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Conserved domains on  [gi|28571791|ref|NP_650948|]
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ubiquitin specific protease 8, isoform A [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 564-887 2.76e-98

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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 306.52  E-value: 2.76e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCLSNtpqlteycisdkyknyisrsnktngqvieevaalikelwngqykcvasrdlryvvgqyqk 643
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 644 ifrgvDQQDSHEFLTILMDWLHSdlqtlhvprqremisasekawleftkakesMILHLFYGQMKSTVKCVACHKESATYE 723
Cdd:cd02674  21 -----DQQDAQEFLLFLLDGLHS------------------------------IIVDLFQGQLKSRLTCLTCGKTSTTFE 65

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 724 SFSNLSLELPPNS---NVCQLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADPsnsGS 797
Cdd:cd02674  66 PFTYLSLPIPSGSgdaPKVTLEDCLRLFTKEETLDGDNawkCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR---GS 142

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 798 YMKKQNYLRFPLENLDMNPYIAraESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNVV 877
Cdd:cd02674 143 TRKLTTPVTFPLNDLDLTPYVD--TRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVV 220

                       330
                ....*....|
gi 28571791 878 SSAAYILFYT 887
Cdd:cd02674 221 SSSAYILFYE 230
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 2-114 1.50e-43

USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.


:

Pssm-ID: 462647  Cd Length: 113  Bit Score: 153.22  E-value: 1.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791     2 AKLKKLHMSSNLDDLEKMS-IIPDLRSKGMKILLNTARKLYMTAEEYRLDGDEELAYITYMKYFNMLTAIHKKSDYPSHK 80
Cdd:pfam08969   1 APLKPLHLSSSLEDLEKLTeKLEVDKNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 28571791    81 TTVRQMLGDTESNRRiMDTLEEIINSLRHRYAQQ 114
Cdd:pfam08969  81 ATVRQMLGKTKINEV-LDELEKLKTSLLERYEEE 113
RHOD super family cl00125
Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese ...
 148-278 3.30e-06

Rhodanese Homology Domain (RHOD); an alpha beta fold domain found duplicated in the rhodanese protein. The cysteine containing enzymatically active version of the domain is also found in the Cdc25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and certain stress proteins such as senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions (no active site cysteine) are also seen in dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases, where they are believed to play a regulatory role in multidomain proteins.


The actual alignment was detected with superfamily member cd01446:

Pssm-ID: 444705 [Multi-domain]  Cd Length: 132  Bit Score: 47.28  E-value: 3.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 148 LITCQDLYRRMQE--KSVLVMDCRPSADYEASHLtyYCAFNVP------------EELITPGMSAGRLQARLSSSAkasw 213
Cdd:cd01446   1 TIDCAWLAALLREggERLLLLDCRPFLEYSSSHI--RGAVNVCcptilrrrlqggKILLQQLLSCPEDRDRLRRGE---- 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571791 214 asrsvKDSVVLMDWNTKDaqPATNTAISTLLDILKNWDPDVTYRAPIQIVEGGYEYFIMMYPTHC 278
Cdd:cd01446  75 -----SLAVVVYDESSSD--RERLREDSTAESVLGKLLRKLQEGCSVYLLKGGFEQFSSEFPELC 132
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 361-511 4.46e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 4.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 361 LQRAEQNDEQLEKASKMWKRQAAEGDglnaTEDQELHFRILQLESKAQDYIVENNRLREELSRIQELHNVTQQLSQkevE 440
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELE----AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---E 313

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28571791 441 ATRNIESKIRERQRLDEQHELERQERERLLAIARETKKHYKSPTPSGPPSPGRNLEDVHVVSDSLESLLQL 511
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 564-887 2.76e-98

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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 306.52  E-value: 2.76e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCLSNtpqlteycisdkyknyisrsnktngqvieevaalikelwngqykcvasrdlryvvgqyqk 643
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 644 ifrgvDQQDSHEFLTILMDWLHSdlqtlhvprqremisasekawleftkakesMILHLFYGQMKSTVKCVACHKESATYE 723
Cdd:cd02674  21 -----DQQDAQEFLLFLLDGLHS------------------------------IIVDLFQGQLKSRLTCLTCGKTSTTFE 65

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 724 SFSNLSLELPPNS---NVCQLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADPsnsGS 797
Cdd:cd02674  66 PFTYLSLPIPSGSgdaPKVTLEDCLRLFTKEETLDGDNawkCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR---GS 142

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 798 YMKKQNYLRFPLENLDMNPYIAraESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNVV 877
Cdd:cd02674 143 TRKLTTPVTFPLNDLDLTPYVD--TRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVV 220

                       330
                ....*....|
gi 28571791 878 SSAAYILFYT 887
Cdd:cd02674 221 SSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
563-886 5.97e-94

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 298.59  E-value: 5.97e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   563 TGLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYISRSNKtNGQVIEEVAALIKELW-NGQYKCVASRDLRYVVGQY 641
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK-DINLLCALRDLFKALQkNSKSSSVSPKMFKKSLGKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   642 QKIFRGVDQQDSHEFLTILMDWLHSDLQTLHvprqremisasekawlefTKAKESMILHLFYGQMKSTVKCVACHKESAT 721
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGNH------------------STENESLITDLFRGQLKSRLKCLSCGEVSET 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   722 YESFSNLSLELPPNSNV---CQLNQCMDMYFSGERIHG---WNCPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADpsns 795
Cdd:pfam00443 142 FEPFSDLSLPIPGDSAElktASLQICFLQFSKLEELDDeekYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN---- 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   796 GSYMKKQN-YLRFPLEnLDMNPYIAR-AESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDS 873
Cdd:pfam00443 218 RSTWEKLNtEVEFPLE-LDLSRYLAEeLKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDE 296

                         330
                  ....*....|....
gi 28571791   874 SNVV-SSAAYILFY 886
Cdd:pfam00443 297 ETAVlSSSAYILFY 310
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
561-886 1.24e-46

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 179.69  E-value: 1.24e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 561 GLTGLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYISRSNK--TNGQVIEEVAALIKELWNGQYKCVASRDLRYVV 638
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPlgMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 639 GQYQKIFRGVDQQDSHEFLTILMDWLHSDLQTLHVPRQREMISAS-----------EKAWLEFTKAKESMILHLFYGQMK 707
Cdd:COG5560 344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSpgddvvvkkkaKECWWEHLKRNDSIITDLFQGMYK 423

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 708 STVKCVACHKESATYESFSNLSLELP-------------PNSN-----------------------VCQLNQC-----MD 746
Cdd:COG5560 424 STLTCPGCGSVSITFDPFMDLTLPLPvsmvwkhtivvfpESGRrqplkieldasstirglkklvdaEYGKLGCfeikvMC 503

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 747 MYFSGER----------------------------------IHGWNCPSCKTKRD------------------------- 767
Cdd:COG5560 504 IYYGGNYnmlepadkvllqdipqtdfvylyetndngievpvVHLRIEKGYKSKRLfgdpflqlnvlikasiydklvkefe 583

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 768 ------AIKKLD-------------------------------------------------------------------- 773
Cdd:COG5560 584 ellvlvEMKKTDvdlvseqvrllreesspsswlkleteidtkreeqveeegqmnfndavvisceweekrylslfsydplw 663

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 774 -------------------------------------------------ISKLPPVLVVHLKRFYADPSNSgsyMKKQNY 804
Cdd:COG5560 664 tireigaaertitlqdclnefskpeqlglsdswycpgckefrqaskqmeLWRLPMILIIHLKRFSSVRSFR---DKIDDL 740

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 805 LRFPLENLDMNPYIARAESRAVtpkTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNVVSSAAYIL 884
Cdd:COG5560 741 VEYPIDDLDLSGVEYMVDDPRL---IYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVL 817


                ..
gi 28571791 885 FY 886
Cdd:COG5560 818 FY 819
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 2-114 1.50e-43

USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.


