ID G3AHY5_SPAPN Unreviewed; 723 AA.
AC G3AHY5;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Creatinase/aminopeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SPAPADRAFT_134418 {ECO:0000313|EMBL:EGW34299.1};
OS Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN [1] {ECO:0000313|EMBL:EGW34299.1, ECO:0000313|Proteomes:UP000000709}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA Barry K.W., Grigoriev I.V., Gasch A.P.;
RT "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT production.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|ARBA:ARBA00008766}.
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DR EMBL; GL996500; EGW34299.1; -; Genomic_DNA.
DR RefSeq; XP_007373883.1; XM_007373821.1.
DR AlphaFoldDB; G3AHY5; -.
DR STRING; 619300.G3AHY5; -.
DR MEROPS; M24.A10; -.
DR GeneID; 18869812; -.
DR KEGG; spaa:SPAPADRAFT_134418; -.
DR eggNOG; KOG2413; Eukaryota.
DR HOGENOM; CLU_011781_2_6_1; -.
DR InParanoid; G3AHY5; -.
DR OMA; AMAKFPP; -.
DR OrthoDB; 869at2759; -.
DR Proteomes; UP000000709; Unassembled WGS sequence.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 2.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR032416; Peptidase_M24_C.
DR PANTHER; PTHR43763; XAA-PRO AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR43763:SF6; XAA-PRO AMINOPEPTIDASE 1; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF16189; Creatinase_N_2; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR Pfam; PF16188; Peptidase_M24_C; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000709}.
FT DOMAIN 90..214
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 448..644
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT DOMAIN 659..723
FT /note="Peptidase M24 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF16188"
SQ SEQUENCE 723 AA; 82246 MW; DA0DF3A940BD0D37 CRC64;
MTHISEKEPL LGYPRKIADE NEISTHQLCP SFKSILSFPF QSCLPSFTRS EKSHTEDYEC
IDYDEDYEPV PDLPYNLTIA KSKLSTQEKL TEIRKLMRDH HIGVYIIPSE DEHQSEYTAL
ADKRREFISG FTGSAGIAIV TLTNGATLEG KAALSTDGRY FLQAEKQLDL NYWRLLKQGA
AGYPSWPKYC IQQAVHNDFS NVISCDPRLI SLSLGDYFNN ARLTYTNKFK FQPLIDINLV
DQVWGDEKPS RSLEPVYQLD LKFSGEHTND KLHRIRVRMR EHDATHYVVN ELDSIAWLLN
LRADSDIPFN PVFFAYAIIT LDSVVLYINK VKIDNGNEEL HKYLQTINNL SIRDYSQFYE
DIGKLKSTVD EPDLAVILPE KSSTTYALFQ AFPESYSKRI IIHESIIANL KIYKNSTESF
NAKIAQYKDS LAFIIFSSWL EHQLINKKAS ISEYDAACKI YSIRTKLPNF KGLSYETISS
TGANAAIIHY APTKEENDII DPAKIYLIDS GAQFLEGTTD ITRSYKFGHE GLTKEYQKFY
TLVLKGHLAV AMAKFPPHSS STGTVLDGYS RQPLWNEGLD FNHGTGHGVG SFGNVHEGPL
YISTTSSGPS SKADLYRPGA ILTDEPGYYV DGKLGIRIES ELEVIECDDS VGKTRNGDNF
LGFEYLTKIP FCRKLIDCDY LTLIELTWIN EYHKSIRAEF ANKLLQMGDR RAYNWLIKET
EPL
//
