|
Name |
Accession |
Description |
Interval |
E-value |
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1557-1960 |
2.16e-149 |
|
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: 467.50 E-value: 2.16e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1557 GFVGLKNAGATCYMNSVIQQLYMIPSIRNSILAIegtgsdlhddmfgdekqdsesnvdprddvfgyphqfedkpalsKTE 1636
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSI-------------------------------------------PPT 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1637 DRKEYNIGVLRHLQVIFGHLAASQLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKALGHPAILSKVL 1716
Cdd:cd02659 38 EDDDDNKSVPLALQRLFLFLQLSESPVKTTELTDKTRSFGWDSLNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1717 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYIKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPRVLA 1796
Cdd:cd02659 118 GGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1797 IQLKRFDYDWERECAIKFNDYFEFPRELDMGPYTVAGVANLERDNVNSENELieqkeqsdnetaggTKYRLVGVLVHSGQ 1876
Cdd:cd02659 198 LQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLAKKEGDSEKKDSES--------------YIYELHGVLVHSGD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1877 ASGGHYYSYIIQRNgkDDQtdhWYKFDDGDVTECKMDDDEEmknQCFGGEYMGEVFDHMmkrmsYRRQKRWWNAYILFYE 1956
Cdd:cd02659 264 AHGGHYYSYIKDRD--DGK---WYKFNDDVVTPFDPNDAEE---ECFGGEETQKTYDSG-----PRAFKRTTNAYMLFYE 330
|
....
gi 74319833 1957 QMDM 1960
Cdd:cd02659 331 RKSP 334
|
|
| DUF3517 |
pfam12030 |
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. ... |
2098-2477 |
8.20e-106 |
|
Domain of unknown function (DUF3517); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is about 340 amino acids in length. This domain is found associated with pfam00443.
Pssm-ID: 463438 Cd Length: 407 Bit Score: 345.44 E-value: 8.20e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 2098 SNRFSEYLLECPSAEVRGAFAKLIVFIAH-----FSLQDGSCPspfaspgPSSQACDNLSLSDHLLRATLNLLRR---EV 2169
Cdd:pfam12030 1 PEALRELLLRNPDAEVRSAFGKLIVFALHklkelYGLPDGPCD-------PDDLEEEWRSLSDSVLEAVVALLDHlwkEF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 2170 SEHGHHLQQYFNLFVMYANLGVAEKTQLLKLN-VPATFMLVSLDEGPGPPIKYQYAEL------------GKLYSVVSQL 2236
Cdd:pfam12030 74 HTHLRSWDEYFGLLLSYANLGPREVAQLLDLGfLLKCLEIIAADEGDGPPLKYQYARMlrlvekrrppsyEKLIQLLSVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 2237 IRCCNVSSTMQSSINGNPPLPNpfgdlNLSQPIMPIQQNVLDIL--FVRT---SYVKKIIEDCSNSEDTIKLLRFCSWEN 2311
Cdd:pfam12030 154 LRCCDLSLPPQSINEGAEPLPN-----SLPDGPFPLTSEEADLLrpLGRTngsIFVKKLLEIDQNPEATRKILRFLLWEN 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 2312 PQFSSTVLSELLWQVAYSYTYELRPyLDLLFQILLIEDSWQTHRIHNALKGIPDDRDGLFDTIQRSKNHYQKRAYQCIKC 2391
Cdd:pfam12030 229 PELSDSILKTLLWGIRGAPAHLLRD-PFLRAAIVFCEDSWQAHRIHNLIDHVAKQADSLNNTEGRAFLHFFKRAYQCINC 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 2392 MvALFSSCPVAYQILQgngdlkrkwtwavewlgdelerrpytgnpqySYNNWSPPVQSNETAN----------------- 2454
Cdd:pfam12030 308 R-LGFDKEWFASQVLE-------------------------------NIPDWAPPLLSYPDSNvrsetedflqeelfshe 355
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 74319833 2455 --------------------------GYFLERS---HSARMTLAKACELCPE 2477
Cdd:pfam12030 356 mgpdpqfrlreaarrlgiacleylrgTYVLRRSqveRSAVETLQRVIELCPE 407
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
1559-1955 |
1.47e-74 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 251.59 E-value: 1.47e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1559 VGLKNAGATCYMNSVIQQLYMIPSIRNSILAIEGTGSDlhddmfgdekqdsesnvdprddvfgyphqfedkpalskteDR 1638
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSED----------------------------------------SR 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1639 KEYNIGVLRHLQVIFGHLA-ASQLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEALKA---LGHPAILSK 1714
Cdd:pfam00443 41 YNKDINLLCALRDLFKALQkNSKSSSVSPKMFKKSLGKLNPDFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1715 VLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLL------DSLEQYIKGDLLEGANAYHCEKCDKKVDTVKRLLI 1788
Cdd:pfam00443 121 LFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGDSAELktaslqICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1789 KKLPRVLAIQLKRFDYDweRECAIKFNDYFEFPRELDMGPYTVAGVanlerdnvnsenelieqkeqsDNETAGGTKYRLV 1868
Cdd:pfam00443 201 SRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSRYLAEEL---------------------KPKTNNLQDYRLV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1869 GVLVHSGQASGGHYYSYIiqrngKDDQTDHWYKFDDGDVTECKMDDDEEMknqcfggeymgevfdhmmkrmsyrrqkrwW 1948
Cdd:pfam00443 258 AVVVHSGSLSSGHYIAYI-----KAYENNRWYKFDDEKVTEVDEETAVLS-----------------------------S 303
|
....*..
