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Conserved domains on  [gi|1954668664|ref|NP_001376579|]
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ubiquitin carboxyl-terminal hydrolase 42 isoform 3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
110-410 0e+00

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: 564.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  110 GAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQAHITQALSNPGDVIKPMFVINEMRRIARH 189
Cdd:cd02661      1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  190 FRFGNQEDAHEFLQYTVDAMQKACLNGSNKL---DRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKA 266
Cdd:cd02661     81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  267 AQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQ 346
Cdd:cd02661    161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954668664  347 PNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 410
Cdd:cd02661    241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
735-940 9.42e-12

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 69.63  E-value: 9.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  735 APGAERGPPEDRDAEPQPGSPAAESleEPDAaaglsSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTA 814
Cdd:PRK07764   589 GPAPGAAGGEGPPAPASSGPPEEAA--RPAA-----PAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPD 661
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  815 PPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPE 894
Cdd:PRK07764   662 ASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPL 741
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1954668664  895 aaerPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKE 940
Cdd:PRK07764   742 ----PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
PRK12678 super family cl36163
transcription termination factor Rho; Provisional
846-1113 3.47e-04

transcription termination factor Rho; Provisional


The actual alignment was detected with superfamily member PRK12678:

Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.89  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  846 SALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVE 925
Cdd:PRK12678    53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  926 DAAAPKAPGPSPAKEKIGSLRKVDRGHyrsrRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDR 1005
Cdd:PRK12678   133 RGEAARRGAARKAGEGGEQPATEARAD----AAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDR 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 1006 LSPGERRslgrcSHHHSRHRsgveldwvrhhytEGERGWGRekfypDRPRWDRCRYYHDRYALYAARDWKPFHGGReher 1085
Cdd:PRK12678   209 REQGDRR-----EERGRRDG-------------GDRRGRRR-----RRDRRDARGDDNREDRGDRDGDDGEGRGGR---- 261
                          250       260
                   ....*....|....*....|....*...
gi 1954668664 1086 aglherphkdhnRGRRGcepaRERERHR 1113
Cdd:PRK12678   262 ------------RGRRF----RDRDRRG 273
PHA03247 super family cl33720
large tegument protein UL36; Provisional
422-938 4.95e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  422 THPTHSPGQSSPRPVISQRVVTNKQAAPGFIGPQLPSHMIKNP---PHLNGTGPLKDTPSSSMSSPNGNSSVNRASPVNA 498
Cdd:PHA03247  2587 RRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPspsPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR 2666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  499 SASVQNWSvnRSSVIPEHPKKQKITISIHnklPVRQCQSQPnlhsnSLENPTKPVPSSTITNSAVQSTSNASTMSVSSKV 578
Cdd:PHA03247  2667 ARRLGRAA--QASSPPQRPRRRAARPTVG---SLTSLADPP-----PPPPTPEPAPHALVSATPLPPGPAAARQASPALP 2736
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  579 TKPIPRSeSCSQPVMNGKSKLNSSVLVPYGAESSEDSDEESKGLGKEngiGTIVSSHSPGQDAEDEEATPHELQEPMTLN 658
Cdd:PHA03247  2737 AAPAPPA-VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR---LTRPAVASLSESRESLPSPWDPADPPAAVL 2812
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  659 GANSADSDSDPKENGLAPDGASCQGQPALHSEnPFAKANGLPGKLMPAPLLSlpedkiletfrlsnKLKGSTDEMSAPGA 738
Cdd:PHA03247  2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPG-PPPPSLPLGGSVAPGGDVR--------------RRPPSRSPAAKPAA 2877
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  739 ERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTAPPDL 818
Cdd:PHA03247  2878 PARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  819 CDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPeglSPAPPARSEEP----CEQPLLVHPSGDHArdAQDPSQSLGAPE 894
Cdd:PHA03247  2958 AVPQPWLGALVPGRVAVPRFRVPQPAPSREAPAS---STPPLTGHSLSrvssWASSLALHEETDPP--PVSLKQTLWPPD 3032
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1954668664  895 AAERPPAPVLDMAPAGHPEGDA-EPSPGERVEDAAAPKAPGPSPA 938
Cdd:PHA03247  3033 DTEDSDADSLFDSDSERSDLEAlDPLPPEPHDPFAHEPDPATPEA 3077
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
110-410 0e+00

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: 564.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  110 GAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQAHITQALSNPGDVIKPMFVINEMRRIARH 189
Cdd:cd02661      1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  190 FRFGNQEDAHEFLQYTVDAMQKACLNGSNKL---DRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKA 266
Cdd:cd02661     81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  267 AQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQ 346
Cdd:cd02661    161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954668664  347 PNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 410
Cdd:cd02661    241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
111-409 1.29e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 261.99  E-value: 1.29e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  111 AGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFC--MMCTMQAHITQALSN-PGDVIKPMFVINEMRRIA 187
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNsKSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  188 RHFRFGNQEDAHEFLQYTVDAMQKAClngsnKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAA 267
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  268 QSV------NKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA--NFTGGKIAKDVKYPEYLD 339
Cdd:pfam00443  156 SAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1954668664  340 IRPYMSQPNGEPIV----YVLYAVLVHTGfNCHAGHYFCYIKA-SNGLWYQMNDSIVSTSD-IRSVLSQQAYVLFY 409
Cdd:pfam00443  236 LSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
112-411 3.28e-25

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 113.81  E-value: 3.28e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYTPPLAN--YMLSHEHSKTCHAEGFCMM-CTMQahiTQALSNPGDVIKpmFVINEMRRIAR 188
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRGRDSVALALQrLFYN---LQTGEEPVDTTE--LTRSFGWDSDD 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  189 HFrfgNQEDAHEFLQYTVDAMQKAClngsnkldRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQ 268
Cdd:COG5077    270 SF---MQHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMK 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  269 SVNKALEQFVKPEQLDGENSYKCSKcKKMVPASKRFTIHRSSNVLTLSLKRF-ANFTGG---KIAKDVKYPEYLDIRPYM 344
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFL 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  345 S----QPNGEPIVYVLYAVLVHTGfNCHAGHYFCYIKAS-NGLWYQMNDSIVSTSDIRSVLSQ----------------- 402
Cdd:COG5077    418 DrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsg 496
                          330
                   ....*....|....
gi 1954668664  403 -----QAYVLFYIR 411
Cdd:COG5077    497 ikrfmSAYMLVYLR 510
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
735-940 9.42e-12

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 69.63  E-value: 9.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  735 APGAERGPPEDRDAEPQPGSPAAESleEPDAaaglsSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTA 814
Cdd:PRK07764   589 GPAPGAAGGEGPPAPASSGPPEEAA--RPAA-----PAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPD 661
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  815 PPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPE 894
Cdd:PRK07764   662 ASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPL 741
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1954668664  895 aaerPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKE 940
Cdd:PRK07764   742 ----PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
PRK12678 PRK12678
transcription termination factor Rho; Provisional
846-1113 3.47e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.89  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  846 SALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVE 925
Cdd:PRK12678    53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  926 DAAAPKAPGPSPAKEKIGSLRKVDRGHyrsrRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDR 1005
Cdd:PRK12678   133 RGEAARRGAARKAGEGGEQPATEARAD----AAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDR 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 1006 LSPGERRslgrcSHHHSRHRsgveldwvrhhytEGERGWGRekfypDRPRWDRCRYYHDRYALYAARDWKPFHGGReher 1085
Cdd:PRK12678   209 REQGDRR-----EERGRRDG-------------GDRRGRRR-----RRDRRDARGDDNREDRGDRDGDDGEGRGGR---- 261
                          250       260
                   ....*....|....*....|....*...
gi 1954668664 1086 aglherphkdhnRGRRGcepaRERERHR 1113
Cdd:PRK12678   262 ------------RGRRF----RDRDRRG 273
PHA03247 PHA03247
large tegument protein UL36; Provisional
422-938 4.95e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  422 THPTHSPGQSSPRPVISQRVVTNKQAAPGFIGPQLPSHMIKNP---PHLNGTGPLKDTPSSSMSSPNGNSSVNRASPVNA 498
Cdd:PHA03247  2587 RRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPspsPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR 2666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  499 SASVQNWSvnRSSVIPEHPKKQKITISIHnklPVRQCQSQPnlhsnSLENPTKPVPSSTITNSAVQSTSNASTMSVSSKV 578
Cdd:PHA03247  2667 ARRLGRAA--QASSPPQRPRRRAARPTVG---SLTSLADPP-----PPPPTPEPAPHALVSATPLPPGPAAARQASPALP 2736
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  579 TKPIPRSeSCSQPVMNGKSKLNSSVLVPYGAESSEDSDEESKGLGKEngiGTIVSSHSPGQDAEDEEATPHELQEPMTLN 658
Cdd:PHA03247  2737 AAPAPPA-VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR---LTRPAVASLSESRESLPSPWDPADPPAAVL 2812
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  659 GANSADSDSDPKENGLAPDGASCQGQPALHSEnPFAKANGLPGKLMPAPLLSlpedkiletfrlsnKLKGSTDEMSAPGA 738
Cdd:PHA03247  2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPG-PPPPSLPLGGSVAPGGDVR--------------RRPPSRSPAAKPAA 2877
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  739 ERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTAPPDL 818
Cdd:PHA03247  2878 PARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  819 CDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPeglSPAPPARSEEP----CEQPLLVHPSGDHArdAQDPSQSLGAPE 894
Cdd:PHA03247  2958 AVPQPWLGALVPGRVAVPRFRVPQPAPSREAPAS---STPPLTGHSLSrvssWASSLALHEETDPP--PVSLKQTLWPPD 3032
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1954668664  895 AAERPPAPVLDMAPAGHPEGDA-EPSPGERVEDAAAPKAPGPSPA 938
Cdd:PHA03247  3033 DTEDSDADSLFDSDSERSDLEAlDPLPPEPHDPFAHEPDPATPEA 3077
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
732-939 6.16e-04

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 43.90  E-value: 6.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  732 EMSAPG----AERGPPEDRDAEPQPGSPAAESLEEPDAAA------------GLSSTKKAPPP-------RDPGTPATKE 788
Cdd:COG5180    254 EMRPPAdakeRRRAAIGDTPAAEPPGLPVLEAGSEPQSDApeaetarpidvkGVASAPPATRPvrppggaRDPGTPRPGQ 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  789 GAWEAMAV----APEEPPPS----AGEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAP-------- 852
Cdd:COG5180    334 PTERPAGVpeaaSDAGQPPSayppAEEAVPGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMgagdlvqa 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  853 EGLSPAPPARSEEPCEQPLLVHPSGDH-ARDAQDPSQSLGAPEAAERPPAPVldMAPAGHPEGDAePSPGERVEDAAAPK 931
Cdd:COG5180    414 ALDGGGRETASLGGAAGGAGQGPKADFvPGDAESVSGPAGLADQAGAAASTA--MADFVAPVTDA-TPVDVADVLGVRPD 490

                   ....*...
gi 1954668664  932 APGPSPAK 939
Cdd:COG5180    491 AILGGNVA 498
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
761-939 1.64e-03

N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF14.


