ID A0A0B7NA61_9FUNG Unreviewed; 778 AA.
AC A0A0B7NA61;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=SH3 domain-containing protein {ECO:0000259|PROSITE:PS50002};
GN Name=PARPA_05756.1 scaffold 19604 {ECO:0000313|EMBL:CEP11864.1};
OS Parasitella parasitica.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP11864.1, ECO:0000313|Proteomes:UP000054107};
RN [1] {ECO:0000313|EMBL:CEP11864.1, ECO:0000313|Proteomes:UP000054107}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP11864.1,
RC ECO:0000313|Proteomes:UP000054107};
RA Ellenberger Sabrina;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; LN726998; CEP11864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B7NA61; -.
DR STRING; 35722.A0A0B7NA61; -.
DR OrthoDB; 2025446at2759; -.
DR Proteomes; UP000054107; Unassembled WGS sequence.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IEA:UniProt.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:UniProt.
DR CDD; cd00174; SH3; 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; IPR001060; FCH_dom.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065:SF7; CYTOKINESIS PROTEIN 2; 1.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 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; PS50002; SH3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054107};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 710..776
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 273..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 463..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 683..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 88050 MW; E9142CF714D9A8E5 CRC64;
MPPNIQQQVE QASFIDHFWS KDKSGMDTLL NYMSSTHRDL EMIHQIYVQR SIMENEFGER
LLDLYNKYKR QEEDAQQGVS AAYNTVSEEL NRTATTHLEL SEALADQVAA KCQAKLTEYQ
ELLSKWTVSL NDLYQVRKEK ILQLLKIRAQ YTKEHDISKG KSTPTLEALS KLCFGQVYKN
MVIKVDEGAQ EWNSAWEEAC EVMEAMEKDR VEFLKCNVWD YANQMSSTLL VQDECCENIR
AQLEKCHAEQ EIEKCISLLA TGTEIPTTKE YVDELAKEQK KKNQTERRST ETNLPKPPSK
SARQQGVQSQ QKQMSKSAQK DRRTQEQDKM DPKLKKQQES ELEGGEQKKQ QQQSSKVSTV
STATEEEEKK NTLGPKNGIS HQFRGNVSNN MGSTASRSQI KRKPLDKSLM KQVSSEMSLP
HQQSKVESQN PAYSSVRGVN KAYKSEADSS LDILLKSFEK SDISSTNATD EAKTVPHPNA
VVSEEARFRR QPSEYKPDAG SIPSRRLNHS TNHAIQEAAD TCSTNSSLRS TPDSLAHPVA
APKSPRPPAQ QIAKDLQNNM YGSPVQQQNL PDQSLGYQQT SSYMGHPQQY QPVYSPMMQP
MKSPMMQPMH SPMMQPIHSP MMQPIHSPMV QPMHSPMMQP MHSPMIQPFS LPMQSQSGKY
PPPISTNFEQ SPSMAYGTLR SVSPGGILPP PPSGAHPTPS RPSQFTDGRP IRFWVRAKYD
YKGNDDDELT FRANTLMGII EADETQDSWW YGAVYNESGW STAASIPSNF VERLIYYC
//