gi 74319833 1949 NAYILFY 1955
Cdd:pfam00443 304 SAYILFY 310
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
1682-1956 |
4.80e-53 |
|
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: 187.69 E-value: 4.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1682 LREQHDALEFFNSLVDSLDEALKALG--------HPAILSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI----RNH 1749
Cdd:cd02257 19 FSEQQDAHEFLLFLLDKLHEELKKSSkrtsdsssLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1750 QNLLDSLEQYIKGDLLEGANAYHCEKCdKKVDTVKRLLIKKLPRVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMGPY 1829
Cdd:cd02257 99 VSLEDCLEKFFKEEILEGDNCYKCEKK-KKQEATKRLKIKKLPPVLIIHLKRFSFN-EDGTKEKLNTKVSFPLELDLSPY 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1830 TVAGVANLERDNvnsenelieqkeqsdnetaGGTKYRLVGVLVHSGQ-ASGGHYYSYIiqrngKDDQTDHWYKFDDGDVT 1908
Cdd:cd02257 177 LSEGEKDSDSDN-------------------GSYKYELVAVVVHSGTsADSGHYVAYV-----KDPSDGKWYKFNDDKVT 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 74319833 1909 ECKMDDDEEMKNqcfggeymgevfdhmmkrmsyrrqkRWWNAYILFYE 1956
Cdd:cd02257 233 EVSEEEVLEFGS-------------------------LSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1956 |
1.94e-52 |
|
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: 188.40 E-value: 1.94e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1560 GLKNAGATCYMNSVIQQLYMIPSIRNSILAIEGTGSDLHDDMFGDekQDSESNvdprddvfgyphqfedkpalsktedrk 1639
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPD--KPHEPQ--------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1640 eyniGVLRHLQVIFGHLAASQLQYYVPRGFWKQFRLwgepvNLREQHDALEFFNSLVDSLDEALKALGHP---AILSKVL 1716
Cdd:cd02668 52 ----TIIDQLQLIFAQLQFGNRSVVDPSGFVKALGL-----DTGQQQDAQEFSKLFLSLLEAKLSKSKNPdlkNIVQDLF 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1717 GGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYIKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPRVLA 1796
Cdd:cd02668 123 RGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLN 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1797 IQLKRFDYDWERECAIKFNDYFEFPRELDMGPYtvagvanlerdnvnseneLIEQKEQSdnetaggTKYRLVGVLVHSGQ 1876
Cdd:cd02668 203 FQLLRFVFDRKTGAKKKLNASISFPEILDMGEY------------------LAESDEGS-------YVYELSGVLIHQGV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1877 -ASGGHYYSYIiqrngKDDQTDHWYKFDDGDVTE-----CKMDDDEEMKNQCFGgeymgevfDHMMKRMSYRrqkrwwNA 1950
Cdd:cd02668 258 sAYSGHYIAHI-----KDEQTGEWYKFNDEDVEEmpgkpLKLGNSEDPAKPRKS--------EIKKGTHSSR------TA 318
|
....*.
gi 74319833 1951 YILFYE 1956
Cdd:cd02668 319 YMLVYK 324
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
1557-1994 |
7.58e-46 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 182.38 E-value: 7.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1557 GFVGLKNAGATCYMNSVIQQLYMIPSIRNSILAIEgtgsdlhddmfgdekqdsESNVDPRDDV-------FgYPHQFEDK 1629
Cdd:COG5077 192 GYVGLRNQGATCYMNSLLQSLFFIAKFRKDVYGIP------------------TDHPRGRDSValalqrlF-YNLQTGEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1630 PaLSKTEdrkeynigvlrhLQVIFGhlaasqlqyyvprgfwkqfrlWGEPVNLReQHDALEFFNSLVDSLDEALKALGHP 1709
Cdd:COG5077 253 P-VDTTE------------LTRSFG---------------------WDSDDSFM-QHDIQEFNRVLQDNLEKSMRGTVVE 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1710 AILSKVLGGSFadqKICQGCPHR-YECE--ESFTTLNVDIRNHQNLLDSLEQYIKGDLLEGANAYHCEKcDKKVDTVKRL 1786
Cdd:COG5077 298 NALNGIFVGKM---KSYIKCVNVnYESArvEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGV 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1787 LIKKLPRVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMGPYtvagvanLERDnvnsenelIEQKEQSDNEtaggtkYR 1866
Cdd:COG5077 374 IFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLLPF-------LDRD--------ADKSENSDAV------YV 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1867 LVGVLVHSGQASGGHYYSYIiqRNGKDDQtdhWYKFDDGDVTECKMdddEEMKNQCFGGEYMGEVfdhmmKRMSYRRQKR 1946
Cdd:COG5077 433 LYGVLVHSGDLHEGHYYALL--KPEKDGR---WYKFDDTRVTRATE---KEVLEENFGGDHPYKD-----KIRDHSGIKR 499