Pssm-ID: 462647  Cd Length: 113  Bit Score: 153.22  E-value: 1.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791     2 AKLKKLHMSSNLDDLEKMS-IIPDLRSKGMKILLNTARKLYMTAEEYRLDGDEELAYITYMKYFNMLTAIHKKSDYPSHK 80
Cdd:pfam08969   1 APLKPLHLSSSLEDLEKLTeKLEVDKNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 28571791    81 TTVRQMLGDTESNRRiMDTLEEIINSLRHRYAQQ 114
Cdd:pfam08969  81 ATVRQMLGKTKINEV-LDELEKLKTSLLERYEEE 113
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 148-278 3.30e-06

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 47.28  E-value: 3.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 148 LITCQDLYRRMQE--KSVLVMDCRPSADYEASHLtyYCAFNVP------------EELITPGMSAGRLQARLSSSAkasw 213
Cdd:cd01446   1 TIDCAWLAALLREggERLLLLDCRPFLEYSSSHI--RGAVNVCcptilrrrlqggKILLQQLLSCPEDRDRLRRGE---- 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571791 214 asrsvKDSVVLMDWNTKDaqPATNTAISTLLDILKNWDPDVTYRAPIQIVEGGYEYFIMMYPTHC 278
Cdd:cd01446  75 -----SLAVVVYDESSSD--RERLREDSTAESVLGKLLRKLQEGCSVYLLKGGFEQFSSEFPELC 132
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 361-511 4.46e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 4.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 361 LQRAEQNDEQLEKASKMWKRQAAEGDglnaTEDQELHFRILQLESKAQDYIVENNRLREELSRIQELHNVTQQLSQkevE 440
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELE----AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---E 313

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28571791 441 ATRNIESKIRERQRLDEQHELERQERERLLAIARETKKHYKSPTPSGPPSPGRNLEDVHVVSDSLESLLQL 511
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 352-475 8.78e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.27  E-value: 8.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   352 EIMRDQAEflqraEQNDEQLEKASKMWKRQAAEgdglnatedqELHFRILQLESKA-QDYIVENNRLREELSR-IQELHN 429
Cdd:pfam17380 463 ERLRQQEE-----ERKRKKLELEKEKRDRKRAE----------EQRRKILEKELEErKQAMIEEERKRKLLEKeMEERQK 527

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 28571791   430 -VTQQLSQKEVEATRNIESKIRERQRLDEQHELERQERERLLAIARE 475
Cdd:pfam17380 528 aIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERE 574
mukB PRK04863
chromosome partition protein MukB;
351-473 2.33e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.95  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   351 AEIMRDQAEFLQR-AEQNDEQLEKASKMwKRQAAEGDGLNATEDQELHFRILQLESKAQDYIVEN---NRLRE----ELS 422
Cdd:PRK04863  546 LGKNLDDEDELEQlQEELEARLESLSES-VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQdalARLREqsgeEFE 624

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 28571791   423 RIQELHNVTQQLSQKEVEATRNIESKIRERQRLDEQ-HEL---ERQERERLLAIA 473
Cdd:PRK04863  625 DSQDVTEYMQQLLERERELTVERDELAARKQALDEEiERLsqpGGSEDPRLNALA 679
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 358-480 6.35e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 6.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791    358 AEFLQRAEQNDEQLEKASKMWKRQAAEGDGLNAtEDQELHFRILQLESKAQDYiveNNRLREELSRIQELHNVTQQLSQK 437
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRA-ELTLLNEEAANLRERLESL---ERRIAATERRLEDLEEQIEELSED 853

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 28571791    438 EVEATRNIESKIRERQRLDEQHELERQERERLLAIARETKKHY 480
Cdd:TIGR02168  854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
 
Name Accession Description Interval E-value
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 564-887 2.76e-98

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: 239139 [Multi-domain]  Cd Length: 230  Bit Score: 306.52  E-value: 2.76e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCLSNtpqlteycisdkyknyisrsnktngqvieevaalikelwngqykcvasrdlryvvgqyqk 643
Cdd:cd02674   1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 644 ifrgvDQQDSHEFLTILMDWLHSdlqtlhvprqremisasekawleftkakesMILHLFYGQMKSTVKCVACHKESATYE 723
Cdd:cd02674  21 -----DQQDAQEFLLFLLDGLHS------------------------------IIVDLFQGQLKSRLTCLTCGKTSTTFE 65

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 724 SFSNLSLELPPNS---NVCQLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADPsnsGS 797
Cdd:cd02674  66 PFTYLSLPIPSGSgdaPKVTLEDCLRLFTKEETLDGDNawkCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFSR---GS 142

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 798 YMKKQNYLRFPLENLDMNPYIAraESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNVV 877
Cdd:cd02674 143 TRKLTTPVTFPLNDLDLTPYVD--TRSFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVSESSVV 220

                       330
                ....*....|
gi 28571791 878 SSAAYILFYT 887
Cdd:cd02674 221 SSSAYILFYE 230
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
563-886 5.97e-94

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 298.59  E-value: 5.97e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   563 TGLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYISRSNKtNGQVIEEVAALIKELW-NGQYKCVASRDLRYVVGQY 641
Cdd:pfam00443   1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNK-DINLLCALRDLFKALQkNSKSSSVSPKMFKKSLGKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   642 QKIFRGVDQQDSHEFLTILMDWLHSDLQTLHvprqremisasekawlefTKAKESMILHLFYGQMKSTVKCVACHKESAT 721
Cdd:pfam00443  80 NPDFSGYKQQDAQEFLLFLLDGLHEDLNGNH------------------STENESLITDLFRGQLKSRLKCLSCGEVSET 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   722 YESFSNLSLELPPNSNV---CQLNQCMDMYFSGERIHG---WNCPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADpsns 795
Cdd:pfam00443 142 FEPFSDLSLPIPGDSAElktASLQICFLQFSKLEELDDeekYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN---- 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   796 GSYMKKQN-YLRFPLEnLDMNPYIAR-AESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDS 873
Cdd:pfam00443 218 RSTWEKLNtEVEFPLE-LDLSRYLAEeLKPKTNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDE 296

                         330
                  ....*....|....
gi 28571791   874 SNVV-SSAAYILFY 886
Cdd:pfam00443 297 ETAVlSSSAYILFY 310
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
 564-886 1.72e-72

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: 238.92  E-value: 1.72e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCLSNtpqlteycisdkyknyisrsnktngqvieevaalikelwngqykcvasrdlryvvgqyqk 643
Cdd:cd02257   1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 644 ifrgvDQQDSHEFLTILMDWLHSDLQTLHVPRqremisasekawlEFTKAKESMILHLFYGQMKSTVKCVACHKESATYE 723
Cdd:cd02257  21 -----EQQDAHEFLLFLLDKLHEELKKSSKRT-------------SDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTE 82

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 724 SFSNLSLELPPNSNVCQ-LNQCMDMYFSGERIHGWNCPSC--KTKRDAIKKLDISKLPPVLVVHLKRFYADpsNSGSYMK 800
Cdd:cd02257  83 PELFLSLPLPVKGLPQVsLEDCLEKFFKEEILEGDNCYKCekKKKQEATKRLKIKKLPPVLIIHLKRFSFN--EDGTKEK 160

