CAZyme Information: SAPIO_CDS1199-t41_1-p1

Basic Information

• Species: Scedosporium apiospermum
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Scedosporium; Scedosporium apiospermum
• CAZyme ID: SAPIO_CDS1199-t41_1-p1
• CAZy Family: AA7
• CAZyme Description: Carboxypeptidase B

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
707	JOWA01000044|CGC7	77908.74	5.7081

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_SapiospermumIHEM14462	10920	N/A	2544	8376

• Gene Location: location=JOWA01000044:1315078-1319219(+)

Full Sequence      

MKSLAWSAVFLPFALASAVPRADAGAKVDYTGFKGLRVKIPHGHSHFDVEKDLAGLLTHV
VNFGHGDYLDIVVSPEKVASVEQRVDAEVVVHDVGAALAEEGEPIRTYAVPSESWFTGYH
TYADHLQFLKDLQGGFPQQSELINIGNSVQNRAISGIHIWGSGGKGSKPAVLFHGTVHAR
EWISTMTAEYMAWQLLTLYSNTPAVRALVDNYDFYILPIVNPDGFVYTQTNDRYWRKNRQ
TVSSSSCVGRDINRNWSYKWEIPGGASTSPCSETYKGQAPGDSPEARALMRHVDSLRDGK
GIKFYIDFHSYGQYILWPFGYDCSFVAPDDAAHNSLASKGRTAISNVYGTSYTIGNSCRA
LYATTGDSVDYVHGVGNSTYSYTIELRDTGRSGFALPASQIQPTVKETWAGVIAMLANIY
HKVEPGRPPPGESDDGDSSGHGLQLVVKANTVDGMVPVGEIATKRGDIYHGTFRASIKLT
RSLGTCTAFYWYFNDSQEIDMEFLSKEFNFETNTFPVNLVLHSKESVAAGFDAVKAGTWA
RVNLPFDPTEDYHEYRFDFIPGSVNFYAEGVNIATMDGPAVPTSSGHILLSHWSSGNPKW
SGGPPEQDATVAIRYFKAYFNSSDADRQTEWERRCRDANDPDTLCHVPSVLDDPDAAAHF
FTATTPTDEKTGDGNAGSTISRPLGFLSWMAVVWAGYWHSSWMDLYI

Enzyme Prediction     

No EC number prediction in SAPIO_CDS1199-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH16	436	619	3.7e-80	0.953125