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 74319833 1947 WWNAYILFYEQMDMIdedDEMIRYISELTIARPHQIIMSPAIERSVRK 1994
Cdd:COG5077 500 FMSAYMLVYLRKSML---DDLLNPVAAVDIPPHVEEVLSEEIDKTEVR 544
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1914 |
6.22e-42 |
|
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: 157.44 E-value: 6.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1560 GLKNAGATCYMNSVIQQLYMIPSIRNSILaiegtgSDLHddmfgdekqdsesnvdprddvfgyphqfedkpalskTEDRK 1639
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPLANYLL------SREH------------------------------------SKDCC 40
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1640 EYNIGVLRHLQVIFGHLAASQLQYYVPRGFWKQFRLWGEPVNLREQHDALEFFNSLVDSLDEA-------LKALGHPA-- 1710
Cdd:cd02661 41 NEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQKAcldrfkkLKAVDPSSqe 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1711 --ILSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDSLEQYIKGDLLEGANAYHCEKCDKKVDTVKRLLI 1788
Cdd:cd02661 121 ttLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKGADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1789 KKLPRVLAIQLKRFDYDWERecaiKFNDYFEFPRELDMGPYTVagvanlerdnvnsenelieqkeqsdNETAGGTKYRLV 1868
Cdd:cd02661 201 HRAPNVLTIHLKRFSNFRGG----KINKQISFPETLDLSPYMS-------------------------QPNDGPLKYKLY 251
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 74319833 1869 GVLVHSG-QASGGHYYSYIIQRNGKddqtdhWYKFDDGDVTECKMDD 1914
Cdd:cd02661 252 AVLVHSGfSPHSGHYYCYVKSSNGK------WYNMDDSKVSPVSIET 292
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1684-1956 |
4.50e-37 |
|
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: 140.50 E-value: 4.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1684 EQHDALEFFNSLVDSLDealkalghpAILSKVLGGSFADQKICQGCPHRYECEESFTTLNVDI------RNHQNLLDSLE 1757
Cdd:cd02674 21 DQQDAQEFLLFLLDGLH---------SIIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdAPKVTLEDCLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1758 QYIKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPRVLAIQLKRFDYDweRECAIKFNDYFEFP-RELDMGPYTVAGvan 1836
Cdd:cd02674 92 LFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRFSFS--RGSTRKLTTPVTFPlNDLDLTPYVDTR--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1837 lerdnvnsenelieqkeqsdnETAGGTKYRLVGVLVHSGQASGGHYYSYIiqrngKDDQTDHWYKFDDGDVTecKMDDDE 1916
Cdd:cd02674 167 ---------------------SFTGPFKYDLYAVVNHYGSLNGGHYTAYC-----KNNETNDWYKFDDSRVT--KVSESS 218
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 74319833 1917 EMKNqcfggeymgevfdhmmkrmsyrrqkrwwNAYILFYE 1956
Cdd:cd02674 219 VVSS----------------------------SAYILFYE 230
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1909 |
9.10e-36 |
|
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: 140.20 E-value: 9.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1560 GLKNAGATCYMNSVIQQLYMIPSIRNSILaiegtgSDLHDdMFGDEKQDSESNVDPRDDVFGYPHQFEDKPalsktedrk 1639
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFL------SDRHS-CTCLSCSPNSCLSCAMDEIFQEFYYSGDRS--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1640 eynigvlrhlqvifGHLAASQLQyyvprGFWKQFRlwgepvNL--REQHDALEFFNSLVDSLDEALKALGHPA------- 1710
Cdd:cd02660 66 --------------PYGPINLLY-----LSWKHSR------NLagYSQQDAHEFFQFLLDQLHTHYGGDKNEAndeshcn 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1711 -ILSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRN---------------HQNLLDSLEQYIKGDLLeGANAYHCE 1774
Cdd:cd02660 121 cIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPNkstpswalgesgvsgTPTLSDCLDRFTRPEKL-GDFAYKCS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1775 KCDKKVDTVKRLLIKKLPRVLAIQLKRFDYDwERECAIKFNDYFEFPRELDMGPYTVAGvanlerdnvnseneliEQKEQ 1854
Cdd:cd02660 200 GCGSTQEATKQLSIKKLPPVLCFQLKRFEHS-LNKTSRKIDTYVQFPLELNMTPYTSSS----------------IGDTQ 262
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 74319833 1855 SDNETAGGTKYRLVGVLVHSGQASGGHYYSYIIQRNgkddqtDHWYKFDDGDVTE 1909
Cdd:cd02660 263 DSNSLDPDYTYDLFAVVVHKGTLDTGHYTAYCRQGD------GQWFKFDDAMITR 311
