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Conserved domains on  [gi|470322789|ref|XP_004349333|]
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hypothetical protein CAOG_02583 [Capsaspora owczarzaki ATCC 30864]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
70-536 1.07e-34

Ubiquitin carboxyl-terminal hydrolase;


:

Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 134.88  E-value: 1.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789   70 RGLTNATgdNHCFMNGVVQLLWHLAPFRDAFaAVDSHHCSDTQNQLDC-VFCALKTIFN----NTTDSHVPPDALRSALS 144
Cdd:pfam00443   1 TGLVNLG--NTCYMNSVLQSLFSIPPFRDYL-LRISPLSEDSRYNKDInLLCALRDLFKalqkNSKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  145 SVYKSssrFQLGDMNDAVECLEAIQSTIHSQVVGdqvkddhyDSCTAPTCPVHSVFALRVSEHVKCSSCGAQSKDFEFEK 224
Cdd:pfam00443  78 KLNPD---FSGYKQQDAQEFLLFLLDGLHEDLNG--------NHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  225 SIHYVAVEALAEQVHHerkrrrktntyrlsiiapntkdappangnpraslssgsagnvedepwpagwekveapegklyfh 304
Cdd:pfam00443 147 DLSLPIPGDSAELKTA---------------------------------------------------------------- 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  305 dhnskitywtdprlrvraglphgwdfsttetgemyyvdhvtkgsawtpplatrsiqatlHECIPPVALDHLLNAVNESDV 384
Cdd:pfam00443 163 -----------------------------------------------------------SLQICFLQFSKLEELDDEEKY 183
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  385 RSCQKTCGTVNTIVPTLHSAPSVFalalvwgstrpqselisevlellapaldlatVFHRTRPT---EPKAKRRWSLADPD 461
Cdd:pfam00443 184 YCDKCGCKQDAIKQLKISRLPPVL-------------------------------IIHLKRFSynrSTWEKLNTEVEFPL 232
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  462 nRLNADAFAAKDALP-------MSLTGLVCYYG----KHYIAFFYNPRDRMWMMYDDATVKPVGPTWASLiakckasKFQ 530
Cdd:pfam00443 233 -ELDLSRYLAEELKPktnnlqdYRLVAVVVHSGslssGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVL-------SSS 304

                  ....*.
gi 470322789  531 PAVLLY 536
Cdd:pfam00443 305 AYILFY 310
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
288-318 3.92e-08

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


:

Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 49.83  E-value: 3.92e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 470322789 288 PAGWEKVEAPEGKLYFHDHNSKITYWTDPRL 318
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
324-353 5.41e-05

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


:

Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 40.95  E-value: 5.41e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 470322789  324 LPHGWDFSTTETGEMYYVDHVTKGSAWTPP 353
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
776-929 2.26e-04

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


:

Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 41.38  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789   776 REGSLFLKERKHliKSAWKERRFSLRGPYLTFVKPNKVDSIKVVDHldkcvllVIDqshtrLSGSSglesVRDRSKPAAA 855
Cdd:smart00233   3 KEGWLYKKSGGG--KKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKG-------SID-----LSGCT----VREAPDPDSS 64
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470322789   856 DAslsrspsaassassasvlsrassnerigtvngkkaatptPFYFQLRHP-KMLYELCAASEEDMQQWLLMLERA 929
Cdd:smart00233  65 KK---------------------------------------PHCFEIKTSdRKTLLLQAESEEEREKWVEALRKA 100
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
70-536 1.07e-34

