ID R9AGQ1_WALI9 Unreviewed; 934 AA.
AC R9AGQ1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Septation protein imp2 {ECO:0000313|EMBL:EOQ99230.1};
GN ORFNames=J056_002355 {ECO:0000313|EMBL:EOQ99230.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOQ99230.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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DR EMBL; KE007243; EOQ99230.1; -; Genomic_DNA.
DR RefSeq; XP_009269895.1; XM_009271620.1.
DR AlphaFoldDB; R9AGQ1; -.
DR STRING; 1299270.R9AGQ1; -.
DR GeneID; 20375307; -.
DR KEGG; wic:J056_002355; -.
DR eggNOG; KOG2398; Eukaryota.
DR HOGENOM; CLU_004415_0_0_1; -.
DR OMA; PMLDRMH; -.
DR OrthoDB; 2025446at2759; -.
DR Proteomes; UP000014064; 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; IPR031160; F_BAR.
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 PRINTS; PR00452; SH3DOMAIN.
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; PS50002; SH3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|PROSITE-ProRule:PRU01077};
KW Reference proteome {ECO:0000313|Proteomes:UP000014064};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 43..298
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 871..934
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..794
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 934 AA; 104104 MW; D1A6E36B9E63E00C CRC64;
MSILSTSPAK SFLSRKKHSS QPDIHISQQP TQQFYTSNDI NTKDFCNSFW GVDSNGYGFD
TLTNKLKSSS KTVDDLKLFW KERSAIEDEY ARKMAKLSRF LVGTGETGAV RDSLDTLSTE
LEQTSQNHFN LCQTIHRDLE RPTNEWSIRL SNLKKSSLAT IEKKYKVLQT QESYVDKAKA
KYTDNCVSIN TFTAQKSLLQ GKDLDRVDVK LEKAKSVVGA NERDYQNFVK ALSDTRKRWE
ADWRMFCDLC QDEEEERIEF LKSNMWSYAN EVSTVCVADD ESCEKLRQSL EQVDPELDVE
FFVDESMTGN ILPNQPTFID FSRETQVPSP APRYATFHRN SIRPLDMPRD SHRPLQSHNQ
PPKHEVLDHP PPSSPKKQVV QEEPKLQKSQ PKESSHDENA PFKVPQLPAR NIDRPPPTKV
EPPSFDTASA PQTAPKFDEA PPRPEKEDKV ETKKESGDVD ELAAALAQLR NAPPATGNLR
ANVAAQAEKK PRSRPVSQHS AVSPGPQVGA PAGQQVSPTK TQQQPQRPPF NPQNPIYQGM
DASQIQALQI QHKYAPHTTP PFPAMMQRPT SSQSNAGGPV EDVMTTYHQQ LPHERSHRNS
RLDQTQQTQQ HISRPPSSTG RSPSREGFAG IGAGGGFGAS YGSRQPSPAV SNASPVRAAT
PLGISLNASG EVAHDQKAEE YRKRRSVSPA LAPAPSATPA PANTLANQQQ QMQMQQQHQA
QAYYQYQMMM AQQAQQGQGQ GQQQQPQHPY QPYQYYPYGQ PQQQPYVMTT TPGPGYNPYP
PSSTPAPAPT PAPSGPIMNA QQQHRAPSPS PTPIYNGTPG PHQHQQNQQT PFIPQIQTQQ
LSHTPQIHSA TNTSMYRQHS PSPLASPSKE PILFHVKALY DYAAQTTEEF DFKAGDVIAV
TKTPEDGWWT GQLTDEARCL PGKTLFPSNF VSLF
//