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1920 |
4.12e-33 |
|
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: 132.23 E-value: 4.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1560 GLKNAGATCYMNSVIQQLYMIPSIRNSILaiegtgsdlhddmfgdekqdsesnvdprddvfgyphqfedkpalSKTEDRK 1639
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVL--------------------------------------------SLNLPRL 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1640 EYNIGVLRHLQVIFGHLAASQLQYY-VPRGFWKQfrLWGEPVNLREQHDALEFFNSLVDSLDealkalghpAILSKVLGG 1718
Cdd:cd02664 37 GDSQSVMKKLQLLQAHLMHTQRRAEaPPDYFLEA--SRPPWFTPGSQQDCSEYLRYLLDRLH---------TLIEKMFGG 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1719 SFADQKICQGCPHRYECEESFTTLNVDIRNHQNLLDsleQYIKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPRVLAIQ 1798
Cdd:cd02664 106 KLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDLLN---YFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILT 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1799 LKRFDYDWERECAIKFNDYFEFPRELDMgPYTVAgvanlerdNVNSENELIEQKEQSDNETAGGTK---YRLVGVLVHSG 1875
Cdd:cd02664 183 LLRFSYDQKTHVREKIMDNVSINEVLSL-PVRVE--------SKSSESPLEKKEEESGDDGELVTRqvhYRLYAVVVHSG 253
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74319833 1876 QAS-GGHYYSYIiqRNGKD-----------------DQTDHWYKFDDGDVTECKMdddEEMKN 1920
Cdd:cd02664 254 YSSeSGHYFTYA--RDQTDadstgqecpepkdaeenDESKNWYLFNDSRVTFSSF---ESVQN 311
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1956 |
1.52e-26 |
|
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: 111.71 E-value: 1.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1560 GLKNAGATCYMNSVIQQLYMIPSIRnsilaiegtgsdlhdDMFGdekqdsesnvdprddvfgyphqfedkpalsktEDRK 1639
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALR---------------ELLS--------------------------------ETPK 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1640 EynigvlrhlqvIFGHLAASQLQYyvpRGFwkqfrlwgepvnlrEQHDALEFFNSLVDSLDEALKalghpailsKVLGGS 1719
Cdd:cd02667 34 E-----------LFSQVCRKAPQF---KGY--------------QQQDSHELLRYLLDGLRTFID---------SIFGGE 76
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1720 FADQKICQGCPHRYECEESFTTLN----VDIRNHQNLLDSLEQYIKGDLLEGANAYHCEKCDKkvdTVKRLLIKKLPRVL 1795
Cdd:cd02667 77 LTSTIMCESCGTVSLVYEPFLDLSlprsDEIKSECSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVL 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1796 AIQLKRFDYDwERECAIKFNDYFEFPRELDMGPYTVAGVANLErDNVNSenelieqkeqsdnetaggtKYRLVGVLVHSG 1875
Cdd:cd02667 154 VIHLKRFQQP-RSANLRKVSRHVSFPEILDLAPFCDPKCNSSE-DKSSV-------------------LYRLYGVVEHSG 212
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1876 QASGGHYYSYIIQRNGKDDQTDH----------------WYKFDDGDVTEckMDDDEEMKNQcfggeymgevfdhmmkrm 1939
Cdd:cd02667 213 TMRSGHYVAYVKVRPPQQRLSDLtkskpaadeagpgsgqWYYISDSDVRE--VSLEEVLKSE------------------ 272
|
410
....*....|....*..
gi 74319833 1940 syrrqkrwwnAYILFYE 1956
Cdd:cd02667 273 ----------AYLLFYE 279
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1685-1956 |
1.70e-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: 239128 [Multi-domain] Cd Length: 300 Bit Score: 109.32 E-value: 1.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1685 QHDALEFFNSLVDSLDEALKALG-----------------HPAILSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIR 1747
Cdd:cd02663 65 HQDAHEFLNFLLNEIAEILDAERkaekanrklnnnnnaepQPTWVHEIFQGILTNETRCLTCETVSSRDETFLDLSIDVE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1748 NHQNLLDSLEQYIKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPRVLAIQLKRFDYDWERECAIKFNDYFEFPRELDMg 1827
Cdd:cd02663 145 QNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLELRL- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1828 pytvagvanlerdnvnsenelieqKEQSDNETAGGTKYRLVGVLVHSGQ-ASGGHYYSyIIQRNGkddqtdHWYKFDDGD 1906
Cdd:cd02663 224 ------------------------FNTTDDAENPDRLYELVAVVVHIGGgPNHGHYVS-IVKSHG------GWLLFDDET 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 74319833 1907 VTecKMDDdeemknqcfggEYMGEVFDHmmkrmsyrrQKRWWNAYILFYE 1956