Pssm-ID: 409238 [Multi-domain]  Cd Length: 195  Bit Score: 41.34  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  761 EEPDAAAGLSSTKKAPPPRDPGtPATKEGAWEAMAVAPEEPPPSAGedivgDTAPPDLCdpgsltgdASPLSqDAKGMIA 840
Cdd:cd21576     32 EGAGGAAGSEVGAAPPESALPG-PGPPGPAWVPPLLQVPAPSPGAG-----GAAPHLLA--------ASVLA-DLRGGAG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  841 EGPRDSALaEAPEGLSPAP-PARSEEPCEQPLLVHPSGDHArdAQDPSQSLGAPEAAERPPAPvldmapaghpegdaePS 919
Cdd:cd21576     97 EGSREDSG-EAPRASSGSSdPARGSSPTLGSEPAPASGEDA--VSGPESSFGAPAIPSAPAAP---------------GA 158
                          170       180
                   ....*....|....*....|
gi 1954668664  920 PGERVEDAAAPKAPGPSPAK 939
Cdd:cd21576    159 PAVSGEVPGGAPGAGPAPAA 178
 
Name Accession Description Interval E-value
Peptidase_C19E cd02661
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
110-410 0e+00

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: 564.21  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  110 GAGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMQAHITQALSNPGDVIKPMFVINEMRRIARH 189
Cdd:cd02661      1 GAGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCNEGFCMMCALEAHVERALASSGPGSAPRIFSSNLKQISKH 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  190 FRFGNQEDAHEFLQYTVDAMQKACLNGSNKL---DRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKA 266
Cdd:cd02661     81 FRIGRQEDAHEFLRYLLDAMQKACLDRFKKLkavDPSSQETTLVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLSLDIKG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  267 AQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQ 346
Cdd:cd02661    161 ADSLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGGKINKQISFPETLDLSPYMSQ 240
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954668664  347 PNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 410
Cdd:cd02661    241 PNDGPLKYKLYAVLVHSGFSPHSGHYYCYVKSSNGKWYNMDDSKVSPVSIETVLSQKAYILFYI 304
UCH pfam00443
Ubiquitin carboxyl-terminal hydrolase;
111-409 1.29e-78

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 425685 [Multi-domain]  Cd Length: 310  Bit Score: 261.99  E-value: 1.29e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  111 AGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFC--MMCTMQAHITQALSN-PGDVIKPMFVINEMRRIA 187
Cdd:pfam00443    1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDinLLCALRDLFKALQKNsKSSSVSPKMFKKSLGKLN 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  188 RHFRFGNQEDAHEFLQYTVDAMQKAClngsnKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAA 267
Cdd:pfam00443   81 PDFSGYKQQDAQEFLLFLLDGLHEDL-----NGNHSTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGD 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  268 QSV------NKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA--NFTGGKIAKDVKYPEYLD 339
Cdd:pfam00443  156 SAElktaslQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHLKRFSynRSTWEKLNTEVEFPLELD 235
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1954668664  340 IRPYMSQPNGEPIV----YVLYAVLVHTGfNCHAGHYFCYIKA-SNGLWYQMNDSIVSTSD-IRSVLSQQAYVLFY 409
Cdd:pfam00443  236 LSRYLAEELKPKTNnlqdYRLVAVVVHSG-SLSSGHYIAYIKAyENNRWYKFDDEKVTEVDeETAVLSSSAYILFY 310
Peptidase_C19D cd02660
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
112-410 1.28e-71

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: 242.66  E-value: 1.28e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEG--FCMMCTMqAHITQALSNPGDVIK--PMFVINEMRRIA 187
Cdd:cd02660      2 GLINLGATCFMNVILQALLHNPLLRNYFLSDRHSCTCLSCSpnSCLSCAM-DEIFQEFYYSGDRSPygPINLLYLSWKHS 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  188 RHFRFGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIK-- 265
Cdd:cd02660     81 RNLAGYSQQDAHEFFQFLLDQLHTHYGGDKNEANDESHCNCIIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLDIPnk 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  266 ------AAQSVNKA-------LEQFVKPEQLdGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFANFTGG---KIA 329
Cdd:cd02660    161 stpswaLGESGVSGtptlsdcLDRFTRPEKL-GDFAYKCSGCGSTQEATKQLSIKKLPPVLCFQLKRFEHSLNKtsrKID 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  330 KDVKYPEYLDIRPYMSQPNGEP---------IVYVLYAVLVHTGfNCHAGHYFCYIKASNGLWYQMNDSIVSTSDIRSVL 400
Cdd:cd02660    240 TYVQFPLELNMTPYTSSSIGDTqdsnsldpdYTYDLFAVVVHKG-TLDTGHYTAYCRQGDGQWFKFDDAMITRVSEEEVL 318
                          330
                   ....*....|
gi 1954668664  401 SQQAYVLFYI 410
Cdd:cd02660    319 KSQAYLLFYH 328
Peptidase_C19 cd02257
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ...
112-410 6.59e-69

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: 231.99  E-value: 6.59e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLtytpplanymlshehsktchaegfcmmctmqahitqalsnpgdvikpmfvinemrriarhfr 191
Cdd:cd02257      1 GLNNLGNTCYLNSVLQAL-------------------------------------------------------------- 18
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  192 FGNQEDAHEFLQYTVDAMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI----KAA 267
Cdd:cd02257     19 FSEQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSLKSLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQ 98
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  268 QSVNKALEQFVKPEQLDGENSYKCSKCKKmVPASKRFTIHRSSNVLTLSLKRFA---NFTGGKIAKDVKYPEYLDIRPYM 344
Cdd:cd02257     99 VSLEDCLEKFFKEEILEGDNCYKCEKKKK-QEATKRLKIKKLPPVLIIHLKRFSfneDGTKEKLNTKVSFPLELDLSPYL 177
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954668664  345 SQP------NGEPIVYVLYAVLVHTGFNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVL-----SQQAYVLFYI 410
Cdd:cd02257    178 SEGekdsdsDNGSYKYELVAVVVHSGTSADSGHYVAYVKdPSDGKWYKFNDDKVTEVSEEEVLefgslSSSAYILFYE 255
Peptidase_C19R cd02674
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
112-410 1.57e-53

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: 187.11  E-value: 1.57e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLtytpplanymlshehsktchaegfcmmctmqahitqalsnpgdvikpmfvinemrriarhfr 191
Cdd:cd02674      1 GLRNLGNTCYMNSILQCL-------------------------------------------------------------- 18
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  192 FGNQEDAHEFLQYTVDAMqkaclngsnkldrHTqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEI------K 265
Cdd:cd02674     19 SADQQDAQEFLLFLLDGL-------------HS----IIVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdA 81
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  266 AAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFaNFTGG---KIAKDVKYP-EYLDIR 341
Cdd:cd02674     82 PKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKRF-SFSRGstrKLTTPVTFPlNDLDLT 160
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1954668664  342 PY-MSQPNGEPIVYVLYAVLVHTG-FNChaGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYI 410
Cdd:cd02674    161 PYvDTRSFTGPFKYDLYAVVNHYGsLNG--GHYTAYCKnNETNDWYKFDDSRVTKVSESSVVSSSAYILFYE 230
Peptidase_C19K cd02667
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
112-409 7.98e-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: 181.05  E-value: 7.98e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYTPPLANYMLShehsktchaegfcmmctmqahitqalsNPgdviKPMFviNEMRRIARHFR 191
Cdd:cd02667      1 GLSNLGNTCFFNAVMQNLSQTPALRELLSE---------------------------TP----KELF--SQVCRKAPQFK 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  192 FGNQEDAHEFLQYTVDAMQkaclngsnkldrhtqatTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITL----EIKAA 267
Cdd:cd02667     48 GYQQQDSHELLRYLLDGLR-----------------TFIDSIFGGELTSTIMCESCGTVSLVYEPFLDLSLprsdEIKSE 110
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  268 QSVNKALEQFVKPEQLDGENSYKCSKCKKmvpASKRFTIHRSSNVLTLSLKRF-----ANFTggKIAKDVKYPEYLDIRP 342
Cdd:cd02667    111 CSIESCLKQFTEVEILEGNNKFACENCTK---AKKQYLISKLPPVLVIHLKRFqqprsANLR--KVSRHVSFPEILDLAP 185
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  343 YMSQPN-----GEPIVYVLYAVLVHTGfNCHAGHYFCYIKASN----------------------GLWYQMNDSIVSTSD 395
Cdd:cd02667    186 FCDPKCnssedKSSVLYRLYGVVEHSG-TMRSGHYVAYVKVRPpqqrlsdltkskpaadeagpgsGQWYYISDSDVREVS 264
                          330
                   ....*....|....
gi 1954668664  396 IRSVLSQQAYVLFY 409
Cdd:cd02667    265 LEEVLKSEAYLLFY 278
peptidase_C19C cd02659
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
112-412 1.03e-50

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: 182.84  E-value: 1.03e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYTPPLAN--YMLSHEHSKTCHAEGFCMMcTMQAHITQALSNPGDVIKPMfvinemrriARH 189
Cdd:cd02659      4 GLKNQGATCYMNSLLQQLYMTPEFRNavYSIPPTEDDDDNKSVPLAL-QRLFLFLQLSESPVKTTELT---------DKT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  190 FRFG-------NQEDAHEFLQYTVDAMQkaclNGSNKLDRHTqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITL 262
Cdd:cd02659     74 RSFGwdslntfEQHDVQEFFRVLFDKLE----EKLKGTGQEG----LIKNLFGGKLVNYIICKECPHESEREEYFLDLQV 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  263 EIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-NFTGGKIAKD---VKYPEYL 338
Cdd:cd02659    146 AVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTLQLKRFEfDFETMMRIKIndrFEFPLEL 225
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  339 DIRPYMSQPNG-----------EPIVYVLYAVLVHTGfNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQ--- 403
Cdd:cd02659    226 DMEPYTEKGLAkkegdsekkdsESYIYELHGVLVHSG-DAHGGHYYSYIKdRDDGKWYKFNDDVVTPFDPNDAEEECfgg 304
                          330       340
                   ....*....|....*....|....*...
gi 1954668664  404 -------------------AYVLFYIRS 412
Cdd:cd02659    305 eetqktydsgprafkrttnAYMLFYERK 332
Peptidase_C19G cd02663
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
112-409 6.16e-44

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: 162.09  E-value: 6.16e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYtpplaNYMLshehskTCHAEGFCMMctmqahITQALSnpGDVIKPMFVINEMRRIARHFR 191
Cdd:cd02663      1 GLENFGNTCYCNSVLQALYF-----ENLL------TCLKDLFESI------SEQKKR--TGVISPKKFITRLKRENELFD 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  192 FGNQEDAHEFLQY-------TVDAMQKACL---NGSNKLDRHTQaTTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDIT 261
Cdd:cd02663     62 NYMHQDAHEFLNFllneiaeILDAERKAEKanrKLNNNNNAEPQ-PTWVHEIFQGILTNETRCLTCETVSSRDETFLDLS 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  262 LEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFAnFTGG-----KIAKDVKYPE 336
Cdd:cd02663    141 IDVEQNTSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKRFK-YDEQlnryiKLFYRVVFPL 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  337 YLdiRPYMSQPNGEP--IVYVLYAVLVHTGFNCHAGHYFCYIKaSNGLWYQMNDSIVSTSDIRSVL--------SQQAYV 406
Cdd:cd02663    220 EL--RLFNTTDDAENpdRLYELVAVVVHIGGGPNHGHYVSIVK-SHGGWLLFDDETVEKIDENAVEeffgdspnQATAYV 296

                   ...
gi 1954668664  407 LFY 409
Cdd:cd02663    297 LFY 299
Peptidase_C19L cd02668
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
112-409 6.89e-41

