|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
777-1106 |
2.82e-111 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 348.66 E-value: 2.82e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 777 TGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHkgeVAEEFGIIMKALWTG-QYRYISPKDFKITIG 855
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 856 KINDQFAGYSQQDSQELLLFLMDGLHEDLNkadnrkrykeenndhlddfkaaehawQKHKQLNESIIVALFQGQFKSTVQ 935
Cdd:pfam00443 78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 936 CLTCHKKSRTFEAFMYLSLPLASTSKCT----LQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHL 1011
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDSAELktasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1012 KRFSYDGRWKQKLQTSVDFPLEnLDLSQYVIGPK----NNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHE 1087
Cdd:pfam00443 212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELkpktNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290
|
330 340
....*....|....*....|
gi 190684690 1088 -VSDISVSSVKSSAAYILFY 1106
Cdd:pfam00443 291 vTEVDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
778-1107 |
5.34e-106 |
|
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: 331.56 E-value: 5.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLCNaphladyfnrncyqddinrsnllghkgevaeefgiimkalwtgqyryispkdfkitigki 857
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 858 ndqfagySQQDSQELLLFLMDGLHedlnkadnrkrykeenndhlddfkaaehawqkhkqlneSIIVALFQGQFKSTVQCL 937
Cdd:cd02674 21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 938 TCHKKSRTFEAFMYLSLPLASTS----KCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKR 1013
Cdd:cd02674 56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1014 FSYDGRWKQKLQTSVDFPLENLDLSQYVIGP-KNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDIS 1092
Cdd:cd02674 136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215
|
330
....*....|....*
gi 190684690 1093 VSSVKSSAAYILFYT 1107
Cdd:cd02674 216 ESSVVSSSAYILFYE 230
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
700-1106 |
4.81e-55 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 206.66 E-value: 4.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 700 PQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGgsgpaLTGL 779
Cdd:COG5560 194 PEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDSIVDDHNRSINKEAG-----TCGL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 780 RNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKIND 859
Cdd:COG5560 269 RNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 860 QFAGYSQQDSQELLLFLMDGLHEDLNKAdNRKRYKEE----NNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQ 935
Cdd:COG5560 349 EFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLT 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 936 CLTCHKKSRTFEAFMYLSLPL---------------------------ASTSKCTLQD----------CLRLFS------ 972
Cdd:COG5560 428 CPGCGSVSITFDPFMDLTLPLpvsmvwkhtivvfpesgrrqplkieldASSTIRGLKKlvdaeygklgCFEIKVmciyyg 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 973 --------------KEEKLTDNNRFYCS----------HCRAR------------------------RDSL--------- 995
Cdd:COG5560 508 gnynmlepadkvllQDIPQTDFVYLYETndngievpvvHLRIEkgykskrlfgdpflqlnvlikasiYDKLvkefeellv 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 996 ----------------------KKIEIW--------------------KLPPVLLV---------HLKRFSYDGRW---- 1020
Cdd:COG5560 588 lvemkktdvdlvseqvrllreeSSPSSWlkleteidtkreeqveeegqMNFNDAVVisceweekrYLSLFSYDPLWtire 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1021 ----------------------------------KQKLQTS--------------------------------VDFPLEN 1034
Cdd:COG5560 668 igaaertitlqdclnefskpeqlglsdswycpgcKEFRQASkqmelwrlpmiliihlkrfssvrsfrdkiddlVEYPIDD 747
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190684690 1035 LDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFY 1106
Cdd:COG5560 748 LDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819
|
|
| USP8_dimer |
pfam08969 |
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ... |
6-116 |
6.39e-37 |
|
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.
Pssm-ID: 462647 Cd Length: 113 Bit Score: 134.73 E-value: 6.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 6 SVPKELYLSSSLKDLNKKTEVKP--EKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQ 83
Cdd:pfam08969 1 APLKPLHLSSSLEDLEKLTEKLEvdKNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80
|
90 100 110
....*....|....*....|....*....|...
gi 190684690 84 DYFHSILGPGNIKKAVEEAERLSESLKLRYEEA 116
Cdd:pfam08969 81 ATVRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
375-547 |
6.97e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.54 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 375 LNISTPVEPVAASKSDVSPIIQPVP--SIKNVPQIDRTK--KPAVKLPEEHRIKSEstnhEQQSPQsgkVIPDRSTKPVV 450
Cdd:TIGR02794 18 LILGSLYHSVKPEPGGGAEIIQAVLvdPGAVAQQANRIQqqKKPAAKKEQERQKKL----EQQAEE---AEKQRAAEQAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 451 FSPTLMLTDEEKARIHAETAllmeknKQEKELRERQQEEQKEKlrkEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKES 530
Cdd:TIGR02794 91 QKELEQRAAAEKAAKQAEQA------AKQAEEKQKQAEEAKAK---QAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAA 161
|
170
....*....|....*..
gi 190684690 531 EQAKKEDKETSAKRGKE 547
Cdd:TIGR02794 162 AEAKKKAEEAKKKAEAE 178
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
192-304 |
1.89e-05 |
|
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.
Pssm-ID: 425764 [Multi-domain] Cd Length: 92 Bit Score: 44.40 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 192 MTDKNISLIimDARRMQDYQDSCILHSLSVPEEAIspgvtasWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLqig 271
Cdd:pfam00581 1 LEDGKVVLI--DVRPPEEYAKGHIPGAVNVPLSSL-------SLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAA--- 68
|
90 100 110
....*....|....*....|....*....|...
gi 190684690 272 tTLRSLKDALFKwesktvlrnEPLVLEGGYENW 304
Cdd:pfam00581 69 -AAALLKALGYK---------NVYVLDGGFEAW 91
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
343-509 |
2.80e-05 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 48.61 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 343 IPSKPAAQTPPASIEVDENIELISGQNERMGPLNISTPVepvAASKSDVSPIIQpvpsIKNVPqIDRTKKPAVKLPEEHR 422
Cdd:pfam03154 468 VPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPV---PAAVSCPLPPVQ----IKEEA-LDEAEEPESPPPPPRS 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 423 IKSEST-----NHEQQSPQSGKVIpDR-----STKPVVFSPtlmLTDEEKARIHAETallMEKNKQE-----KELRERQQ 487
Cdd:pfam03154 540 PSPEPTvvntpSHASQSARFYKHL-DRgynscARTDLYFMP---LAGSKLAKKREEA---LEKAKREaeqkaREEKEREK 612
|
170 180
....*....|....*....|..
gi 190684690 488 EEQKEKLRKEEQEQKAKKKQEA 509
Cdd:pfam03154 613 EKEKEREREREREREAERAAKA 634
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
477-587 |
4.17e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 477 KQEKELRERQ---QEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKE-----TSAKRGKEI 548
Cdd:PRK09510 87 QQAEELQQKQaaeQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEakraaAAAKKAAAE 166
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 190684690 549 TGVKRQSKSEHET-SDAKKSVEDRGKRCPTPEIQKKSTGD 587
Cdd:PRK09510 167 AKKKAEAEAAKKAaAEAKKKAEAEAAAKAAAEAKKKAEAE 206
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
309-614 |
1.99e-04 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 45.86 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 309 PQYTTNAKVTPPPRRQN--------EEVSISLDFT-YPS-LEESIPSKPAAQTPPASIEVDENIELISGQNERmgplniS 378
Cdd:NF033875 50 PGTTTVQPDNPDPQSGSetpktavsEEATVQKDTTsQPTkVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEK------S 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 379 TPVEPVAASKSDVSPIIQPVpsiknvpqidrtkkpAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKP---VVFSPTL 455
Cdd:NF033875 124 AQEQPVVSPETTNEPLGQPT---------------EVAPAENEANKSTSIPKEFETPDVDKAVDEAKKDPnitVVEKPAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 456 MLTDEEKARIHAetallmeknkQEKELrERQQEEQKEKLRKEEQEQKAKKKQEAEEN-EITEKQQKAKEEMEKKESEQAK 534
Cdd:NF033875 189 DLGNVSSKDLAA----------KEKEV-DQLQKEQAKKIAQQAAELKAKNEKIAKENaEIAAKNKAEKERYEKEVAEYNK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 535 KEDKETSAKRGKEITGVKRQSKSeheTSDAKKSVEDRGKRCPTPEIQKKSTGDVP----------HTSVTGDSGSGKPFK 604
Cdd:NF033875 258 HKNENGYVNEAISKNLVFDQSVV---TKDTKISSIKGGKFIKATDFNKVNAGDSKdiftklskdmGGKATGNFQNSFVKE 334
|
330
....*....|
gi 190684690 605 IKGQPESGIL 614
Cdd:NF033875 335 ANLGSNGGYA 344
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
472-574 |
8.24e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 472 LMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQkakeeMEKKESEQAKKEDKETSAKRGKEItgV 551
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKR-----QAEEEAREAKAEAEQRAAELAAEA--A 76
|
90 100
....*....|....*....|...