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 801 KQNYLRFPLEnLDMNPYIARAESRAVT---PKTYQLYAVSNHYGT-MEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNV 876
Cdd:cd02257 161 LNTKVSFPLE-LDLSPYLSEGEKDSDSdngSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEV 239

                       330
                ....*....|....*
gi 28571791 877 V-----SSAAYILFY 886
Cdd:cd02257 240 LefgslSSSAYILFY 254
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 564-887 1.09e-62

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: 214.93  E-value: 1.09e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYkNYISRSNKTNGQVIEEVAALIKELW----NGQYKCVAsrdLRYVVG 639
Cdd:cd02660   2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRH-SCTCLSCSPNSCLSCAMDEIFQEFYysgdRSPYGPIN---LLYLSW 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 640 QYQKIFRGVDQQDSHEFLTILMDWLHSDLQTLHVPRQREMISasekawleftkakeSMILH-LFYGQMKSTVKCVACHKE 718
Cdd:cd02660  78 KHSRNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHC--------------NCIIHqTFSGSLQSSVTCQRCGGV 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 719 SATYESFSNLSLELPPNSNVCQ------------LNQCMDMYFSGERI--HGWNCPSCKTKRDAIKKLDISKLPPVLVVH 784
Cdd:cd02660 144 STTVDPFLDLSLDIPNKSTPSWalgesgvsgtptLSDCLDRFTRPEKLgdFAYKCSGCGSTQEATKQLSIKKLPPVLCFQ 223

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 785 LKRFyaDPSNSGSYMKKQNYLRFPLEnLDMNPYIARA------ESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANyG 858
Cdd:cd02660 224 LKRF--EHSLNKTSRKIDTYVQFPLE-LNMTPYTSSSigdtqdSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGD-G 299

                       330       340
                ....*....|....*....|....*....
gi 28571791 859 KWFKFDDQVVSALDSSNVVSSAAYILFYT 887
Cdd:cd02660 300 QWFKFDDAMITRVSEEEVLKSQAYLLFYH 328
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 563-886 1.22e-62

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: 239126 [Multi-domain]  Cd Length: 304  Bit Score: 214.06  E-value: 1.22e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 563 TGLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYISRSNKTNGQVIEEVAALIkeLWNGQYKcVASRDLRYVVGQYQ 642
Cdd:cd02661   2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERA--LASSGPG-SAPRIFSSNLKQIS 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 643 KIFRGVDQQDSHEFLTILMDWLHS------DLQTLHVPRQREMisasekawleftkakeSMILHLFYGQMKSTVKCVACH 716
Cdd:cd02661  79 KHFRIGRQEDAHEFLRYLLDAMQKacldrfKKLKAVDPSSQET----------------TLVQQIFGGYLRSQVKCLNCK 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 717 KESATYESFSNLSLELPpnsNVCQLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFyadps 793
Cdd:cd02661 143 HVSNTYDPFLDLSLDIK---GADSLEDALEQFTKPEQLDGENkykCERCKKKVKASKQLTIHRAPNVLTIHLKRF----- 214

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 794 nSGSYMKKQN-YLRFPlENLDMNPYIARAESravTPKTYQLYAVSNHYGT-MEGGHYTAFCKSANyGKWFKFDDQVVSAL 871
Cdd:cd02661 215 -SNFRGGKINkQISFP-ETLDLSPYMSQPND---GPLKYKLYAVLVHSGFsPHSGHYYCYVKSSN-GKWYNMDDSKVSPV 288

                       330
                ....*....|....*
gi 28571791 872 DSSNVVSSAAYILFY 886
Cdd:cd02661 289 SIETVLSQKAYILFY 303
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 564-886 3.23e-51

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: 239132 [Multi-domain]  Cd Length: 279  Bit Score: 181.43  E-value: 3.23e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCLSNTPQLTEycisdkyknyisrsnktngqvieevaaLIKELWNGQYKCVASRDLRyvvgqyqk 643
Cdd:cd02667   1 GLSNLGNTCFFNAVMQNLSQTPALRE---------------------------LLSETPKELFSQVCRKAPQ-------- 45

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 644 iFRGVDQQDSHEFLTILMDWLhsdlqtlhvprqremisasekawleftkakESMILHLFYGQMKSTVKCVACHKESATYE 723
Cdd:cd02667  46 -FKGYQQQDSHELLRYLLDGL------------------------------RTFIDSIFGGELTSTIMCESCGTVSLVYE 94

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 724 SFSNLSL-ELPPNSNVCQLNQCMDMYFSGERIHGWNCPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADPsnSGSYMKKQ 802
Cdd:cd02667  95 PFLDLSLpRSDEIKSECSIESCLKQFTEVEILEGNNKFACENCTKAKKQYLISKLPPVLVIHLKRFQQPR--SANLRKVS 172

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 803 NYLRFPlENLDMNPYI--ARAESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKS---------------------ANYGK 859
Cdd:cd02667 173 RHVSFP-EILDLAPFCdpKCNSSEDKSSVLYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQ 251

                       330       340
                ....*....|....*....|....*..
gi 28571791 860 WFKFDDQVVSALDSSNVVSSAAYILFY 886
Cdd:cd02667 252 WYYISDSDVREVSLEEVLKSEAYLLFY 278
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 561-886 5.51e-48

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: 239124 [Multi-domain]  Cd Length: 334  Bit Score: 173.98  E-value: 5.51e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 561 GLTGLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYisrsNKTNGQVIEEVAALIKELWNGQYKCVASRDLRYVVGQ 640
Cdd:cd02659   1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTED----DDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSF 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 641 YQKIFRGVDQQDSHEFLTILMDWLHSDLQTLhvprqremisasekawleftkAKESMILHLFYGQMKSTVKCVACHKESA 720
Cdd:cd02659  77 GWDSLNTFEQHDVQEFFRVLFDKLEEKLKGT---------------------GQEGLIKNLFGGKLVNYIICKECPHESE 135

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 721 TYESFSNLSLELPPNSNvcqLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADPsNSGS 797
Cdd:cd02659 136 REEYFLDLQVAVKGKKN---LEESLDAYVQGETLEGDNkyfCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEFDF-ETMM 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 798 YMKKQNYLRFPLEnLDMNPYIARAESRAVTPKT--------YQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVS 869
Cdd:cd02659 212 RIKINDRFEFPLE-LDMEPYTEKGLAKKEGDSEkkdsesyiYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVT 290

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 28571791 870 ALDSSNVV----------------------SSAAYILFY 886
Cdd:cd02659 291 PFDPNDAEeecfggeetqktydsgprafkrTTNAYMLFY 329
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
561-886 1.24e-46

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 179.69  E-value: 1.24e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 561 GLTGLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYISRSNK--TNGQVIEEVAALIKELWNGQYKCVASRDLRYVV 638
Cdd:COG5560 264 GTCGLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPlgMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTI 343

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 639 GQYQKIFRGVDQQDSHEFLTILMDWLHSDLQTLHVPRQREMISAS-----------EKAWLEFTKAKESMILHLFYGQMK 707
Cdd:COG5560 344 GSFNEEFSGYDQQDSQEFIAFLLDGLHEDLNRIIKKPYTSKPDLSpgddvvvkkkaKECWWEHLKRNDSIITDLFQGMYK 423

