ID A0A093USJ9_TALMA Unreviewed; 928 AA.
AC A0A093USJ9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Alpha-actinin-like protein 1 {ECO:0000313|EMBL:KFX43277.1};
GN ORFNames=GQ26_0360050 {ECO:0000313|EMBL:KFX43277.1};
OS Talaromyces marneffei PM1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=1077442 {ECO:0000313|EMBL:KFX43277.1, ECO:0000313|Proteomes:UP000029285};
RN [1] {ECO:0000313|EMBL:KFX43277.1, ECO:0000313|Proteomes:UP000029285}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PM1 {ECO:0000313|EMBL:KFX43277.1,
RC ECO:0000313|Proteomes:UP000029285};
RX PubMed=25330172; DOI=10.1371/journal.pgen.1004662;
RA Yang E., Wang G., Cai J., Woo P.C., Lau S.K., Yuen K.-Y., Chow W.-N.,
RA Lin X.;
RT "Signature Gene Expression Reveals Novel Clues to the Molecular Mechanisms
RT of Dimorphic Transition in Penicillium marneffei.";
RL PLoS Genet. 10:e1004662-e1004662(2014).
CC -!- SIMILARITY: Belongs to the alpha-actinin family.
CC {ECO:0000256|ARBA:ARBA00010255}.
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:KFX43277.1}.
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DR EMBL; JPOX01000036; KFX43277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093USJ9; -.
DR eggNOG; KOG0035; Eukaryota.
DR HOGENOM; CLU_010193_0_0_1; -.
DR Proteomes; UP000029285; Unassembled WGS sequence.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd21215; CH_SpAIN1-like_rpt1; 1.
DR CDD; cd21291; CH_SpAIN1-like_rpt2; 1.
DR CDD; cd00051; EFh; 1.
DR CDD; cd12418; RRM_Aly_REF_like; 1.
DR Gene3D; 1.20.58.60; -; 2.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 1.10.418.10; Calponin-like domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 2.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH_dom.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR014837; EF-hand_Ca_insen.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR025715; FoP_C.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR PANTHER; PTHR11915:SF435; SPECTRIN BETA CHAIN, NON-ERYTHROCYTIC 5; 1.
DR PANTHER; PTHR11915; SPECTRIN/FILAMIN RELATED CYTOSKELETAL PROTEIN; 1.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR Pfam; PF13865; FoP_duplication; 1.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM01184; efhand_Ca_insen; 1.
DR SMART; SM01218; FoP_duplication; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR SUPFAM; SSF46966; Spectrin repeat; 2.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS50102; RRM; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 10..115
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 124..230
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 484..519
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 678..755
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT REGION 610..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..786
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 839..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 928 AA; 104872 MW; CB48C3D9D2ECC7AB CRC64;
MLMVEKQWIL VQQKTFTKWL NNKLKARNLA INDLRQDLSD GVNLIHLLEI LGDESLGRYA
SKPKLRVQKF ENVNKGLDFI KLRGIQMTNI GAEDIVDGNQ KIILGLIWTL ISKFTISDIS
SEGMSAKEGL LLWCQRKTAC YPEVEVRDFS ASWNDGLAFC ALLDIHRPDL IDFDSLDKND
HRGNMQLAFD IAANEIGIPD LLDVEDVCDV DKPDERSLMT YIAYWFHAFS QLEKVENAGR
RVEKFVSNMQ GAWEMQSSYE KRMKELLAQI ANQRSEWQGA SFEGTYTDAK VQLAEFSHYK
RNQKRKWVAE KSDLAALLGN IKTKLSTYRL RPYEPPADLA LDKCDRDWEE LMKEEHERSQ
LINEAIRDIK NKLRRSFADK ANDFALTLKT LTLAISGLEG DVEDQLTHVK RLNDNLPPLD
AFLETIADLE EQCAEANIDE NDYTTYTLDE LSYELGLVKS SVAKKLAFLE NQMVARNMTN
LTPIQLEEFE SVFRHFDRDG SNTLQEIEFS AALASLGLVY DEEEMHEVFL ETCGRNSTVS
FEQFIRFMVS VTEDQNTAEQ VFQSFREVAD GKPYVTELDL RHSLIPDELI DNLLELCPST
KTNVVILQAK QQQNRRGRGG RNNSNAPRDG VKKSYRDRVD LDRDWVHDRF EDTGDSRSSR
RDNRSRRERE SPDSDQPARL RIENLHWDLT EEDLEGLFGN IGPVQRVRIN FDRAGRSEGT
ATVTYQYLED AKQAIREFDG ANAKGQPIRL TLLPAGGRGG PRAEKSKSLF DRIERPLADR
TERSLSPDGE GATGGGRRRR GGRGGRAGRS DTSKPAPDNI DRYVPGQEQS QRSPTRRGQG
GRRPGERRDD RRGGNRDGRR GANGGTGPRP KKTQEELDAE MDDYWGNTAA AAEGGAEEKV
AAAPATVATG DSAGAAPAVN DDDIDMIE
//