Cdd:cd02663 273 VE--KIDE-----------NAVEEFFGD---------SPNQATAYVLFYQ 300
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1956 |
1.73e-20 |
|
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: 94.71 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1560 GLKNAGATCYMNSVIQQLYMIPSIRNSIL--AIEGTGSDLHDDMFGDEKQDsesnvdprddvfgyphqfedkpaLSKTED 1637
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALKnyNPARRGANQSSDNLTNALRD-----------------------LFDTMD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1638 RKEYNIGVLRHLQVIfgHLAASQLQYYVPRGFWKQfrlwgepvnlreqHDALEFFNSLVDSLDEALK-ALGHPAILSKVL 1716
Cdd:cd02657 58 KKQEPVPPIEFLQLL--RMAFPQFAEKQNQGGYAQ-------------QDAEECWSQLLSVLSQKLPgAGSKGSFIDQLF 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1717 GGSFADQKICQGCPHRYECE-ESFTTLNVDIrNHQNLLDSLEQYIKgDLLEGANAYHCEKCDKKVDTVKRLLIKKLPRVL 1795
Cdd:cd02657 123 GIELETKMKCTESPDEEEVStESEYKLQCHI-SITTEVNYLQDGLK-KGLEEEIEKHSPTLGRDAIYTKTSRISRLPKYL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1796 AIQLKRFDydWERECAI--KFNDYFEFPRELDMGPY-TVAGVanlerdnvnsenelieqkeqsdnetaggtkYRLVGVLV 1872
Cdd:cd02657 201 TVQFVRFF--WKRDIQKkaKILRKVKFPFELDLYELcTPSGY------------------------------YELVAVIT 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1873 HSGQ-ASGGHYYSYIiqrngKDDQTDHWYKFDDGDVTECKMDDDEEMKNqcfGGEYmgevfdHMmkrmsyrrqkrwwnAY 1951
Cdd:cd02657 249 HQGRsADSGHYVAWV-----RRKNDGKWIKFDDDKVSEVTEEDILKLSG---GGDW------HI--------------AY 300
|
....*
gi 74319833 1952 ILFYE 1956
Cdd:cd02657 301 ILLYK 305
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1560-1920 |
5.39e-18 |
|
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: 87.38 E-value: 5.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1560 GLKNAGATCYMNSVIQQLYMIPSIRNSilaiegtgsdlhddmFGDEKQDSESNV-DPRDDvfgYPHQF-----------E 1627
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWR---------------YDDLENKFPSDVvDPAND---LNCQLikladgllsgrY 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1628 DKPALSKTEDrKEYNIGVLrhlqvifghlaasqlqyyvPRGFwKqfRLWGEpvNLRE-----QHDALEFFNSLVDSLDEA 1702
Cdd:cd02658 63 SKPASLKSEN-DPYQVGIK-------------------PSMF-K--ALIGK--GHPEfstmrQQDALEFLLHLIDKLDRE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1703 LKALGHPAI--LSKVlggsFADQKI-CQGCPHRYECEESFTTLNVDIRNH--------------QNLLDSLEQYIKGDLL 1765
Cdd:cd02658 118 SFKNLGLNPndLFKF----MIEDRLeCLSCKKVKYTSELSEILSLPVPKDeatekeegelvyepVPLEDCLKAYFAPETI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1766 EganaYHCEKCDKKVDTVKRLLIKKLPRVLAIQLKRFDY--DWErecaikfndyfefPRELDMgpytvagvanlerdNVN 1843
Cdd:cd02658 194 E----DFCSTCKEKTTATKTTGFKTFPDYLVINMKRFQLleNWV-------------PKKLDV--------------PID 242
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74319833 1844 SENELieqkeqsdnetaGGTKYRLVGVLVHSG-QASGGHYYSYIIQrngKDDQTDHWYKFDDGDVteCKMDDDEEMKN 1920
Cdd:cd02658 243 VPEEL------------GPGKYELIAFISHKGtSVHSGHYVAHIKK---EIDGEGKWVLFNDEKV--VASQDPPEMKK 303
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1535-1907 |
3.67e-16 |
|
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: 82.25 E-value: 3.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1535 ITTCEALtewEYLPPvgprppkgFVGLKNAGATCYMNSVIQQLYMIPSIRNSILAIEGTGSdlhddmfgdekqdSESNvd 1614
Cdd:cd02671 12 ATSCEKR---ENLLP--------FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLIS-------------SVEQ-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1615 prddvfgypHQ--FEDKPALSKTEDRKEYNIGVLRHLQVIFGHLAASQlqyyvprgfwkqfrlwgepvnlreQHDALEFF 1692
Cdd:cd02671 66 ---------LQssFLLNPEKYNDELANQAPRRLLNALREVNPMYEGYL------------------------QHDAQEVL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1693 NSLVDSLDEalkalghpaILSKVLGGSFADQKICQGCPHRYECEESFTTLNVDIRNHQ-------------------NLL 1753
Cdd:cd02671 113 QCILGNIQE---------LVEKDFQGQLVLRTRCLECETFTERREDFQDISVPVQESElskseesseispdpktemkTLK 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1754 DSLEQYIKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPRVLAIQLKRFDYDWERECAI----KFNDYFEFPRELdmgpy 1829
