ID A0A163M888_ABSGL Unreviewed; 683 AA.
AC A0A163M888;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Signal recognition particle subunit SRP72 {ECO:0000256|ARBA:ARBA00018350, ECO:0000256|PIRNR:PIRNR038922};
GN Name=ABSGL_08038.1 scaffold 9578 {ECO:0000313|EMBL:SAM02259.1};
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:SAM02259.1};
RN [1] {ECO:0000313|EMBL:SAM02259.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM02259.1};
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 -!- FUNCTION: Component of the signal recognition particle (SRP) complex, a
CC ribonucleoprotein complex that mediates the cotranslational targeting
CC of secretory and membrane proteins to the endoplasmic reticulum (ER).
CC {ECO:0000256|PIRNR:PIRNR038922}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR038922}. Endoplasmic reticulum
CC {ECO:0000256|ARBA:ARBA00004240}.
CC -!- SIMILARITY: Belongs to the SRP72 family.
CC {ECO:0000256|ARBA:ARBA00007676, ECO:0000256|PIRNR:PIRNR038922}.
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DR EMBL; LT553800; SAM02259.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163M888; -.
DR STRING; 4829.A0A163M888; -.
DR InParanoid; A0A163M888; -.
DR OMA; NDMKVLA; -.
DR OrthoDB; 91080at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-UniRule.
DR GO; GO:0008312; F:7S RNA binding; IEA:InterPro.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:UniProtKB-UniRule.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR InterPro; IPR005158; BTAD.
DR InterPro; IPR013699; Signal_recog_part_SRP72_RNA-bd.
DR InterPro; IPR026270; SRP72.
DR InterPro; IPR031545; SRP72_TPR-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR14094; SIGNAL RECOGNITION PARTICLE 72; 1.
DR PANTHER; PTHR14094:SF9; SIGNAL RECOGNITION PARTICLE SUBUNIT SRP72; 1.
DR Pfam; PF03704; BTAD; 1.
DR Pfam; PF08492; SRP72; 1.
DR Pfam; PF17004; SRP_TPR_like; 1.
DR PIRSF; PIRSF038922; SRP72; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|PIRNR:PIRNR038922};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|PIRNR:PIRNR038922};
KW Signal recognition particle {ECO:0000256|ARBA:ARBA00023135,
KW ECO:0000256|PIRNR:PIRNR038922};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 430..525
FT /note="Bacterial transcriptional activator"
FT /evidence="ECO:0000259|Pfam:PF03704"
FT REPEAT 477..510
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 566..609
FT /note="Signal recognition particle SRP72 subunit RNA-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF08492"
FT REGION 454..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 558..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..479
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..683
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 683 AA; 75621 MW; 1CFEE6A243A81752 CRC64;
MASKEQQVAS VITELSTSTH DYDDERSLSL CDQWLKLQGD NDTLALHCKI VTLIRLGKYH
DALSLIGRKF RDNKEIDLTF EKLYCYYRTN QWQQAAELLD DAKATHPNNT AVRFLEAQLL
YGQDKFQQAI DIYEPLLQEL DEQDPMLSEV QVNLLAAKAG LGFLQPEADG VVDVDGLDYS
GCEVTYNSAS IHLAQGNYAR AAELLELARK QCNERSKLQD VAQEEVDEDL AVIATQLAYT
YQVQGRTKEA LTIYQDVVNS KIHDGAVNAV IANNMMTIQN KDDLFDAAKK MKLATGKEAD
AKLKQYQKRI ISRNEALLQM FMNKHGSCKE TAQRLLKQYP DMDELYVILA AATYHQQHKA
DKAIEELKTY AKQHPASLAI RFAAVQLDLL SSQPAAALNT LEDYLDHVHD DVKATHRPAV
VALQVWLYEQ TGQAEKAMSV LDQASKYWKD NHQAGMPVSA KSSSSPSAES QQQQTTPSIL
KQTAAFKLKT GRYSDAAADY EQLVKADPTD TQAIAGLISA YAEVDPAKAE QYGDVLPPIT
ANDTLNVDDL ESVVPGVKKG YMKKDPSSDY VKAPKSKKKR APLLPKDYDE NKTPDPERWI
ATRDRSTYRA KGKAKKAASR GPQGMVMEGG GIGSTGSARL AGRQPASPEP AAVEPTKTEP
APSPSKPKPK QQQKKKKGGK GKW
//