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: 154.12  E-value: 6.89e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYTPPLANYMLShehsktchaegfcmmCTMQAHITQALSNPGDVIKPMFVINEMRRIARHFR 191
Cdd:cd02668      1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYE---------------CNSTEDAELKNMPPDKPHEPQTIIDQLQLIFAQLQ 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  192 FGN-------------------QEDAHEFLQYTVDAMQkACLNGSNKLDrhtqATTLVCQIFGGYLRSRVKCLNCKGVSD 252
Cdd:cd02668     66 FGNrsvvdpsgfvkalgldtgqQQDAQEFSKLFLSLLE-AKLSKSKNPD----LKNIVQDLFRGEYSYVTQCSKCGRESS 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  253 TFDPYLDITLEIKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFAnF---TGG--K 327
Cdd:cd02668    141 LPSKFYELELQLKGHKTLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLRFV-FdrkTGAkkK 219
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  328 IAKDVKYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGFNCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVL------ 400
Cdd:cd02668    220 LNASISFPEILDMGEYLAESDEGSYVYELSGVLIHQGVSAYSGHYIAHIKdEQTGEWYKFNDEDVEEMPGKPLKlgnsed 299
                          330       340
                   ....*....|....*....|....
gi 1954668664  401 ---------------SQQAYVLFY 409
Cdd:cd02668    300 pakprkseikkgthsSRTAYMLVY 323
Peptidase_C19H cd02664
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
112-409 8.91e-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: 239129 [Multi-domain]  Cd Length: 327  Bit Score: 139.16  E-value: 8.91e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKT--CHAEGFCM-MCTMQAHITQALSNPgdviKPMFVINEMRriAR 188
Cdd:cd02664      1 GLINLGNTCYMNSVLQALFMAKDFRRQVLSLNLPRLgdSQSVMKKLqLLQAHLMHTQRRAEA----PPDYFLEASR--PP 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  189 HFRFGNQEDAHEFLQYTVDamqkaclngsnKLDrhtqatTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLeikAAQ 268
Cdd:cd02664     75 WFTPGSQQDCSEYLRYLLD-----------RLH------TLIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDL---SFP 134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  269 SVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-NFTGG---KIAKDVKYPEYLD--IRP 342
Cdd:cd02664    135 SVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSyDQKTHvreKIMDNVSINEVLSlpVRV 214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  343 YMS----------QPNGE-------PIVYVLYAVLVHTGFNCHAGHYFCYI---------------------KASNGLWY 384
Cdd:cd02664    215 ESKssesplekkeEESGDdgelvtrQVHYRLYAVVVHSGYSSESGHYFTYArdqtdadstgqecpepkdaeeNDESKNWY 294
                          330       340       350
                   ....*....|....*....|....*....|..
gi 1954668664  385 QMNDSIVS---TSDIRSVLS----QQAYVLFY 409
Cdd:cd02664    295 LFNDSRVTfssFESVQNVTSrfpkDTPYILFY 326
Peptidase_C19B cd02658
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
112-409 2.62e-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 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: 113.96  E-value: 2.62e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEG--FCMMCTMqAHITQAL-----SNPGDV----------I 174
Cdd:cd02658      1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDDLENKFPSDVVDpaNDLNCQL-IKLADGLlsgrySKPASLksendpyqvgI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  175 KP-MF--VI---NEMrriarhFRFGNQEDAHEFLQYTVDAMQKACLNgsnkldRHTQATTlvcQIFGGYLRSRVKCLNCK 248
Cdd:cd02658     80 KPsMFkaLIgkgHPE------FSTMRQQDALEFLLHLIDKLDRESFK------NLGLNPN---DLFKFMIEDRLECLSCK 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  249 GVSDTFD---------PYLDIT-----LEIKAAQSVNKALEQFVKPEQLDgensYKCSKCKKMVPASKRFTIHRSSNVLT 314
Cdd:cd02658    145 KVKYTSElseilslpvPKDEATekeegELVYEPVPLEDCLKAYFAPETIE----DFCSTCKEKTTATKTTGFKTFPDYLV 220
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  315 LSLKRFA---NFTGGKIAKDVKYPEYLDIRPYMsqpngepivyvLYAVLVHTGFNCHAGHYFCYIK---ASNGLWYQMND 388
Cdd:cd02658    221 INMKRFQlleNWVPKKLDVPIDVPEELGPGKYE-----------LIAFISHKGTSVHSGHYVAHIKkeiDGEGKWVLFND 289
                          330       340
                   ....*....|....*....|.
gi 1954668664  389 SIVSTSDIRSVLSQQAYVLFY 409
Cdd:cd02658    290 EKVVASQDPPEMKKLGYIYFY 310
Peptidase_C19O cd02671
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
111-409 6.83e-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: 239136 [Multi-domain]  Cd Length: 332  Bit Score: 110.37  E-value: 6.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  111 AGLQNLGNTCFANAALQCLTYTPPLAN---YMLSHEHSKTCHAEGFCMMCTM--QAHITQAlsnpgdvikPMFVINEMRR 185
Cdd:cd02671     25 VGLNNLGNTCYLNSVLQVLYFCPGFKHglkHLVSLISSVEQLQSSFLLNPEKynDELANQA---------PRRLLNALRE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  186 IARHFRFGNQEDAHEFLQYTVDAMQKaclngsnkldrhtqattLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDIT---- 261
Cdd:cd02671     96 VNPMYEGYLQHDAQEVLQCILGNIQE-----------------LVEKDFQGQLVLRTRCLECETFTERREDFQDISvpvq 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  262 ------------------LEIKAAQsvnKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA-- 321
Cdd:cd02671    159 eselskseesseispdpkTEMKTLK---WAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKLPEVITIHLKCFAan 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  322 ----NFTGG--KIAKDVKYPEYLDIRPYMSQPNGEpiVYVLYAVLVHTGFNCHAGHYFCYIKasnglWYQMNDS---IVS 392
Cdd:cd02671    236 gsefDCYGGlsKVNTPLLTPLKLSLEEWSTKPKND--VYRLFAVVMHSGATISSGHYTAYVR-----WLLFDDSevkVTE 308
                          330       340
                   ....*....|....*....|...
gi 1954668664  393 TSDIRSVLSQQA------YVLFY 409
Cdd:cd02671    309 EKDFLEALSPNTsststpYLLFY 331
COG5077 COG5077
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ...
112-411 3.28e-25

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


Pssm-ID: 227409 [Multi-domain]  Cd Length: 1089  Bit Score: 113.81  E-value: 3.28e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYTPPLAN--YMLSHEHSKTCHAEGFCMM-CTMQahiTQALSNPGDVIKpmFVINEMRRIAR 188
Cdd:COG5077    195 GLRNQGATCYMNSLLQSLFFIAKFRKdvYGIPTDHPRGRDSVALALQrLFYN---LQTGEEPVDTTE--LTRSFGWDSDD 269
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  189 HFrfgNQEDAHEFLQYTVDAMQKAClngsnkldRHTQATTLVCQIFGGYLRSRVKCLNCKGVSDTFDPYLDITLEIKAAQ 268
Cdd:COG5077    270 SF---MQHDIQEFNRVLQDNLEKSM--------RGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMK 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  269 SVNKALEQFVKPEQLDGENSYKCSKcKKMVPASKRFTIHRSSNVLTLSLKRF-ANFTGG---KIAKDVKYPEYLDIRPYM 344
Cdd:COG5077    339 NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFeYDFERDmmvKINDRYEFPLEIDLLPFL 417
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  345 S----QPNGEPIVYVLYAVLVHTGfNCHAGHYFCYIKAS-NGLWYQMNDSIVSTSDIRSVLSQ----------------- 402
Cdd:COG5077    418 DrdadKSENSDAVYVLYGVLVHSG-DLHEGHYYALLKPEkDGRWYKFDDTRVTRATEKEVLEEnfggdhpykdkirdhsg 496
                          330
                   ....*....|....
gi 1954668664  403 -----QAYVLFYIR 411
Cdd:COG5077    497 ikrfmSAYMLVYLR 510
COG5533 COG5533
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
112-411 1.53e-23

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


Pssm-ID: 444284 [Multi-domain]  Cd Length: 284  Bit Score: 102.19  E-value: 1.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLT-YTPPLANYM---------LSHEHSKTCHAEGFCMMctmqahiTQALSNpgdvikpmFVIN 181
Cdd:COG5533      1 GLPNLGNTCFMNSVLQILAlYLPKLDELLddlskelkvLKNVIRKPEPDLNQEEA-------LKLFTA--------LWSS 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  182 EMRRIARHFRFGNQEDAHEFLQYTVDAMqkaclngsnKLDRHTQATTLVCQIFGGYLRSrvkclnckgvsdTFDPYLDIT 261
Cdd:COG5533     66 KEHKVGWIPPMGSQEDAHELLGKLLDEL---------KLDLVNSFTIRIFKTTKDKKKT------------STGDWFDII 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  262 LEIKAAQSVN--KALEQFVKP--EQLD-------GENSYKCSKCKKMVPASKRftihRSSNVLTLSLKRFANFTGG-KIA 329
Cdd:COG5533    125 IELPDQTWVNnlKTLQEFIDNmeELVDdetgvkaKENEELEVQAKQEYEVSFV----KLPKILTIQLKRFANLGGNqKID 200
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  330 KDVKYPEYLDIRPYMSQPNGEPIVYVLYAVLVHTGfNCHAGHYFCYIKaSNGLWYQMNDSIVST---SDIRSVLSQQAYV 406
Cdd:COG5533    201 TEVDEKFELPVKHDQILNIVKETYYDLVGFVLHQG-SLEGGHYIAYVK-KGGKWEKANDSDVTPvseEEAINEKAKNAYL 278

                   ....*
gi 1954668664  407 LFYIR 411
Cdd:COG5533    279 YFYER 283
Peptidase_C19A cd02657
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
112-409 1.85e-23

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: 102.41  E-value: 1.85e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYTPP----LANYMLSHEHSktchaegfcmmctMQAHIT---------QALSNPGDVIKPMF 178
Cdd:cd02657      1 GLTNLGNTCYLNSTLQCLRSVPElrdaLKNYNPARRGA-------------NQSSDNltnalrdlfDTMDKKQEPVPPIE 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  179 VINEMRriaRHF-RFGNQEDAHEFLQytvdamQKA--CLNG-----SNKLDRHTQATTLVCQIFGGYLRSRVKCL-NCKG 249
Cdd:cd02657     68 FLQLLR---MAFpQFAEKQNQGGYAQ------QDAeeCWSQllsvlSQKLPGAGSKGSFIDQLFGIELETKMKCTeSPDE 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  250 VSDTFDP------YLDITLEIKAAQS-VNKALEQFVK--PEQLDGENSYkcskckkmvpaSKRFTIHRSSNVLTLSLKRF 320
Cdd:cd02657    139 EEVSTESeyklqcHISITTEVNYLQDgLKKGLEEEIEkhSPTLGRDAIY-----------TKTSRISRLPKYLTVQFVRF 207
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  321 -----ANfTGGKIAKDVKYPEYLDIRPYMSqPNGepiVYVLYAVLVHTGFNCHAGHYFCYIKASN-GLWYQMND---SIV 391
Cdd:cd02657    208 fwkrdIQ-KKAKILRKVKFPFELDLYELCT-PSG---YYELVAVITHQGRSADSGHYVAWVRRKNdGKWIKFDDdkvSEV 282
                          330       340
                   ....*....|....*....|...
gi 1954668664  392 STSDIRSvLS-----QQAYVLFY 409
Cdd:cd02657    283 TEEDILK-LSgggdwHIAYILLY 304
Peptidase_C19F cd02662
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
112-409 3.36e-22

