|
Name |
Accession |
Description |
Interval |
E-value |
| COG5077 |
COG5077 |
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, ... |
57-1114 |
0e+00 |
|
Ubiquitin carboxyl-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227409 [Multi-domain] Cd Length: 1089 Bit Score: 655.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 57 FTWTIPNFSrQNTRKHYSDVFVVGGYKWRILIFPKGNNVDHLSMYLDV----SDAASLPYgWSRYAQFSLAVVNQIHTRY 132
Cdd:COG5077 41 FTWKVKRWS-ELAKKVESPPFSVGGHTWKIILFPQGNNQCNVSVYLEYepqeLEETGGKY-YDCCAQFAFDISNPKYPTI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 133 TVRKETQHQFNARESDWGFTSFMPLSELYDPSRG---YLVNDTVLVEAEVAVRK----VL--DYWSYDSKKETGFVGLKN 203
Cdd:COG5077 119 EYINKSHHRFSMESTDWGFTNFIDLNKLIEPSPGrppFLEEGTLVITVYVRVLKdptgVLwhSFLNYNSKKETGYVGLRN 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 204 QGATCYMNSLLQTLYHIPYFRKAVYHMPTtENDAPTASIPLALQSLFYKLQYNDTSVATKELTKSFGWDTYDSFMQHDVQ 283
Cdd:COG5077 199 QGATCYMNSLLQSLFFIAKFRKDVYGIPT-DHPRGRDSVALALQRLFYNLQTGEEPVDTTELTRSFGWDSDDSFMQHDIQ 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 284 ELNRVLCEKLEDKMKGTVVEGTIQQLFEGHHMNYIECINVDFKSTRKESFYDLQLDVKGCKDVYASFDKYVEVERLEGDN 363
Cdd:COG5077 278 EFNRVLQDNLEKSMRGTVVENALNGIFVGKMKSYIKCVNVNYESARVEDFWDIQLNVKGMKNLQESFRRYIQVETLDGDN 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 364 KYHAEGHGLQDAKKGVLFIDFPPVLQLQLKRFEYDFMRDTMVKINDRYEFPLELDLDredgKYLSPDADRS--VRNLYTL 441
Cdd:COG5077 358 RYNAEKHGLQDAKKGVIFESLPPVLHLQLKRFEYDFERDMMVKINDRYEFPLEIDLL----PFLDRDADKSenSDAVYVL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 442 HSVLVHSGGVHGGHYYAFIRPTLSDQWYKFDDERVTKEDLKRALEEQYGGEEelPQTNPGFNNNPPFKFTkysNAYMLVY 521
Cdd:COG5077 434 YGVLVHSGDLHEGHYYALLKPEKDGRWYKFDDTRVTRATEKEVLEENFGGDH--PYKDKIRDHSGIKRFM---SAYMLVY 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 522 IRESDKDKIICNVDEKDIAEHLRVRLKKEQEEKEDKRRYKAQAHLYTIIKVARDEDLKEQIGKDiYFDLVDHDK---VRS 598
Cdd:COG5077 509 LRKSMLDDLLNPVAAVDIPPHVEEVLSEEIDKTEVRCKEIDEIHLYRGVRLYTIDSFIHYHGFD-YPDFSSELNdsgLAQ 587
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 599 FRIQKQTPFQQFKEEVAKEFGVPVQLQ-RFWIWAKRQNHTYRPNRPLTPQEELqpvgqIREASNKANTA--ELKLFLE-- 673
Cdd:COG5077 588 FVIKRGAKISDLRNNIAEHLNTPQSLYlREWTMIKRHNKTVRVDRPCNRVNIT-----TRELVGMNTRTgeELRSYLEri 662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 674 VEHLDLRPIPPPEKSKE-DILLFFKLYDPEKAVLSYAGRLMVKSSSKPMDITGKLNEmvGFAPDEEIELFEEIKFEpcvM 752
Cdd:COG5077 663 IEHNQLDSQRKVALTKDgVINIFVKYFDYTTQPISGFGGLHVNKFLKISSISPWIED--SISSNLPLTLYEEIKPG---M 737
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 753 CEHLDKKTSFRLCQIEDGDIICFQKP-LVNKEIECLYPAVPSFLEYVQNRQLVRFRAL-EKPKEDEFVLELSKQHTYDDV 830
Cdd:COG5077 738 VDTIGDNITFIGSEIGTGDIICFEVPgAVEFDTSSAYDSALKLYDFLQGRVLVAFRRFsDEYRENVFEFLLFIGDFYDDL 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 831 VEKVAEKLGLdDPSKLRLTSHNCYSQQPK---PQPIKYRGVDHLSDMLVHynQTSDILYYEVLDIPLPELQGLKTLKVAF 907
Cdd:COG5077 818 CRNVSCKLHV-TPFYLRGTKSTELEDRIRrvvGSKSIFLLKEALSSSSEF--RQAPVDFYEVLDVPLSELERKRLIRLCF 894
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 908 HHATKEEVVIHNIRLPKQSTVGDVINELKTKVELSHPDAE-LRLLEVFYHKIYKIFPSTERIENINdQYWTLRAEEIPEE 986