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 708 STVKCVACHKESATYESFSNLSLELP-------------PNSN-----------------------VCQLNQC-----MD 746
Cdd:COG5560 424 STLTCPGCGSVSITFDPFMDLTLPLPvsmvwkhtivvfpESGRrqplkieldasstirglkklvdaEYGKLGCfeikvMC 503

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 747 MYFSGER----------------------------------IHGWNCPSCKTKRD------------------------- 767
Cdd:COG5560 504 IYYGGNYnmlepadkvllqdipqtdfvylyetndngievpvVHLRIEKGYKSKRLfgdpflqlnvlikasiydklvkefe 583

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 768 ------AIKKLD-------------------------------------------------------------------- 773
Cdd:COG5560 584 ellvlvEMKKTDvdlvseqvrllreesspsswlkleteidtkreeqveeegqmnfndavvisceweekrylslfsydplw 663

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 774 -------------------------------------------------ISKLPPVLVVHLKRFYADPSNSgsyMKKQNY 804
Cdd:COG5560 664 tireigaaertitlqdclnefskpeqlglsdswycpgckefrqaskqmeLWRLPMILIIHLKRFSSVRSFR---DKIDDL 740

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 805 LRFPLENLDMNPYIARAESRAVtpkTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNVVSSAAYIL 884
Cdd:COG5560 741 VEYPIDDLDLSGVEYMVDDPRL---IYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVL 817


                ..
gi 28571791 885 FY 886
Cdd:COG5560 818 FY 819
USP8_dimer pfam08969
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ...
 2-114 1.50e-43

USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.


Pssm-ID: 462647  Cd Length: 113  Bit Score: 153.22  E-value: 1.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791     2 AKLKKLHMSSNLDDLEKMS-IIPDLRSKGMKILLNTARKLYMTAEEYRLDGDEELAYITYMKYFNMLTAIHKKSDYPSHK 80
Cdd:pfam08969   1 APLKPLHLSSSLEDLEKLTeKLEVDKNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 28571791    81 TTVRQMLGDTESNRRiMDTLEEIINSLRHRYAQQ 114
Cdd:pfam08969  81 ATVRQMLGKTKINEV-LDELEKLKTSLLERYEEE 113
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 564-887 5.34e-43

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: 239128 [Multi-domain]  Cd Length: 300  Bit Score: 158.63  E-value: 5.34e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCLSNTPQLTeyCISDKYKnYISRSNKTNGQVieevaalikelwngqykcvASRDLRYVVGQYQK 643
Cdd:cd02663   1 GLENFGNTCYCNSVLQALYFENLLT--CLKDLFE-SISEQKKRTGVI-------------------SPKKFITRLKRENE 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 644 IFRGVDQQDSHEFLTILMDWLHSDLQtlhvpRQREMISASEKAWLEFTKAKESMILH-LFYGQMKSTVKCVACHKESATY 722
Cdd:cd02663  59 LFDNYMHQDAHEFLNFLLNEIAEILD-----AERKAEKANRKLNNNNNAEPQPTWVHeIFQGILTNETRCLTCETVSSRD 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 723 ESFSNLSLELPPNSNVcqlNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADpSNSGSYM 799
Cdd:cd02663 134 ETFLDLSIDVEQNTSI---TSCLRQFSATETLCGRNkfyCDECCSLQEAEKRMKIKKLPKILALHLKRFKYD-EQLNRYI 209

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 800 KKQNYLRFPLEnLDMNPYIARAESravTPKTYQLYAVSNHYG-TMEGGHYTAFCKSAnyGKWFKFDDQVVSALDSSNVV- 877
Cdd:cd02663 210 KLFYRVVFPLE-LRLFNTTDDAEN---PDRLYELVAVVVHIGgGPNHGHYVSIVKSH--GGWLLFDDETVEKIDENAVEe 283

                       330
                ....*....|....*..
gi 28571791 878 -------SSAAYILFYT 887
Cdd:cd02663 284 ffgdspnQATAYVLFYQ 300
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 564-887 2.59e-40

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: 239133 [Multi-domain]  Cd Length: 324  Bit Score: 151.42  E-value: 2.59e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCL-SNTP-QLTEY---CISDKYKNYISRSNKTNGQ-VIEEVAALIKELWNGQYKCVAS----RD 633
Cdd:cd02668   1 GLKNLGATCYVNSFLQLWfMNLEfRKAVYecnSTEDAELKNMPPDKPHEPQtIIDQLQLIFAQLQFGNRSVVDPsgfvKA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 634 LRYVVGQyqkifrgvdQQDSHEFLTILMDWLHSDLQTLHVPrqremisasekawleftKAKeSMILHLFYGQMKSTVKCV 713
Cdd:cd02668  81 LGLDTGQ---------QQDAQEFSKLFLSLLEAKLSKSKNP-----------------DLK-NIVQDLFRGEYSYVTQCS 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 714 ACHKESATYESFSNLSLELPPNSnvcQLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFYA 790
Cdd:cd02668 134 KCGRESSLPSKFYELELQLKGHK---TLEECIDEFLKEEQLTGDNqyfCESCNSKTDATRRIRLTTLPPTLNFQLLRFVF 210

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 791 DpSNSGSYMKKQNYLRFPlENLDMNPYIARAESRAvtpKTYQLYAVSNHYGT-MEGGHYTAFCKSANYGKWFKFDDQVVS 869
Cdd:cd02668 211 D-RKTGAKKKLNASISFP-EILDMGEYLAESDEGS---YVYELSGVLIHQGVsAYSGHYIAHIKDEQTGEWYKFNDEDVE 285

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 28571791 870 ALDSSNV---------------------VSSAAYILFYT 887
Cdd:cd02668 286 EMPGKPLklgnsedpakprkseikkgthSSRTAYMLVYK 324
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 564-886 1.56e-38

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: 239127 [Multi-domain]  Cd Length: 240  Bit Score: 143.66  E-value: 1.56e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCLSNTPQLTEYcisdkyknyisrsnktngqvIEEVaalikelwngqykcvasrdlryvvgqyqk 643
Cdd:cd02662   1 GLVNLGNTCFMNSVLQALASLPSLIEY--------------------LEEF----------------------------- 31

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 644 ifrgVDQQDSHEFLTILMDWLHSDLQtlhvprqremisasekawleftkakesmilHLFYGQMKSTVKCVAC-HKESATY 722
Cdd:cd02662  32 ----LEQQDAHELFQVLLETLEQLLK------------------------------FPFDGLLASRIVCLQCgESSKVRY 77

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 723 ESFSNLSLELPPNSNV--CQLNQCMDMYFSGERIHGWNCPSCKTKrdaikkldISKLPPVLVVHLKRFYADPSnsGSYMK 800
Cdd:cd02662  78 ESFTMLSLPVPNQSSGsgTTLEHCLDDFLSTEIIDDYKCDRCQTV--------IVRLPQILCIHLSRSVFDGR--GTSTK 147

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 801 KQNYLRFPLEnldmnpyiaraesraVTPKTYQLYAVSNHYGTMEGGHYTAF--------------------CKSANYGKW 860
Cdd:cd02662 148 NSCKVSFPER---------------LPKVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPW 212

                       330       340
                ....*....|....*....|....*..
gi 28571791 861 FKFDDQVVSALDSSNVV-SSAAYILFY 886
Cdd:cd02662 213 WRISDTTVKEVSESEVLeQKSAYMLFY 239
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 564-886 3.53e-32