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 134.88  E-value: 1.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789   70 RGLTNATgdNHCFMNGVVQLLWHLAPFRDAFaAVDSHHCSDTQNQLDC-VFCALKTIFN----NTTDSHVPPDALRSALS 144
Cdd:pfam00443   1 TGLVNLG--NTCYMNSVLQSLFSIPPFRDYL-LRISPLSEDSRYNKDInLLCALRDLFKalqkNSKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  145 SVYKSssrFQLGDMNDAVECLEAIQSTIHSQVVGdqvkddhyDSCTAPTCPVHSVFALRVSEHVKCSSCGAQSKDFEFEK 224
Cdd:pfam00443  78 KLNPD---FSGYKQQDAQEFLLFLLDGLHEDLNG--------NHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  225 SIHYVAVEALAEQVHHerkrrrktntyrlsiiapntkdappangnpraslssgsagnvedepwpagwekveapegklyfh 304
Cdd:pfam00443 147 DLSLPIPGDSAELKTA---------------------------------------------------------------- 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  305 dhnskitywtdprlrvraglphgwdfsttetgemyyvdhvtkgsawtpplatrsiqatlHECIPPVALDHLLNAVNESDV 384
Cdd:pfam00443 163 -----------------------------------------------------------SLQICFLQFSKLEELDDEEKY 183
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  385 RSCQKTCGTVNTIVPTLHSAPSVFalalvwgstrpqselisevlellapaldlatVFHRTRPT---EPKAKRRWSLADPD 461
Cdd:pfam00443 184 YCDKCGCKQDAIKQLKISRLPPVL-------------------------------IIHLKRFSynrSTWEKLNTEVEFPL 232
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  462 nRLNADAFAAKDALP-------MSLTGLVCYYG----KHYIAFFYNPRDRMWMMYDDATVKPVGPTWASLiakckasKFQ 530
Cdd:pfam00443 233 -ELDLSRYLAEELKPktnnlqdYRLVAVVVHSGslssGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVL-------SSS 304

                  ....*.
gi 470322789  531 PAVLLY 536
Cdd:pfam00443 305 AYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
70-218 7.10e-12

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 67.78  E-value: 7.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  70 RGLTN--ATgdnhCFMNGVVQLLWHLAPFRDAFAAvDSHHC-SDTQNQLDCVFCALKTIFNN-TTDSHVPPDALRSALSS 145
Cdd:cd02660    1 RGLINlgAT----CFMNVILQALLHNPLLRNYFLS-DRHSCtCLSCSPNSCLSCAMDEIFQEfYYSGDRSPYGPINLLYL 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470322789 146 VYKSSSRFQLGDMNDAVECLEAIQSTIHSQVVGDQVKDDHYDSCtapTCPVHSVFALRVSEHVKCSSCGAQSK 218
Cdd:cd02660   76 SWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHC---NCIIHQTFSGSLQSSVTCQRCGGVST 145
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
288-318 3.92e-08

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 49.83  E-value: 3.92e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 470322789 288 PAGWEKVEAPEGKLYFHDHNSKITYWTDPRL 318
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
288-318 3.53e-07

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 47.21  E-value: 3.53e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 470322789   288 PAGWEKVEAPEGKLYFHDHNSKITYWTDPRL 318
Cdd:smart00456   3 PPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
288-316 3.76e-07

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 47.11  E-value: 3.76e-07
                          10        20
                  ....*....|....*....|....*....
gi 470322789  288 PAGWEKVEAPEGKLYFHDHNSKITYWTDP 316
Cdd:pfam00397   2 PPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
324-353 5.41e-05

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 40.95  E-value: 5.41e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 470322789  324 LPHGWDFSTTETGEMYYVDHVTKGSAWTPP 353
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
776-929 2.26e-04

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 41.38  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789   776 REGSLFLKERKHliKSAWKERRFSLRGPYLTFVKPNKVDSIKVVDHldkcvllVIDqshtrLSGSSglesVRDRSKPAAA 855
Cdd:smart00233   3 KEGWLYKKSGGG--KKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKG-------SID-----LSGCT----VREAPDPDSS 64
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470322789   856 DAslsrspsaassassasvlsrassnerigtvngkkaatptPFYFQLRHP-KMLYELCAASEEDMQQWLLMLERA 929
Cdd:smart00233  65 KK---------------------------------------PHCFEIKTSdRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
776-929 7.03e-04

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 40.24  E-value: 7.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  776 REGslFLKERKHLIKSAWKERRFSLRGPYLTFVKPNKVDSikvvdhldkcvllvidqsHTRLSGSSGLESVRDRSKPAAA 855
Cdd:pfam00169   3 KEG--WLLKKGGGKKKSWKKRYFVLFDGSLLYYKDDKSGK------------------SKEPKGSISLSGCEVVEVVASD 62
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 470322789  856 DaslsrspsaassassasvlsrassnerigtvngkkaaTPTPFYFQLRHPKM----LYELCAASEEDMQQWLLMLERA 929
Cdd:pfam00169  63 S-------------------------------------PKRKFCFELRTGERtgkrTYLLQAESEEERKDWIKAIQSA 103
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
323-353 2.64e-03

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 36.42  E-value: 2.64e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 470322789   323 GLPHGWDFSTTETGEMYYVDHVTKGSAWTPP 353
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
325-353 3.63e-03

