ID A0A163K0U1_ABSGL Unreviewed; 704 AA.
AC A0A163K0U1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN Name=ABSGL_11681.1 scaffold 12295 {ECO:0000313|EMBL:SAM05806.1};
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:SAM05806.1};
RN [1] {ECO:0000313|EMBL:SAM05806.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM05806.1};
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 -!- CATALYTIC ACTIVITY:
CC Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000256|PROSITE-
CC ProRule:PRU00277};
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. Septin GTPase family.
CC {ECO:0000256|RuleBase:RU004560}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT554468; SAM05806.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163K0U1; -.
DR STRING; 4829.A0A163K0U1; -.
DR InParanoid; A0A163K0U1; -.
DR OrthoDB; 1386862at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.10.50.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR030379; G_SEPTIN_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46512; PEPTIDYLPROLYL ISOMERASE; 1.
DR PANTHER; PTHR46512:SF9; TETRATRICOPEPTIDE REPEAT DOMAIN 9; 1.
DR Pfam; PF00254; FKBP_C; 1.
DR Pfam; PF00735; Septin; 2.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF54534; FKBP-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 1.
DR PROSITE; PS51719; G_SEPTIN; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|RuleBase:RU004560};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU004560};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 29..128
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REPEAT 224..257
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 320..682
FT /note="Septin-type G"
FT /evidence="ECO:0000259|PROSITE:PS51719"
FT REGION 511..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..530
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 704 AA; 79569 MW; 3F71C8387EADD052 CRC64;
MESSTFLTDD LGVSKQVMEP GTGEMPNAKD CVKVHYEGFL LDDGTKFDSS YGRNAPLEFI
LGEGKVIKGW EIAVKAMRVG ETCKVTCSSE YGRGNSTDEA NAYGERGRLS IVPPNATLQF
IITLLSTEQS VDSPAYLIKM AADLKAQGND FYKTGDVTSA LSRYKQAQGY TARQDDVSKE
DLDQMQALSV SILANMAACY TKTQDWKNTI DCCKEVLELD PCHVKSYYRI GQSYSAINDI
EEAMQYVRQG LKNIPNDPSL ESLYQQLEQK YIVWKSRNKE KFSKLFTSYS LSCYANAMYA
NLDHCYLIGW RRFKNDSKPI VSHFNVMVVG FSGLGKTSFV RTMLESLKLK LTKEKRDTMF
QPSSSGQSLI QGPLERTLVP YTVSVDTEVD GEKMVLTLID TPGFQTDYTV DKQLHDILGY
IEHQFDLTLA EENKVKRNPK AVDTQVHACL YFVDPNKKDL DEYDIRVLSK LANRVNVIPV
IGKSDTLTLA QRNRLKPTII KSIYNTHKIP LYGMPDEDED EEDDNDCNND SHNEDDLAIN
SNGDSETSAV VSAKTNGTLD SNGDTVTKDA NKKESPSLDV FLQQFDYDQE DDEVQSFIDY
LRAIPFTFIA CEEDPATGKP IELAPPIQLG RDYGWGIIDC LGDDYSDFNK LKTMLLLSHR
RILMTETVER YYEKYRTERL LQKRATKMKS MVASKKILED LTHL
//