ID A0A0N1H7N3_9EURO Unreviewed; 1124 AA.
AC A0A0N1H7N3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Cytoplasmic dynein 1 light intermediate chain 2 {ECO:0000313|EMBL:KPI42570.1};
GN ORFNames=AB675_9698 {ECO:0000313|EMBL:KPI42570.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI42570.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI42570.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI42570.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI42570.1}.
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DR EMBL; LFJN01000007; KPI42570.1; -; Genomic_DNA.
DR RefSeq; XP_018002533.1; XM_018150256.1.
DR AlphaFoldDB; A0A0N1H7N3; -.
DR STRING; 1664694.A0A0N1H7N3; -.
DR GeneID; 28742136; -.
DR OrthoDB; 48125at2759; -.
DR Proteomes; UP000038010; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005868; C:cytoplasmic dynein complex; IEA:InterPro.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:InterPro.
DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 3.
DR InterPro; IPR008467; Dynein1_light_intermed_chain.
DR InterPro; IPR022780; Dynein_light_int_chain.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR026893; Tyr/Ser_Pase_IphP-type.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR PANTHER; PTHR12688; DYNEIN LIGHT INTERMEDIATE CHAIN; 1.
DR PANTHER; PTHR12688:SF0; DYNEIN LIGHT INTERMEDIATE CHAIN; 1.
DR Pfam; PF05783; DLIC; 2.
DR Pfam; PF13350; Y_phosphatase3; 2.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Microtubule {ECO:0000256|ARBA:ARBA00022701};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 893..941
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 395..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..506
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 815..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 857..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 400..423
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..840
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..899
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 973..991
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1010
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1124 AA; 123238 MW; 331712F568E1C253 CRC64;
MSAFVRPSAP PRKSLRPVSK DGEKQQIWVP MLNNASKGKD LAEKQLLILG GSPEQQQEFL
EHLNPAPSRI RFNDRQQSRK APISNRYALG YTYHNVLDAD QEDVLARLNI YMLSNPSAAF
APLLKPLFAP QTAKETLVTI LLDWSDPFRW ARQLRQWIRL LRRVIASLDD ETKIALEENI
NDWKEKRVGV LQGPGEWDEA LGVPLSVVCI QSEKSERLER DLGWHDEHFD FLTQWLRCVL
LKHGASLVYT ATFDPNNVRT LLHSSLSIHS LLKREVAKPN YIEREKILIP PNWDSWGKIR
PLREGTDLEA ISEAWTVEIQ TSPEDEPNLD SSQPTTETDT AVSVYESTLP QPLAATATQQ
STTQEDETPL ATVQEFLASQ LTILESLKAD DEKAARKAAS STTSRRIATT GTSSITSSSD
AGRMADQIGP YQINVNGIDF DAEEATRRLK EREAERNAAA AAAAVDDAPV QQTPVSRATA
TGSGVSTPTR RTGAAASGAG EEGKASNEAM SAFFQNLIKK DRRTPAGNRD GGERQPEHRR
ITYGRFLFPL QQLIKHKAVS NQGAPLPASF SAPSHGLNTP LNVHHPRLPH QTVHNRPLGQ
PPPTTPIRPE HGTLPPKDFV SSMPANLPTP PFIFVPGIPN FRDLGGYACP PPAQLHNTSI
INTTGTAPRF QIRRNILFRC AHPTQLSTQG LMVLDHLGVT DIFDLRSEPE LKKLSAPEPD
AETPFLKAGE GWIEVPGITR HFTPVYQSED YGPVALAKKL KWYTAPLDGK GDGEKDLSYS
EGFVSAYRDI GTFAATGGSY AKILRQTIRA IDAEEQREKE VEAKVAADGA ARRRPERPGR
SQIRPVSAYA DLNGILDHHE RFPSPDPSKL SLNGRSSGTA TPPTSTLSPQ PQQQLQQPED
DGGDPIRTNG GLIFHCTAGK DRTGVLAALI LYLCGVDMED IAWEYAITEP GLGSWRRIFI
DRISKSGMGS GGSGKPVEQQ QQQQEPSSEP QAATFKEGYL DDDKEKSAPT ANGSPDKVAP
APPTTAGGVA GAQTDVLTRA EAARICGSRA GNIRRFLTQV VDGEWGGVEA YLTGMIGLSQ
EEVERLKSGL VVRVDDEEGE DAMVRRRGIE GWTLEGGMDD DREG
//