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: 97.05  E-value: 3.36e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYTPPLANYmlshehsktchaegfcmmctmqahitqalsnpgdvikpmfvINemrriarhfR 191
Cdd:cd02662      1 GLVNLGNTCFMNSVLQALASLPSLIEY-----------------------------------------LE---------E 30
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  192 FGNQEDAHEFLQYTVDAMQKACLNgsnkldrhtqattlvcqIFGGYLRSRVKCLNCKGVS-DTFDPYLDITLEIKAAQSV 270
Cdd:cd02662     31 FLEQQDAHELFQVLLETLEQLLKF-----------------PFDGLLASRIVCLQCGESSkVRYESFTMLSLPVPNQSSG 93
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  271 NKA-----LEQFVKPEQLDGensYKCSKCK-KMVPASKRFTIH--RSS-NVLTLSLKRFANftggkiakdVKYPEYLdiR 341
Cdd:cd02662     94 SGTtlehcLDDFLSTEIIDD---YKCDRCQtVIVRLPQILCIHlsRSVfDGRGTSTKNSCK---------VSFPERL--P 159
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  342 PYMsqpngepivYVLYAVLVHTGFnCHAGHYFCY--------------------IKASNGL-WYQMNDSIVSTSDIRSVL 400
Cdd:cd02662    160 KVL---------YRLRAVVVHYGS-HSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHpWWRISDTTVKEVSESEVL 229
                          330
                   ....*....|
gi 1954668664  401 SQ-QAYVLFY 409
Cdd:cd02662    230 EQkSAYMLFY 239
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
269-413 2.37e-20

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 97.65  E-value: 2.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  269 SVNKALEQFVKPEQLDGENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRFA--NFTGGKIAKDVKYP-EYLDIRPYMS 345
Cdd:COG5560    676 TLQDCLNEFSKPEQLGLSDSWYCPGCKEFRQASKQMELWRLPMILIIHLKRFSsvRSFRDKIDDLVEYPiDDLDLSGVEY 755
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1954668664  346 QPNGEPIVYVLYAVLVHTGFnCHAGHYFCYIK-ASNGLWYQMNDSIVSTSDIRSVLSQQAYVLFYIRSH 413
Cdd:COG5560    756 MVDDPRLIYDLYAVDNHYGG-LSGGHYTAYARnFANNGWYLFDDSRITEVDPEDSVTSSAYVLFYRRKS 823
UBP12 COG5560
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
112-264 1.25e-14

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


Pssm-ID: 227847 [Multi-domain]  Cd Length: 823  Bit Score: 79.16  E-value: 1.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGfcmMCTMQAHITQALSnpgDVIKPMFVINEMRRIARHFR 191
Cdd:COG5560    267 GLRNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEEN---PLGMHGSVASAYA---DLIKQLYDGNLHAFTPSGFK 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  192 F----------GN-QEDAHEFLQYTVDAMQKAcLN------------------------GSNKLDRHTQAT-TLVCQIFG 235
Cdd:COG5560    341 KtigsfneefsGYdQQDSQEFIAFLLDGLHED-LNriikkpytskpdlspgddvvvkkkAKECWWEHLKRNdSIITDLFQ 419
                          170       180
                   ....*....|....*....|....*....
gi 1954668664  236 GYLRSRVKCLNCKGVSDTFDPYLDITLEI 264
Cdd:COG5560    420 GMYKSTLTCPGCGSVSITFDPFMDLTLPL 448
UCH_1 pfam13423
Ubiquitin carboxyl-terminal hydrolase;
111-391 6.13e-14

Ubiquitin carboxyl-terminal hydrolase;


Pssm-ID: 463872 [Multi-domain]  Cd Length: 305  Bit Score: 74.23  E-value: 6.13e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  111 AGLQNLGNTCFANAALQCLTYTPPLANYMLSH-------EHS-----------------KTCHAEGFCmmctmqahitQA 166
Cdd:pfam13423    1 SGLETHIPNSYTNSLLQLLRFIPPLRNLALSHlateclkEHCllcelgflfdmlekakgKNCQASNFL----------RA 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  167 LSNPGDViKPMFVINEMRRIARHFRFGNQEDA-HEFLqytvdaMQKACLNGSNKLDRHTQATTLVCQIFGGYLRSRVKCL 245
Cdd:pfam13423   71 LSSIPEA-SALGLLDEDRETNSAISLSSLIQSfNRFL------LDQLSSEENSTPPNPSPAESPLEQLFGIDAETTIRCS 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  246 NCKGVSDTFDPYLDITLEIKAAQSVNKALEQFVKPEQ-----LDGENSYK--CSKCKKMVPASKRFTIHRSSNVLTLSlk 318
Cdd:pfam13423  144 NCGHESVRESSTHVLDLIYPRKPSSNNKKPPNQTFSSilkssLERETTTKawCEKCKRYQPLESRRTVRNLPPVLSLN-- 221
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  319 rfANFTGGKIAKDVKYPEYL--DIRPYMS---QPNGEPIVYVLYAVLVHTGFNCHAGHYFCYIKASN--------GLWYQ 385
Cdd:pfam13423  222 --AALTNEEWRQLWKTPGWLppEIGLTLSddlQGDNEIVKYELRGVVVHIGDSGTSGHLVSFVKVADseledpteSQWYL 299

                   ....*.
gi 1954668664  386 MNDSIV 391
Cdd:pfam13423  300 FNDFLV 305
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
735-940 9.42e-12

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 69.63  E-value: 9.42e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  735 APGAERGPPEDRDAEPQPGSPAAESleEPDAaaglsSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTA 814
Cdd:PRK07764   589 GPAPGAAGGEGPPAPASSGPPEEAA--RPAA-----PAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPD 661
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  815 PPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPE 894
Cdd:PRK07764   662 ASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPL 741
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1954668664  895 aaerPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKE 940
Cdd:PRK07764   742 ----PPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEE 783
Peptidase_C19M cd02669
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
112-388 1.27e-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: 239134 [Multi-domain]  Cd Length: 440  Bit Score: 68.50  E-value: 1.27e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  112 GLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGFCMMCTMqAHITQALSNPGD---VIKPMFVINE-MRRIA 187
Cdd:cd02669    121 GLNNIKNNDYANVIIQALSHVKPIRNFFLLYENYENIKDRKSELVKRL-SELIRKIWNPRNfkgHVSPHELLQAvSKVSK 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  188 RHFRFGNQEDAHEFLQYTVDAMqKACLNGSNKldrhtQATTLVCQIFGGYLR--------------SRVKCLNCKGVSDT 253
Cdd:cd02669    200 KKFSITEQSDPVEFLSWLLNTL-HKDLGGSKK-----PNSSIIHDCFQGKVQietqkikphaeeegSKDKFFKDSRVKKT 273
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  254 FD-PYLDITLEIKAA---QSVNKA--LEQfVKPEQLdgENSYKCSKCKKMVPASKRFTIHRSSNVLTLSLKRF--ANFTG 325
Cdd:cd02669    274 SVsPFLLLTLDLPPPplfKDGNEEniIPQ-VPLKQL--LKKYDGKTETELKDSLKRYLISRLPKYLIFHIKRFskNNFFK 350
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954668664  326 GKIAKDVKYP-EYLDIRPYMSQP---NGEPIVYVLYAVLVHTGFNCHAGHYFCYI-KASNGLWYQMND 388
Cdd:cd02669    351 EKNPTIVNFPiKNLDLSDYVHFDkpsLNLSTKYNLVANIVHEGTPQEDGTWRVQLrHKSTNKWFEIQD 418
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
735-929 2.65e-09

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 61.79  E-value: 2.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  735 APGAERGPPEDRDAePQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPP----PSAGEDIV 810
Cdd:PRK07003   361 AVTGGGAPGGGVPA-RVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPaapaPPATADRG 439
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  811 GDTAPPDLCDPGSLTGDASPLSQDAKgMIAEGPRDSALAEAPEGLSPAPPARSEEPceqpllvhPSGDHARDAQDPSQSL 890
Cdd:PRK07003   440 DDAADGDAPVPAKANARASADSRCDE-RDAQPPADSGSASAPASDAPPDAAFEPAP--------RAAAPSAATPAAVPDA 510
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1954668664  891 GAPEAAERP--PAPVLDMAPAGHPEGDAEPSPGERVEDAAA 929
Cdd:PRK07003   511 RAPAAASREdaPAAAAPPAPEARPPTPAAAAPAARAGGAAA 551
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
734-935 3.14e-09

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 61.54  E-value: 3.14e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  734 SAPGAERGPPEDR--DAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVG 811
Cdd:PRK07764   601 PAPASSGPPEEAArpAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAA 680
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  812 DTAPPDLCDPGSLTGDASPLSQDAkgmiAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLG 891
Cdd:PRK07764   681 PPPAPAPAAPAAPAGAAPAQPAPA----PAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPA 756
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1954668664  892 APEAAERPPAPVldmAPAGHPEGDAEPSPGERVEDAAAPKAPGP 935
Cdd:PRK07764   757 QPPPPPAPAPAA---APAAAPPPSPPSEEEEMAEDDAPSMDDED 797
PHA03247 PHA03247
large tegument protein UL36; Provisional
734-939 1.01e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 60.34  E-value: 1.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  734 SAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAP-PPRDPGTPATkegaweamAVAPEEPPPSAGEDIVGD 812
Cdd:PHA03247  2727 AARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPaPPAAPAAGPP--------RRLTRPAVASLSESRESL 2798
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  813 TAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQpllVHPSGDHARDAqdPSQSLGA 892
Cdd:PHA03247  2799 PSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGS---VAPGGDVRRRP--PSRSPAA 2873
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1954668664  893 -PEAAERPPA-----------------PVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAK 939
Cdd:PHA03247  2874 kPAAPARPPVrrlarpavsrstesfalPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR 2938
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
735-941 3.66e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 57.94  E-value: 3.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  735 APGAERGPPEDRDAEPQPGSPAAESLEE--PDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAV-------APEEPPPSA 805
Cdd:PRK07003   382 APGARAAAAVGASAVPAVTAVTGAAGAAlaPKAAAAAAATRAEAPPAAPAPPATADRGDDAADGdapvpakANARASADS 461
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  806 GEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPceqpllvhpsgdhARDAQD 885
Cdd:PRK07003   462 RCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAP-------------AAAAPP 528
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1954668664  886 PSQSLGAPEAAERPPAPVLDMAPAghpeGDAEPSPGERVED------AAAPKAPGPSPAKEK 941
Cdd:PRK07003   529 APEARPPTPAAAAPAARAGGAAAA----LDVLRNAGMRVSSdrgaraAAAAKPAAAPAAAPK 586
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
728-938 4.23e-08