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: 239123 [Multi-domain]  Cd Length: 311  Bit Score: 127.44  E-value: 3.53e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCLSNTPQLTEYCISDKYKNYISRSNKTNGQVIeEVAALIKELWNGQYKCVASRD---------- 633
Cdd:cd02658   1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDPANDLNC-QLIKLADGLLSGRYSKPASLKsendpyqvgi 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 634 ----LRYVVGQYQKIFRGVDQQDSHEFLTILMDWLHSDLQTLHVprqremisasekawLEFTKakesmilhLFYGQMKST 709
Cdd:cd02658  80 kpsmFKALIGKGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLG--------------LNPND--------LFKFMIEDR 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 710 VKCVACHKESATYESFSNLSLELP--PNSNVCQ---------LNQCMDMYFSGERIHGwNCPSCKTKRDAIKKLDISKLP 778
Cdd:cd02658 138 LECLSCKKVKYTSELSEILSLPVPkdEATEKEEgelvyepvpLEDCLKAYFAPETIED-FCSTCKEKTTATKTTGFKTFP 216

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 779 PVLVVHLKRFYAdpsNSGSYMKKqnylrfplenLDMnpYIARAESRAvtPKTYQLYAVSNHYGT-MEGGHYTAFCK--SA 855
Cdd:cd02658 217 DYLVINMKRFQL---LENWVPKK----------LDV--PIDVPEELG--PGKYELIAFISHKGTsVHSGHYVAHIKkeID 279

                       330       340       350
                ....*....|....*....|....*....|.
gi 28571791 856 NYGKWFKFDDQVVSALDSSNVVSSAAYILFY 886
Cdd:cd02658 280 GEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 564-886 2.80e-31

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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 125.30  E-value: 2.80e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCLSNTPQlteycisdkYKNYISRSNKTNGQviEEVAALIKELW--------NGQYKCVASRDLR 635
Cdd:cd02664   1 GLINLGNTCYMNSVLQALFMAKD---------FRRQVLSLNLPRLG--DSQSVMKKLQLlqahlmhtQRRAEAPPDYFLE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 636 YVVGQYqkiFRGVDQQDSHEFLTILMDWLHSdlqtlhvprqremisasekawleftkakesMILHLFYGQMKSTVKCVAC 715
Cdd:cd02664  70 ASRPPW---FTPGSQQDCSEYLRYLLDRLHT------------------------------LIEKMFGGKLSTTIRCLNC 116

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 716 HKESATYESFSNLSLelppnsNVCQLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVLVVHLKRFYADP 792
Cdd:cd02664 117 NSTSARTERFRDLDL------SFPSVQDLLNYFLSPEKLTGDNqyyCEKCASLQDAEKEMKVTGAPEYLILTLLRFSYDQ 190

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 793 SnSGSYMKKQNYLRFPlENLDMNPYIARAESRAVTPKT----------------YQLYAVSNHYGT-MEGGHYtaFCKSA 855
Cdd:cd02664 191 K-THVREKIMDNVSIN-EVLSLPVRVESKSSESPLEKKeeesgddgelvtrqvhYRLYAVVVHSGYsSESGHY--FTYAR 266

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 856 N----------------------YGKWFKFDDQVVSALDSS---NVVS----SAAYILFY 886
Cdd:cd02664 267 DqtdadstgqecpepkdaeendeSKNWYLFNDSRVTFSSFEsvqNVTSrfpkDTPYILFY 326
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
 561-869 7.28e-30

Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 127.68  E-value: 7.28e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791  561 GLTGLKNLGNTCYMNSILQCLSNTpqlteycisDKYKNYISRSNKTNGQVIEEVA-ALIKELWNGQYKCVASRDLRYVVG 639
Cdd:COG5077  192 GYVGLRNQGATCYMNSLLQSLFFI---------AKFRKDVYGIPTDHPRGRDSVAlALQRLFYNLQTGEEPVDTTELTRS 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791  640 QYQKIFRGVDQQDSHEFLTILMDWLHSDLQTLHVprqremisasekawleftkakESMILHLFYGQMKSTVKCVACHKES 719
Cdd:COG5077  263 FGWDSDDSFMQHDIQEFNRVLQDNLEKSMRGTVV---------------------ENALNGIFVGKMKSYIKCVNVNYES 321

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791  720 ATYESFSNLSLELPPNSNvcqLNQCMDMYFSGERIHGWNCPSCKTK--RDAIKKLDISKLPPVLVVHLKRFYADpSNSGS 797
Cdd:COG5077  322 ARVEDFWDIQLNVKGMKN---LQESFRRYIQVETLDGDNRYNAEKHglQDAKKGVIFESLPPVLHLQLKRFEYD-FERDM 397

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 28571791  798 YMKKQNYLRFPLEnLDMNPYIAR-AESRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVS 869
Cdd:COG5077  398 MVKINDRYEFPLE-IDLLPFLDRdADKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVT 469
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 562-886 6.17e-28

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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 115.76  E-value: 6.17e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 562 LTGLKNLGNTCYMNSILQCLSNTPQLTEycisdKYKNYISR-SNKTNGQVIEEvaaLIKELWNGQYKCVASRDLRYVVGQ 640
Cdd:cd02671  24 FVGLNNLGNTCYLNSVLQVLYFCPGFKH-----GLKHLVSLiSSVEQLQSSFL---LNPEKYNDELANQAPRRLLNALRE 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 641 YQKIFRGVDQQDSHEFLTILMDWLhsdlqtlhvprqREMISAsekawleftkakesmilhLFYGQMKSTVKCVACHKESA 720
Cdd:cd02671  96 VNPMYEGYLQHDAQEVLQCILGNI------------QELVEK------------------DFQGQLVLRTRCLECETFTE 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 721 TYESFSNLSLELP----------------PNSNVCQLNQCMDMYFSGERIHGWN---CPSCKTKRDAIKKLDISKLPPVL 781
Cdd:cd02671 146 RREDFQDISVPVQeselskseesseispdPKTEMKTLKWAISQFASVERIVGEDkyfCENCHHYTEAERSLLFDKLPEVI 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 782 VVHLKRFYADPSNSGSY--MKKQNY-----LRFPLENLDMNPyiaraesravTPKTYQLYAVSNHYG-TMEGGHYTAfck 853
Cdd:cd02671 226 TIHLKCFAANGSEFDCYggLSKVNTplltpLKLSLEEWSTKP----------KNDVYRLFAVVMHSGaTISSGHYTA--- 292

                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 28571791 854 sanYGKWFKFDDQVV---------SALDSSNVVSSAAYILFY 886
Cdd:cd02671 293 ---YVRWLLFDDSEVkvteekdflEALSPNTSSTSTPYLLFY 331
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 564-886 2.99e-27

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: 113.19  E-value: 2.99e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCLSNTPQLteyciSDKYKNY---ISRSNKTNGQVIEEVAALIKELWNGQ--------------- 625
Cdd:cd02657   1 GLTNLGNTCYLNSTLQCLRSVPEL-----RDALKNYnpaRRGANQSSDNLTNALRDLFDTMDKKQepvppieflqllrma 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 626 YKCVASRDLRyvvGQYQkifrgvdQQDSHEFLTilmdwlhsdlQTLHVPRQRemisasekawLEFTKAKESMILHLFYGQ 705
Cdd:cd02657  76 FPQFAEKQNQ---GGYA-------QQDAEECWS----------QLLSVLSQK----------LPGAGSKGSFIDQLFGIE 125