gi 190684690 552 KRQSKSEHETSDAKKSVEDRGKR 574
Cdd:COG3064 77 KKLAEAEKAAAEAEKKAAAEKAK 99
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
199-310 |
3.58e-03 |
|
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
Pssm-ID: 197731 [Multi-domain] Cd Length: 100 Bit Score: 38.21 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 199 LIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWieaHLPDDSKDTWKKRGNVEYVVLLDwfssakdlqiGTTLRSlk 278
Cdd:smart00450 5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELD---ILEFEELLKRLGLDKDKPVVVYC----------RSGNRS-- 69
|
90 100 110
....*....|....*....|....*....|..
gi 190684690 279 dALFKWESKTVLRNEPLVLEGGYENWLLCYPQ 310
Cdd:smart00450 70 -AKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
459-656 |
3.64e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.18 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 459 DEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQkakeemekkesEQAKKEDK 538
Cdd:COG3064 54 EEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAA-----------AAAEKEKA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 539 ETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILRTGT 618
Cdd:COG3064 123 EEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAA 202
|
170 180 190
....*....|....*....|....*....|....*...
gi 190684690 619 FREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWA 656
Cdd:COG3064 203 LAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
777-1106 |
2.82e-111 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 348.66 E-value: 2.82e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 777 TGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHkgeVAEEFGIIMKALWTG-QYRYISPKDFKITIG 855
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLSEDSRYNKDIN---LLCALRDLFKALQKNsKSSSVSPKMFKKSLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 856 KINDQFAGYSQQDSQELLLFLMDGLHEDLNkadnrkrykeenndhlddfkaaehawQKHKQLNESIIVALFQGQFKSTVQ 935
Cdd:pfam00443 78 KLNPDFSGYKQQDAQEFLLFLLDGLHEDLN--------------------------GNHSTENESLITDLFRGQLKSRLK 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 936 CLTCHKKSRTFEAFMYLSLPLASTSKCT----LQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHL 1011
Cdd:pfam00443 132 CLSCGEVSETFEPFSDLSLPIPGDSAELktasLQICFLQFSKLEELDDEEKYYCDKCGCKQDAIKQLKISRLPPVLIIHL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1012 KRFSYDGRWKQKLQTSVDFPLEnLDLSQYVIGPK----NNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHE 1087
Cdd:pfam00443 212 KRFSYNRSTWEKLNTEVEFPLE-LDLSRYLAEELkpktNNLQDYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEK 290
|
330 340
....*....|....*....|
gi 190684690 1088 -VSDISVSSVKSSAAYILFY 1106
Cdd:pfam00443 291 vTEVDEETAVLSSSAYILFY 310
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
778-1107 |
5.34e-106 |
|
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: 331.56 E-value: 5.34e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLCNaphladyfnrncyqddinrsnllghkgevaeefgiimkalwtgqyryispkdfkitigki 857
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 858 ndqfagySQQDSQELLLFLMDGLHedlnkadnrkrykeenndhlddfkaaehawqkhkqlneSIIVALFQGQFKSTVQCL 937
Cdd:cd02674 21 -------DQQDAQEFLLFLLDGLH--------------------------------------SIIVDLFQGQLKSRLTCL 55
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 938 TCHKKSRTFEAFMYLSLPLASTS----KCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKR 1013
Cdd:cd02674 56 TCGKTSTTFEPFTYLSLPIPSGSgdapKVTLEDCLRLFTKEETLDGDNAWKCPKCKKKRKATKKLTISRLPKVLIIHLKR 135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1014 FSYDGRWKQKLQTSVDFPLENLDLSQYVIGP-KNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDIS 1092
Cdd:cd02674 136 FSFSRGSTRKLTTPVTFPLNDLDLTPYVDTRsFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTKVS 215
|
330
....*....|....*
gi 190684690 1093 VSSVKSSAAYILFYT 1107
Cdd:cd02674 216 ESSVVSSSAYILFYE 230
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
778-1106 |
4.92e-72 |
|
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239072 [Multi-domain] Cd Length: 255 Bit Score: 240.08 E-value: 4.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLCNaphladyfnrncyqddinrsnllghkgevaeefgiimkalwtgqyryispkdfkitigki 857
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS------------------------------------------------------------ 20
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 858 ndqfagySQQDSQELLLFLMDGLHEDLNKADNRKRYKEENndhlddfkaaehawqkhkqlnESIIVALFQGQFKSTVQCL 937
Cdd:cd02257 21 -------EQQDAHEFLLFLLDKLHEELKKSSKRTSDSSSL---------------------KSLIHDLFGGKLESTIVCL 72
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 938 TCHKKSRTFEAFMYLSLPL--ASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRaRRDSLKKIEIWKLPPVLLVHLKRFS 1015
Cdd:cd02257 73 ECGHESVSTEPELFLSLPLpvKGLPQVSLEDCLEKFFKEEILEGDNCYKCEKKK-KQEATKRLKIKKLPPVLIIHLKRFS 151
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1016 YDGRW-KQKLQTSVDFPLEnLDLSQYVI------GPKNNLKKYNLFSVSNHYGGL-DGGHYTAYCKNAARQRWFKFDD-- 1085
Cdd:cd02257 152 FNEDGtKEKLNTKVSFPLE-LDLSPYLSegekdsDSDNGSYKYELVAVVVHSGTSaDSGHYVAYVKDPSDGKWYKFNDdk 230
|
330 340
....*....|....*....|....
gi 190684690 1086 ---HEVSDISVSSVKSSAAYILFY 1106
Cdd:cd02257 231 vteVSEEEVLEFGSLSSSAYILFY 254
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
778-1107 |
5.40e-67 |
|
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: 228.80 E-value: 5.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLCNAPHLADYF--NRNCYQDDINRSN--LLGHKGEVAEEFGIIMKalwTGQYryiSPKDFKIT 853
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNYFlsDRHSCTCLSCSPNscLSCAMDEIFQEFYYSGD---RSPY---GPINLLYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 854 IGKINDQFAGYSQQDSQELLLFLMDGLHEDLnkadnrKRYKEENNDhlddfkaaehawqkHKQLNeSIIVALFQGQFKST 933
Cdd:cd02660 76 SWKHSRNLAGYSQQDAHEFFQFLLDQLHTHY------GGDKNEAND--------------ESHCN-CIIHQTFSGSLQSS 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 934 VQCLTCHKKSRTFEAFMYLSLPLASTSKC-------------TLQDCLRLFSKEEKLTDNNrFYCSHCRARRDSLKKIEI 1000
Cdd:cd02660 135 VTCQRCGGVSTTVDPFLDLSLDIPNKSTPswalgesgvsgtpTLSDCLDRFTRPEKLGDFA-YKCSGCGSTQEATKQLSI 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1001 WKLPPVLLVHLKRFSYD-GRWKQKLQTSVDFPLEnLDLSQYVIG---------PKNNLKKYNLFSVSNHYGGLDGGHYTA 1070
Cdd:cd02660 214 KKLPPVLCFQLKRFEHSlNKTSRKIDTYVQFPLE-LNMTPYTSSsigdtqdsnSLDPDYTYDLFAVVVHKGTLDTGHYTA 292
|
330 340 350
....*....|....*....|....*....|....*..
