ID A0A168KPR4_ABSGL Unreviewed; 599 AA.
AC A0A168KPR4;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:SAL95136.1};
GN Name=ABSGL_00437.1 scaffold 537 {ECO:0000313|EMBL:SAL95136.1};
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:SAL95136.1};
RN [1] {ECO:0000313|EMBL:SAL95136.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL95136.1};
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 polyadenylate-binding protein type-1 family.
CC {ECO:0000256|ARBA:ARBA00008557}.
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DR EMBL; LT550170; SAL95136.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A168KPR4; -.
DR STRING; 4829.A0A168KPR4; -.
DR InParanoid; A0A168KPR4; -.
DR OMA; RIMWARR; -.
DR OrthoDB; 1368317at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd12379; RRM2_I_PABPs; 1.
DR CDD; cd12380; RRM3_I_PABPs; 1.
DR CDD; cd12381; RRM4_I_PABPs; 1.
DR Gene3D; 3.30.70.330; -; 4.
DR Gene3D; 1.10.1900.10; c-terminal domain of poly(a) binding protein; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR036053; PABP-dom.
DR InterPro; IPR002004; PABP_HYD.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR045305; RRM2_I_PABPs.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR PANTHER; PTHR24012:SF883; RBM-28; 1.
DR PANTHER; PTHR24012; RNA BINDING PROTEIN; 1.
DR Pfam; PF00658; PABP; 1.
DR Pfam; PF00076; RRM_1; 4.
DR SMART; SM00517; PolyA; 1.
DR SMART; SM00360; RRM; 4.
DR SMART; SM00361; RRM_1; 4.
DR SUPFAM; SSF63570; PABC (PABP) domain; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS51309; PABC; 1.
DR PROSITE; PS50102; RRM; 4.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT DOMAIN 56..134
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 145..222
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 238..315
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 350..428
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT DOMAIN 519..596
FT /note="PABC"
FT /evidence="ECO:0000259|PROSITE:PS51309"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 315..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 315..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 599 AA; 67658 MW; C7FBE638AB557953 CRC64;
MTGPSSLVVQ HGYTSGPLGP RGLSTKQQQA IAMAQGHSAL QSQQQRRQSS SSQATSSVYV
GELDPSVDES TLRSIFCPMA PGDNIHLCRD AITNKSLGYA YVDFTSDTEG ARAIQRLNQT
MINGRPCRIM WARRTKSLKH PVSTGNLFIK NLDPMVTTKS LLDTFSLYGH INCCKIVTDE
RGQSKGYGFI HYDTVESAER AIDKVNGMTL YDREVFVGHH IPKQERIQRS EGARQRFTNV
YVKNLVTDIT EEELKELFGA YGPIASVLIQ RDDQGASRGF GFVNFERHED AEKAVSQMHD
TEYIGKRLFV SRAQKRSERE EELRKQHDKP ASPTATTTTT TTTPSKYHGV NLYIKNLADD
VDDDVLREVF APFGTITSAK VMRDEKSHLS KGFGFVCFTT PDEANKAVAE MNGKPLGNKT
LYVAMAQKKE DRKYHMDQRA QMMHLQQPYI PIPMNGYMAG NPMYYDPYSQ HNYQPSLMTP
RPLRWNPSFM MKQNYPHYPG YAVRPPPPPT PTATLIPSDN HWTPDTLQDY PLETQKQLLG
EQIYTVVNAI YPNTAGKVTG MLLEMEVDDL MELINNKHLL EERAQEAMAV LEQHRGLDR
//