Cdd:COG5077 895 LSNGYQHVYLAEFYVEKDYTAVDHLHIVVTKVGCTDELKKsVLVYEVVNLRPVRGHSLKTLIIDDN-VRSTLYGEVFPLE 973
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 987 EKNIGPNDRLILVYHFAKETgqnqqVQNFGEPFFLVIHEGETLEEIKNRIQKKLHVSDEDFAKWKFA---FMSMG----R 1059
Cdd:COG5077 974 QEQLTTNEMCVVVQHFFKDL-----IRTHGIPFMFVIVPFETFLDTKVRLVARFGYKYKLFSKIKLFvgkSYTDGeldwP 1048
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*
gi 18415260 1060 PEYLQDTDVVYNRFQRRDvygafeqYLGLEHADttpkrayaANQNRHAYEKPVKI 1114
Cdd:COG5077 1049 MSYFNDEDILYDLIERLD-------YILLDHPD--------RLRSHSSYDRAIIM 1088
|
|
| peptidase_C19C |
cd02659 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
197-526 |
3.24e-169 |
|
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: 501.02 E-value: 3.24e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 197 GFVGLKNQGATCYMNSLLQTLYHIPYFRKAVYHMPTTENDAPTASIPLALQSLFYKLQYNDTSVATKEL---TKSFGWDT 273
Cdd:cd02659 1 GYVGLKNQGATCYMNSLLQQLYMTPEFRNAVYSIPPTEDDDDNKSVPLALQRLFLFLQLSESPVKTTELtdkTRSFGWDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 274 YDSFMQHDVQELNRVLCEKLEDKMKGTVVEGTIQQLFEGHHMNYIECINVDFKSTRKESFYDLQLDVKGCKDVYASFDKY 353
Cdd:cd02659 81 LNTFEQHDVQEFFRVLFDKLEEKLKGTGQEGLIKNLFGGKLVNYIICKECPHESEREEYFLDLQVAVKGKKNLEESLDAY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 354 VEVERLEGDNKYHAEGHGLQ-DAKKGVLFIDFPPVLQLQLKRFEYDFMRDTMVKINDRYEFPLELDLDREDGKYL----- 427
Cdd:cd02659 161 VQGETLEGDNKYFCEKCGKKvDAEKGVCFKKLPPVLTLQLKRFEFDFETMMRIKINDRFEFPLELDMEPYTEKGLakkeg 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 428 SPDADRSVRNLYTLHSVLVHSGGVHGGHYYAFIRPTLSDQWYKFDDERVTKEDLKRALEEQYGGEEELPQTNPGfnnnpP 507
Cdd:cd02659 241 DSEKKDSESYIYELHGVLVHSGDAHGGHYYSYIKDRDDGKWYKFNDDVVTPFDPNDAEEECFGGEETQKTYDSG-----P 315
|
330
....*....|....*....
gi 18415260 508 FKFTKYSNAYMLVYIRESD 526
Cdd:cd02659 316 RAFKRTTNAYMLFYERKSP 334
|
|
| USP7_ICP0_bdg |
pfam12436 |
ICP0-binding domain of Ubiquitin-specific protease 7; This domain is one of two C-terminal ... |
625-875 |
5.71e-98 |
|
ICP0-binding domain of Ubiquitin-specific protease 7; This domain is one of two C-terminal domains on the much longer ubiquitin-specific proteases. This particular one is found to interact with the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110.
Pssm-ID: 463580 [Multi-domain] Cd Length: 239 Bit Score: 310.21 E-value: 5.71e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 625 QRFWIWAKRQNHTYRPNRPLTPQEELQPVGQIREASNkANTAELKLFLEVEhldlrPIPPPEKSKEDILLFFKLYDPEKA 704
Cdd:pfam12436 1 IRLWPMVNRQNKTVRPDQPLPEADPAKTVEEIRDKMA-TRDNPLRLFLEVA-----EELPPFDKNDDILLFLKYYDPEKQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 705 VLSYAGRLMVKSSSKPMDITGKLNEMVGFAPDEEIELFEEIKfePCvMCEHLDKKTSFRLCQIEDGDIICFQKPLVNKEi 784
Cdd:pfam12436 75 TLRGVGHVYVPKSSKVSDLVPIINERMGWPPDTPLLLYEEIK--PN-MIEIMKPKQTLKKSELQDGDIICFQRELSEKE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 785 ECLYPAVPSFLEYVQNRQLVRFRALEKPKEDEFVLELSKQHTYDDVVEKVAEKLGlDDPSKLRLTSHNCYSQQPKpQPIK 864
Cdd:pfam12436 151 QDEYPTAKDYYDFLLNRVEVTFRPKDNPNDPGFTLELSKKMTYDQLAEKVAERLG-VDPTKLRFTTVNNYSGQPK-TPIK 228
|
250
....*....|.
