ID A0A163JW99_ABSGL Unreviewed; 641 AA.
AC A0A163JW99;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Actinin-like protein {ECO:0008006|Google:ProtNLM};
GN Name=ABSGL_09790.1 scaffold 11617 {ECO:0000313|EMBL:SAM03934.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM03934.1};
RN [1] {ECO:0000313|EMBL:SAM03934.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM03934.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the alpha-actinin family.
CC {ECO:0000256|ARBA:ARBA00010255}.
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DR EMBL; LT554307; SAM03934.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163JW99; -.
DR STRING; 4829.A0A163JW99; -.
DR InParanoid; A0A163JW99; -.
DR OMA; CYEGVEV; -.
DR OrthoDB; 2872403at2759; -.
DR Proteomes; UP000078561; 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:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd00051; EFh; 1.
DR Gene3D; 1.20.58.60; -; 2.
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 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; PF13405; EF-hand_6; 1.
DR Pfam; PF08726; EFhand_Ca_insen; 1.
DR SMART; SM00033; CH; 2.
DR SMART; SM00054; EFh; 1.
DR SMART; SM01184; efhand_Ca_insen; 1.
DR SUPFAM; SSF47576; Calponin-homology domain, CH-domain; 1.
DR SUPFAM; SSF47473; EF-hand; 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.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 30..136
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 145..251
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000259|PROSITE:PS50021"
FT DOMAIN 505..540
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
SQ SEQUENCE 641 AA; 74248 MW; D49A1E00B0F598AC CRC64;
MLKRASFLPS GTLQQPLEDS ARIMDKAWEL IQQKTFTKWL NNKLDIRGVE HIQSLADDLA
NGVTLIQLLE IIGDAPMGRY NRNPRMRIQY VENVNMALEF IKQRGVALTN IGAEDIVDKN
LKLILGMLWT IILRFTIADI SQEGKNAKDG LLLWCQRKTA PYREVDVRDF TYSWTDGLAF
CALIHRHRPD LLDFDALDKT DRHGNTALAF NVAEQHLGIP QLLDVEDVCD ISKPDERSVM
TYVAEYFHAF SALDKVETAG RRVAKFAEVI ASVWQMRNDY ERRVLALMDA VLLAQREWQS
TQLTDHYIST KQKGLEFNHY KNTQKREWVA EKREIDSLLG NIQTKLKTYN LKPYYPPEGL
TLKDLDNIWC ELLQNEAFYH RSINSKIREI KENLRKAYAQ AANDFQQQLD SISMEQSLLD
GNLDNQLQRV QLLQKKIEPL TATLHKVQVL DQDCVDANTE ENDYTVYSVE DLTFGLDLLR
QAIQKKNAFI QNQVVSRNMT NLTPAQLEEF EQAFRYFDKD NSNTLSAMEF NAALASLGVF
YDDDDFDQVF SHVTGRQEHA SFEQFIRFMV SVTEDKSTPE QIRDSFRTIA GDKPYVTELD
LRMCLVPDDI VDHLKIDMPR SSYDGHQEAM EYHQYIDTMF R
//