Cdd:cd02671 184 WAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAANGSEFDCYgglsKVNTPLLTPLKL----- 258
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74319833 1830 tvagvanlerdnvnsenELIEQKEQSDNETaggtkYRLVGVLVHSG-QASGGHYYSYIiqrngkddqtdHWYKFDDGDV 1907
Cdd:cd02671 259 -----------------SLEEWSTKPKNDV-----YRLFAVVMHSGaTISSGHYTAYV-----------RWLLFDDSEV 304
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1560-1957 |
4.71e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 81.00 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1560 GLKNAGATCYMNSVIQQL-YMIPSIRNSILAIEGTGSDLHDDMFGDEKQDsesNVDPRDDVF-----GYPHQFEDKPALS 1633
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKELKVLKNVIRKPEPDL---NQEEALKLFtalwsSKEHKVGWIPPMG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1634 KTEDRKEYNIGVLRHLQVifgHLAASQLQYYVPrgfwkqfrlwgepvnlreqhdaleFFNSLVDSLDEALkalgHPAILS 1713
Cdd:COG5533 78 SQEDAHELLGKLLDELKL---DLVNSFTIRIFK------------------------TTKDKKKTSTGDW----FDIIIE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1714 KVLGGSFADQKICQGCPhryECEESFTTLNVDIRNHQNllDSLEQYIKgdllegaNAYHcekcdkkvdtvkrLLIKKLPR 1793
Cdd:COG5533 127 LPDQTWVNNLKTLQEFI---DNMEELVDDETGVKAKEN--EELEVQAK-------QEYE-------------VSFVKLPK 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1794 VLAIQLKRFDYDwerecaikfNDyfefPRELDmgpytvagvanlerDNVNSENELIEQKEQSDNETAgGTKYRLVGVLVH 1873
Cdd:COG5533 182 ILTIQLKRFANL---------GG----NQKID--------------TEVDEKFELPVKHDQILNIVK-ETYYDLVGFVLH 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1874 SGQASGGHYYSYIiqrngkdDQTDHWYKFDDGDVTECKMDDDEEMKNQcfggeymgevfdhmmkrmsyrrqkrwwNAYIL 1953
Cdd:COG5533 234 QGSLEGGHYIAYV-------KKGGKWEKANDSDVTPVSEEEAINEKAK---------------------------NAYLY 279
|
....
gi 74319833 1954 FYEQ 1957
Cdd:COG5533 280 FYER 283
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1559-1909 |
1.50e-15 |
|
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: 80.61 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1559 VGLKNAGATCYMNSVIQQLYMIPSIRNSILAIEGTGSDLHDDMFGDEKQdsesnvdprddvfgyphqfedkPALSKTEDR 1638
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASDYPTERRI----------------------GGREVSRSE 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1639 KEYNIGVLRHLQVIFGHLAASQLQYYVPRGfwkqfrlwgEPVNLR-EQHDALEFFNSLVDSLDEALKALG-HPAILSKVL 1716
Cdd:cd02666 60 LQRSNQFVYELRSLFNDLIHSNTRSVTPSK---------ELAYLAlRQQDVTECIDNVLFQLEVALEPISnAFAGPDTED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1717 GGSFADQ-------KICQ--------GCPHRYECEESFTTLNVDIR---------NH-QNLLDSLEQYIKGDLLEganay 1771
Cdd:cd02666 131 DKEQSDLikrlfsgKTKQqlvpesmgNQPSVRTKTERFLSLLVDVGkkgreivvlLEpKDLYDALDRYFDYDSLT----- 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1772 hcekcdkkvdtvkrllikKLPRVLAIQLKrfdydwerecaikfNDYFEFPRELDMGPYT----VAGVANLERDNVNSENE 1847
Cdd:cd02666 206 ------------------KLPQRSQVQAQ--------------LAQPLQRELISMDRYElpssIDDIDELIREAIQSESS 253
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74319833 1848 LIEQKEQSDNETA-------GGTK---YRLVGVLVHSGQASGGHYYSYIiqrngKDDQTDHWYKFDDGDVTE 1909
Cdd:cd02666 254 LVRQAQNELAELKheiekqfDDLKsygYRLHAVFIHRGEASSGHYWVYI-----KDFEENVWRKYNDETVTV 320
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1671-1914 |
2.16e-15 |
|
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: 78.18 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1671 KQFRLWGEpvNLREQHDALEFFNSLVDSLDEALKalgHPailskvLGGSFADQKICQGCPH----RYECeESFTTLNV-- 1744
Cdd:cd02662 22 PSLIEYLE--EFLEQQDAHELFQVLLETLEQLLK---FP------FDGLLASRIVCLQCGEsskvRYES-FTMLSLPVpn 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1745 -DIRNHQNLLDSLEQYIKGDLLEGanaYHCEKCdkkvdtvkRLLIKKLPRVLAIQLKRFDYDwERECAIKFNDYFEFPRE 1823
Cdd:cd02662 90 qSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPER 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1824 LDmgpytvagvanlerdnvnsenelieqkeqsdnetagGTKYRLVGVLVHSGQASGGHYYSY---------------IIQ 1888
Cdd:cd02662 158 LP------------------------------------KVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfVRM 201
|
250 260
....*....|....*....|....*.