gi 18415260 865 YRGVDHLSDML 875
Cdd:pfam12436 229 RNPNQTLKDIL 239
|
|
| UCH |
pfam00443 |
Ubiquitin carboxyl-terminal hydrolase; |
199-521 |
1.21e-79 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 425685 [Multi-domain] Cd Length: 310 Bit Score: 263.15 E-value: 1.21e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 199 VGLKNQGATCYMNSLLQTLYHIPYFRKAVYHMPTT---ENDAPTASIPLALQSLFYKLQYN--DTSVATKELTKSFGWDT 273
Cdd:pfam00443 1 TGLVNLGNTCYMNSVLQSLFSIPPFRDYLLRISPLsedSRYNKDINLLCALRDLFKALQKNskSSSVSPKMFKKSLGKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 274 --YDSFMQHDVQELNRVLCEKLEDKMKG---TVVEGTIQQLFEGHHMNYIECINVDFKSTRKESFYDLQLDVKG---CKD 345
Cdd:pfam00443 81 pdFSGYKQQDAQEFLLFLLDGLHEDLNGnhsTENESLITDLFRGQLKSRLKCLSCGEVSETFEPFSDLSLPIPGdsaELK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 346 VYASFDKYVE---VERLEGDNKYH-AEGHGLQDAKKGVLFIDFPPVLQLQLKRFEYDfmRDTMVKINDRYEFPLELDLDR 421
Cdd:pfam00443 161 TASLQICFLQfskLEELDDEEKYYcDKCGCKQDAIKQLKISRLPPVLIIHLKRFSYN--RSTWEKLNTEVEFPLELDLSR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 422 EDGKYLSPDADRSVrnLYTLHSVLVHSGGVHGGHYYAFIRPTLSDQWYKFDDERVTKEDLKRALEEqyggeeelpqtnpg 501
Cdd:pfam00443 239 YLAEELKPKTNNLQ--DYRLVAVVVHSGSLSSGHYIAYIKAYENNRWYKFDDEKVTEVDEETAVLS-------------- 302
|
330 340
....*....|....*....|
gi 18415260 502 fnnnppfkftkySNAYMLVY 521
Cdd:pfam00443 303 ------------SSAYILFY 310
|
|
| USP7_C2 |
pfam14533 |
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific ... |
884-1095 |
2.44e-68 |
|
Ubiquitin-specific protease C-terminal; This C-terminal domain on many long ubiquitin-specific proteases has no known function.
Pssm-ID: 464201 Cd Length: 204 Bit Score: 227.75 E-value: 2.44e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 884 ILYYEVLDIPLPELQGLKTLKVAFHHATKEEVVIHNIRLPKQSTVGDVINELKTKVELSHPDA-ELRLLEVFYHKIYKIF 962
Cdd:pfam14533 1 ALYYEVLDISLSELENKKSIKVTWLSPGLKKEEELELLVPKNGTVADLLEELQKKVKLSEEGSgKIRLYEVSNHKIYKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 963 PSTERIENINDqYWTLRAEEIPEEEKNIGPNDRLILVYHFAKEtgqnqqVQN-FGEPFFLVIHEGETLEEIKNRIQKKLH 1041
Cdd:pfam14533 81 SEDEPIDSLND-YLTLYAEEIPEEELNLDEGERLIPVFHFQKE------PSRtHGIPFLFVLKPGEPFSDTKKRLQKRLG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 18415260 1042 VSDEDFAKWKFAFMSMGR-PEYLQDTDVVYNRFQRRDVygafEQYLGLEHADTTP 1095
Cdd:pfam14533 154 LPDKEFEKIKFALVQRGKkPEYLEDDDVLFDLLGQPDD----LPWLGLDHPDKTP 204
|
|
| Peptidase_C19 |
cd02257 |
Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ... |
200-522 |
1.89e-64 |
|
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: 218.89 E-value: 1.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTLYHipyfrkavyhmpttendaptasiplalqslfyklqyndtsvatkeltksfgwdtydsfMQ 279
Cdd:cd02257 1 GLNNLGNTCYLNSVLQALFS----------------------------------------------------------EQ 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 280 HDVQELNRVLCEKLEDKMKGTVVEG--------TIQQLFEGHHMNYIECINVDFKSTRKESFYDLQLDV----KGCKDVY 347
Cdd:cd02257 23 QDAHEFLLFLLDKLHEELKKSSKRTsdssslksLIHDLFGGKLESTIVCLECGHESVSTEPELFLSLPLpvkgLPQVSLE 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 348 ASFDKYVEVERLEGDNKYHAEGHGLQDAKKGVLFIDFPPVLQLQLKRFEYDFmRDTMVKINDRYEFPLELDLDREDGKYL 427
Cdd:cd02257 103 DCLEKFFKEEILEGDNCYKCEKKKKQEATKRLKIKKLPPVLIIHLKRFSFNE-DGTKEKLNTKVSFPLELDLSPYLSEGE 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 428 SPDADRSVRNLYTLHSVLVHSGG-VHGGHYYAFIRPTLSDQWYKFDDERVTKEDLKRALEEqyggeeelpqtnpgfnnnp 506
Cdd:cd02257 182 KDSDSDNGSYKYELVAVVVHSGTsADSGHYVAYVKDPSDGKWYKFNDDKVTEVSEEEVLEF------------------- 242
|
330
....*....|....*.
