ID A0A2H3ICK4_9EURO Unreviewed; 1295 AA.
AC A0A2H3ICK4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Myosin light chain kinase-related {ECO:0000313|EMBL:PCG99861.1};
GN ORFNames=PENO1_051070 {ECO:0000313|EMBL:PCG99861.1};
OS Penicillium occitanis (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=290292 {ECO:0000313|EMBL:PCG99861.1, ECO:0000313|Proteomes:UP000218381};
RN [1] {ECO:0000313|EMBL:PCG99861.1, ECO:0000313|Proteomes:UP000218381}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CL100 {ECO:0000313|EMBL:PCG99861.1,
RC ECO:0000313|Proteomes:UP000218381};
RX PubMed=28951729; DOI=10.3389/fmicb.2017.01627;
RA Bravo-Ruiz G., Sassi A.H., Marcet-Houben M., Di Pietro A., Gargouri A.,
RA Gabaldon T., Roncero M.I.G.;
RT "Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium
RT occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen
RT Fusarium oxysporum.";
RL Front. Microbiol. 8:1627-1627(2017).
CC -!- SIMILARITY: Belongs to the UPF0507 family.
CC {ECO:0000256|ARBA:ARBA00007428}.
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:PCG99861.1}.
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DR EMBL; NPFK01000131; PCG99861.1; -; Genomic_DNA.
DR STRING; 290292.A0A2H3ICK4; -.
DR OrthoDB; 1387097at2759; -.
DR Proteomes; UP000218381; Unassembled WGS sequence.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06093; PX_domain; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 1.20.1050.80; VPS9 domain; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR InterPro; IPR003123; VPS9.
DR InterPro; IPR037191; VPS9_dom_sf.
DR PANTHER; PTHR24170; ANKYRIN REPEAT DOMAIN-CONTAINING PROTEIN 27; 1.
DR PANTHER; PTHR24170:SF1; DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G09870)-RELATED; 1.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00787; PX; 1.
DR Pfam; PF02204; VPS9; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF64268; PX domain; 1.
DR SUPFAM; SSF109993; VPS9 domain; 1.
DR PROSITE; PS51205; VPS9; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:PCG99861.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218381};
KW Transferase {ECO:0000313|EMBL:PCG99861.1}.
FT DOMAIN 329..485
FT /note="VPS9"
FT /evidence="ECO:0000259|PROSITE:PS51205"
FT REGION 215..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1201..1232
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 232..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1295 AA; 144357 MW; 84E815FBB12D51D9 CRC64;
MHPLNPFLRA FFRSTVPGQC VPVENHVLLV PTTESLFGSR DRDSNALYSD LVSSEEFLGS
HVLRIPNPPG PSHKLDAPNA RDTRAKAKQV TTVNGRTVIV KENSVYSNKG FKSLCQAQII
SDVLYHTPNH SSQPWLIYYI SKPLMGTYDP GKIVPAVPSG NMQVTDAEPS NRNAGDASSI
QKRDIKSFAE LLSHFPMIAR QMQPGLDRLF REFGKELGKP LPPPPSQSPV SPSKPEQWDS
EGTDPSQVDR LPFNSDEYFA DDEDLMRRSL ETAVTAAIDL FRLVDKQQLS LLGATTDLTG
PLVERLIEKY IAQQVHETLL FPRLCSFRRT EDVELDTRIR QIEHIDVSQV GIAIEGGLAG
KKELMNRLSR GVEAFRKMNE ATCPQDMLDV LLATIKAVTV SDESDRSLDA SEKQPPVFTV
NADILVSMLL IVVIRSQVRR LQARLLYMQH FIFVDDVESG EMGYALSTLE AVLTYLVSDY
APLRKASARN KRLWQATKTG NTRDIRSILE PNENEHDGDF SAYDDIDTNS DTLNKEAIKT
PPLEQQSIRF AVANETSSQL HADTEVESSP LEPPPLAHVF PFQTWTDSTS SNTDKRPRKR
VSMDVSSISG SSMISLLSRT TTITSTFSGI EGDTSIETLS HTHDPAGDSV PMMAVESHQP
GALKYLLSLQ EYYSIDVILE DTNRDGTTLL SAAVQHANRK VVDIITDFLL AEADIHTISS
YLEKEDVRGR TVAHYLFSAP YLMSSLGSLL PWQKKDKHGQ TPLFAICRSY DHTNYQAMVN
EALTVARRAQ DDGQPLRVGD HVDLKGNTLL HIVSDPAIIT RILAECDCDP NATNEKKFTP
LMVASKYGRV DLMRRLFADP RVDTHITESR GLTAIELAKD DEVRNRIDDM ILFLNPPVSS
GDITGRITTV VRSLFVEDAT VRFILKSGAQ TSSDMTSING TTYTITTCRR SFADFEHLAK
CLAVEHPASY IPSITEARSP FQIHSKPSRA VLHDMQGRLD QFLRILLTHP TFATHEMLWE
FFLMPELQPD MMIDRSQRKA SALYESIYDD YSPITTDGIR DTEQFVAHAQ EVVRAVHANT
RSVIRRGHSA QHAAFDFGDA ASLCASILST FKAPSNAIPV SHIDAFAQYA AAMSTSSSDS
SPLLQFLTTI TSIQSTTTAV LNALSRPGRL IYTLSSTNRN LSRSRSSLAS SSLPRKFNLN
LSVLEESRQK NLRELEQKIN ESEAQASRLS REISWNKDVV VSELAGWTSW REKVGRDAIR
AFVRATVVQE KERGRRLERC LRNIKELPPL PGAAK
//