gi 190684690 1071 YCKNAARQrWFKFDDHEVSDISVSSVKSSAAYILFYT 1107
Cdd:cd02660 293 YCRQGDGQ-WFKFDDAMITRVSEEEVLKSQAYLLFYH 328
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
777-1106 |
7.99e-61 |
|
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: 210.21 E-value: 7.99e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 777 TGLRNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRsnllghkgevaEEFGI-------IMKALWTGQYrYISPKD 849
Cdd:cd02661 2 AGLQNLGNTCFLNSVLQCLTHTPPLANYLLSREHSKDCCN-----------EGFCMmcaleahVERALASSGP-GSAPRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 850 FKITIGKINDQFAGYSQQDSQELLLFLMDGLHedlnKADNRKRYKEENNDHLddfkaaehawQKHKqlneSIIVALFQGQ 929
Cdd:cd02661 70 FSSNLKQISKHFRIGRQEDAHEFLRYLLDAMQ----KACLDRFKKLKAVDPS----------SQET----TLVQQIFGGY 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 930 FKSTVQCLTCHKKSRTFEAFMYLSLPLASTSkcTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLV 1009
Cdd:cd02661 132 LRSQVKCLNCKHVSNTYDPFLDLSLDIKGAD--SLEDALEQFTKPEQLDGENKYKCERCKKKVKASKQLTIHRAPNVLTI 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1010 HLKRFSYDGRwkQKLQTSVDFPlENLDLSQYVIGPKNNLKKYNLFSVSNHYGG-LDGGHYTAYCKnAARQRWFKFDDHEV 1088
Cdd:cd02661 210 HLKRFSNFRG--GKINKQISFP-ETLDLSPYMSQPNDGPLKYKLYAVLVHSGFsPHSGHYYCYVK-SSNGKWYNMDDSKV 285
|
330
....*....|....*...
gi 190684690 1089 SDISVSSVKSSAAYILFY 1106
Cdd:cd02661 286 SPVSIETVLSQKAYILFY 303
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
700-1106 |
4.81e-55 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 206.66 E-value: 4.81e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 700 PQIPAERDREPSKLKRSYSSPDITQAIQEEEKRKPTVTPTVNRENKPTCYPKAEISRLSASQIRNLNPVFGgsgpaLTGL 779
Cdd:COG5560 194 PEIMGLRLGLDSFFRRYRVLASDGRVLHPLTRLELFEDRSVLLLSKITRNPDWLVDSIVDDHNRSINKEAG-----TCGL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 780 RNLGNTCYMNSILQCLCNAPHLADYFNRNCYQDDINRSNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKITIGKIND 859
Cdd:COG5560 269 RNLGNTCYMNSALQCLMHTWELRDYFLSDEYEESINEENPLGMHGSVASAYADLIKQLYDGNLHAFTPSGFKKTIGSFNE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 860 QFAGYSQQDSQELLLFLMDGLHEDLNKAdNRKRYKEE----NNDHLDDFKAAEHAWQKHKQLNESIIVALFQGQFKSTVQ 935
Cdd:COG5560 349 EFSGYDQQDSQEFIAFLLDGLHEDLNRI-IKKPYTSKpdlsPGDDVVVKKKAKECWWEHLKRNDSIITDLFQGMYKSTLT 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 936 CLTCHKKSRTFEAFMYLSLPL---------------------------ASTSKCTLQD----------CLRLFS------ 972
Cdd:COG5560 428 CPGCGSVSITFDPFMDLTLPLpvsmvwkhtivvfpesgrrqplkieldASSTIRGLKKlvdaeygklgCFEIKVmciyyg 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 973 --------------KEEKLTDNNRFYCS----------HCRAR------------------------RDSL--------- 995
Cdd:COG5560 508 gnynmlepadkvllQDIPQTDFVYLYETndngievpvvHLRIEkgykskrlfgdpflqlnvlikasiYDKLvkefeellv 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 996 ----------------------KKIEIW--------------------KLPPVLLV---------HLKRFSYDGRW---- 1020
Cdd:COG5560 588 lvemkktdvdlvseqvrllreeSSPSSWlkleteidtkreeqveeegqMNFNDAVVisceweekrYLSLFSYDPLWtire 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1021 ----------------------------------KQKLQTS--------------------------------VDFPLEN 1034
Cdd:COG5560 668 igaaertitlqdclnefskpeqlglsdswycpgcKEFRQASkqmelwrlpmiliihlkrfssvrsfrdkiddlVEYPIDD 747
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 190684690 1035 LDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDDHEVSDISVSSVKSSAAYILFY 1106
Cdd:COG5560 748 LDLSGVEYMVDDPRLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVDPEDSVTSSAYVLFY 819
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
778-1106 |
2.79e-49 |
|
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: 176.42 E-value: 2.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLCNAPHLADYFNRNcyqddinRSNLLGhkgevaeefgiimkalwtgQYRYISPkdfkitigki 857
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSET-------PKELFS-------------------QVCRKAP---------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 858 ndQFAGYSQQDSQELLLFLMDGLhedlnkadnrkrykeenndhlddfkaaehawqkhkqlnESIIVALFQGQFKSTVQCL 937
Cdd:cd02667 45 --QFKGYQQQDSHELLRYLLDGL--------------------------------------RTFIDSIFGGELTSTIMCE 84
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 938 TCHKKSRTFEAFMYLSLPLA--STSKCTLQDCLRLFSKEEKLTDNNRFYCSHC-RARRDSLkkieIWKLPPVLLVHLKRF 1014
Cdd:cd02667 85 SCGTVSLVYEPFLDLSLPRSdeIKSECSIESCLKQFTEVEILEGNNKFACENCtKAKKQYL----ISKLPPVLVIHLKRF 160
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1015 SYDGRWK-QKLQTSVDFPlENLDLSQYVIGPKNNLK-----KYNLFSVSNHYGGLDGGHYTAYCK--------------- 1073
Cdd:cd02667 161 QQPRSANlRKVSRHVSFP-EILDLAPFCDPKCNSSEdkssvLYRLYGVVEHSGTMRSGHYVAYVKvrppqqrlsdltksk 239
|
330 340 350
....*....|....*....|....*....|....*....
gi 190684690 1074 ------NAARQRWFKFDDHEVSDISVSSVKSSAAYILFY 1106
Cdd:cd02667 240 paadeaGPGSGQWYYISDSDVREVSLEEVLKSEAYLLFY 278
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
778-1107 |
7.32e-48 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 172.88 E-value: 7.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLcnaphladYFNR--NCYQDdinrsnllghkgevaeefgiIMKALWTGQYRY--ISPKDFKIT 853
Cdd:cd02663 1 GLENFGNTCYCNSVLQAL--------YFENllTCLKD--------------------LFESISEQKKRTgvISPKKFITR 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 854 IGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKAdnRKRYKEENNDHLDDFKAAEHAWqkhkqlnesiIVALFQGQFKST 933
Cdd:cd02663 53 LKRENELFDNYMHQDAHEFLNFLLNEIAEILDAE--RKAEKANRKLNNNNNAEPQPTW----------VHEIFQGILTNE 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 934 VQCLTCHKKSRTFEAFMYLSLPLASTskCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKR 1013
Cdd:cd02663 121 TRCLTCETVSSRDETFLDLSIDVEQN--TSITSCLRQFSATETLCGRNKFYCDECCSLQEAEKRMKIKKLPKILALHLKR 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1014 FSYDGRWKQ--KLQTSVDFPLEnLDLSQYVIGPKNNLKKYNLFSVSNHYG-GLDGGHYTAYCKNAArqRWFKFDD----- 1085
Cdd:cd02663 199 FKYDEQLNRyiKLFYRVVFPLE-LRLFNTTDDAENPDRLYELVAVVVHIGgGPNHGHYVSIVKSHG--GWLLFDDetvek 275
|
330 340
....*....|....*....|....*
gi 190684690 1086 ---HEVSDISVSSVKSSAAYILFYT 1107
Cdd:cd02663 276 ideNAVEEFFGDSPNQATAYVLFYQ 300
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
778-1087 |
2.09e-47 |
|
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: 172.61 E-value: 2.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCL-CNAPHLADYFNRNCYQDDINR---SNLLGHKGEVAEEFGIIMKALWTGQYRYISPKDFKIT 853
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWfMNLEFRKAVYECNSTEDAELKnmpPDKPHEPQTIIDQLQLIFAQLQFGNRSVVDPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 854 IGKINDQfagysQQDSQELLLFLMDGLHEDLNKADNRKrykeenndhlddfkaaehawqkhkqlNESIIVALFQGQFKST 933
Cdd:cd02668 81 LGLDTGQ-----QQDAQEFSKLFLSLLEAKLSKSKNPD--------------------------LKNIVQDLFRGEYSYV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 934 VQCLTCHKKSRTFEAFMYLSLPLASTSkcTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKR 1013
Cdd:cd02668 130 TQCSKCGRESSLPSKFYELELQLKGHK--TLEECIDEFLKEEQLTGDNQYFCESCNSKTDATRRIRLTTLPPTLNFQLLR 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 190684690 1014 FSYD--GRWKQKLQTSVDFPlENLDLSQYVIGPKNNLKKYNLFSVSNHYG-GLDGGHYTAYCKNAARQRWFKFDDHE 1087
Cdd:cd02668 208 FVFDrkTGAKKKLNASISFP-EILDMGEYLAESDEGSYVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYKFNDED 283
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
778-1085 |
1.57e-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: 239124 [Multi-domain] Cd Length: 334 Bit Score: 164.74 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLCNAPhladYFNRNCYQ--------DDINRSNLLghkgEVaeefgiIMKALWTGQYRYISPKD 849
Cdd:cd02659 4 GLKNQGATCYMNSLLQQLYMTP----EFRNAVYSipptedddDNKSVPLAL----QR------LFLFLQLSESPVKTTEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 850 FKITIGKINDQFAGYSQQDSQELLLFLMDGLhedlnkadnrkrykeenndhlddfkaaEHAWQKHKQlnESIIVALFQGQ 929
Cdd:cd02659 70 TDKTRSFGWDSLNTFEQHDVQEFFRVLFDKL---------------------------EEKLKGTGQ--EGLIKNLFGGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 930 FKSTVQCLTCHKKSRTFEAFmyLSLPLASTSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLV 1009
Cdd:cd02659 121 LVNYIICKECPHESEREEYF--LDLQVAVKGKKNLEESLDAYVQGETLEGDNKYFCEKCGKKVDAEKGVCFKKLPPVLTL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1010 HLKRFSYDGR--WKQKLQTSVDFPLEnLDLSQYVIGPKNNLK-----------KYNLFSVSNHYGGLDGGHYTAYCKNAA 1076
Cdd:cd02659 199 QLKRFEFDFEtmMRIKINDRFEFPLE-LDMEPYTEKGLAKKEgdsekkdsesyIYELHGVLVHSGDAHGGHYYSYIKDRD 277
|
....*....