gi 18415260 507 pfkFTKYSNAYMLVYI 522
Cdd:cd02257 243 ---GSLSSSAYILFYE 255
|
|
| Peptidase_C19L |
cd02668 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-521 |
1.06e-54 |
|
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: 193.79 E-value: 1.06e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTLYHIPYFRKAVYHMPTTENDAPTASIPLA----------LQSLFYKLQYNDTSVA-TKELTKS 268
Cdd:cd02668 1 GLKNLGATCYVNSFLQLWFMNLEFRKAVYECNSTEDAELKNMPPDKphepqtiidqLQLIFAQLQFGNRSVVdPSGFVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 269 FGWDTYDsfmQHDVQELNRVLCEKLEDKM---KGTVVEGTIQQLFEGHHMNYIECINVDFKSTRKESFYDLQLDVKGCKD 345
Cdd:cd02668 81 LGLDTGQ---QQDAQEFSKLFLSLLEAKLsksKNPDLKNIVQDLFRGEYSYVTQCSKCGRESSLPSKFYELELQLKGHKT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 346 VYASFDKYVEVERLEGDNKYHAEGHG-LQDAKKGVLFIDFPPVLQLQLKRFEYDfmRDTMV--KINDRYEFPLELDLdre 422
Cdd:cd02668 158 LEECIDEFLKEEQLTGDNQYFCESCNsKTDATRRIRLTTLPPTLNFQLLRFVFD--RKTGAkkKLNASISFPEILDM--- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 423 dGKYLSPDADRSvrNLYTLHSVLVHSG-GVHGGHYYAFIRPTLSDQWYKFDDERVTKEDLKRALEeqyGGEEELPQTNPG 501
Cdd:cd02668 233 -GEYLAESDEGS--YVYELSGVLIHQGvSAYSGHYIAHIKDEQTGEWYKFNDEDVEEMPGKPLKL---GNSEDPAKPRKS 306
|
330 340
....*....|....*....|
gi 18415260 502 FNNNppfKFTKYSNAYMLVY 521
Cdd:cd02668 307 EIKK---GTHSSRTAYMLVY 323
|
|
| Peptidase_C19E |
cd02661 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-488 |
1.98e-43 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239126 [Multi-domain] Cd Length: 304 Bit Score: 160.52 E-value: 1.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTLYHIPYFrkAVY-----HMPTTENDAPTAS------IPLALQSLFYKLQYNDTSVATKELTKS 268
Cdd:cd02661 3 GLQNLGNTCFLNSVLQCLTHTPPL--ANYllsreHSKDCCNEGFCMMcaleahVERALASSGPGSAPRIFSSNLKQISKH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 269 FGWDtydsfMQHDVQELNRVLCEKLE----DKMKGTVVEGT-------IQQLFEGHHMNYIECINVDFKSTRKESFYDLQ 337
Cdd:cd02661 81 FRIG-----RQEDAHEFLRYLLDAMQkaclDRFKKLKAVDPssqettlVQQIFGGYLRSQVKCLNCKHVSNTYDPFLDLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 338 LDVKGCKDVYASFDKYVEVERLEGDNKYHAEG-HGLQDAKKGVLFIDFPPVLQLQLKRFEYDFMRdtmvKINDRYEFPLE 416
Cdd:cd02661 156 LDIKGADSLEDALEQFTKPEQLDGENKYKCERcKKKVKASKQLTIHRAPNVLTIHLKRFSNFRGG----KINKQISFPET 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18415260 417 LDLdredGKYLSPDADRSVRnlYTLHSVLVHSGG-VHGGHYYAFIRpTLSDQWYKFDDERVTKEDLKRALEEQ 488
Cdd:cd02661 232 LDL----SPYMSQPNDGPLK--YKLYAVLVHSGFsPHSGHYYCYVK-SSNGKWYNMDDSKVSPVSIETVLSQK 297
|
|
| MATH |
cd00121 |
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded ... |
55-179 |
6.64e-40 |
|
MATH (meprin and TRAF-C homology) domain; an independent folding unit with an eight-stranded beta-sandwich structure found in meprins, TRAFs and other proteins. Meprins comprise a class of extracellular metalloproteases which are anchored to the membrane and are capable of cleaving growth factors, extracellular matrix proteins, and biologically active peptides. TRAF molecules serve as adapter proteins that link cell surface receptors of the Tumor Necrosis Factor and 1nterleukin-1/Toll-like families to downstream kinase cascades, which results in the activation of transcription factors and the regulation of cell survival, proliferation and stress responses in the immune and inflammatory systems. Other members include the ubiquitin ligases, TRIM37 and SPOP, and the ubiquitin-specific proteases, HAUSP and Ubp21p. A large number of uncharacterized members mostly from lineage-specific expansions in C. elegans and rice contain MATH and BTB domains, similar to SPOP. The MATH domain has been shown to bind peptide/protein substrates in TRAFs and HAUSP. It is possible that the MATH domain in other members of this superfamily also interacts with various protein substrates. The TRAF domain may also be involved in the trimerization of TRAFs. Based on homology, it is postulated that the MATH domain in meprins may be involved in its tetramer assembly and that the MATH domain, in general, may take part in diverse modular arrangements defined by adjacent multimerization domains.
