ID A0A183BYN5_GLOPA Unreviewed; 912 AA.
AC A0A183BYN5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Mediator of RNA polymerase II transcription subunit 20 {ECO:0000313|WBParaSite:GPLIN_000572500};
OS Globodera pallida (Potato cyst nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC Globodera.
OX NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_000572500};
RN [1] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Aslett M.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000050741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT "The genome and life-stage specific transcriptomes of Globodera pallida
RT elucidate key aspects of plant parasitism by a cyst nematode.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|WBParaSite:GPLIN_000572500}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the FNBP1 family.
CC {ECO:0000256|ARBA:ARBA00009426}.
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 20 family.
CC {ECO:0000256|ARBA:ARBA00010743}.
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DR AlphaFoldDB; A0A183BYN5; -.
DR WBParaSite; GPLIN_000572500; GPLIN_000572500; GPLIN_000572500.
DR Proteomes; UP000050741; Unassembled WGS sequence.
DR GO; GO:0016592; C:mediator complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd11619; HR1_CIP4-like; 1.
DR CDD; cd11911; SH3_CIP4-like; 1.
DR Gene3D; 6.10.140.470; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR013921; Mediator_Med20.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15735:SF12; CDC42-INTERACTING PROTEIN 4, ISOFORM B; 1.
DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF08612; Med20; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS50002; SH3; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..253
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 351..428
FT /note="REM-1"
FT /evidence="ECO:0000259|PROSITE:PS51860"
FT DOMAIN 630..696
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 286..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..510
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 912 AA; 99309 MW; 151EF9336DA39FF5 CRC64;
APVVSAHTSR GIDFLERFGQ FAKERALIEE EYAAKLKSLA KRSRGKKNED DESKMYSTTM
AFLTMLDEIE SLASQHEVVG ERLRNDLCPK LVEKCRQLRT MRKKQFQYFE MMEKHLQARV
DELAKQKKNY EKAHLDAQGA HVKGAKADKN MNLSRIELEK AKTNANTKNA ICEQSKQNYA
AQLGATNQAK FEHYNVILPK VLEVMRQLDV ERIEFSKKAM LECVAAETSV LNIIQRCYSD
MNMAIGTINP NSDTLAVVEQ TKTGFVHPLD FQFEDLGDPA DILQDGTESF DGSTLKRQPG
QGKGANGKGG GGVPRRRTLL ISKFTNGSAG THGGGSGGGT CGVNTGSEYG TLPPQQRCRK
IQQKLEELEA ELNIKDQSQA GMKRMHVAYT QNPQLGAPAK VAEQLLQNQQ EMHTLQTQIQ
RFKELLQSAQ GELNQPLGGN PHQHQAAQQQ MYNATTTSLS SPGSSPRGST GNVAGKLKNG
QQHHRGGRFN GGGTQMGSAE QHRASSYSEV SSISSADGLV MSSASSFNSG SDASSTAART
TSGTIYAQLP PMSAHPQQHQ QMNGINGGAD GGVLHQSASG TTLSSNGAAN CAPAVAPPNN
TDSDDFYEEC DTPAAAASNG CPVPQQQSDM VLGTASALYA YDATPDEVGG TTISMKDGDE
LSLLERDVGD GWTRVRHVHS NAEGFVPTSY LDCAMGVTWV FESQRSEKAL ELLFEQAGAT
LQGQPKSFKV DCLWYKPQSQ IAAQISGFFV LHHSHFPDSS FIINANRSAD GTAPSTAGRP
SPVPPRATAD RGFELQLDKF HNAGLVTDPT RYEVTGNEYR LKDFRIRVGT VATAGATVSV
KGVVVEIEYA ASNIVHQCRG LLEEIVEFFF GRPKVPEPDV FRRNSEQPDN YMAIDTLSQY
LDIFSAIRKR SF
//