gi 190684690 1077 RQRWFKFDD 1085
Cdd:cd02659 278 DGKWYKFND 286
|
|
| USP8_dimer |
pfam08969 |
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of ... |
6-116 |
6.39e-37 |
|
USP8 dimerization domain; This domain is predominantly found in the amino terminal region of Ubiquitin carboxyl-terminal hydrolase 8 (USP8). It forms a five helical bundle that dimerizes.
Pssm-ID: 462647 Cd Length: 113 Bit Score: 134.73 E-value: 6.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 6 SVPKELYLSSSLKDLNKKTEVKP--EKISTKSYVHSALKIFKTAEECRLDRDEERAYVLYMKYVTVYNLIKKRPDFKQQQ 83
Cdd:pfam08969 1 APLKPLHLSSSLEDLEKLTEKLEvdKNKSPKRYYRSALKLYKTAEEYRLEGDEENAYILYMKYFNLFEKIRKHPDYKSVK 80
|
90 100 110
....*....|....*....|....*....|...
gi 190684690 84 DYFHSILGPGNIKKAVEEAERLSESLKLRYEEA 116
Cdd:pfam08969 81 ATVRQMLGKTKINEVLDELEKLKTSLLERYEEE 113
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
778-1106 |
1.11e-32 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239129 [Multi-domain] Cd Length: 327 Bit Score: 129.92 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLcnapHLADYFNRncyqdDINRSNLLGHKGEVAEEFGIIM-KALWTGQYRYISPKDFKITIGK 856
Cdd:cd02664 1 GLINLGNTCYMNSVLQAL----FMAKDFRR-----QVLSLNLPRLGDSQSVMKKLQLlQAHLMHTQRRAEAPPDYFLEAS 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 857 INDQFAGYSQQDSQELLLFLMDGLHedlnkadnrkrykeenndhlddfkaaehawqkhkqlneSIIVALFQGQFKSTVQC 936
Cdd:cd02664 72 RPPWFTPGSQQDCSEYLRYLLDRLH--------------------------------------TLIEKMFGGKLSTTIRC 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 937 LTCHKKSRTFEAFMYLSLplastSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSY 1016
Cdd:cd02664 114 LNCNSTSARTERFRDLDL-----SFPSVQDLLNYFLSPEKLTGDNQYYCEKCASLQDAEKEMKVTGAPEYLILTLLRFSY 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1017 D--GRWKQKLQTSVDFPlENLDLSQYV----IGPKNNLKK---------------YNLFSVSNHYG-GLDGGHYTAYCKN 1074
Cdd:cd02664 189 DqkTHVREKIMDNVSIN-EVLSLPVRVesksSESPLEKKEeesgddgelvtrqvhYRLYAVVVHSGySSESGHYFTYARD 267
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 190684690 1075 AA--------------------RQRWFKFDDH-------EVSDISVSSVKSSAAYILFY 1106
Cdd:cd02664 268 QTdadstgqecpepkdaeendeSKNWYLFNDSrvtfssfESVQNVTSRFPKDTPYILFY 326
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
778-1085 |
2.96e-29 |
|
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: 119.36 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLCNAPHLAD---YFNRNCYQDDINRSNLLghkgevaEEFGIIMKALWTGQYRyISPKDFKITI 854
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDalkNYNPARRGANQSSDNLT-------NALRDLFDTMDKKQEP-VPPIEFLQLL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 855 GKINDQFA------GYSQQDSQELLLFLMDGLHEDLNKADnrkrykeenndhlddfkaaehawqkhkqLNESIIVALFQG 928
Cdd:cd02657 73 RMAFPQFAekqnqgGYAQQDAEECWSQLLSVLSQKLPGAG----------------------------SKGSFIDQLFGI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 929 QFKSTVQCL-TCHKKSRTFEAFMYLSLPLASTSKC-TLQDCLRLFSKEE--KLTDNnrfycshcrARRDSL--KKIEIWK 1002
Cdd:cd02657 125 ELETKMKCTeSPDEEEVSTESEYKLQCHISITTEVnYLQDGLKKGLEEEieKHSPT---------LGRDAIytKTSRISR 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1003 LPPVLLVHLKRFSydgrWKQKLQT------SVDFPLEnLDLSQYVigpkNNLKKYNLFSVSNHYG-GLDGGHYTAYCKNA 1075
Cdd:cd02657 196 LPKYLTVQFVRFF----WKRDIQKkakilrKVKFPFE-LDLYELC----TPSGYYELVAVITHQGrSADSGHYVAWVRRK 266
|
330
....*....|
gi 190684690 1076 ARQRWFKFDD 1085
Cdd:cd02657 267 NDGKWIKFDD 276
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
774-1087 |
4.37e-29 |
|
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: 119.61 E-value: 4.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 774 PALTGLRNLGNTCYMNSILQCLCNAPH----LADYFNRNCYQDDINRSNLLGHKgevaeefgiimkaLWTGQYRYISPKD 849
Cdd:cd02671 22 LPFVGLNNLGNTCYLNSVLQVLYFCPGfkhgLKHLVSLISSVEQLQSSFLLNPE-------------KYNDELANQAPRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 850 FKITIGKINDQFAGYSQQDSQELLLFLMDGLHEDLNKadnrkrykeenndhlddfkaaehawqkhkqlnesiivaLFQGQ 929
Cdd:cd02671 89 LLNALREVNPMYEGYLQHDAQEVLQCILGNIQELVEK--------------------------------------DFQGQ 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 930 FKSTVQCLTCHKKSRTFEAFMYLSLPLAS-----------------TSKCTLQDCLRLFSKEEKLTDNNRFYCSHCRARR 992
Cdd:cd02671 131 LVLRTRCLECETFTERREDFQDISVPVQEselskseesseispdpkTEMKTLKWAISQFASVERIVGEDKYFCENCHHYT 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 993 DSLKKIEIWKLPPVLLVHLKRFSYDGRWK------QKLQTSVDFPLEnLDLSQYVIGPKNNLkkYNLFSVSNHYGG-LDG 1065
Cdd:cd02671 211 EAERSLLFDKLPEVITIHLKCFAANGSEFdcygglSKVNTPLLTPLK-LSLEEWSTKPKNDV--YRLFAVVMHSGAtISS 287
|
330 340
....*....|....*....|..