Pssm-ID: 238068 Cd Length: 126 Bit Score: 143.67 E-value: 6.64e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 55 LKFTWTIPNFSRQNTRKHYSDVFVVGGYKWRILIFPKGNNV--DHLSMYLDVSDAASLPYGWSRYAQFSLAVVNQIHTRY 132
Cdd:cd00121 1 GKHTWKIVNFSELEGESIYSPPFEVGGYKWRIRIYPNGDGEsgDYLSLYLELDKGESDLEKWSVRAEFTLKLVNQNGGKS 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 18415260 133 TVRKETQHQFNARESDWGFTSFMPLSELYDPsrGYLVNDTVLVEAEV 179
Cdd:cd00121 81 LSKSFTHVFFSEKGSGWGFPKFISWDDLEDS--YYLVDDSLTIEVEV 125
|
|
| Peptidase_C19D |
cd02660 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-488 |
4.26e-37 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239125 [Multi-domain] Cd Length: 328 Bit Score: 142.90 E-value: 4.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTLYHIPYFRK---AVYHMPTTENDAPTASIPLALQSLFYKLQYNDTSV---ATKELTKSfgWD- 272
Cdd:cd02660 2 GLINLGATCFMNVILQALLHNPLLRNyflSDRHSCTCLSCSPNSCLSCAMDEIFQEFYYSGDRSpygPINLLYLS--WKh 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 273 -----TYDsfmQHDVQELNRVLCEKLEDKMKGTVVEGT--------IQQLFEGHHMNYIECINVDFKSTRKESFYDLQLD 339
Cdd:cd02660 80 srnlaGYS---QQDAHEFFQFLLDQLHTHYGGDKNEANdeshcnciIHQTFSGSLQSSVTCQRCGGVSTTVDPFLDLSLD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 340 VK---------------GCKDVYASFDKYVEVERLeGDNKYHAEG-HGLQDAKKGVLFIDFPPVLQLQLKRFEYdFMRDT 403
Cdd:cd02660 157 IPnkstpswalgesgvsGTPTLSDCLDRFTRPEKL-GDFAYKCSGcGSTQEATKQLSIKKLPPVLCFQLKRFEH-SLNKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 404 MVKINDRYEFPLELD----LDREDGKYLSPDADRSvRNLYTLHSVLVHSGGVHGGHYYAFIRpTLSDQWYKFDDERVTKE 479
Cdd:cd02660 235 SRKIDTYVQFPLELNmtpyTSSSIGDTQDSNSLDP-DYTYDLFAVVVHKGTLDTGHYTAYCR-QGDGQWFKFDDAMITRV 312
|
....*....
gi 18415260 480 DLKRALEEQ 488
Cdd:cd02660 313 SEEEVLKSQ 321
|
|
| Peptidase_C19G |
cd02663 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-491 |
2.97e-36 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239128 [Multi-domain] Cd Length: 300 Bit Score: 139.37 E-value: 2.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTLYHipyfrkavyhmpttendaptASIPLALQSLFYKLQYNDT---SVATKELTKSFGWDT--Y 274
Cdd:cd02663 1 GLENFGNTCYCNSVLQALYF--------------------ENLLTCLKDLFESISEQKKrtgVISPKKFITRLKRENelF 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 275 DSFMQHDVQE-LNRVL---CEKLEDKMKGTVVEGT-------------IQQLFEGHHMNYIECINVDFKSTRKESFYDLQ 337
Cdd:cd02663 61 DNYMHQDAHEfLNFLLneiAEILDAERKAEKANRKlnnnnnaepqptwVHEIFQGILTNETRCLTCETVSSRDETFLDLS 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 338 LDVKGCKDVYASFDKYVEVERLEGDNKYHAEG-HGLQDAKKGVLFIDFPPVLQLQLKRFEYDFMRDTMVKINDRYEFPLE 416
Cdd:cd02663 141 IDVEQNTSITSCLRQFSATETLCGRNKFYCDEcCSLQEAEKRMKIKKLPKILALHLKRFKYDEQLNRYIKLFYRVVFPLE 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18415260 417 LDLDREDGKylSPDADRsvrnLYTLHSVLVHSG-GVHGGHYYAFIRptLSDQWYKFDDERVTKEDlKRALEEQYGG 491
Cdd:cd02663 221 LRLFNTTDD--AENPDR----LYELVAVVVHIGgGPNHGHYVSIVK--SHGGWLLFDDETVEKID-ENAVEEFFGD 287
|
|
| Peptidase_C19R |
cd02674 |
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-478 |
1.74e-33 |
|
A subfamily of peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239139 [Multi-domain] Cd Length: 230 Bit Score: 129.33 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTLYHipyfrkavyhmpttendaptasiplalqslfyklqyndtsvatkeltksfgwdtydsfMQ 279
Cdd:cd02674 1 GLRNLGNTCYMNSILQCLSA----------------------------------------------------------DQ 22
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 280 HDVQELNRVLCEKLEDKmkgtvvegtIQQLFEGHHMNYIECINVDFKSTRKESFYDLQLDV-------KGCKdVYASFDK 352
Cdd:cd02674 23 QDAQEFLLFLLDGLHSI---------IVDLFQGQLKSRLTCLTCGKTSTTFEPFTYLSLPIpsgsgdaPKVT-LEDCLRL 92
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 353 YVEVERLEGDNKYHAEGHG-LQDAKKGVLFIDFPPVLQLQLKRFEYDFMRdtMVKINDRYEFPLELDLDRedgkYLSPDA 431
Cdd:cd02674 93 FTKEETLDGDNAWKCPKCKkKRKATKKLTISRLPKVLIIHLKRFSFSRGS--TRKLTTPVTFPLNDLDLT----PYVDTR 166
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 18415260 432 DRSVRNLYTLHSVLVHSGGVHGGHYYAFIRPTLSDQWYKFDDERVTK 478
Cdd:cd02674 167 SFTGPFKYDLYAVVNHYGSLNGGHYTAYCKNNETNDWYKFDDSRVTK 213
|
|
| Peptidase_C19H |
cd02664 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-477 |
1.55e-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: 129.53 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTLYHIPYFRKAVYhMPTTENDAPTASIPLALQSLFYKLQY-NDTSVATKELTKSFGWDTY--DS 276