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 706 MKSTVKCVAC-HKESATYESFSNLSlelppnsnvCQLNQCMDMYFSGERI-HGWN----CPSCKTKRDAI--KKLDISKL 777
Cdd:cd02657 126 LETKMKCTESpDEEEVSTESEYKLQ---------CHISITTEVNYLQDGLkKGLEeeieKHSPTLGRDAIytKTSRISRL 196

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 778 PPVLVVHLKRFYADPSNSgsymKKQNYLR---FPLEnLDMNPYiaraesraVTPK-TYQLYAVSNHYG-TMEGGHYTAFC 852
Cdd:cd02657 197 PKYLTVQFVRFFWKRDIQ----KKAKILRkvkFPFE-LDLYEL--------CTPSgYYELVAVITHQGrSADSGHYVAWV 263

                       330       340       350       360
                ....*....|....*....|....*....|....*....|.
gi 28571791 853 KSANYGKWFKFDDQVVSALDSSNVVSSA-------AYILFY 886
Cdd:cd02657 264 RRKNDGKWIKFDDDKVSEVTEEDILKLSgggdwhiAYILLY 304
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 527-886 8.51e-25

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: 108.56  E-value: 8.51e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 527 PTFDRAmkpQPRNVERTSQRVRDFSpviGQNVGRGLTGLKNLGNTCYMNSILQCLSNTPQLTEYCIS-DKYKNYISRSnk 605
Cdd:cd02669  90 PTYTKE---QISDLDRDPKLSRDLD---GKPYLPGFVGLNNIKNNDYANVIIQALSHVKPIRNFFLLyENYENIKDRK-- 161

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 606 tnGQVIEEVAALIKELWNGQ-YKCVASRD--LRYVVGQYQKIFRGVDQQDSHEFLTILMDWLHSDLQ--------TLHVP 674
Cdd:cd02669 162 --SELVKRLSELIRKIWNPRnFKGHVSPHelLQAVSKVSKKKFSITEQSDPVEFLSWLLNTLHKDLGgskkpnssIIHDC 239

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 675 RQREMISASEKAWLEFTKAKESMILHLFYGQMKSTVKCvachkesatyesFSNLSLELPPN---------SNVCQLN--Q 743
Cdd:cd02669 240 FQGKVQIETQKIKPHAEEEGSKDKFFKDSRVKKTSVSP------------FLLLTLDLPPPplfkdgneeNIIPQVPlkQ 307

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 744 CMDMYFSgerihgwncPSCKTKRDAIKKLDISKLPPVLVVHLKRFyadPSNSGSYMKKQNYLRFPLENLDMNPYIARAES 823
Cdd:cd02669 308 LLKKYDG---------KTETELKDSLKRYLISRLPKYLIFHIKRF---SKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKP 375

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571791 824 RAVTPKTYQLYAVSNHYGT-MEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNVVSSAAYILFY 886
Cdd:cd02669 376 SLNLSTKYNLVANIVHEGTpQEDGTWRVQLRHKSTNKWFEIQDLNVKEVLPQLIFLSESYIQIW 439
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
564-886 2.12e-23

Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 101.03  E-value: 2.12e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 564 GLKNLGNTCYMNSILQCLS-NTPQLTEYcISDKYKNYISRSNKTNG----QVIEEVAALIKELWNGQYKCVAsrdlryvv 638
Cdd:COG5533   1 GLPNLGNTCFMNSVLQILAlYLPKLDEL-LDDLSKELKVLKNVIRKpepdLNQEEALKLFTALWSSKEHKVG-------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 639 gqyqKIFRGVDQQDSHEFLTILMDWLHSDL----QTLHVPRQREMISASEKAWLEFTKAKesmilhlfygQMKSTVkcva 714
Cdd:COG5533  72 ----WIPPMGSQEDAHELLGKLLDELKLDLvnsfTIRIFKTTKDKKKTSTGDWFDIIIEL----------PDQTWV---- 133

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 715 chKESATYESFSNLSLELPPNSnvCQLNQCMDmyfSGERIhgwncpSCKTKRDAIKKldisKLPPVLVVHLKRFyadpSN 794
Cdd:COG5533 134 --NNLKTLQEFIDNMEELVDDE--TGVKAKEN---EELEV------QAKQEYEVSFV----KLPKILTIQLKRF----AN 192

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 795 SGSYMKKQNYLRfplENLDMNpyIARAESRAVTPKT-YQLYAVSNHYGTMEGGHYTAFCKSAnyGKWFKFDDQVVSALDS 873
Cdd:COG5533 193 LGGNQKIDTEVD---EKFELP--VKHDQILNIVKETyYDLVGFVLHQGSLEGGHYIAYVKKG--GKWEKANDSDVTPVSE 265

                       330
                ....*....|....*.
gi 28571791 874 SNVVSSA---AYILFY 886
Cdd:COG5533 266 EEAINEKaknAYLYFY 281
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 565-886 2.75e-13

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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 70.64  E-value: 2.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 565 LKNLGNTCYMNSILQCLSNtpqlteycisdkyknyisrsnktngqvieevaalikelwngqykcvasrdlryvVGQYQKI 644
Cdd:cd02673   2 LVNTGNSCYFNSTMQALSS------------------------------------------------------IGKINTE 27

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 645 FRGVDQQDSHEFLTIL---MDWLHSDLQTLHVPRQREMISASEKAWLEFTKakESMILhlfygqmkstvkCVACHKESAT 721
Cdd:cd02673  28 FDNDDQQDAHEFLLTLleaIDDIMQVNRTNVPPSNIEIKRLNPLEAFKYTI--ESSYV------------CIGCSFEENV 93

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 722 YESFSNLSLELPPN-SNVCQLNQCMDMYFSG-ERIhgwnCPSCKTKrDAIKKLDISKLPPVLVVHLKRFYADPSNSgSYM 799
Cdd:cd02673  94 SDVGNFLDVSMIDNkLDIDELLISNFKTWSPiEKD----CSSCKCE-SAISSERIMTFPECLSINLKRYKLRIATS-DYL 167

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 800 KKQNYLRFPLENldmnpyiaraesravTPKTYQLYAVSNHYG-TMEGGHYTAFCKS-ANYGKWFKFDDQVVSALDSSNV- 876
Cdd:cd02673 168 KKNEEIMKKYCG---------------TDAKYSLVAVICHLGeSPYDGHYIAYTKElYNGSSWLYCSDDEIRPVSKNDVs 232

                       330
                ....*....|..
gi 28571791 877 --VSSAAYILFY 886
Cdd:cd02673 233 tnARSSGYLIFY 244
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 650-886 1.18e-11

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: 239130 [Multi-domain]  Cd Length: 228  Bit Score: 65.27  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 650 QQDSHEFLTILMDWLHSDLQ-TLHVPRQREmisasekawleftKAKESMIlHLFYGqmKSTVKCVACHKESATYESFSNL 728
Cdd:cd02665  22 QQDVSEFTHLLLDWLEDAFQaAAEAISPGE-------------KSKNPMV-QLFYG--TFLTEGVLEGKPFCNCETFGQY 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 729 SLELPPNSNvcqLNQCMDMYFSGERIHgwNCPSCKTKRDAIKKLdISKLPPVLVVHLKRFYAdpsNSGSYMKKQNYLRFP 808
Cdd:cd02665  86 PLQVNGYGN---LHECLEAAMFEGEVE--LLPSDHSVKSGQERW-FTELPPVLTFELSRFEF---NQGRPEKIHDKLEFP 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 809 lenldmnpyiaraesRAVTPKTYQLYAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNVVSSA-------- 880
Cdd:cd02665 157 ---------------QIIQQVPYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSfgggrnps 221