gi 74319833 1889 RNGKDDQTDHWYKFDDGDVTECKMDD 1914
Cdd:cd02662 202 REGPSSTSHPWWRISDTTVKEVSESE 227
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1685-1925 |
9.70e-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: 239130 [Multi-domain] Cd Length: 228 Bit Score: 70.28 E-value: 9.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1685 QHDALEFFNSLVDSLDEALKALGHPAILSK--------VLGGSFADQKICQGcpHRYECEESFTTLNVDIRNHQNLLDSL 1756
Cdd:cd02665 22 QQDVSEFTHLLLDWLEDAFQAAAEAISPGEksknpmvqLFYGTFLTEGVLEG--KPFCNCETFGQYPLQVNGYGNLHECL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1757 EqyikGDLLEGAnaYHCEKCDKKVDTVKRLLIKKLPRVLAIQLKRFDYDWERECaiKFNDYFEFPRELdmgpytvagvan 1836
Cdd:cd02665 100 E----AAMFEGE--VELLPSDHSVKSGQERWFTELPPVLTFELSRFEFNQGRPE--KIHDKLEFPQII------------ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1837 lerdnvnsenelieQKEqsdnetaggtKYRLVGVLVHSGQASGGHYYSYIIQRNGKDdqtdhWYKFDDGDVTECkmdDDE 1916
Cdd:cd02665 160 --------------QQV----------PYELHAVLVHEGQANAGHYWAYIYKQSRQE-----WEKYNDISVTES---SWE 207
|
....*....
gi 74319833 1917 EMKNQCFGG 1925
Cdd:cd02665 208 EVERDSFGG 216
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
1752-1909 |
4.87e-11 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 68.37 E-value: 4.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1752 LLDSLEQYIKGDLLEGANAYHCEKCDKKVDTVKRLLIKKLPRVLAIQLKRFDYDweRECAIKFNDYFEFP-RELDMGPYT 1830
Cdd:COG5560 677 LQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYPiDDLDLSGVE 754
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74319833 1831 VAgvanlerdnvNSENELIEQKEQSDNetaggtkyrlvgvlvHSGQASGGHYYSYIiqRNGKDDQtdhWYKFDDGDVTE 1909
Cdd:COG5560 755 YM----------VDDPRLIYDLYAVDN---------------HYGGLSGGHYTAYA--RNFANNG---WYLFDDSRITE 803
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
1559-1904 |
1.60e-09 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 61.90 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1559 VGLKNAGATCYMNSVIQQLYMIPSIRNsiLAIEGTGSDLHD------------DMFGD-EKQD-SESNvdprddvfgyph 1624
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRN--LALSHLATECLKehcllcelgflfDMLEKaKGKNcQASN------------ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1625 qfedkpaLSKTedrkeynigvlrhlqviFGHLA-ASQLqyyvprGFWKQFRLWGEPVNLREQHDALEFFnsLVDSL-DEA 1702
Cdd:pfam13423 67 -------FLRA-----------------LSSIPeASAL------GLLDEDRETNSAISLSSLIQSFNRF--LLDQLsSEE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1703 LKALGHP----AILSKVLGGSFADQKICQGCPHRYECEESFTTLN------VDIRNHQNLLDSLEQYIKGDLL-EGANAY 1771
Cdd:pfam13423 115 NSTPPNPspaeSPLEQLFGIDAETTIRCSNCGHESVRESSTHVLDliyprkPSSNNKKPPNQTFSSILKSSLErETTTKA 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1772 HCEKCDKKVDTVKRLLIKKLPRVLAIQLKRFDYDWEREcaIKFNDYfeFPRELDMGpytvagvanlerdnvnsenelIEQ 1851
Cdd:pfam13423 195 WCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL--WKTPGW--LPPEIGLT---------------------LSD 249
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 74319833 1852 KEQSDNEtagGTKYRLVGVLVH-SGQASGGHYYSYI--IQRNGKDDQTDHWYKFDD 1904
Cdd:pfam13423 250 DLQGDNE---IVKYELRGVVVHiGDSGTSGHLVSFVkvADSELEDPTESQWYLFND 302
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1545-1910 |
1.26e-08 |
|
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: 60.02 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1545 EYLPpvgprppkGFVGLKNAGATCYMNSVIQQLYMIPSIRNSILaiegtgsdLHDDmfgdekqdsesnvdprddvfgYPH 1624
Cdd:cd02669 114 PYLP--------GFVGLNNIKNNDYANVIIQALSHVKPIRNFFL--------LYEN---------------------YEN 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1625 QFEDKPALSKTED---RKEYNIGVLRhlqvifGHLAASQLQYYVPRGFWKQFRLwgepvnlREQHDALEFFNSLVDSLde 1701
Cdd:cd02669 157 IKDRKSELVKRLSeliRKIWNPRNFK------GHVSPHELLQAVSKVSKKKFSI-------TEQSDPVEFLSWLLNTL-- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1702 alkalgHPAILSKVLGGSFADQKICQG---------CPHRYECEES----------------FTTLNVDIRN-----HQN 1751
Cdd:cd02669 222 ------HKDLGGSKKPNSSIIHDCFQGkvqietqkiKPHAEEEGSKdkffkdsrvkktsvspFLLLTLDLPPpplfkDGN 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1752 LLDSLEQYIKGDLLEGANAYHCEKCDKKVdtvKRLLIKKLPRVLAIQLKRFDYdwerecaikfNDYF--------EFPRE 1823
Cdd:cd02669 296 EENIIPQVPLKQLLKKYDGKTETELKDSL---KRYLISRLPKYLIFHIKRFSK----------NNFFkeknptivNFPIK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1824 LDMGPYTVAgvanlerDNVNSENElieqkeqsdnetagGTKYRLVGVLVHSGQASGGHYYSYIIQRNGkddqTDHWYKFD 1903
Cdd:cd02669 363 NLDLSDYVH-------FDKPSLNL--------------STKYNLVANIVHEGTPQEDGTWRVQLRHKS----TNKWFEIQ 417
|
....*..