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 57.58  E-value: 4.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  728 GSTDEMSAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGE 807
Cdd:PRK12323   367 QSGGGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGG 446
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  808 DIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAP----PARSEEPCEQPLLVHPSGDHARDA 883
Cdd:PRK12323   447 APAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPweelPPEFASPAPAQPDAAPAGWVAESI 526
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1954668664  884 QDPSQSLGAPEAAERPPAPVldMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPA 938
Cdd:PRK12323   527 PDPATADPDDAFETLAPAPA--AAPAPRAAAATEPVVAPRPPRASASGLPDMFDG 579
PHA03247 PHA03247
large tegument protein UL36; Provisional
735-938 7.68e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.26  E-value: 7.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  735 APGAERGPPEDRDAEPQPGSPAAESLeePDAAAG----------------LSSTKKAPPPrdPGTPATKEGAWEAMAVAP 798
Cdd:PHA03247  2495 APDPGGGGPPDPDAPPAPSRLAPAIL--PDEPVGepvhprmltwirgleeLASDDAGDPP--PPLPPAAPPAAPDRSVPP 2570
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  799 EEPPPSAGEDIVGD-----TAPPDLCDPGSLTGDasplSQDAKGMIAEGPRDSAlAEAPEGLSPAPPARSEEPCEQPLLV 873
Cdd:PHA03247  2571 PRPAPRPSEPAVTSrarrpDAPPQSARPRAPVDD----RGDPRGPAPPSPLPPD-THAPDPPPPSPSPAANEPDPHPPPT 2645
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1954668664  874 HPSGDHARDAQDPSQsLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPA 938
Cdd:PHA03247  2646 VPPPERPRDDPAPGR-VSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLADPPPPPPTPE 2709
Peptidase_C19Q cd02673
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
113-409 1.43e-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: 239138 [Multi-domain]  Cd Length: 245  Bit Score: 54.07  E-value: 1.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  113 LQNLGNTCFANAALQcltytpplanymlshehsktchaegfcmmctmqahitqALSNPGDVIKpmfvinemrriarHFRF 192
Cdd:cd02673      2 LVNTGNSCYFNSTMQ--------------------------------------ALSSIGKINT-------------EFDN 30
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  193 GNQEDAHEFLQYTVDAMQKAC-LNGSNKLDRHTQATTL-VCQIFGGYLRSRVKCLNCKGVSDTFDpyLDITLEIKAAQSV 270
Cdd:cd02673     31 DDQQDAHEFLLTLLEAIDDIMqVNRTNVPPSNIEIKRLnPLEAFKYTIESSYVCIGCSFEENVSD--VGNFLDVSMIDNK 108
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  271 NKALEQFVKPEQLDGENSYKCSKCK-KMVPASKRFTihRSSNVLTLSLKRFANFTGgkIAKDVKypeylDIRPYMSQPNG 349
Cdd:cd02673    109 LDIDELLISNFKTWSPIEKDCSSCKcESAISSERIM--TFPECLSINLKRYKLRIA--TSDYLK-----KNEEIMKKYCG 179
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1954668664  350 EPIVYVLYAVLVHTGFNCHAGHYFCYIKAS--NGLWYQMNDSI---VSTSDIRSVLSQQAYVLFY 409
Cdd:cd02673    180 TDAKYSLVAVICHLGESPYDGHYIAYTKELynGSSWLYCSDDEirpVSKNDVSTNARSSGYLIFY 244
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
727-929 2.41e-07

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 55.38  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  727 KGSTDEMSAPGAERGP--PEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMA--VAPEEPP 802
Cdd:PRK07764   606 SGPPEEAARPAAPAAPaaPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAapAAPPPAP 685
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  803 PSAGEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPceQPLLVHPSGDHARD 882
Cdd:PRK07764   686 APAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPP--DPAGAPAQPPPPPA 763
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1954668664  883 AQDPSQSLGAPEAAERPPAPVLDMapaghpegDAEPSPGERVEDAAA 929
Cdd:PRK07764   764 PAPAAAPAAAPPPSPPSEEEEMAE--------DDAPSMDDEDRRDAE 802
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
705-949 3.47e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 55.18  E-value: 3.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  705 PAPLLSLPEDKILETFRLSNKLKGSTDEMSAPGAE-RGPPEDRDAEPQPGSPAaesleePDAAAGLSSTKK---APPPRD 780
Cdd:PHA03307    75 PGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPgPSSPDPPPPTPPPASPP------PSPAPDLSEMLRpvgSPGPPP 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  781 PG-----------TPATKEGAWEA-----MAVAPEEPPPSAGEDIVGDTAPPDLCDPGSLTGdaSPLSQDAKGMIAEGPR 844
Cdd:PHA03307   149 AAsppaagaspaaVASDAASSRQAalplsSPEETARAPSSPPAEPPPSTPPAAASPRPPRRS--SPISASASSPAPAPGR 226
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  845 DSAlAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPvldmaPAGHPEGDAEPSPGERV 924
Cdd:PHA03307   227 SAA-DDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPG-----PASSSSSPRERSPSPSP 300
                          250       260
                   ....*....|....*....|....*
gi 1954668664  925 EDAAAPKAPGPSPAKEKIGSLRKVD 949
Cdd:PHA03307   301 SSPGSGPAPSSPRASSSSSSSRESS 325
PHA03247 PHA03247
large tegument protein UL36; Provisional
735-941 3.56e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 55.33  E-value: 3.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  735 APGAERGPPEDRDAEPQPGSPAAESLEEPDAA---------AGLSSTKKAPPPRDPGTPAT----KEGAWEAMAVA---- 797
Cdd:PHA03247   262 GEGADRAPETARGATGPPPPPEAAAPNGAAAPpdgvwgaalAGAPLALPAPPDPPPPAPAGdaeeEDDEDGAMEVVsplp 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  798 ---------------PEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPlsqDAKGMIAEGPrdsalaeapeGLSPAPPAR 862
Cdd:PHA03247   342 rprqhyplgfpkrrrPTWTPPSSLEDLSAGRHHPKRASLPTRKRRSAR---HAATPFARGP----------GGDDQTRPA 408
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1954668664  863 SEEPCEQPLLVHPsgdhardaqdpsqslGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEK 941
Cdd:PHA03247   409 APVPASVPTPAPT---------------PVPASAPPPPATPLPSAEPGSDDGPAPPPERQPPAPATEPAPDDPDDATRK 472
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
762-951 6.86e-07

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 54.09  E-value: 6.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  762 EPDAAAGlSSTKKAPPPRDPG---TPATKEGAWEAMAVAPEEPPPSAGediVGDTAPPDLCDPGSLTGDASPLSQDAKGM 838
Cdd:PRK07003   359 EPAVTGG-GAPGGGVPARVAGavpAPGARAAAAVGASAVPAVTAVTGA---AGAALAPKAAAAAAATRAEAPPAAPAPPA 434
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  839 IAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEgDAEP 918
Cdd:PRK07003   435 TADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPD-ARAP 513
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1954668664  919 SPGERVEDAAAPKAPGPSPAKEKIGSLRKVDRG 951
Cdd:PRK07003   514 AAASREDAPAAAAPPAPEARPPTPAAAAPAARA 546
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
730-940 2.08e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 52.48  E-value: 2.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  730 TDEMSAPGAERGPPEDR-DAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPR--DPGTPATKEG--AWEAMAVAPEEPPPS 804
Cdd:PHA03307    69 TGPPPGPGTEAPANESRsTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPtpPPASPPPSPApdLSEMLRPVGSPGPPP 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  805 AGEDI---VGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPAR-SEEPCEQPLLVHPSGDHA 880
Cdd:PHA03307   149 AASPPaagASPAAVASDAASSRQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRsSPISASASSPAPAPGRSA 228
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  881 RDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPgERVEDAAAPKAPGPSPAKE 940
Cdd:PHA03307   229 ADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTR-IWEASGWNGPSSRPGPASS 287
PHA03247 PHA03247
large tegument protein UL36; Provisional
628-938 2.57e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 52.25  E-value: 2.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  628 IGTIVSSHSPGQDAEDEEATPHelqepmtLNGANSADSDSDPKENGLAPDGASCQGQPAlhseNPFAKANGLPGKlMPAP 707
Cdd:PHA03247  2578 SEPAVTSRARRPDAPPQSARPR-------APVDDRGDPRGPAPPSPLPPDTHAPDPPPP----SPSPAANEPDPH-PPPT 2645
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  708 LLSLPEDKILETFRLSNKLKGSTDEMSAPGAErGPPEdrdaepQPGSPAAesleePDAAAGLSSTKKAPPPrdPGTPATK 787
Cdd:PHA03247  2646 VPPPERPRDDPAPGRVSRPRRARRLGRAAQAS-SPPQ------RPRRRAA-----RPTVGSLTSLADPPPP--PPTPEPA 2711
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  788 EGAWEAmavAPEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPlsqdakGMIAEGPRDSALAEAPeglSPAPPARSEEPc 867
Cdd:PHA03247  2712 PHALVS---ATPLPPGPAAARQASPALPAAPAPPAVPAGPATP------GGPARPARPPTTAGPP---APAPPAAPAAG- 2778
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1954668664  868 EQPLLVHPSGDHARDAqdpSQSLGAPEAAERPPAPVLDMAPAGHPEgdAEPSPGERVEDAAAPKAPGPSPA 938
Cdd:PHA03247  2779 PPRRLTRPAVASLSES---RESLPSPWDPADPPAAVLAPAAALPPA--ASPAGPLPPPTSAQPTAPPPPPG 2844
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
735-1055 2.67e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 51.91  E-value: 2.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  735 APGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTA 814
Cdd:PRK07764   413 AAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAA 492
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  815 PPdlcdpgsltGDASPLSQDAKGMIAEGPRDS--ALAEAPEGLSPA------PPARSEEPCEQPL-LVHPSGDHAR--DA 883
Cdd:PRK07764   493 AP---------AAPAAPAAPAGADDAATLRERwpEILAAVPKRSRKtwaillPEATVLGVRGDTLvLGFSTGGLARrfAS 563
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  884 QDPSQSL---------------------GAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEKI 942
Cdd:PRK07764   564 PGNAEVLvtalaeelggdwqveavvgpaPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAP 643
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  943 GSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDRLSPGERRSLGRCSH--- 1019
Cdd:PRK07764   644 APGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQppq 723
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1954668664 1020 --HHSRHRSGVELDWVRHHYTEGERGWGREKFYPDRPR 1055
Cdd:PRK07764   724 aaQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPP 761
Peptidase_C19J cd02666
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
111-392 2.78e-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: 239131 [Multi-domain]  Cd Length: 343  Bit Score: 50.95  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  111 AGLQNLGNTCFANAALQCLTYTPPLANYMLSHEHSKTCHAEGfcmMCTMQAHITQALSNpGDVIKPMFVINEMRRIARHF 190
Cdd:cd02666      2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVLNFDESKAELASD---YPTERRIGGREVSR-SELQRSNQFVYELRSLFNDL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  191 RFGN----------------QEDAHEFLQYTVDAMQKACLNGSN-----KLDRHTQATTLVCQIF-GGYLRSRVKCLNCK 248
Cdd:cd02666     78 IHSNtrsvtpskelaylalrQQDVTECIDNVLFQLEVALEPISNafagpDTEDDKEQSDLIKRLFsGKTKQQLVPESMGN 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  249 GVSD---------TFDPYLDITLEIKA---AQSVNKALEQFVKPEQLDGENSYKCSKCKKMVPASK------RFTIHRSS 310
Cdd:cd02666    158 QPSVrtkterflsLLVDVGKKGREIVVllePKDLYDALDRYFDYDSLTKLPQRSQVQAQLAQPLQRelismdRYELPSSI 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  311 NVlTLSLKRFANFTGGKIAKDVKYPEYLDIRPYMSQPNGE-PIVYVLYAVLVHTGfNCHAGHYFCYIK-ASNGLWYQMND 388
Cdd:cd02666    238 DD-IDELIREAIQSESSLVRQAQNELAELKHEIEKQFDDLkSYGYRLHAVFIHRG-EASSGHYWVYIKdFEENVWRKYND 315

                   ....
gi 1954668664  389 SIVS 392
Cdd:cd02666    316 ETVT 319
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
735-951 2.78e-06