Cdd:cd02664 1 GLINLGNTCYMNSVLQALFMAKDFRRQVL-SLNLPRLGDSQSVMKKLQLLQAHLMHtQRRAEAPPDYFLEASRPPWftPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 277 FmQHDVQELNRVLCEKLEDkmkgtvvegTIQQLFEGHHMNYIECINVDFKSTRKESFYDLQLDVKGCKDVyasFDKYVEV 356
Cdd:cd02664 80 S-QQDCSEYLRYLLDRLHT---------LIEKMFGGKLSTTIRCLNCNSTSARTERFRDLDLSFPSVQDL---LNYFLSP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 357 ERLEGDNKYHAEG-HGLQDAKKGVLFIDFPPVLQLQLKRFEYDFMRDTMVKINDRYEFPLELDL---------DREDGKY 426
Cdd:cd02664 147 EKLTGDNQYYCEKcASLQDAEKEMKVTGAPEYLILTLLRFSYDQKTHVREKIMDNVSINEVLSLpvrveskssESPLEKK 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18415260 427 LSPDADRS----VRNLYTLHSVLVHSG-GVHGGHYYAFIR-PTLSDQ-------------------WYKFDDERVT 477
Cdd:cd02664 227 EEESGDDGelvtRQVHYRLYAVVVHSGySSESGHYFTYARdQTDADStgqecpepkdaeendesknWYLFNDSRVT 302
|
|
| MATH_Ubp21p |
cd03775 |
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with ... |
57-179 |
2.19e-31 |
|
Ubiquitin-specific protease 21 (Ubp21p) family, MATH domain; composed of fungal proteins with similarity to Ubp21p of fission yeast. Ubp21p is a deubiquitinating enzyme that may be involved in the regulation of the protein kinase Prp4p, which controls the formation of active spliceosomes. Members of this family are similar to human HAUSP (Herpesvirus-associated ubiquitin-specific protease) in that they contain an N-terminal MATH domain and a C-terminal catalytic protease (C19 family) domain. HAUSP is also an ubiquitin-specific protease that specifically catalyzes the deubiquitylation of p53 and MDM2. The MATH domain of HAUSP contains the binding site for p53 and MDM2. Similarly, the MATH domain of members in this family may be involved in substrate binding.
Pssm-ID: 239744 Cd Length: 134 Bit Score: 119.77 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 57 FTWTIPNFSRQNtRKHYSDVFVVGGYKWRILIFPKGNNV-DHLSMYL----DVSDAASLPYGWSRYAQFSLAVVNQIHTR 131
Cdd:cd03775 3 FTWRIKNWSELE-KKVHSPKFKCGGFEWRILLFPQGNSQtGGVSIYLephpEEEEKAPLDEDWSVCAQFALVISNPGDPS 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 18415260 132 YTVRKETQHQFNARESDWGFTSFMPLSELYDPSR----GYLVNDTVLVEAEV 179
Cdd:cd03775 82 IQLSNVAHHRFNAEDKDWGFTRFIELRKLAHRTPdkpsPFLENGELNITVYV 133
|
|
| Peptidase_C19A |
cd02657 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-483 |
1.14e-30 |
|
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: 123.21 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTLYHIPYFRKAV--YHMPTTENDAPTASIPLALQSLFYKLQYNDTSVATKELTKSFGwDTYDSF 277
Cdd:cd02657 1 GLTNLGNTCYLNSTLQCLRSVPELRDALknYNPARRGANQSSDNLTNALRDLFDTMDKKQEPVPPIEFLQLLR-MAFPQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 278 ---------MQHDVQE-LNRVLcEKLEDKMKGTVVEG-TIQQLFEGHHMNYIECI-NVDFKSTRKESFYDLQLDVKGCKD 345
Cdd:cd02657 80 aekqnqggyAQQDAEEcWSQLL-SVLSQKLPGAGSKGsFIDQLFGIELETKMKCTeSPDEEEVSTESEYKLQCHISITTE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 346 VYASFDKYveVERLEGDNKYHAEGHGlQDAK--KGVLFIDFPPVLQLQLKRFEYDfmRDTMV--KINDRYEFPLELDLDR 421
Cdd:cd02657 159 VNYLQDGL--KKGLEEEIEKHSPTLG-RDAIytKTSRISRLPKYLTVQFVRFFWK--RDIQKkaKILRKVKFPFELDLYE 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18415260 422 edgkYLSPDAdrsvrnLYTLHSVLVHSG-GVHGGHYYAFIRPTLSDQWYKFDDE---RVTKEDLKR 483
Cdd:cd02657 234 ----LCTPSG------YYELVAVITHQGrSADSGHYVAWVRRKNDGKWIKFDDDkvsEVTEEDILK 289
|
|
| Peptidase_C19K |
cd02667 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-488 |
7.41e-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: 239132 [Multi-domain] Cd Length: 279 Bit Score: 117.49 E-value: 7.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTLYHIPYFRKAVYHMPTTendaptasiplalqsLF-----YKLQYNDTSvatkeltksfgwdty 274
Cdd:cd02667 1 GLSNLGNTCFFNAVMQNLSQTPALRELLSETPKE---------------LFsqvcrKAPQFKGYQ--------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 275 dsfmQHDVQELNRVLCEKLEdkmkgTVVEgtiqQLFEGHHMNYIECINVDFKSTRKESFYDLQLDVKGCKDVYASFDK-- 352
Cdd:cd02667 51 ----QQDSHELLRYLLDGLR-----TFID----SIFGGELTSTIMCESCGTVSLVYEPFLDLSLPRSDEIKSECSIEScl 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 353 --YVEVERLEGDNKYHAEGhgLQDAKKGVLFIDFPPVLQLQLKRFEYDfMRDTMVKINDRYEFPLELDLdredGKYLSPD 430
Cdd:cd02667 118 kqFTEVEILEGNNKFACEN--CTKAKKQYLISKLPPVLVIHLKRFQQP-RSANLRKVSRHVSFPEILDL----APFCDPK 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 431 ADRS---VRNLYTLHSVLVHSGGVHGGHYYAFIRP---------------------TLSDQWYKFDDERVTKEDLKRALE 486
Cdd:cd02667 191 CNSSedkSSVLYRLYGVVEHSGTMRSGHYVAYVKVrppqqrlsdltkskpaadeagPGSGQWYYISDSDVREVSLEEVLK 270
|
..