gi 190684690 1066 GHYTAYCknaarqRWFKFDDHE 1087
Cdd:cd02671 288 GHYTAYV------RWLLFDDSE 303
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
778-1106 |
1.71e-28 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 117.04 E-value: 1.71e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLCNAPHLADYFN--RNCYQDDIN--RSNLLGHKGEVAeefgiimKALWTGQYRY--------- 844
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWRYDdlENKFPSDVVdpANDLNCQLIKLA-------DGLLSGRYSKpaslksend 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 845 -----ISPKDFKITIGKINDQFAGYSQQDSQELLLFLMDglhedlnKADNRKRYKEENNdhlddfkaaehawqkhkqLNE 919
Cdd:cd02658 74 pyqvgIKPSMFKALIGKGHPEFSTMRQQDALEFLLHLID-------KLDRESFKNLGLN------------------PND 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 920 siivaLFQGQFKSTVQCLTCHKKSRTFEAFMYLSLPL------------ASTSKCTLQDCLRLFSKEEKLTDnnrfYCSH 987
Cdd:cd02658 129 -----LFKFMIEDRLECLSCKKVKYTSELSEILSLPVpkdeatekeegeLVYEPVPLEDCLKAYFAPETIED----FCST 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 988 CRARRDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQ-KLQTSVDFPlenldlsqYVIGPknnlKKYNLFSVSNHYG-GLDG 1065
Cdd:cd02658 200 CKEKTTATKTTGFKTFPDYLVINMKRFQLLENWVPkKLDVPIDVP--------EELGP----GKYELIAFISHKGtSVHS 267
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 190684690 1066 GHYTAYCK--NAARQRWFKFDDHEVSDISVSSVKSSAAYILFY 1106
Cdd:cd02658 268 GHYVAHIKkeIDGEGKWVLFNDEKVVASQDPPEMKKLGYIYFY 310
|
|
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
778-1085 |
6.33e-25 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 112.66 E-value: 6.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLcnapHLADYFNRNCYQ--DDINRSNllghkGEVAEEFGIIMKALWTGQYRyISPKDFkiTIG 855
Cdd:COG5077 195 GLRNQGATCYMNSLLQSL----FFIAKFRKDVYGipTDHPRGR-----DSVALALQRLFYNLQTGEEP-VDTTEL--TRS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 856 KINDQFAGYSQQDSQELLLFLMDGLhedlnkadnrkrykeENNdhlddfkaaehawqKHKQLNESIIVALFQGQFKSTVQ 935
Cdd:COG5077 263 FGWDSDDSFMQHDIQEFNRVLQDNL---------------EKS--------------MRGTVVENALNGIFVGKMKSYIK 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 936 CLTCHKKSRTFEAFMYLSLPLASTSkcTLQDCLRLFSKEEKLTDNNRFYCSHcRARRDSLKKIEIWKLPPVLLVHLKRFS 1015
Cdd:COG5077 314 CVNVNYESARVEDFWDIQLNVKGMK--NLQESFRRYIQVETLDGDNRYNAEK-HGLQDAKKGVIFESLPPVLHLQLKRFE 390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 190684690 1016 YDGRWKQ--KLQTSVDFPLEnLDLSQYV----IGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDD 1085
Cdd:COG5077 391 YDFERDMmvKINDRYEFPLE-IDLLPFLdrdaDKSENSDAVYVLYGVLVHSGDLHEGHYYALLKPEKDGRWYKFDD 465
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
778-1106 |
4.99e-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 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: 99.36 E-value: 4.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLCNAPHLADYFNRNcyqddinrsnllghkgevaeefgiimkalwtgqyryispkdfkitigki 857
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYLEEF------------------------------------------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 858 ndqfagYSQQDSQELLLFLMDGLhedlnkadnrkrykeenndhlddfkaaehawqkhkqlnESIIVALFQGQFKSTVQCL 937
Cdd:cd02662 32 ------LEQQDAHELFQVLLETL--------------------------------------EQLLKFPFDGLLASRIVCL 67
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 938 TCHKKSR-TFEAFMYLSLPL---ASTSKCTLQDCLRLFSKEEKLTDnnrFYCSHCrarrdslkKIEIWKLPPVLLVHLKR 1013
Cdd:cd02662 68 QCGESSKvRYESFTMLSLPVpnqSSGSGTTLEHCLDDFLSTEIIDD---YKCDRC--------QTVIVRLPQILCIHLSR 136
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1014 FSYDGRWK-QKLQTSVDFPLEnldLSQYvigpknnlkKYNLFSVSNHYGGLDGGHYTAY--------------------C 1072
Cdd:cd02662 137 SVFDGRGTsTKNSCKVSFPER---LPKV---------LYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreG 204
|
330 340 350
....*....|....*....|....*....|....*
gi 190684690 1073 KNAARQRWFKF-DDHEVSDISVSSVKSSAAYILFY 1106
Cdd:cd02662 205 PSSTSHPWWRIsDTTVKEVSESEVLEQKSAYMLFY 239
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
774-1085 |
1.88e-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: 239134 [Multi-domain] Cd Length: 440 Bit Score: 101.63 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 774 PALTGLRNLGNTCYMNSILQCLCNAPHLADYF-NRNCYQDDINRSNLLGHKgevaeeFGIIMKALWTGQY--RYISPKDF 850
Cdd:cd02669 117 PGFVGLNNIKNNDYANVIIQALSHVKPIRNFFlLYENYENIKDRKSELVKR------LSELIRKIWNPRNfkGHVSPHEL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 851 KITIGKINDQFAGYSQQ-DSQELLLFLMDGLHEDLNKAdnrkrykeenndhlddfkaaehawqkhKQLNESIIVALFQGQ 929
Cdd:cd02669 191 LQAVSKVSKKKFSITEQsDPVEFLSWLLNTLHKDLGGS---------------------------KKPNSSIIHDCFQGK 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 930 FKSTVQCLTCHK---------------KSRTFEAFMYLS--LPLASTSKCTLQD-CLRLFSKEEKLtdnNRFYCSHCRAR 991
Cdd:cd02669 244 VQIETQKIKPHAeeegskdkffkdsrvKKTSVSPFLLLTldLPPPPLFKDGNEEnIIPQVPLKQLL---KKYDGKTETEL 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 992 RDSLKKIEIWKLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLENLDLSQYVIGPKNNLK---KYNLfsVSN--HYGG-LDG 1065
Cdd:cd02669 321 KDSLKRYLISRLPKYLIFHIKRFSKNNFFKEKNPTIVNFPIKNLDLSDYVHFDKPSLNlstKYNL--VANivHEGTpQED 398
|
330 340
....*....|....*....|
gi 190684690 1066 GHYTAYCKNAARQRWFKFDD 1085
Cdd:cd02669 399 GTWRVQLRHKSTNKWFEIQD 418
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
778-1106 |
2.44e-22 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 98.34 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 778 GLRNLGNTCYMNSILQCLC-NAPHLADY-----FNRNCYQDDINRSnllgHKGEVAEEFGIIMKALWTGQyryispkdfK 851
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILAlYLPKLDELlddlsKELKVLKNVIRKP----EPDLNQEEALKLFTALWSSK---------E 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 852 ITIGKINDQfagYSQQDSQELLLFLMDGLHEDLNKADNRKRYK--EENNDHLDDfkaaehawqkhkQLNEsIIVALFQGQ 929
Cdd:COG5533 68 HKVGWIPPM---GSQEDAHELLGKLLDELKLDLVNSFTIRIFKttKDKKKTSTG------------DWFD-IIIELPDQT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 930 F---KSTVQCltchkksrTFEAFMYLslplaSTSKCTLqdclrlfskeeKLTDNNRFycsHCRARRDSLKKIEiwKLPPV 1006
Cdd:COG5533 132 WvnnLKTLQE--------FIDNMEEL-----VDDETGV-----------KAKENEEL---EVQAKQEYEVSFV--KLPKI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1007 LLVHLKRFSYDGRwKQKLQTSVDFPLEnLDLSQYVIGPKNNLKKYNLFSVSNHYGGLDGGHYTAYCKNaaRQRWFKFDDH 1086
Cdd:COG5533 183 LTIQLKRFANLGG-NQKIDTEVDEKFE-LPVKHDQILNIVKETYYDLVGFVLHQGSLEGGHYIAYVKK--GGKWEKANDS 258
|
330 340
....*....|....*....|...