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 51.52  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  735 APGAERGPP--EDRDAEPQPgspaAESleepdAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGD 812
Cdd:PRK13108   281 APGALRGSEyvVDEALEREP----AEL-----AAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDEVAAESVVQ 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  813 TAPPDlcdpgsltGDASPLSQDAKGMIAEGPRDSALA----EAPEGLSPAPPARSEEPCEQPllvhpsgdhardAQDPSQ 888
Cdd:PRK13108   352 VADRD--------GESTPAVEETSEADIEREQPGDLAgqapAAHQVDAEAASAAPEEPAALA------------SEAHDE 411
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1954668664  889 SlgAPEAAERppapvldmapaghpegdAEPSPGERVEDAAAPKAPGPSPAK-EKIGSLRKVDRG 951
Cdd:PRK13108   412 T--EPEVPEK-----------------AAPIPDPAKPDELAVAGPGDDPAEpDGIRRQDDFSSR 456
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
629-973 7.32e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.55  E-value: 7.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  629 GTIVSSHSPGQDAEDEEATPHelQEPMTLNGANSADSDSDPKENGLAPDGASCQGQPALHSENPFAKANGLPGKLMPAPL 708
Cdd:PHA03307    98 ASPAREGSPTPPGPSSPDPPP--PTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAVASDAASSRQAALP 175
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  709 LSLPEDkiletfrlsnklkgSTDEMSAPGAERGPPEDR----DAEPQPGSPAAESLEEPDAAAGLSStkKAPPPRDPGTP 784
Cdd:PHA03307   176 LSSPEE--------------TARAPSSPPAEPPPSTPPaaasPRPPRRSSPISASASSPAPAPGRSA--ADDAGASSSDS 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  785 ATKEGAWEAMAVAPEEPPPSAGEDIVgdtapPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSE 864
Cdd:PHA03307   240 SSSESSGCGWGPENECPLPRPAPITL-----PTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRA 314
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  865 EPCEQPllVHPSGDHARDAQDPSQSlgaPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEKIGS 944
Cdd:PHA03307   315 SSSSSS--SRESSSSSTSSSSESSR---GAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRR 389
                          330       340
                   ....*....|....*....|....*....
gi 1954668664  945 LRKvDRGHYRSRRERSSSGEPARESRSKT 973
Cdd:PHA03307   390 ARA-AVAGRARRRDATGRFPAGRPRPSPL 417
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
733-1138 3.29e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 48.63  E-value: 3.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  733 MSAPGAERGPPED--RDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAP-------EEPPP 803
Cdd:PHA03307    22 PRPPATPGDAADDllSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTwslstlaPASPA 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  804 SAGEDIVGDTAPPDlcDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEepceqpllvhPSGDHARDA 883
Cdd:PHA03307   102 REGSPTPPGPSSPD--PPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPA----------AVASDAASS 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  884 QDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKA-PGPSPAKE-KIGSLRKVDRGHYRSRRERSS 961
Cdd:PHA03307   170 RQAALPLSSPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASsPAPAPGRSaADDAGASSSDSSSSESSGCGW 249
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  962 SGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDRLSPGERRSLGRCSHHHSRHRSGVELDwvrhhytege 1041
Cdd:PHA03307   250 GPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSS---------- 319
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 1042 rgwgrekfypdrprwdrcryyhdryalyaardwkpfhGGREHERAGLHERPHKDHNRG-RRGCEPARERERHRPSSPRAG 1120
Cdd:PHA03307   320 -------------------------------------SSRESSSSSTSSSSESSRGAAvSPGPSPSRSPSPSRPPPPADP 362
                          410
                   ....*....|....*...
gi 1954668664 1121 APHALAPHPDRFSHDRTA 1138
Cdd:PHA03307   363 SSPRKRPRPSRAPSSPAA 380
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
734-908 3.58e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 48.31  E-value: 3.58e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  734 SAPGAERGPPEDRDAEPQ---------PGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEamAVAPEEPPPS 804
Cdd:PRK07003   454 NARASADSRCDERDAQPPadsgsasapASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDA--PAAAAPPAPE 531
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  805 AGEdivgdTAPPDLCDPGSLTGDASPLS--QDAkGMIAEGPRDSALAEAPEglSPAPPARSEEPCEQPLLVH---PSGDH 879
Cdd:PRK07003   532 ARP-----PTPAAAAPAARAGGAAAALDvlRNA-GMRVSSDRGARAAAAAK--PAAAPAAAPKPAAPRVAVQvptPRARA 603
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1954668664  880 ARDAQDPSQSLGAPEAAE--RPPAPVLDMAP 908
Cdd:PRK07003   604 ATGDAPPNGAARAEQAAEsrGAPPPWEDIPP 634
dnaA PRK14086
chromosomal replication initiator protein DnaA;
737-939 2.49e-04

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 45.59  E-value: 2.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  737 GAERGPP-------EDRDAEPQPGSPAAESLEEPDaaagLSSTKKAPPPRDPGTPATKEG-AWEAMAVAPEEPPpsaged 808
Cdd:PRK14086    75 SRELGRPiriaitvDPSAGEPAPPPPHARRTSEPE----LPRPGRRPYEGYGGPRADDRPpGLPRQDQLPTARP------ 144
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  809 ivgdtAPPDLCD---PGSLTGDASPLS--QDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQPllVHPSGDH-ARD 882
Cdd:PRK14086   145 -----AYPAYQQrpePGAWPRAADDYGwqQQRLGFPPRAPYASPASYAPEQERDREPYDAGRPEYDQ--RRRDYDHpRPD 217
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  883 AQDPSQslgapEAAERP-PAPvldmaPAGHPEGDAEPSPG--ERVEDAAAPKAPGPSPAK 939
Cdd:PRK14086   218 WDRPRR-----DRTDRPePPP-----GAGHVHRGGPGPPErdDAPVVPIRPSAPGPLAAQ 267
PRK12678 PRK12678
transcription termination factor Rho; Provisional
846-1113 3.47e-04

transcription termination factor Rho; Provisional


Pssm-ID: 237171 [Multi-domain]  Cd Length: 672  Bit Score: 44.89  E-value: 3.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  846 SALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVE 925
Cdd:PRK12678    53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  926 DAAAPKAPGPSPAKEKIGSLRKVDRGHyrsrRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHPGHGDR 1005
Cdd:PRK12678   133 RGEAARRGAARKAGEGGEQPATEARAD----AAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDDRDRRDR 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664 1006 LSPGERRslgrcSHHHSRHRsgveldwvrhhytEGERGWGRekfypDRPRWDRCRYYHDRYALYAARDWKPFHGGReher 1085
Cdd:PRK12678   209 REQGDRR-----EERGRRDG-------------GDRRGRRR-----RRDRRDARGDDNREDRGDRDGDDGEGRGGR---- 261
                          250       260
                   ....*....|....*....|....*...
gi 1954668664 1086 aglherphkdhnRGRRGcepaRERERHR 1113
Cdd:PRK12678   262 ------------RGRRF----RDRDRRG 273
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
748-878 3.82e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 44.71  E-value: 3.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  748 AEPQPGSPAAESLEEPDAAAglSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTAPPDLCDPG--SLT 825
Cdd:PRK14951   369 AAEAAAPAEKKTPARPEAAA--PAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAApaAVA 446
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1954668664  826 GDASPLSQDAKGMIAEGPRdsalAEAPEGLSPAPPARSEEPCEQPLLVHPSGD 878
Cdd:PRK14951   447 LAPAPPAQAAPETVAIPVR----VAPEPAVASAAPAPAAAPAAARLTPTEEGD 495
Peptidase_C19I cd02665
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
312-410 3.92e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 43.32  E-value: 3.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  312 VLTLSLKRFA--NFTGGKIAKDVKYPEYLDIRPYMsqpngepivyvLYAVLVHTGfNCHAGHYFCYI-KASNGLWYQMND 388
Cdd:cd02665    131 VLTFELSRFEfnQGRPEKIHDKLEFPQIIQQVPYE-----------LHAVLVHEG-QANAGHYWAYIyKQSRQEWEKYND 198
                           90       100       110
                   ....*....|....*....|....*....|
gi 1954668664  389 SIVSTSDIRSVLSQ--------QAYVLFYI 410
Cdd:cd02665    199 ISVTESSWEEVERDsfgggrnpSAYCLMYI 228
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
727-939 4.92e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 44.53  E-value: 4.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  727 KGSTDEMSAPGAERGPPEDRDAEPQPGSP--AAESLEEPDAAAGLSSTKKAPPPRD------PGTPATKEGAWEAMAVAP 798
Cdd:PLN03209   345 KPVTPEAPSPPIEEEPPQPKAVVPRPLSPytAYEDLKPPTSPIPTPPSSSPASSKSvdavakPAEPDVVPSPGSASNVPE 424
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  799 EEPPPSAGED--------IVGDTAPPDLCDPGSLTGDASPLSQDAK-GMIAEGPRDSALAEA-------PEGLSPAPPAR 862
Cdd:PLN03209   425 VEPAQVEAKKtrplspyaRYEDLKPPTSPSPTAPTGVSPSVSSTSSvPAVPDTAPATAATDAaapppanMRPLSPYAVYD 504
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954668664  863 SEEPCEQPLLVHPSGDHArdaqdPSQSLGAPEAAERPPaPVLDMAPAGHPEGDAEP-SPGERVEDAAAPKAPGPSPAK 939
Cdd:PLN03209   505 DLKPPTSPSPAAPVGKVA-----PSSTNEVVKVGNSAP-PTALADEQHHAQPKPRPlSPYTMYEDLKPPTSPTPSPVL 576
PHA03247 PHA03247
large tegument protein UL36; Provisional
422-938 4.95e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 4.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  422 THPTHSPGQSSPRPVISQRVVTNKQAAPGFIGPQLPSHMIKNP---PHLNGTGPLKDTPSSSMSSPNGNSSVNRASPVNA 498
Cdd:PHA03247  2587 RRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDPPPPspsPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR 2666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  499 SASVQNWSvnRSSVIPEHPKKQKITISIHnklPVRQCQSQPnlhsnSLENPTKPVPSSTITNSAVQSTSNASTMSVSSKV 578
Cdd:PHA03247  2667 ARRLGRAA--QASSPPQRPRRRAARPTVG---SLTSLADPP-----PPPPTPEPAPHALVSATPLPPGPAAARQASPALP 2736
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  579 TKPIPRSeSCSQPVMNGKSKLNSSVLVPYGAESSEDSDEESKGLGKEngiGTIVSSHSPGQDAEDEEATPHELQEPMTLN 658
Cdd:PHA03247  2737 AAPAPPA-VPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPPRR---LTRPAVASLSESRESLPSPWDPADPPAAVL 2812
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  659 GANSADSDSDPKENGLAPDGASCQGQPALHSEnPFAKANGLPGKLMPAPLLSlpedkiletfrlsnKLKGSTDEMSAPGA 738
Cdd:PHA03247  2813 APAAALPPAASPAGPLPPPTSAQPTAPPPPPG-PPPPSLPLGGSVAPGGDVR--------------RRPPSRSPAAKPAA 2877
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  739 ERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIVGDTAPPDL 818
Cdd:PHA03247  2878 PARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  819 CDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPeglSPAPPARSEEP----CEQPLLVHPSGDHArdAQDPSQSLGAPE 894
Cdd:PHA03247  2958 AVPQPWLGALVPGRVAVPRFRVPQPAPSREAPAS---STPPLTGHSLSrvssWASSLALHEETDPP--PVSLKQTLWPPD 3032
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....*
gi 1954668664  895 AAERPPAPVLDMAPAGHPEGDA-EPSPGERVEDAAAPKAPGPSPA 938
Cdd:PHA03247  3033 DTEDSDADSLFDSDSERSDLEAlDPLPPEPHDPFAHEPDPATPEA 3077
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
772-941 5.51e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 5.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  772 TKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEdiVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEA 851
Cdd:PRK12323   376 TAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPA--AAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPA 453
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  852 PeglSPAPPARSEEPCEQPLlvhPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDA---- 927
Cdd:PRK12323   454 P---AAAPAAAARPAAAGPR---PVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAesip 527
                          170
                   ....*....|....*...
gi 1954668664  928 ----AAPKAPGPSPAKEK 941
Cdd:PRK12323   528 dpatADPDDAFETLAPAP 545
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
840-938 5.56e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.59  E-value: 5.56e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  840 AEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDhARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPS 919
Cdd:PRK07764   405 APAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPS-PAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPA 483
                           90
                   ....*....|....*....
gi 1954668664  920 PGERVEDAAAPKAPGPSPA 938
Cdd:PRK07764   484 PPAAPAPAAAPAAPAAPAA 502
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
732-939 6.16e-04

