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Database: UniProt
Entry: A0A163K0U1_ABSGL
LinkDB: A0A163K0U1_ABSGL
Original site: A0A163K0U1_ABSGL 
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}.
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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
//
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