:PVI07488.1,
RC ECO:0000313|Proteomes:UP000244855};
RX PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT "Comparative genomics provides insights into the lifestyle and reveals
RT functional heterogeneity of dark septate endophytic fungi.";
RL Sci. Rep. 8:6321-6321(2018).
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}.
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DR EMBL; KZ805304; PVI07488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1EA37; -.
DR STRING; 97972.A0A2V1EA37; -.
DR Proteomes; UP000244855; 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:UP000244855};
KW Transport {ECO:0000256|PIRNR:PIRNR002291}.
FT DOMAIN 15..533
FT /note="Clathrin/coatomer adaptor adaptin-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01602"
FT REGION 642..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 710..735
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 741 AA; 81614 MW; 53ED3F9E79E9297D CRC64;
MAVNRIKGAF AVPRKGETFE LRAGLVSQYA YERKEAIQKT IMSMTLGKDV SALFPDVLKN
IATGDLDQKK LVYLYLMNYA KSHPDLCILA VNTFVQDSED PNPLVRALAI RTMGCIRVDK
MVDYMEEPLR KTLRDESPYV RKTAALCVAK LFDLNPTMCI ENGFIEQLQE MVGDPNPMVV
ANSVTALVEI QEASNDGNVF VITAATLKKM LMALNECTEW GRVSILTTLA DYKAQDVKES
EHICERVSPQ FQHVNPSVVL AAVKVVFLHM RYVSPELMKS YLKKMAPPLV TLVSSAPEVQ
YVALKNIDLL LQKQPDILSK EMRVFFCKYN DPPYLKLQKL EIMVRIAGDK NVDQLLAELK
EYALEVDMDF VRRAVKAIGQ VAIKIESASE KCVNTLLDLI NTKVNYVVQE AIVVIKDIFR
KYPGYEGIIP TLCQCIDELD EPNARASLIW IVGEYAEKID NAGEILTGFV DTFAEEFSQV
QLQILTAVVK LFLKKPDQSQ GLVQKVLQAA TAENDNPDIR DRAYVYWRLL SSDPQITKSI
VLSDKPAITT TIKSLPPQLL DQLLTELSTL ASVYHKPPEA FLGQGRFGSE AMQKAAIEEQ
REEARENPIA ADAVAAAAAG QAPPQSNVEN LLDIDFDGSA PASLQKEITP GQSGLEGLAG
TPQRVASPAS GNAAPSSNMD DLMGLFGNTS AAAPSAPMTN DDIMNGFAGM DLSGSSQPPP
PTQQLAEQKP QKSNQDLLDL F
//