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 43.90  E-value: 6.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  732 EMSAPG----AERGPPEDRDAEPQPGSPAAESLEEPDAAA------------GLSSTKKAPPP-------RDPGTPATKE 788
Cdd:COG5180    254 EMRPPAdakeRRRAAIGDTPAAEPPGLPVLEAGSEPQSDApeaetarpidvkGVASAPPATRPvrppggaRDPGTPRPGQ 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  789 GAWEAMAV----APEEPPPS----AGEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAP-------- 852
Cdd:COG5180    334 PTERPAGVpeaaSDAGQPPSayppAEEAVPGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMgagdlvqa 413
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  853 EGLSPAPPARSEEPCEQPLLVHPSGDH-ARDAQDPSQSLGAPEAAERPPAPVldMAPAGHPEGDAePSPGERVEDAAAPK 931
Cdd:COG5180    414 ALDGGGRETASLGGAAGGAGQGPKADFvPGDAESVSGPAGLADQAGAAASTA--MADFVAPVTDA-TPVDVADVLGVRPD 490

                   ....*...
gi 1954668664  932 APGPSPAK 939
Cdd:COG5180    491 AILGGNVA 498
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
728-996 6.99e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 6.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  728 GSTDEMSAPGAERGPPEDRDAEPQPGS-PAAESLEEPDAAAGLSSTKKAPPPRDPGtpATKEGAW-EAMAVAPEEPPPSA 805
Cdd:PRK07764   454 PSPPPAAAPSAQPAPAPAAAPEPTAAPaPAPPAAPAPAAAPAAPAAPAAPAGADDA--ATLRERWpEILAAVPKRSRKTW 531
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  806 GedIVGDTAPPDLCDPGSLT-GDASPLsqdAKGMIAEGPRDSALAEA-----------------------PEGLSPAPPA 861
Cdd:PRK07764   532 A--ILLPEATVLGVRGDTLVlGFSTGG---LARRFASPGNAEVLVTAlaeelggdwqveavvgpapgaagGEGPPAPASS 606
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  862 RSEEPCEQPllvhPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPAKEK 941
Cdd:PRK07764   607 GPPEEAARP----AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPP 682
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1954668664  942 IGSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAP 996
Cdd:PRK07764   683 PAPAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADD 737
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
555-778 7.40e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 43.93  E-value: 7.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  555 SSTITNSAVQSTSnASTMSVSSKVTKPIPRSESCSQpvmngksklNSSVLVPYGAESSEDSDEESKGLGKENGIGtivss 634
Cdd:PRK08691   369 NAVIENTELQSPS-AQTAEKETAAKKPQPRPEAETA---------QTPVQTASAAAMPSEGKTAGPVSNQENNDV----- 433
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  635 hSPGQDAEDEEATPhELQEPMTLNGANSADSDSDPKENGLAPDGASCQGQPALHSENPfakanglpgklMPAPLLSLPED 714
Cdd:PRK08691   434 -PPWEDAPDEAQTA-AGTAQTSAKSIQTASEAETPPENQVSKNKAADNETDAPLSEVP-----------SENPIQATPND 500
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1954668664  715 KILETFRLSNKLKGST---------DEMSAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPP 778
Cdd:PRK08691   501 EAVETETFAHEAPAEPfygygfpdnDCPPEDGAEIPPPDWEHAAPADTAGGGADEEAEAGGIGGNNTPSAPPP 573
Peptidase_C19P cd02672
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ...
111-409 8.76e-04

A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They 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: 42.88  E-value: 8.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  111 AGLQNLGNTCFANAALQCLTYTPPLANYMLsheHSKTCHAEGFCMMC-------TMQAHITQALSN--PGDVIKPMFVIN 181
Cdd:cd02672     16 AGLENHITNSYCNSLLQLLYFIPPFRNFTA---IILVACPKESCLLCelgylfsTLIQNFTRFLLEtiSQDQLGTPFSCG 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  182 EMRR-------IARHFRFGNQEDAHEFLQytvdamqkaCLNGSNKLDRHTQATTLVCQifggYLRSRVKCLNCKGVSDTF 254
Cdd:cd02672     93 TSRNsvsllytLSLPLGSTKTSKESTFLQ---------LLKRSLDLEKVTKAWCDTCC----KYQPLEQTTSIRHLPDIL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  255 DPYLDITLEiKAAQSVNKALEQFVKPEQLDGENSYKCSKCKKmvpaskrftihrssnvltlslkrfanftggkiAKDVKY 334
Cdd:cd02672    160 LLVLVINLS-VTNGEFDDINVVLPSGKVMQNKVSPKAIDHDK--------------------------------LVKNRG 206
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  335 PEYLDirpymsqpngepiVYVLYAVLVHTGFNCHAGHYFCYIKASN-----GLWYQMNDSIVSTsdirsvLSQQAYVLFY 409
Cdd:cd02672    207 QESIY-------------KYELVGYVCEINDSSRGQHNVVFVIKVNeesthGRWYLFNDFLVTP------VSELAYILLY 267
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
501-936 9.78e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 43.56  E-value: 9.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  501 SVQNWSVNRSSVIpEHPKKQKITISIHNKLPVRQCQSQPNLHSNSlENPTKPVPSSTiTNSAVQsTSNASTMSVSSKVTK 580
Cdd:PRK14949   362 PVKRWQVDDPAEI-SLPEGQTPSALAAAVQAPHANEPQFVNAAPA-EKKTALTEQTT-AQQQVQ-AANAEAVAEADASAE 437
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  581 PIPRSESCSQPVMNGKSKLNSSVlvpygaessedsdeeskglgkengigTIVSSHSPGQDAEDEEATPHELQEPMTLNGA 660
Cdd:PRK14949   438 PADTVEQALDDESELLAALNAEQ--------------------------AVILSQAQSQGFEASSSLDADNSAVPEQIDS 491
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  661 NSADSDSDPK-ENGLAPD--GASCQGQPALHSENPFAKANGLPGKLMP-------APLLSLPEDKILETFRLSNKLKGST 730
Cdd:PRK14949   492 TAEQSVVNPSvTDTQVDDtsASNNSAADNTVDDNYSAEDTLESNGLDEgdyaqdsAPLDAYQDDYVAFSSESYNALSDDE 571
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  731 DEMSAPGAERGPPEDRDAEPQPGSP-----AAESLEEPD------AA-----AGL-------SSTKKAPPPRDPGTPatk 787
Cdd:PRK14949   572 QHSANVQSAQSAAEAQPSSQSLSPIsavttAAASLADDDildavlAArdsllSDLdalspkeGDGKKSSADRKPKTP--- 648
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  788 egaweamavaPEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPLSQDAkgmIAEGPRDSALAEAPeGLSPAPPARS--EE 865
Cdd:PRK14949   649 ----------PSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQS---VPEAALASGSAPAP-PPVPDPYDRPpwEE 714
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1954668664  866 PCEQPLLVHPSGDHARDAQDPSQslgapEAAERPPAPVLDMAPAGHPEGDAEPSPgerveDAAAPKAPGPS 936
Cdd:PRK14949   715 APEVASANDGPNNAAEGNLSESV-----EDASNSELQAVEQQATHQPQVQAEAQS-----PASTTALTQTS 775
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
736-924 1.21e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  736 PGAERGPPEDRDAEPQPGSPAAESL---------EEPDAAAGLSSTKKAPPPRDPgtPATKEGAWEAMAVAPEEPPPSAg 806
Cdd:PHA03307   284 PASSSSSPRERSPSPSPSSPGSGPApssprasssSSSSRESSSSSTSSSSESSRG--AAVSPGPSPSRSPSPSRPPPPA- 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  807 edivgDTAPPdlcdPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARseePCEQPllvhpsgdhardaqdP 886
Cdd:PHA03307   361 -----DPSSP----RKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRF---PAGRP---------------R 413
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1954668664  887 SQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERV 924
Cdd:PHA03307   414 PSPLDAGAASGAFYARYPLLTPSGEPWPGSPPPPPGRV 451
PHA03321 PHA03321
tegument protein VP11/12; Provisional
734-929 1.24e-03

tegument protein VP11/12; Provisional


Pssm-ID: 223041 [Multi-domain]  Cd Length: 694  Bit Score: 43.02  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  734 SAPGAERGPPEDR--DAEPQPGSPAAESLEEPDAAAglsstkKAPPPRDPGTPATKegaWEAMAVAPEEPPP--SAGEDI 809
Cdd:PHA03321   452 STPACARRARAQRarDAGPEYVDPLGALRRLPAGAA------PPPEPAAAPSPATY---YTRMGGGPPRLPPrnRATETL 522
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  810 VGDTAPP------DLCDPGSLTGDASPLSQDAKGMIAEgpRDSALAEAPEGLSPAPPAR-SEEPCEQPL-----LVHPSG 877
Cdd:PHA03321   523 RPDWGPPaaappeQMEDPYLEPDDDRFDRRDGAAAAAT--SHPREAPAPDDDPIYEGVSdSEEPVYEEIptprvYQNPLP 600
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1954668664  878 DHARDAQDP---------------------SQSLGAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAA 929
Cdd:PHA03321   601 RPMEGAGEPpdldaptspwveeenpiygwgDSPLFSPPPAARFPPPDPALSPEPPALPAHRPRPGALAPDGPA 673
KLF14_N cd21576
N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as ...
761-939 1.64e-03

N-terminal domain of Kruppel-like factor 14; Kruppel-like factor 14 (KLF14; also known as Krueppel-like factor 14 or basic transcription element-binding protein 5/BTEB5) is a protein that in humans is encoded by the KLF14 gene. KLF14 regulates the transcription of various genes, including TGFbetaRII (the type II receptor for TGFbeta). KLF14 is expressed in many tissues, lacks introns, and is subject to parent-specific expression. It also appears to be a master regulator of gene expression in adipose tissue. KLF14 is associated with coronary artery disease, hypercholesterolemia, and type 2 diabetes. KLF9, KLF10, KLF11, KLF13, KLF14, and KLF16 share a conserved alpha-helical motif AA/VXXL that mediates their binding to Sin3A and their activities as transcriptional repressors. KLF14 belongs to a family of proteins, called the Specificity Protein (SP)/KLF family, characterized by a C-terminal DNA-binding domain of 81 amino acids consisting of three Kruppel-like C2H2 zinc fingers. These factors bind to a loose consensus motif, namely NNRCRCCYY (where N is any nucleotide; R is A/G, and Y is C/T), such as the recurring motifs in GC and GT boxes (5'-GGGGCGGGG-3' and 5-GGTGTGGGG-3') that are present in promoters and more distal regulatory elements of mammalian genes. Members of the KLF family can act as activators or repressors of transcription depending on cell and promoter context. KLFs regulate various cellular functions, such as proliferation, differentiation, and apoptosis, as well as the development and homeostasis of several types of tissue. In addition to the C-terminal DNA-binding domain, each KLF also has a unique N-terminal activation/repression domain that confers specificity and allows it to bind specifically to a certain partner, leading to distinct activities in vivo. This model represents the N-terminal domain of KLF14.