gi 190684690 1087 EVSDISVSSVKSSA---AYILFY 1106
Cdd:COG5533 259 DVTPVSEEEAINEKaknAYLYFY 281
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
865-1085 |
1.11e-08 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 56.80 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 865 SQQDSQELLLFLMDGLHedlnkadnrkrykeenndhlDDFKAAEHAWQKHKQlNESIIVALFQGQFkSTVQCLTcHKKSR 944
Cdd:cd02665 21 QQQDVSEFTHLLLDWLE--------------------DAFQAAAEAISPGEK-SKNPMVQLFYGTF-LTEGVLE-GKPFC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 945 TFEafMYLSLPLASTSKCTLQDCLR--LFSKEEKLTDNNRFYCSHCRARRDslkkieiwKLPPVLLVHLKRFSYDGRWKQ 1022
Cdd:cd02665 78 NCE--TFGQYPLQVNGYGNLHECLEaaMFEGEVELLPSDHSVKSGQERWFT--------ELPPVLTFELSRFEFNQGRPE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 190684690 1023 KLQTSVDFPLEnldLSQYvigpknnlkKYNLFSVSNHYGGLDGGHYTAYCKNAARQRWFKFDD 1085
Cdd:cd02665 148 KIHDKLEFPQI---IQQV---------PYELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYND 198
|
|
| Peptidase_C19Q |
cd02673 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
779-1106 |
1.60e-08 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239138 [Multi-domain] Cd Length: 245 Bit Score: 56.77 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 779 LRNLGNTCYMNSILQCLCnaphladyfnrncyqddinrsnllghkgevaeefgiimkalwtgqyryispkdfkiTIGKIN 858
Cdd:cd02673 2 LVNTGNSCYFNSTMQALS--------------------------------------------------------SIGKIN 25
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 859 DQFAGYSQQDSQELLLFL---MDGLHEdlNKADNRKRYKEENndhlddfkaaehawqkhKQLNEsiiVALFQGQFKSTVQ 935
Cdd:cd02673 26 TEFDNDDQQDAHEFLLTLleaIDDIMQ--VNRTNVPPSNIEI-----------------KRLNP---LEAFKYTIESSYV 83
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 936 CLTCHKKSRTFEAFMYLSLPLASTSKCTLQDclrLFSKEEKLTDNNRfYCSHCRARRDSLKKiEIWKLPPVLLVHLKRFs 1015
Cdd:cd02673 84 CIGCSFEENVSDVGNFLDVSMIDNKLDIDEL---LISNFKTWSPIEK-DCSSCKCESAISSE-RIMTFPECLSINLKRY- 157
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1016 ydgrwkqKLQTSVdfpLENLDLSQYVIGP-KNNLKKYNLFSVSNHYG-GLDGGHYTAYCKNAAR-QRWFKFDD---HEVS 1089
Cdd:cd02673 158 -------KLRIAT---SDYLKKNEEIMKKyCGTDAKYSLVAVICHLGeSPYDGHYIAYTKELYNgSSWLYCSDdeiRPVS 227
|
330
....*....|....*..
gi 190684690 1090 DISVSSVKSSAAYILFY 1106
Cdd:cd02673 228 KNDVSTNARSSGYLIFY 244
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
875-1085 |
1.84e-07 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 54.20 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 875 FLMDGLHEDLNKAdnrkrykeenndhlddfkaaehawQKHKQLNESIIVALFQGQFKSTVQCLTC-HKKSRTFEAFMY-L 952
Cdd:pfam13423 105 FLLDQLSSEENST------------------------PPNPSPAESPLEQLFGIDAETTIRCSNCgHESVRESSTHVLdL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 953 SLPLASTS------KCTLQDCLRLFSKEEKLTdnnRFYCSHCRARRDSLKKIEIWKLPPVLLVHLKRFSYDgrWKQKLQT 1026
Cdd:pfam13423 161 IYPRKPSSnnkkppNQTFSSILKSSLERETTT---KAWCEKCKRYQPLESRRTVRNLPPVLSLNAALTNEE--WRQLWKT 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 190684690 1027 SVDFPLE-NLDLSQYVIGPkNNLKKYNLFS-VSNHYGGLDGGHYTAYCK-------NAARQRWFKFDD 1085
Cdd:pfam13423 236 PGWLPPEiGLTLSDDLQGD-NEIVKYELRGvVVHIGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
375-547 |
6.97e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.54 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 375 LNISTPVEPVAASKSDVSPIIQPVP--SIKNVPQIDRTK--KPAVKLPEEHRIKSEstnhEQQSPQsgkVIPDRSTKPVV 450
Cdd:TIGR02794 18 LILGSLYHSVKPEPGGGAEIIQAVLvdPGAVAQQANRIQqqKKPAAKKEQERQKKL----EQQAEE---AEKQRAAEQAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 451 FSPTLMLTDEEKARIHAETAllmeknKQEKELRERQQEEQKEKlrkEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKES 530
Cdd:TIGR02794 91 QKELEQRAAAEKAAKQAEQA------AKQAEEKQKQAEEAKAK---QAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAA 161
|
170
....*....|....*..
gi 190684690 531 EQAKKEDKETSAKRGKE 547
Cdd:TIGR02794 162 AEAKKKAEEAKKKAEAE 178
|
|
| Rhodanese |
pfam00581 |
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single ... |
192-304 |
1.89e-05 |
|
Rhodanese-like domain; Rhodanese has an internal duplication. This Pfam represents a single copy of this duplicated domain. The domain is found as a single copy in other proteins, including phosphatases and ubiquitin C-terminal hydrolases.
Pssm-ID: 425764 [Multi-domain] Cd Length: 92 Bit Score: 44.40 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 192 MTDKNISLIimDARRMQDYQDSCILHSLSVPEEAIspgvtasWIEAHLPDDSKDTWKKRGNVEYVVLLDWFSSAKDLqig 271
Cdd:pfam00581 1 LEDGKVVLI--DVRPPEEYAKGHIPGAVNVPLSSL-------SLPPLPLLELLEKLLELLKDKPIVVYCNSGNRAAA--- 68
|
90 100 110
....*....|....*....|....*....|...
gi 190684690 272 tTLRSLKDALFKwesktvlrnEPLVLEGGYENW 304
Cdd:pfam00581 69 -AAALLKALGYK---------NVYVLDGGFEAW 91
|
|
| Atrophin-1 |
pfam03154 |
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ... |
343-509 |
2.80e-05 |
|
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.
Pssm-ID: 460830 [Multi-domain] Cd Length: 991 Bit Score: 48.61 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 343 IPSKPAAQTPPASIEVDENIELISGQNERMGPLNISTPVepvAASKSDVSPIIQpvpsIKNVPqIDRTKKPAVKLPEEHR 422
Cdd:pfam03154 468 VPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSSSGPV---PAAVSCPLPPVQ----IKEEA-LDEAEEPESPPPPPRS 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 423 IKSEST-----NHEQQSPQSGKVIpDR-----STKPVVFSPtlmLTDEEKARIHAETallMEKNKQE-----KELRERQQ 487
Cdd:pfam03154 540 PSPEPTvvntpSHASQSARFYKHL-DRgynscARTDLYFMP---LAGSKLAKKREEA---LEKAKREaeqkaREEKEREK 612
|
170 180
....*....|....*....|..
gi 190684690 488 EEQKEKLRKEEQEQKAKKKQEA 509
Cdd:pfam03154 613 EKEKEREREREREREAERAAKA 634
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
477-587 |
4.17e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.11 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 477 KQEKELRERQ---QEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKE-----TSAKRGKEI 548
Cdd:PRK09510 87 QQAEELQQKQaaeQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEakraaAAAKKAAAE 166
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 190684690 549 TGVKRQSKSEHET-SDAKKSVEDRGKRCPTPEIQKKSTGD 587
Cdd:PRK09510 167 AKKKAEAEAAKKAaAEAKKKAEAEAAAKAAAEAKKKAEAE 206
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
477-584 |
1.28e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 477 KQEKELRERQQEEQK-EKLrKEEQEQKAKKKQEAEENEITEKQQKAKeemekkeseQAKKEDKETSAKRGKEITGVKRQS 555
Cdd:PRK00409 531 ELEQKAEEAEALLKEaEKL-KEELEEKKEKLQEEEDKLLEEAEKEAQ---------QAIKEAKKEADEIIKELRQLQKGG 600
|
90 100 110
....*....|....*....|....*....|..
