ID K0KN44_WICCF Unreviewed; 618 AA.
AC K0KN44;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Septation protein {ECO:0000313|EMBL:CCH44401.1};
GN ORFNames=BN7_3964 {ECO:0000313|EMBL:CCH44401.1};
OS Wickerhamomyces ciferrii (strain ATCC 14091 / BCRC 22168 / CBS 111 / JCM
OS 3599 / NBRC 0793 / NRRL Y-1031 F-60-10) (Yeast) (Pichia ciferrii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX NCBI_TaxID=1206466 {ECO:0000313|EMBL:CCH44401.1, ECO:0000313|Proteomes:UP000009328};
RN [1] {ECO:0000313|EMBL:CCH44401.1, ECO:0000313|Proteomes:UP000009328}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14091 / BCRC 22168 / CBS 111 / JCM 3599 / NBRC 0793 / NRRL
RC Y-1031 F-60-10 {ECO:0000313|Proteomes:UP000009328};
RX PubMed=23193139; DOI=10.1128/EC.00258-12;
RA Schneider J., Andrea H., Blom J., Jaenicke S., Ruckert C., Schorsch C.,
RA Szczepanowski R., Farwick M., Goesmann A., Puhler A., Schaffer S.,
RA Tauch A., Kohler T., Brinkrolf K.;
RT "Draft genome sequence of Wickerhamomyces ciferrii NRRL Y-1031 F-60-10.";
RL Eukaryot. Cell 11:1582-1583(2012).
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:CCH44401.1}.
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DR EMBL; CAIF01000123; CCH44401.1; -; Genomic_DNA.
DR AlphaFoldDB; K0KN44; -.
DR STRING; 1206466.K0KN44; -.
DR eggNOG; KOG2398; Eukaryota.
DR HOGENOM; CLU_003525_1_1_1; -.
DR InParanoid; K0KN44; -.
DR Proteomes; UP000009328; 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, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000009328};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 1..233
FT /note="F-BAR"
FT /evidence="ECO:0000259|PROSITE:PS51741"
FT DOMAIN 559..618
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 275..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 96..123
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 275..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 618 AA; 70855 MW; 86C5EEE40D43BDFB CRC64;
MHQGAQTCEE LLAFYKERVQ LEEEYSRRLN AISKKSRGTF ETGLLRESFE TLRNETEQMS
RSHLNEARKL HSEALLKVDS FLSNFLARCK PLETSVENIK KTKNQLEIQV ARLKEKYSNE
VTKLNSYIAQ ESLLLGKELE KNQDRAYRQQ RIVNELREEY LLAVQNLEHT QNIWIDEWKN
SSTKLQDLEI ERIQFLISNI WEYTNTVSTS CVTDDASCEN IRSSLELCDP SKEISTFVKK
FKTGSEIYSS PKFIDYLNGD RDEVGLPEVI SAFDSRSTSA STQVPTPTTT TRLHSQKTGE
QRYAPSNNGS QHSSTKLQRR PPPSDDGQTS ISNPSSIGTQ LHRKESEYSN PTSISSFTES
IDNDLRLSKN WNSPSRRRSR NSEFNESWNR KNSNRRSFIL DTTPKKVNQP YVIPSNQDPL
RATLEDLKIG GNGDMNKFRQ VLQNTNQQTS TPQQQQQQQQ MNPIMRSEPR KSKPTFIDLT
ETPTAPDFNS SMSSERTNAT TIRPKSMVID SHPQLITEDP SMKRSSFHAG LRSQSKSTIN
LQSKVATNGL PLITRQGRRV IKHAKAIFDF KATINEELSF KEGDILLVVH MQDDGWWECE
RLEDGNTGLA PYNYLERV
//