gi 18415260 487 EQ 488
Cdd:cd02667 271 SE 272
|
|
| Peptidase_C19O |
cd02671 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
198-485 |
4.46e-27 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239136 [Multi-domain] Cd Length: 332 Bit Score: 113.45 E-value: 4.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 198 FVGLKNQGATCYMNSLLQTLYHIPYFRKAVYHMPTTENDAPTasiplaLQSLFYKL--QYNDTSVAT---------KELT 266
Cdd:cd02671 24 FVGLNNLGNTCYLNSVLQVLYFCPGFKHGLKHLVSLISSVEQ------LQSSFLLNpeKYNDELANQaprrllnalREVN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 267 KsfgwdTYDSFMQHDVQELnrVLCekledkmkgtvVEGTIQQL----FEGHHMNYIECINVDFKSTRKESFYDLQLDVKG 342
Cdd:cd02671 98 P-----MYEGYLQHDAQEV--LQC-----------ILGNIQELvekdFQGQLVLRTRCLECETFTERREDFQDISVPVQE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 343 -------------------CKDVYASFDKYVEVERLEGDNKYHAEG-HGLQDAKKGVLFIDFPPVLQLQLKRFEYDFMRD 402
Cdd:cd02671 160 selskseesseispdpkteMKTLKWAISQFASVERIVGEDKYFCENcHHYTEAERSLLFDKLPEVITIHLKCFAANGSEF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 403 T----MVKINDRYEFPLELDLdreDGKYLSPDadrsvRNLYTLHSVLVHSGG-VHGGHYYAFIRptlsdqWYKFDDERV- 476
Cdd:cd02671 240 DcyggLSKVNTPLLTPLKLSL---EEWSTKPK-----NDVYRLFAVVMHSGAtISSGHYTAYVR------WLLFDDSEVk 305
|
330
....*....|.
gi 18415260 477 --TKEDLKRAL 485
Cdd:cd02671 306 vtEEKDFLEAL 316
|
|
| MATH |
pfam00917 |
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This ... |
61-179 |
7.42e-19 |
|
MATH domain; This motif has been called the Meprin And TRAF-Homology (MATH) domain. This domain is hugely expanded in the nematode C. elegans.
Pssm-ID: 425944 [Multi-domain] Cd Length: 113 Bit Score: 83.07 E-value: 7.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 61 IPNFSRQNTRK-HYSDVFVVGGYKWRILIFPKGnnvDHLSMYLDVSDAASLPYGWSRYAQFSLAVVNQihTRYTVRKETQ 139
Cdd:pfam00917 1 IKNFSKIKEGEsYYSPVEERFNIPWRLQIYRKG---GFLGLYLHCDKEEELERGWSIETEFTLKLVSS--NGKSVTKTDT 75
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 18415260 140 HQFNArESDWGFTSFMPLSELYDpsrGYLVNDTVLVEAEV 179
Cdd:pfam00917 76 HVFEK-PKGWGWGKFISWDDLEK---DYLVDDSITVEAHV 111
|
|
| MATH |
smart00061 |
meprin and TRAF homology; |
57-155 |
5.05e-17 |
|
meprin and TRAF homology;
Pssm-ID: 214496 [Multi-domain] Cd Length: 95 Bit Score: 77.34 E-value: 5.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 57 FTWTIPNFSR-QNTRKHYSDVFVVGGYKWRILIFPKGnnvDHLSMYLDVSDAASLPYGWSRYAQFSLAVVNQIHTRYTVR 135
Cdd:smart00061 2 LSHTFKNVSRlEEGESYFSPSEEHFNIPWRLKIYRKN---GFLSLYLHCEKEECDSRKWSIEAEFTLKLVSQNGKSLSKK 78
|
90 100
....*....|....*....|
gi 18415260 136 KEtqHQFNaRESDWGFTSFM 155
Cdd:smart00061 79 DK--HVFE-KPSGWGFSKFI 95
|
|
| Peptidase_C19F |
cd02662 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-489 |
1.55e-16 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239127 [Multi-domain] Cd Length: 240 Bit Score: 80.49 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTLYHIPYFRKAVyhmpttendaptasiplalqslfyklqyndtsvatkeltksfgwdtyDSFM- 278
Cdd:cd02662 1 GLVNLGNTCFMNSVLQALASLPSLIEYL-----------------------------------------------EEFLe 33
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 279 QHDVQELNRVLCEKLEDKMKgtvvegtiqQLFEGHHMNYIECINVDFKST-RKESFYDL------QLDVKGCKDVyASFD 351
Cdd:cd02662 34 QQDAHELFQVLLETLEQLLK---------FPFDGLLASRIVCLQCGESSKvRYESFTMLslpvpnQSSGSGTTLE-HCLD 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 352 KYVEVERLEGDNKYHAEghglqdakkgVLFIDFPPVLQLQLKRFEYDfMRDTMVKINDRYEFPLELDldredgkylspda 431