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 35.97  E-value: 3.63e-03
                         10        20
                 ....*....|....*....|....*....
gi 470322789 325 PHGWDFSTTETGEMYYVDHVTKGSAWTPP 353
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
 
Name Accession Description Interval E-value
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
70-536 1.07e-34

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 134.88  E-value: 1.07e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789   70 RGLTNATgdNHCFMNGVVQLLWHLAPFRDAFaAVDSHHCSDTQNQLDC-VFCALKTIFN----NTTDSHVPPDALRSALS 144
Cdd:pfam00443   1 TGLVNLG--NTCYMNSVLQSLFSIPPFRDYL-LRISPLSEDSRYNKDInLLCALRDLFKalqkNSKSSSVSPKMFKKSLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  145 SVYKSssrFQLGDMNDAVECLEAIQSTIHSQVVGdqvkddhyDSCTAPTCPVHSVFALRVSEHVKCSSCGAQSKDFEFEK 224
Cdd:pfam00443  78 KLNPD---FSGYKQQDAQEFLLFLLDGLHEDLNG--------NHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  225 SIHYVAVEALAEQVHHerkrrrktntyrlsiiapntkdappangnpraslssgsagnvedepwpagwekveapegklyfh 304
Cdd:pfam00443 147 DLSLPIPGDSAELKTA---------------------------------------------------------------- 162
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  305 dhnskitywtdprlrvraglphgwdfsttetgemyyvdhvtkgsawtpplatrsiqatlHECIPPVALDHLLNAVNESDV 384
Cdd:pfam00443 163 -----------------------------------------------------------SLQICFLQFSKLEELDDEEKY 183
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  385 RSCQKTCGTVNTIVPTLHSAPSVFalalvwgstrpqselisevlellapaldlatVFHRTRPT---EPKAKRRWSLADPD 461
Cdd:pfam00443 184 YCDKCGCKQDAIKQLKISRLPPVL-------------------------------IIHLKRFSynrSTWEKLNTEVEFPL 232
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  462 nRLNADAFAAKDALP-------MSLTGLVCYYG----KHYIAFFYNPRDRMWMMYDDATVKPVGPTWASLiakckasKFQ 530
Cdd:pfam00443 233 -ELDLSRYLAEELKPktnnlqdYRLVAVVVHSGslssGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVL-------SSS 304

                  ....*.
gi 470322789  531 PAVLLY 536
Cdd:pfam00443 305 AYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
70-218 7.10e-12

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239125 [Multi-domain]  Cd Length: 328  Bit Score: 67.78  E-value: 7.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  70 RGLTN--ATgdnhCFMNGVVQLLWHLAPFRDAFAAvDSHHC-SDTQNQLDCVFCALKTIFNN-TTDSHVPPDALRSALSS 145
Cdd:cd02660    1 RGLINlgAT----CFMNVILQALLHNPLLRNYFLS-DRHSCtCLSCSPNSCLSCAMDEIFQEfYYSGDRSPYGPINLLYL 75
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 470322789 146 VYKSSSRFQLGDMNDAVECLEAIQSTIHSQVVGDQVKDDHYDSCtapTCPVHSVFALRVSEHVKCSSCGAQSK 218
Cdd:cd02660   76 SWKHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHC---NCIIHQTFSGSLQSSVTCQRCGGVST 145
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
288-318 3.92e-08

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 49.83  E-value: 3.92e-08
                         10        20        30
                 ....*....|....*....|....*....|.
gi 470322789 288 PAGWEKVEAPEGKLYFHDHNSKITYWTDPRL 318
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
288-318 3.53e-07

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 47.21  E-value: 3.53e-07
                           10        20        30
                   ....*....|....*....|....*....|.
gi 470322789   288 PAGWEKVEAPEGKLYFHDHNSKITYWTDPRL 318
Cdd:smart00456   3 PPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
288-316 3.76e-07

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 47.11  E-value: 3.76e-07
                          10        20
                  ....*....|....*....|....*....
gi 470322789  288 PAGWEKVEAPEGKLYFHDHNSKITYWTDP 316
Cdd:pfam00397   2 PPGWEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
324-353 5.41e-05

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 40.95  E-value: 5.41e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 470322789  324 LPHGWDFSTTETGEMYYVDHVTKGSAWTPP 353
Cdd:pfam00397   1 LPPGWEERWDPDGRVYYYNHETGETQWEKP 30
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
478-537 8.55e-05

Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239072 [Multi-domain]  Cd Length: 255  Bit Score: 45.17  E-value: 8.55e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470322789 478 SLTGLVCYYGK-----HYIAFFYNPRDRMWMMYDDATVKPVGPtwaSLIAKCKASKFQPAVLLYQ 537
Cdd:cd02257  194 ELVAVVVHSGTsadsgHYVAYVKDPSDGKWYKFNDDKVTEVSE---EEVLEFGSLSSSAYILFYE 255
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-210 1.52e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239122 [Multi-domain]  Cd Length: 305  Bit Score: 45.01  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  71 GLTNAtgDNHCFMNGVVQLLWHLAPFRDAFAAVDSHHCSDTQNqLDCVFCALKTIFNN--TTDSHVPPDALRSALSSVYK 148
Cdd:cd02657    1 GLTNL--GNTCYLNSTLQCLRSVPELRDALKNYNPARRGANQS-SDNLTNALRDLFDTmdKKQEPVPPIEFLQLLRMAFP 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470322789 149 SSSRFQLGDM---NDAVECLEAIQSTIHSQVVGDQVKDDHYDsctaptcpvhSVFALRVSEHVKC 210
Cdd:cd02657   78 QFAEKQNQGGyaqQDAEECWSQLLSVLSQKLPGAGSKGSFID----------QLFGIELETKMKC 132
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
776-929 2.26e-04

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 41.38  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789   776 REGSLFLKERKHliKSAWKERRFSLRGPYLTFVKPNKVDSIKVVDHldkcvllVIDqshtrLSGSSglesVRDRSKPAAA 855
Cdd:smart00233   3 KEGWLYKKSGGG--KKSWKKRYFVLFNSTLLYYKSKKDKKSYKPKG-------SID-----LSGCT----VREAPDPDSS 64
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 470322789   856 DAslsrspsaassassasvlsrassnerigtvngkkaatptPFYFQLRHP-KMLYELCAASEEDMQQWLLMLERA 929
Cdd:smart00233  65 KK---------------------------------------PHCFEIKTSdRKTLLLQAESEEEREKWVEALRKA 100
PH pfam00169
PH domain; PH stands for pleckstrin homology.
776-929 7.03e-04

PH domain; PH stands for pleckstrin homology.


Pssm-ID: 459697 [Multi-domain]  Cd Length: 105  Bit Score: 40.24  E-value: 7.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  776 REGslFLKERKHLIKSAWKERRFSLRGPYLTFVKPNKVDSikvvdhldkcvllvidqsHTRLSGSSGLESVRDRSKPAAA 855
Cdd:pfam00169   3 KEG--WLLKKGGGKKKSWKKRYFVLFDGSLLYYKDDKSGK------------------SKEPKGSISLSGCEVVEVVASD 62
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 470322789  856 DaslsrspsaassassasvlsrassnerigtvngkkaaTPTPFYFQLRHPKM----LYELCAASEEDMQQWLLMLERA 929
Cdd:pfam00169  63 S-------------------------------------PKRKFCFELRTGERtgkrTYLLQAESEEERKDWIKAIQSA 103
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
323-353 2.64e-03

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 36.42  E-value: 2.64e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 470322789   323 GLPHGWDFSTTETGEMYYVDHVTKGSAWTPP 353
Cdd:smart00456   1 PLPPGWEERKDPDGRPYYYNHETKETQWEKP 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
325-353 3.63e-03

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 35.97  E-value: 3.63e-03
                         10        20
                 ....*....|....*....|....*....
gi 470322789 325 PHGWDFSTTETGEMYYVDHVTKGSAWTPP 353
Cdd:cd00201    1 PPGWEERWDPDGRVYYYNHNTKETQWEDP 29
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
71-175 4.89e-03

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.


Pssm-ID: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 40.38  E-value: 4.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 470322789  71 GLTNATGDNHCfmNGVVQLLWHLAPFRDAFAAVD-SHHCSDTQNQLDCVFCAL-KTIFN-NTTDSHVPPDALRSALSSVy 147
Cdd:cd02669  121 GLNNIKNNDYA--NVIIQALSHVKPIRNFFLLYEnYENIKDRKSELVKRLSELiRKIWNpRNFKGHVSPHELLQAVSKV- 197
                         90       100
                 ....*....|....*....|....*...
gi 470322789 148 kSSSRFQLGDMNDAVECLEAIQSTIHSQ 175
Cdd:cd02669  198 -SKKKFSITEQSDPVEFLSWLLNTLHKD 224
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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