                ....*.
gi 28571791 881 AYILFY 886
Cdd:cd02665 222 AYCLMY 227
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 563-877 4.08e-09

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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 59.43  E-value: 4.08e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 563 TGLKNLGNTCYMNSILQCL--------------SNTPQLTEYCISDKY--KNYISRSNKTNG-QVIEEVAALIKELWNGQ 625
Cdd:cd02666   2 AGLDNIGNTCYLNSLLQYFftikplrdlvlnfdESKAELASDYPTERRigGREVSRSELQRSnQFVYELRSLFNDLIHSN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 626 YKCVA-SRDLRYVVgqyqkifrgVDQQDSHEFLTILMDWLHSDLqtlhvprqrEMISASE-KAWLEFTKAKESMILHLFY 703
Cdd:cd02666  82 TRSVTpSKELAYLA---------LRQQDVTECIDNVLFQLEVAL---------EPISNAFaGPDTEDDKEQSDLIKRLFS 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 704 GQMK-STVKCVACHKESAT--YESFSNLSL-------ELPPNSNVCQLNQCMDMYFSGERihgwncpscktkrdaikkld 773
Cdd:cd02666 144 GKTKqQLVPESMGNQPSVRtkTERFLSLLVdvgkkgrEIVVLLEPKDLYDALDRYFDYDS-------------------- 203

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 774 ISKLPPVLVVHLK----RFYADPSNSGSYMKK-----QNYLRFPLENLDMNPYIARAESRAVTPK-----------TYQL 833
Cdd:cd02666 204 LTKLPQRSQVQAQlaqpLQRELISMDRYELPSsiddiDELIREAIQSESSLVRQAQNELAELKHEiekqfddlksyGYRL 283

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....
gi 28571791 834 YAVSNHYGTMEGGHYTAFCKSANYGKWFKFDDQVVSALDSSNVV 877
Cdd:cd02666 284 HAVFIHRGEASSGHYWVYIKDFEENVWRKYNDETVTVVPASEVF 327
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
564-865 3.94e-08

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 55.74  E-value: 3.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   564 GLKNLGNTCYMNSILQCLSNTPQLteYCISdkyKNYISRSNKTNGQVIEEVAALIK--ELWNGQYkCVASrdlryvvgQY 641
Cdd:pfam13423   2 GLETHIPNSYTNSLLQLLRFIPPL--RNLA---LSHLATECLKEHCLLCELGFLFDmlEKAKGKN-CQAS--------NF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   642 QKIFRGVDQQDSHEfltiLMDWLHSD---------LQTLHvprqR---EMISASEKAWLEFTKAKESMILHLFYGQMKST 709
Cdd:pfam13423  68 LRALSSIPEASALG----LLDEDRETnsaislsslIQSFN----RfllDQLSSEENSTPPNPSPAESPLEQLFGIDAETT 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   710 VKCVACHKESATYESFSNLSLELP-------PNSNVCQLNQCMDMYFSGERIH-GWnCPSCKTKRDAIKKLDISKLPPVL 781
Cdd:pfam13423 140 IRCSNCGHESVRESSTHVLDLIYPrkpssnnKKPPNQTFSSILKSSLERETTTkAW-CEKCKRYQPLESRRTVRNLPPVL 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   782 VVHLKRFYADPSNSGsymKKQNYLrfPLE-NLDMNPYIARAESRAVtpktYQLYA-VSNHYGTMEGGHYTAFCKSANY-- 857
Cdd:pfam13423 219 SLNAALTNEEWRQLW---KTPGWL--PPEiGLTLSDDLQGDNEIVK----YELRGvVVHIGDSGTSGHLVSFVKVADSel 289

                         330
                  ....*....|...
gi 28571791   858 -----GKWFKFDD 865
Cdd:pfam13423 290 edpteSQWYLFND 302
Peptidase_C19N cd02670
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
 723-886 2.98e-06

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: 239135 [Multi-domain]  Cd Length: 241  Bit Score: 49.45  E-value: 2.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 723 ESFSNLSLELPPNSNVCQLNQCMDMYFSGErihgwncpscktkrdaikklDISKLPPVLVVHLKRFyadpSNSGSYMKKQ 802
Cdd:cd02670  64 ERLLQIPVPDDDDGGGITLEQCLEQYFNNS--------------------VFAKAPSCLIICLKRY----GKTEGKAQKM 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 803 NYLRFPLENLDMNPYIARAE--------SRAVTPKTYQ-----------LYAVSNHYGT-MEGGHYTAFCKSANYG---- 858
Cdd:cd02670 120 FKKILIPDEIDIPDFVADDPracskcqlECRVCYDDKDfsptcgkfklsLCSAVCHRGTsLETGHYVAFVRYGSYSltet 199

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 28571791 859 -------KWFKFDD-------QVVSALDSSNVVSSaAYILFY 886
Cdd:cd02670 200 dneaynaQWVFFDDmadrdgvSNGFNIPAARLLED-PYMLFY 240
DSP_MapKP cd01446
N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk ...
 148-278 3.30e-06

N-terminal regulatory rhodanese domain of dual specificity phosphatases (DSP), such as Mapk Phosphatase. This domain is believed to determine substrate specificity by binding the substrate, such as ERK2, and activating the C-terminal catalytic domain by inducing a conformational change. This domain has homology to the Rhodanese Homology Domain.


Pssm-ID: 238723 [Multi-domain]  Cd Length: 132  Bit Score: 47.28  E-value: 3.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 148 LITCQDLYRRMQE--KSVLVMDCRPSADYEASHLtyYCAFNVP------------EELITPGMSAGRLQARLSSSAkasw 213
Cdd:cd01446   1 TIDCAWLAALLREggERLLLLDCRPFLEYSSSHI--RGAVNVCcptilrrrlqggKILLQQLLSCPEDRDRLRRGE---- 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571791 214 asrsvKDSVVLMDWNTKDaqPATNTAISTLLDILKNWDPDVTYRAPIQIVEGGYEYFIMMYPTHC 278
Cdd:cd01446  75 -----SLAVVVYDESSSD--RERLREDSTAESVLGKLLRKLQEGCSVYLLKGGFEQFSSEFPELC 132
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 361-511 4.46e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 4.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 361 LQRAEQNDEQLEKASKMWKRQAAEGDglnaTEDQELHFRILQLESKAQDYIVENNRLREELSRIQELHNVTQQLSQkevE 440
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELE----AELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR---E 313

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 28571791 441 ATRNIESKIRERQRLDEQHELERQERERLLAIARETKKHYKSPTPSGPPSPGRNLEDVHVVSDSLESLLQL 511
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 351-478 7.68e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 7.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 351 AEIMRDQAEFLQRAEQNDEQLEKASKMWKRQAAEgdglnATEDQELHFRILQLESKAQDYIVENNRLREELSRIQELhnv 430
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEA-----LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA--- 429

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 28571791 431 TQQLSQKEVEATRNIESKIRERQRLDEQHELERQERERLLAIARETKK 478
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 348-478 8.58e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 8.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 348 KPIAEIMRDQAEFLQRAEQNDEQLEKASKMWKRQAAEGDGLNATEDQELHFRILQLESKAQDYIVENNRLREELSRIQEL 427
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL 384

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 28571791 428 HNVTQQLSQKEVEATRNIESKIRERQRLDEQHELERQERERLLAIARETKK 478
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 352-475 8.78e-05