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
349433	M14_CP_A-B_like	2.01e-179	119	419	1	300	Peptidase M14 carboxypeptidase subfamily A/B-like. The Peptidase M14 Carboxypeptidase (CP) A/B subfamily is one of two main M14 CP subfamilies defined by sequence and structural homology, the other being the N/E subfamily. CPs hydrolyze single, C-terminal amino acids from polypeptide chains. They have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. Enzymes belonging to the A/B subfamily are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The A/B enzymes can be further divided based on their substrate specificity; Carboxypeptidase A-like (CPA-like) enzymes favor hydrophobic residues while carboxypeptidase B-like (CPB-like) enzymes only cleave the basic residues lysine or arginine. There are nine members in the A/B family: CPA1, CPA2, CPA3, CPA4, CPA5, CPA6, CPB, CPO and CPU. CPA1, CPA2 and CPB are produced by the pancreas. The A forms have slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA3 is found in secretory granules of mast cells and functions in inflammatory processes. CPA4 is detected in hormone-regulated tissues, and is thought to play a role in prostate cancer. CPA5 is present in discrete regions of pituitary and other tissues, and cleaves aliphatic C-terminal residues. CPA6 is highly expressed in embryonic brain and optic muscle, suggesting that it may play a specific role in cell migration and axonal guidance. CPU (also called CPB2) is produced and secreted by the liver as the inactive precursor, PCPU, commonly referred to as thrombin-activatable fibrinolysis inhibitor (TAFI). Little is known about CPO but it has been suggested to have specificity for acidic residues.
214748	Zn_pept	1.34e-110	119	404	1	276	Zn_pept domain.
395189	Peptidase_M14	3.31e-110	126	411	2	287	Zinc carboxypeptidase.
349432	M14_CPT	1.36e-77	116	412	1	292	Peptidase M14 Carboxypeptidase T subfamily. Peptidase M14-like domain of carboxypeptidase (CP) T (CPT), CPT belongs to the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPT has moderate similarity to CPA and CPB, and exhibits dual-substrate specificity by cleaving C-terminal hydrophobic amino acid residues like CPA and C-terminal positively charged residues like CPB. CPA and CPB are M14 family peptidases but do not belong to this CPT group. The substrate specificity difference between CPT and CPA and CPB is ascribed to a few amino acid substitutions at the substrate-binding pocket while the spatial organization of the binding site remains the same as in all Zn-CPs. CPT has increased thermal stability in presence of Ca2+ ions, and two disulfide bridges which give an additional stabilization factor.
349442	M14_CPA	7.12e-77	116	411	3	290	Peptidase M14 carboxypeptidase subfamily A/B-like; Carboxypeptidase A subgroup. Peptidase M14 Carboxypeptidase (CP) A (CPA) belongs to the A/B subfamily of the M14 family of metallocarboxypeptidases (MCPs). The M14 family are zinc-binding CPs which hydrolyze single, C-terminal amino acids from polypeptide chains, and have a recognition site for the free C-terminal carboxyl group, which is a key determinant of specificity. CPA enzymes generally favor hydrophobic residues. A/B subfamily enzymes are normally synthesized as inactive precursors containing preceding signal peptide, followed by a globular N-terminal pro-region linked to the enzyme; these proenzymes are called procarboxypeptidases. The procarboxypeptidase A (PCPA) is produced by the exocrine pancreas and stored as a stable zymogen in the pancreatic granules until secretion into the digestive tract occurs. This subfamily includes CPA1, CPA2 and CPA4 forms. Within these A forms, there are slightly different specificities, with CPA1 preferring aliphatic and small aromatic residues, and CPA2 preferring the bulkier aromatic side chains. CPA4, detected in hormone-regulated tissues, is thought to play a role in prostate cancer.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
VBB86764.1|GH16_23	4.14e-81	442	694	135	392
CDP32289.1|GH16_23	5.80e-81	442	694	135	392
AEO58087.1|GH16_23	2.32e-80	442	689	157	410
QBZ62950.1|GH16_23	8.86e-80	442	693	130	383
UKZ96476.1|GH16_23	4.77e-77	416	679	95	364

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1AYE_A	2.30e-65	77	419	60	396	Human Procarboxypeptidase A2 [Homo sapiens]
1DTD_A	3.89e-65	116	419	3	298	Crystal Structure Of The Complex Between The Leech Carboxypeptidase Inhibitor And The Human Carboxypeptidase A2 (Lci-Cpa2) [Homo sapiens]
2PCU_A	8.21e-64	116	419	5	301	Human carboxypeptidase A4 in complex with a cleaved hexapeptide. [Homo sapiens]
2BO9_A	8.97e-64	116	419	7	303	Human carboxypeptidase A4 in complex with human latexin. [Homo sapiens],2BO9_C Human carboxypeptidase A4 in complex with human latexin. [Homo sapiens]
4A94_A	9.52e-64	116	419	9	305	Structure of the carboxypeptidase inhibitor from Nerita versicolor in complex with human CPA4 [Homo sapiens],4A94_B Structure of the carboxypeptidase inhibitor from Nerita versicolor in complex with human CPA4 [Homo sapiens],4BD9_A Structure of the complex between SmCI and human carboxypeptidase A4 [Homo sapiens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4AS12|MCPA_ARTBC	7.63e-113	15	419	10	419	Probable metallocarboxypeptidase A OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=MCPA PE=1 SV=2
sp|D4DL57|MCPA_TRIVH	2.14e-112	15	419	10	419	Probable metallocarboxypeptidase A OS=Trichophyton verrucosum (strain HKI 0517) OX=663202 GN=MCPA PE=3 SV=1
sp|A6XGK3|MCPA_TRIRU	2.14e-112	15	419	10	419	Metallocarboxypeptidase A OS=Trichophyton rubrum OX=5551 GN=MCPA PE=1 SV=1
sp|B6V865|MCPA_TRITO	4.67e-111	15	419	10	419	Metallocarboxypeptidase A OS=Trichophyton tonsurans OX=34387 GN=MCPA PE=3 SV=1
sp|B8XGR3|MCPA_TRIEQ	6.58e-111	15	419	10	419	Metallocarboxypeptidase A OS=Trichophyton equinum OX=63418 GN=MCPA PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000215	0.999770	CS pos: 24-25. Pr: 0.4474

TMHMM  Annotations     

There is no transmembrane helices in SAPIO_CDS1199-t41_1-p1.