gi 190684690 556 KS---EHETSDAKKSVEDRGKrcPTPEIQKKS 584
Cdd:PRK00409 601 YAsvkAHELIEARKRLNKANE--KKEKKKKKQ 630
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
1002-1106 |
1.52e-04 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239135 [Multi-domain] Cd Length: 241 Bit Score: 44.44 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 1002 KLPPVLLVHLKRFSYDGRWKQKLQTSVDFPLEnLDL----------------------SQYVIGPKNNLKKYNLFSVSNH 1059
Cdd:cd02670 97 KAPSCLIICLKRYGKTEGKAQKMFKKILIPDE-IDIpdfvaddpracskcqlecrvcyDDKDFSPTCGKFKLSLCSAVCH 175
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 190684690 1060 YG-GLDGGHYTAYCK-----------NAARQRWFKFDDHEVSDISVSSVKSSA------AYILFY 1106
Cdd:cd02670 176 RGtSLETGHYVAFVRygsysltetdnEAYNAQWVFFDDMADRDGVSNGFNIPAarlledPYMLFY 240
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
309-614 |
1.99e-04 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 45.86 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 309 PQYTTNAKVTPPPRRQN--------EEVSISLDFT-YPS-LEESIPSKPAAQTPPASIEVDENIELISGQNERmgplniS 378
Cdd:NF033875 50 PGTTTVQPDNPDPQSGSetpktavsEEATVQKDTTsQPTkVEEVASEKNGAEQSSATPNDTTNAQQPTVGAEK------S 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 379 TPVEPVAASKSDVSPIIQPVpsiknvpqidrtkkpAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKP---VVFSPTL 455
Cdd:NF033875 124 AQEQPVVSPETTNEPLGQPT---------------EVAPAENEANKSTSIPKEFETPDVDKAVDEAKKDPnitVVEKPAE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 456 MLTDEEKARIHAetallmeknkQEKELrERQQEEQKEKLRKEEQEQKAKKKQEAEEN-EITEKQQKAKEEMEKKESEQAK 534
Cdd:NF033875 189 DLGNVSSKDLAA----------KEKEV-DQLQKEQAKKIAQQAAELKAKNEKIAKENaEIAAKNKAEKERYEKEVAEYNK 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 535 KEDKETSAKRGKEITGVKRQSKSeheTSDAKKSVEDRGKRCPTPEIQKKSTGDVP----------HTSVTGDSGSGKPFK 604
Cdd:NF033875 258 HKNENGYVNEAISKNLVFDQSVV---TKDTKISSIKGGKFIKATDFNKVNAGDSKdiftklskdmGGKATGNFQNSFVKE 334
|
330
....*....|
gi 190684690 605 IKGQPESGIL 614
Cdd:NF033875 335 ANLGSNGGYA 344
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
459-594 |
2.25e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.99 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 459 DEEKARIHAETAllmEKN--KQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQkaKEEMEKKESEQAKKE 536
Cdd:pfam05262 228 DADKAQQKADFA---QDNadKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQ--IEIKKNDEEALKAKD 302
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 190684690 537 DKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVT 594
Cdd:pfam05262 303 HKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAIDSSN 360
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
453-560 |
4.64e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.95 E-value: 4.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 453 PTLMLTDEEKArihaeTALLMEKNKQEKELRERQQEE---QKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKE 529
Cdd:pfam05672 2 PSAGTTDAEEA-----ARILAEKRRQAREQREREEQErleKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEE 76
|
90 100 110
....*....|....*....|....*....|.
gi 190684690 530 SEQAKKEDKETSAKRGKEITGVKRQSKSEHE 560
Cdd:pfam05672 77 RQRKAEEEAEEREQREQEEQERLQKQKEEAE 107
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
411-574 |
5.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 411 KKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVvfsptlMLTDEEKARIHAETALLMEKNKQEKELRERQQEEQ 490
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV------MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 491 K--EKLRKEEQEQKAKKKQ---EAEENEITEKQQKAKEEMEKKESEQAKKEDKEtsaKRGKEiTGVKRQSKSEHETSDAK 565
Cdd:PTZ00121 1633 KkvEQLKKKEAEEKKKAEElkkAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED---EKKAA-EALKKEAEEAKKAEELK 1708
|
....*....
gi 190684690 566 KSVEDRGKR 574
Cdd:PTZ00121 1709 KKEAEEKKK 1717
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
476-587 |
7.12e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 476 NKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEemekKESEQAKKEDKETSAKRGKEITGVKRQS 555
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAE----EAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110
....*....|....*....|....*....|...
gi 190684690 556 KSEHE-TSDAKKSVEDRGKRCPTPEIQKKSTGD 587
Cdd:PRK09510 150 EAEAKrAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
485-574 |
7.70e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 43.26 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 485 RQQEEQKEKLRKEEQEQKAKKKQEAEENE-ITEKQQKAKEEMEKKESEQAKKEDKETSAKRGKEitgvkRQSKSE----H 559
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQkQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAAL-----KQKQAEeaaaK 140
|
90
....*....|....*
gi 190684690 560 ETSDAKKSVEDRGKR 574
Cdd:PRK09510 141 AAAAAKAKAEAEAKR 155
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
472-574 |
8.24e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 8.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 472 LMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQkakeeMEKKESEQAKKEDKETSAKRGKEItgV 551
Cdd:COG3064 4 ALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKR-----QAEEEAREAKAEAEQRAAELAAEA--A 76
|
90 100
....*....|....*....|...
gi 190684690 552 KRQSKSEHETSDAKKSVEDRGKR 574
Cdd:COG3064 77 KKLAEAEKAAAEAEKKAAAEKAK 99
|
|
| MAT1 |
pfam06391 |
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for ... |
457-552 |
1.08e-03 |
|
CDK-activating kinase assembly factor MAT1; MAT1 is an assembly/targeting factor for cyclin-dependent kinase-activating kinase (CAK), which interacts with the transcription factor TFIIH. The domain found to the N-terminal side of this domain is a C3HC4 RING finger.
Pssm-ID: 461894 [Multi-domain] Cd Length: 202 Bit Score: 41.46 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 457 LTDEEKARIHAETALLMEKNKQEKELRERQQEEQkeklRKEEQEQKAKKKQEAEE------------NEITEKQQKAKEE 524
Cdd:pfam06391 80 LILKNKMKLSQEEEELEELLELEKREKEERRKEE----KQEEEEEKEKKEKAKQElidelmtsnkdaEEIIAQHKKTAKK 155
|
90 100
....*....|....*....|....*...