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 46.27  E-value: 8.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   352 EIMRDQAEflqraEQNDEQLEKASKMWKRQAAEgdglnatedqELHFRILQLESKA-QDYIVENNRLREELSR-IQELHN 429
Cdd:pfam17380 463 ERLRQQEE-----ERKRKKLELEKEKRDRKRAE----------EQRRKILEKELEErKQAMIEEERKRKLLEKeMEERQK 527

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 28571791   430 -VTQQLSQKEVEATRNIESKIRERQRLDEQHELERQERERLLAIARE 475
Cdd:pfam17380 528 aIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMERE 574
mukB PRK04863
chromosome partition protein MukB;
351-473 2.33e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.95  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   351 AEIMRDQAEFLQR-AEQNDEQLEKASKMwKRQAAEGDGLNATEDQELHFRILQLESKAQDYIVEN---NRLRE----ELS 422
Cdd:PRK04863  546 LGKNLDDEDELEQlQEELEARLESLSES-VSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQdalARLREqsgeEFE 624

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 28571791   423 RIQELHNVTQQLSQKEVEATRNIESKIRERQRLDEQ-HEL---ERQERERLLAIA 473
Cdd:PRK04863  625 DSQDVTEYMQQLLERERELTVERDELAARKQALDEEiERLsqpGGSEDPRLNALA 679
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 351-479 5.66e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 5.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 351 AEIMRDQAEfLQRAEQNDEQLEKASKMWKRQAAEgdglNATEDQELHFRILQLESKAQDYIVENNRLREELSRIQELHNV 430
Cdd:COG1196 281 LELEEAQAE-EYELLAELARLEQDIARLEERRRE----LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE 355

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 28571791 431 TQQLSQKEVEATRNIESKIRERQRLDEQHELERQERERLLAIARETKKH 479
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
356-478 1.72e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791  356 DQAEFLQRAEQNDEQL-EKASKMWKRQAAEGDGLNATEDQ--ELHFRILQLESKAQDY-----------------IVENN 415
Cdd:PRK02224 499 ERAEDLVEAEDRIERLeERREDLEELIAERRETIEEKRERaeELRERAAELEAEAEEKreaaaeaeeeaeeareeVAELN 578

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571791  416 RLREEL-SRIQELHNVTQQLSQKEvEATRNIEskiRERQRLDEQHELERQERERlLAIARETKK 478
Cdd:PRK02224 579 SKLAELkERIESLERIRTLLAAIA-DAEDEIE---RLREKREALAELNDERRER-LAEKRERKR 637
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 350-478 1.91e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 350 IAEIMRDQAEFLQRAEQNDEQLEKAskmwkRQAAEGDGLNATEDQELHFRIL-QLESKAQDYIVENNRLREELSRIQELH 428
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEEL-----RLELEELELELEEAQAEEYELLaELARLEQDIARLEERRRELEERLEELE 322

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 28571791 429 NVTQQLSQKEVEATRNIESKIRERQRLDEQ---------------HELERQERERLLAIARETKK 478
Cdd:COG1196 323 EELAELEEELEELEEELEELEEELEEAEEEleeaeaelaeaeealLEAEAELAEAEEELEELAEE 387
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
350-481 2.84e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791 350 IAEIMRDQAEFLQRAEQNDEQLEKASKMWKRQAAEGDglnateDQELHFRILQLESKAQDYIVENNRLREELSRIQelhn 429
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALD------EEELEEELEELEEELEELEEELEELREELAELE---- 459

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 28571791 430 vtQQLSQkeVEATRNIESKIRERQRLDEqhELERQERER-----LLAIARETKKHYK 481
Cdd:COG4717 460 --AELEQ--LEEDGELAELLQELEELKA--ELRELAEEWaalklALELLEEAREEYR 510
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 358-480 6.35e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 6.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791    358 AEFLQRAEQNDEQLEKASKMWKRQAAEGDGLNAtEDQELHFRILQLESKAQDYiveNNRLREELSRIQELHNVTQQLSQK 437
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRA-ELTLLNEEAANLRERLESL---ERRIAATERRLEDLEEQIEELSED 853

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 28571791    438 EVEATRNIESKIRERQRLDEQHELERQERERLLAIARETKKHY 480
Cdd:TIGR02168  854 IESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 352-469 6.41e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 39.88  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   352 EIMRDQAEFLQRAEQNDEQLEKASKMWKRQAAEGDGlnatEDQELHFRILQLESKAQDY----------IVENNRLREEL 421
Cdd:pfam07888  38 ECLQERAELLQAQEAANRQREKEKERYKRDREQWER----QRRELESRVAELKEELRQSrekheeleekYKELSASSEEL 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 28571791   422 S---------------RIQELHNVTQQLSQKEVEATRNIEsKIRERQ-RLDEQHELERQERERL 469
Cdd:pfam07888 114 SeekdallaqraaheaRIRELEEDIKTLTQRVLERETELE-RMKERAkKAGAQRKEEEAERKQL 176
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 355-481 6.62e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.93  E-value: 6.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   355 RDQAEflQRAEQNdEQLEKASKMwkRQAAEGDGLNATEDQELHFRILQLESKAQDYIVENNRLREELSR------IQELH 428
Cdd:pfam15709 355 REQEE--QRRLQQ-EQLERAEKM--REELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQerarqqQEEFR 429

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 28571791   429 NVTQQLSQK--EVEATRNIEskirERQRLDEQHELERQERERLLAIARETKKHYK 481
Cdd:pfam15709 430 RKLQELQRKkqQEEAERAEA----EKQRQKELEMQLAEEQKRLMEMAEEERLEYQ 480
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
351-468 6.74e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 6.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791  351 AEIMRDQAEFLQRAEQNDEQLEKAskmwKRQAAEGDGLNATEDQELHFRILQLESKAQDyivennRLREELSRIQ-ELHN 429
Cdd:COG4913  244 LEDAREQIELLEPIRELAERYAAA----RERLAELEYLRAALRLWFAQRRLELLEAELE------ELRAELARLEaELER 313

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 28571791  430 VTQQLSQKEVEAtRNIESKIRER--QRLDE-QHELERQERER 468
Cdd:COG4913  314 LEARLDALREEL-DELEAQIRGNggDRLEQlEREIERLEREL 354
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 355-473 7.51e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.32  E-value: 7.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791  355 RDQAEFLQR-AEQNDEQLEKASKMWKRQAAEGDGLNATEDQeLHFRILQLESKAQDYIVEN---NRLREE----LSRIQE 426
Cdd:COG3096  549 LDAAEELEElLAELEAQLEELEEQAAEAVEQRSELRQQLEQ-LRARIKELAARAPAWLAAQdalERLREQsgeaLADSQE 627

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 28571791  427 LHNVTQQLSQKEVEATRNiESKIRERQRldeqhELERQERE----------RLLAIA 473
Cdd:COG3096  628 VTAAMQQLLEREREATVE-RDELAARKQ-----ALESQIERlsqpggaedpRLLALA 678
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 362-478 8.06e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 38.10  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 28571791   362 QRAEQNDEQLEKASKMWKRQAAEgdglnatEDQELHFRILQLESKAQdyivennRLREELSRIQelhnvtQQLSQKEVEA 441
Cdd:pfam05672  51 RAEEERARREEEARRLEEERRRE-------EEERQRKAEEEAEEREQ-------REQEEQERLQ------KQKEEAEAKA 110

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 28571791   442 TRNIESKIRERQRLDEQHELERQER-ERLLAIARETKK 478
Cdd:pfam05672 111 REEAERQRQEREKIMQQEEQERLERkKRIEEIMKRTRK 148
 
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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