Pssm-ID: 409238 [Multi-domain]  Cd Length: 195  Bit Score: 41.34  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  761 EEPDAAAGLSSTKKAPPPRDPGtPATKEGAWEAMAVAPEEPPPSAGedivgDTAPPDLCdpgsltgdASPLSqDAKGMIA 840
Cdd:cd21576     32 EGAGGAAGSEVGAAPPESALPG-PGPPGPAWVPPLLQVPAPSPGAG-----GAAPHLLA--------ASVLA-DLRGGAG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  841 EGPRDSALaEAPEGLSPAP-PARSEEPCEQPLLVHPSGDHArdAQDPSQSLGAPEAAERPPAPvldmapaghpegdaePS 919
Cdd:cd21576     97 EGSREDSG-EAPRASSGSSdPARGSSPTLGSEPAPASGEDA--VSGPESSFGAPAIPSAPAAP---------------GA 158
                          170       180
                   ....*....|....*....|
gi 1954668664  920 PGERVEDAAAPKAPGPSPAK 939
Cdd:cd21576    159 PAVSGEVPGGAPGAGPAPAA 178
PHA01929 PHA01929
putative scaffolding protein
858-951 2.29e-03

putative scaffolding protein


Pssm-ID: 177328  Cd Length: 306  Bit Score: 41.58  E-value: 2.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  858 APPARSEEPCEQPLLVHPSGDHARDAQDPSQSlgAPEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKA---PG 934
Cdd:PHA01929    19 VPPAAAPTPQPNPVIQPQAPVQPGQPGAPQQL--AIPTQQPQPVPTSAMTPHVVQQAPAQPAPAAPPAAGAALPEaleVP 96
                           90
                   ....*....|....*..
gi 1954668664  935 PSPAKEKIGSLRKVDRG 951
Cdd:PHA01929    97 PPPAFTPNGEIVGTLAG 113
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
724-970 3.10e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 41.97  E-value: 3.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  724 NKLKGSTDEMSAPGAERGPPEDRDAEP--QPGSPAAESLEEPDAAAGLSStkKAPPPRDPGTPATKEGAWEAMAVAPEEP 801
Cdd:COG5180     70 GKPQLPSVAEPEAYLDPAPPKSSPDTPeeQLGAPAGDLLVLPAAKTPELA--AGALPAPAAAAALPKAKVTREATSASAG 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  802 PPSAGEDIvGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDsALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHAR 881
Cdd:COG5180    148 VALAAALL-QRSDPILAKDPDGDSASTLPPPAEKLDKVLTEPRD-ALKDSPEKLDRPKVEVKDEAQEEPPDLTGGADHPR 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  882 DAQDPSQSLGAPEAAE--------------RPPAPVLDMAPAGHPEGDAEPSPGERVedaaAPKAPGPSPAKEKIGSLRK 947
Cdd:COG5180    226 PEAASSPKVDPPSTSEarsrpatvdaqpemRPPADAKERRRAAIGDTPAAEPPGLPV----LEAGSEPQSDAPEAETARP 301
                          250       260
                   ....*....|....*....|...
gi 1954668664  948 VDRGHYRSRRERSSSGEPARESR 970
Cdd:COG5180    302 IDVKGVASAPPATRPVRPPGGAR 324
PHA03379 PHA03379
EBNA-3A; Provisional
756-939 3.35e-03

EBNA-3A; Provisional


Pssm-ID: 223066 [Multi-domain]  Cd Length: 935  Bit Score: 41.97  E-value: 3.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  756 AAESLEEPDAAAGLSSTKKAPPPRdPGTPATKEGAWEAMAVAPEEPPPsagediVGDTAPPDLCDPGSLT------GDAS 829
Cdd:PHA03379   401 AREALEKASEPTYGTPRPPVEKPR-PEVPQSLETATSHGSAQVPEPPP------VHDLEPGPLHDQHSMApcpvaqLPPG 473
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  830 PLSQDAKGMIAEGP-RDSALAEAPeglSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAAERPPAPVLDMAP 908
Cdd:PHA03379   474 PLQDLEPGDQLPGVvQDGRPACAP---VPAPAGPIVRPWEASLSQVPGVAFAPVMPQPMPVEPVPVPTVALERPVCPAPP 550
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1954668664  909 AGHPEGDAEPSPGERVEDAAAPKAPGPSPAK 939
Cdd:PHA03379   551 LIAMQGPGETSGIVRVRERWRPAPWTPNPPR 581
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
762-1008 3.44e-03

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 41.84  E-value: 3.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  762 EPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDivgDTAPPDLCDPGSLTG-DASPLSQDAKGMIA 840
Cdd:PLN03209   332 ESDAADGPKPVPTKPVTPEAPSPPIEEEPPQPKAVVPRPLSPYTAYE---DLKPPTSPIPTPPSSsPASSKSVDAVAKPA 408
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  841 EgPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSlgaPEAAERPPApvldmapaghPEGDAEPSP 920
Cdd:PLN03209   409 E-PDVVPSPGSASNVPEVEPAQVEAKKTRPLSPYARYEDLKPPTSPSPT---APTGVSPSV----------SSTSSVPAV 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  921 GERVEDAAAPKAPGPSPAKEKIGSLRKVDRGHYRSRRERSSSGEPARESRSKTEGHRHRRRRTCPRERDRQDRHAPEHHP 1000
Cdd:PLN03209   475 PDTAPATAATDAAAPPPANMRPLSPYAVYDDLKPPTSPSPAAPVGKVAPSSTNEVVKVGNSAPPTALADEQHHAQPKPRP 554

                   ....*...
gi 1954668664 1001 ghgdrLSP 1008
Cdd:PLN03209   555 -----LSP 557
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
843-940 3.85e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 41.33  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  843 PRDSALAEAPEGLSPAP----PARSEEPCEQPLLVHPSGDHARDAQDPSqslgapeaaerPPAPVLDMAPAGHPEGDAEP 918
Cdd:PRK14950   362 PVPAPQPAKPTAAAPSPvrptPAPSTRPKAAAAANIPPKEPVRETATPP-----------PVPPRPVAPPVPHTPESAPK 430
                           90       100
                   ....*....|....*....|..
gi 1954668664  919 SPGERVEDAAAPKAPGPSPAKE 940
Cdd:PRK14950   431 LTRAAIPVDEKPKYTPPAPPKE 452
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
734-898 4.05e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 41.62  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  734 SAPGAERGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGEDIvgdt 813
Cdd:PRK14951   372 AAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAPAAAAPAAAPAAAPAAVAL---- 447
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  814 aPPDLCDPGSLTGDASPLsqdakgMIAEGPRDSALAEAPEGLSPAPPARSEEPCE------------------------Q 869
Cdd:PRK14951   448 -APAPPAQAAPETVAIPV------RVAPEPAVASAAPAPAAAPAAARLTPTEEGDvwhatvqqlaaaeaitalarelalQ 520
                          170       180
                   ....*....|....*....|....*....
gi 1954668664  870 PLLVHPSGDHArDAQDPSQSLGAPEAAER 898
Cdd:PRK14951   521 SELVARDGDQW-LLRVERESLNQPGARER 548
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
795-942 4.48e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 41.51  E-value: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  795 AVAPEEPPPSAGEDIVGDTAPPDLCDPGSLTGDASPlSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPCEQPLLVH 874
Cdd:PRK07764   373 GLLARLERLERRLGVAGGAGAPAAAAPSAAAAAPAA-APAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAG 451
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1954668664  875 PSGDHARDAQDPSQSLGAPEAAERPPApvldmAPAghPEGDAEPSPGERVEDAAAPKAPGPSPAKEKI 942
Cdd:PRK07764   452 GAPSPPPAAAPSAQPAPAPAAAPEPTA-----APA--PAPPAAPAPAAAPAAPAAPAAPAGADDAATL 512
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
821-938 5.96e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 41.01  E-value: 5.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  821 PGSLTGDASPLSQDAKGMIAEGPRDSAL-----AEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDP---SQSLGA 892
Cdd:PRK12323   365 PGQSGGGAGPATAAAAPVAQPAPAAAAPaaaapAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAarqASARGP 444
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1954668664  893 PEAAERPPAPVLDMAPAGHPEGDAEPSPGERVEDAAAPKAPGPSPA 938
Cdd:PRK12323   445 GGAPAPAPAPAAAPAAAARPAAAGPRPVAAAAAAAPARAAPAAAPA 490
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
652-807 6.57e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 40.73  E-value: 6.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  652 QEPMTLNGANSADSDSDPKENGLAPDGASCQGQPALHSENPFAKANGLPGKlMPAPLLSLPEDKILETfrlsnklKGSTD 731
Cdd:PRK13108   293 DEALEREPAELAAAAVASAASAVGPVGPGEPNQPDDVAEAVKAEVAEVTDE-VAAESVVQVADRDGES-------TPAVE 364
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1954668664  732 EMSAPGAERGPPEDRDAEP--QPGSPAAESLEEPDAAAGL-SSTKKAPPPRDPGTPATKEGAWEAMAVAPEEPPPSAGE 807
Cdd:PRK13108   365 ETSEADIEREQPGDLAGQApaAHQVDAEAASAAPEEPAALaSEAHDETEPEVPEKAAPIPDPAKPDELAVAGPGDDPAE 443
PRK14951 PRK14951
DNA polymerase III subunits gamma and tau; Provisional
803-938 6.58e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237865 [Multi-domain]  Cd Length: 618  Bit Score: 40.85  E-value: 6.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  803 PSAGEDIVGDTAPPDLCDPGSLTGDASPLSQDAKGMIAEGPRDSALAEAPEGLSPAPPARSEEPceqpllvhpsgdhard 882
Cdd:PRK14951   366 PAAAAEAAAPAEKKTPARPEAAAPAAAPVAQAAAAPAPAAAPAAAASAPAAPPAAAPPAPVAAP---------------- 429
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1954668664  883 AQDPSQSLGAPEAAERPPAPVLDMAPAghPEGDAEP---SPGERVEDAAAPKAPGPSPA 938
Cdd:PRK14951   430 AAAAPAAAPAAAPAAVALAPAPPAQAA--PETVAIPvrvAPEPAVASAAPAPAAAPAAA 486
COG5373 COG5373
Uncharacterized membrane protein [Function unknown];
708-806 6.83e-03

Uncharacterized membrane protein [Function unknown];


Pssm-ID: 444140 [Multi-domain]  Cd Length: 854  Bit Score: 40.75  E-value: 6.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  708 LLSLPEDKILETFRLSNKLKGSTDEMSAPGAERGPPedrdAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPGTPATK 787
Cdd:COG5373     12 VLALLVGLLGRVARLRRRVEELEAELAEAAEAASAP----AEPEPEAAAAATAAAPEAAPAPVPEAPAAPPAAAEAPAPA 87
                           90
                   ....*....|....*....
gi 1954668664  788 EGAwEAMAVAPEEPPPSAG 806
Cdd:COG5373     88 AAA-PPAEAEPAAAPAAAS 105
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
740-896 7.14e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 7.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1954668664  740 RGPPEDRDAEPQPGSPAAESLEEPDAAAGLSSTKKAPPPRDPgtPATKEgawEAMAVAPEEPPPSAGEDIVGDTAPPDlc 819
Cdd:PRK07764   384 RLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAP--AAAPQ---PAPAPAPAPAPPSPAGNAPAGGAPSP-- 456
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1954668664  820 dpgsltgdasplsqdakgmiaegPRDSALAEAPEGLSPAPPARSEEPCEQPLLVHPSGDHARDAQDPSQSLGAPEAA 896
Cdd:PRK07764   457 -----------------------PPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAA 510
 
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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