gi 74319833 1904 DGDVTEC 1910
Cdd:cd02669 418 DLNVKEV 424
|
|
| Ubl_UBP24 |
cd17065 |
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and ... |
882-965 |
1.71e-08 |
|
ubiquitin-like (Ubl) domain found in ubiquitin carboxyl-terminal hydrolase 24 (UBP24) and similar proteins; UBP24 (EC 3.4.19.12), also termed deubiquitinating enzyme 24, or ubiquitin thioesterase 24, or ubiquitin-specific-processing protease 24 (USP24), is a deubiquitinating protein that interacts with damage-specific DNA-binding protein 2 (DDB2) and regulates DDB2 stability. It may also play a role in the pathogenesis of Parkinson's disease (PD). UBP24 proteins contain an N-terminal ubiquitin-associated (UBA) domain, a ubiquitin-like (Ubl) domain, and a C-terminal peptidase C19 domain.
Pssm-ID: 340585 Cd Length: 79 Bit Score: 53.47 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 882 FRGKHLSLIVRFPNQGrqvDELDIWSHTNDTIGSVRRCIVNRIKANVAHkkIELFVGGELIDSEDDRKLIGQLNLKDKSL 961
Cdd:cd17065 1 FHGHPLTLHVTCESTK---QEFTLEVHSNETLGSVRQKIAERLNCPVDQ--VQIFANEKLLPSNKDQKLLHQLGFTDEQI 75
|
....
gi 74319833 962 ITAK 965
Cdd:cd17065 76 LTVK 79
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1777-1956 |
1.01e-07 |
|
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: 55.61 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1777 DKKVDTVKRLL--------IKKLPRVLAIQLKRfdYDWERECAIKFNDYFEFPRELDMgPYTVAGvANLERDNVNSEnEL 1848
Cdd:cd02670 76 DGGGITLEQCLeqyfnnsvFAKAPSCLIICLKR--YGKTEGKAQKMFKKILIPDEIDI-PDFVAD-DPRACSKCQLE-CR 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1849 IEQKEQSDNETAGGTKYRLVGVLVHSGQA-SGGHYYSYIIQRNGKDDQTD------HWYKFDDgdvteckMDDDEemknq 1921
Cdd:cd02670 151 VCYDDKDFSPTCGKFKLSLCSAVCHRGTSlETGHYVAFVRYGSYSLTETDneaynaQWVFFDD-------MADRD----- 218
|
170 180 190
....*....|....*....|....*....|....*
gi 74319833 1922 cfGGEYmgeVFDHMMKRmsyrrqkRWWNAYILFYE 1956
Cdd:cd02670 219 --GVSN---GFNIPAAR-------LLEDPYMLFYQ 241
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1723-1909 |
3.20e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 42.11 E-value: 3.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1723 QKICQGCPHRYECEESFTTLNVDIRNHQNL-----LDSLEQYIKGDL-LEGANAYHCEKCDKKVDTVKRLLIKKLP---- 1792
Cdd:cd02672 81 SQDQLGTPFSCGTSRNSVSLLYTLSLPLGStktskESTFLQLLKRSLdLEKVTKAWCDTCCKYQPLEQTTSIRHLPdill 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74319833 1793 RVLAIQLKRFDydweRECAIKFNDYFEFpreldmgpytvagvanLERDNVNSENELIEQKEQSDNETAGGTKYRLVGVLV 1872
Cdd:cd02672 161 LVLVINLSVTN----GEFDDINVVLPSG----------------KVMQNKVSPKAIDHDKLVKNRGQESIYKYELVGYVC 220
|
170 180 190
....*....|....*....|....*....|....*...
gi 74319833 1873 H-SGQASGGHYYSYIIQRNGKDDQtDHWYKFDDGDVTE 1909
Cdd:cd02672 221 EiNDSSRGQHNVVFVIKVNEESTH-GRWYLFNDFLVTP 257
|
|
| |