gi 190684690 525 MEKKESEQAKKEDKETSAKRGKEITGVK 552
Cdd:pfam06391 156 RKSERRRKLEELNRVLEQKPTQFSTGIK 183
|
|
| Peptidase_C19P |
cd02672 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
912-1085 |
1.39e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239137 [Multi-domain] Cd Length: 268 Bit Score: 41.73 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 912 QKHKQLNE-----SIIVALFQGQFKSTVQC-----LTCHKKSRTFEAFMY-LSLPLASTSKCTLQDCLRLFSKEEKLTDN 980
Cdd:cd02672 53 KESCLLCElgylfSTLIQNFTRFLLETISQdqlgtPFSCGTSRNSVSLLYtLSLPLGSTKTSKESTFLQLLKRSLDLEKV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 981 NRFYCSHCRARRDSLKKIEIWKLPP----VLLVHLKRFSYDGRWKQ-------KLQTSVDFPLENLDLSQYVIGPKNNlK 1049
Cdd:cd02672 133 TKAWCDTCCKYQPLEQTTSIRHLPDilllVLVINLSVTNGEFDDINvvlpsgkVMQNKVSPKAIDHDKLVKNRGQESI-Y 211
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 190684690 1050 KYNLFS-VSNHYGGLDGGHYTA----YCKNAARQRWFKFDD 1085
Cdd:cd02672 212 KYELVGyVCEINDSSRGQHNVVfvikVNEESTHGRWYLFND 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
470-573 |
1.40e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 470 ALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDKETSAKR-GKEI 548
Cdd:COG4942 150 EQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEElEALI 229
|
90 100
....*....|....*....|....*
gi 190684690 549 TGVKRQSKSEHETSDAKKSVEDRGK 573
Cdd:COG4942 230 ARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
457-574 |
1.43e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 457 LTDEEKARIHAETALLMEKNKQEKELRERQQEEQK---EKLRKEEQEQKAKKKQEAEEneiTEKQQKAKEEMEKKESEQA 533
Cdd:PTZ00121 1612 AKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkkaEELKKAEEENKIKAAEEAKK---AEEDKKKAEEAKKAEEDEK 1688
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 190684690 534 KKED----KETSAKRGKEITgvKRQSKSEHETSDAKKSVEDRGKR 574
Cdd:PTZ00121 1689 KAAEalkkEAEEAKKAEELK--KKEAEEKKKAEELKKAEEENKIK 1731
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
401-587 |
2.30e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 401 IKNVPQIDRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARIHAETALLMEKNKQE- 479
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKa 1677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 480 KELRERQQEEQK---------------EKLRKEEQEQKAKKKQ---EAEENEITEKQQKAKEEMEKKESEQAKKEDKETS 541
Cdd:PTZ00121 1678 EEAKKAEEDEKKaaealkkeaeeakkaEELKKKEAEEKKKAEElkkAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 190684690 542 --AKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGD 587
Cdd:PTZ00121 1758 kiAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFD 1805
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
457-573 |
3.33e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 457 LTDEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEE----NEITEKQQKAKEEMEKKESEQ 532
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkkaEEKKKAEEAKKAEEDKNMALR 1581
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 190684690 533 AKKEDKETSAKRGKEITGVKRQSKsEHETSDAKKSVEDRGK 573
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEK-KMKAEEAKKAEEAKIK 1621
|
|
| RHOD |
smart00450 |
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The ... |
199-310 |
3.58e-03 |
|
Rhodanese Homology Domain; An alpha beta fold found duplicated in the Rhodanese protein. The the Cysteine containing enzymatically active version of the domain is also found in the CDC25 class of protein phosphatases and a variety of proteins such as sulfide dehydrogenases and stress proteins such as Senesence specific protein 1 in plants, PspE and GlpE in bacteria and cyanide and arsenate resistance proteins. Inactive versions with a loss of the cysteine are also seen in Dual specificity phosphatases, ubiquitin hydrolases from yeast and in sulfuryltransferases. These are likely to play a role in protein interactions.
Pssm-ID: 197731 [Multi-domain] Cd Length: 100 Bit Score: 38.21 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 199 LIIMDARRMQDYQDSCILHSLSVPEEAISPGVTASWieaHLPDDSKDTWKKRGNVEYVVLLDwfssakdlqiGTTLRSlk 278
Cdd:smart00450 5 VVLLDVRSPEEYEGGHIPGAVNIPLSELLDRRGELD---ILEFEELLKRLGLDKDKPVVVYC----------RSGNRS-- 69
|
90 100 110
....*....|....*....|....*....|..
gi 190684690 279 dALFKWESKTVLRNEPLVLEGGYENWLLCYPQ 310
Cdd:smart00450 70 -AKAAWLLRELGFKNVYLLDGGYKEWSAAGPP 100
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
459-656 |
3.64e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 41.18 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 459 DEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQkakeemekkesEQAKKEDK 538
Cdd:COG3064 54 EEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAA-----------AAAEKEKA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 539 ETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPESGILRTGT 618
Cdd:COG3064 123 EEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAA 202
|
170 180 190
....*....|....*....|....*....|....*...
gi 190684690 619 FREDTDDTERNKAQREPLTRARSEEMGRIVPGLPSGWA 656
Cdd:COG3064 203 LAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
459-519 |
3.73e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 41.01 E-value: 3.73e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 190684690 459 DEEKARIHAETAL-LMEKNKQEKELRERQQEEQKEKLRKEEQ------EQKAKKKQEAEEN-EITEKQQ 519
Cdd:COG2268 222 EAEEAELEQEREIeTARIAEAEAELAKKKAEERREAETARAEaeaayeIAEANAEREVQRQlEIAERER 290
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
459-571 |
4.20e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 459 DEEKARiHAETALLMEKNKQEKELRERQQE-EQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKED 537
Cdd:pfam17380 441 EEERAR-EMERVRLEEQERQQQVERLRQQEeERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE 519
|
90 100 110
....*....|....*....|....*....|....
gi 190684690 538 KETSaKRGKEITGVKRQSKSEHETSDAKKSVEDR 571
Cdd:pfam17380 520 KEME-ERQKAIYEEERRREAEEERRKQQEMEERR 552
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
474-606 |
4.74e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 39.29 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 474 EKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKED----KETSAKRGKEIT 549
Cdd:pfam11600 21 DKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKAEklrlKEEKRKEKQEAL 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 550 GVKRQSKSEHETSDAKKSVEDR---GKRCPTPEIQKKSTGDVPHTsVTGDSGSGKPFKIK 606
Cdd:pfam11600 101 EAKLEEKRKKEEEKRLKEEEKRikaEKAEITRFLQKPKTQQAPKT-LAGSCGKFAPFEIK 159
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
457-574 |
4.93e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 457 LTDEEKARIHAETALL-MEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKK 535
Cdd:COG1196 297 LARLEQDIARLEERRReLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
90 100 110
....*....|....*....|....*....|....*....
gi 190684690 536 EDKETSAKRGKEITGVKRQSKSEHETSDAKKSVEDRGKR 574
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
408-584 |
5.48e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 408 DRTKKPAVKLPEEHRIKSESTNHEQQSPQSGKVIPDRSTKPVVFSPTLMLTDEEKARiHAETALLMEKNKQEKELRERQQ 487
Cdd:PTZ00121 1222 DAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR-KADELKKAEEKKKADEAKKAEE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 488 EEQKEKLRKEEQEQK----AKKKQE-----AEENEITEKQQKAKEEMEKKESEQAKKE----------DKETSAKRGKEI 548
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKkadeAKKKAEeakkkADAAKKKAEEAKKAAEAAKAEAEAAADEaeaaeekaeaAEKKKEEAKKKA 1380
|
170 180 190
....*....|....*....|....*....|....*.
gi 190684690 549 TGVKRQSKSEHETSDAKKSVEDRGKRcpTPEIQKKS 584
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAKKKAEEDKKK--ADELKKAA 1414
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
473-583 |
5.88e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 40.21 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 473 MEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQkakeeMEKKESEQAKKEDKETSAKRGKEitgVK 552
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAE-----QAAKQAEEKQKQAEEAKAKQAAE---AK 133
|
90 100 110
....*....|....*....|....*....|....
gi 190684690 553 RQSKSEHE---TSDAKKSVEDRGKRCPTPEIQKK 583
Cdd:TIGR02794 134 AKAEAEAErkaKEEAAKQAEEEAKAKAAAEAKKK 167
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
777-793 |
5.98e-03 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 40.17 E-value: 5.98e-03
|
| Caldesmon |
pfam02029 |
Caldesmon; |
481-611 |
6.09e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 40.62 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 481 ELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQ---QKAKEEMEKKESEQAKKEDKETSAKRGKEITGVKRQSKS 557
Cdd:pfam02029 102 ERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEyqeNKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKD 181
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 190684690 558 EHETSDAK-----KSVEDRGKRCPTPEIQKKSTGDVPHTSVTGDSGSGKPFKIKGQPES 611
Cdd:pfam02029 182 EKIKKEKKvkyesKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEA 240
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
459-544 |
6.35e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 40.69 E-value: 6.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 459 DEEKARIHAETALLMEKNKQEKELRERQQEEQKEKLRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKEDK 538
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
....*.
gi 190684690 539 ETSAKR 544
Cdd:COG1196 364 EEALLE 369
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
460-519 |
6.53e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.24 E-value: 6.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 460 EEKARIHAETALLMEKNKQEKEL--------RERQQE-EQKEKLRKEEQEQKAKKKQ-EAEENEITEKQQ 519
Cdd:COG2268 257 AETARAEAEAAYEIAEANAEREVqrqleiaeREREIElQEKEAEREEAELEADVRKPaEAEKQAAEAEAE 326
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
461-543 |
8.79e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.15 E-value: 8.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 190684690 461 EKARIHAETALLMEKNKQEKELRERQQE-EQKEK--LRKEEQEQKAKKKQEAEENEITEKQQKAKEEMEKKESEQAKKED 537
Cdd:PRK12704 56 KEALLEAKEEIHKLRNEFEKELRERRNElQKLEKrlLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135
|
....*.
gi 190684690 538 KETSAK 543
Cdd:PRK12704 136 LIEEQL 141
|
|
| |