Cdd:cd02662 104 DFLSTEIIDDYKCDRCQ----------TVIVRLPQILCIHLSRSVFD-GRGTSTKNSCKVSFPERLP------------- 159
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18415260 432 drsvRNLYTLHSVLVHSGGVHGGHYYAF--------------------IRPTLSDQWYKFDDERVTKEDLKRALEEQY 489
Cdd:cd02662 160 ----KVLYRLRAVVVHYGSHSSGHYVCYrrkplfskdkepgsfvrmreGPSSTSHPWWRISDTTVKEVSESEVLEQKS 233
|
|
| COG5533 |
COG5533 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
200-488 |
7.72e-16 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444284 [Multi-domain] Cd Length: 284 Bit Score: 79.08 E-value: 7.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTL-YHIPYFRKAVYHMPTT--------ENDAPTASIPLALQSLfyklqyndTSVATKELTKsFG 270
Cdd:COG5533 1 GLPNLGNTCFMNSVLQILaLYLPKLDELLDDLSKElkvlknviRKPEPDLNQEEALKLF--------TALWSSKEHK-VG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 271 WdTYDSFMQHDVQELNRVLCEKLE-----------DKMKGTVVEGTIQQLFEGHHMNYIECINVDFKSTRK--ESFYDLQ 337
Cdd:COG5533 72 W-IPPMGSQEDAHELLGKLLDELKldlvnsftiriFKTTKDKKKTSTGDWFDIIIELPDQTWVNNLKTLQEfiDNMEELV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 338 LDVKGCkdvyasfdKYVEVERLEGDNKyhaeghglqdAKKGVLFIDFPPVLQLQLKRFEYDfmrDTMVKINDRYEFPLEL 417
Cdd:COG5533 151 DDETGV--------KAKENEELEVQAK----------QEYEVSFVKLPKILTIQLKRFANL---GGNQKIDTEVDEKFEL 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18415260 418 DLDREDGKYLSPDAdrsvrnLYTLHSVLVHSGGVHGGHYYAFIRptLSDQWYKFDDERVTKEDLKRALEEQ 488
Cdd:COG5533 210 PVKHDQILNIVKET------YYDLVGFVLHQGSLEGGHYIAYVK--KGGKWEKANDSDVTPVSEEEAINEK 272
|
|
| Peptidase_C19I |
cd02665 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-522 |
9.52e-16 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239130 [Multi-domain] Cd Length: 228 Bit Score: 77.60 E-value: 9.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTLYhipyfrkavyhmpTTENDAptasiplalqslfyklqyndtsvaTKELTKSFGWDTYDSFMQ 279
Cdd:cd02665 1 GLKNVGNTCWFSAVIQSLF-------------SQQQDV------------------------SEFTHLLLDWLEDAFQAA 43
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 280 HDVQELNrvlcEKLEDKMkgtvvegtiQQLFEGHHMnyIECINVDFKSTRKESFYDLQLDVKGCKDVY-----ASFDKYV 354
Cdd:cd02665 44 AEAISPG----EKSKNPM---------VQLFYGTFL--TEGVLEGKPFCNCETFGQYPLQVNGYGNLHecleaAMFEGEV 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 355 EVERLEGDNKYHAEGhglqdakkgvLFIDFPPVLQLQLKRFEydFMRDTMVKINDRYEFPLELdldredgkylspdadRS 434
Cdd:cd02665 109 ELLPSDHSVKSGQER----------WFTELPPVLTFELSRFE--FNQGRPEKIHDKLEFPQII---------------QQ 161
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 435 VRnlYTLHSVLVHSGGVHGGHYYAFIRPTLSDQWYKFDDERVTKEDLKRALEEQYGGeeelpqtnpgfNNNPpfkftkys 514
Cdd:cd02665 162 VP--YELHAVLVHEGQANAGHYWAYIYKQSRQEWEKYNDISVTESSWEEVERDSFGG-----------GRNP-------- 220
|
....*...
gi 18415260 515 NAYMLVYI 522
Cdd:cd02665 221 SAYCLMYI 228
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
351-480 |
1.43e-15 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 81.85 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 351 DKYVEVERLEGDNKYHAEG-HGLQDAKKGVLFIDFPPVLQLQLKRFEYDfmRDTMVKINDRYEFPL-ELDLDREDGKYLS 428
Cdd:COG5560 682 NEFSKPEQLGLSDSWYCPGcKEFRQASKQMELWRLPMILIIHLKRFSSV--RSFRDKIDDLVEYPIdDLDLSGVEYMVDD 759
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 18415260 429 PdadrsvRNLYTLHSVLVHSGGVHGGHYYAFIRPTLSDQWYKFDDERVTKED 480
Cdd:COG5560 760 P------RLIYDLYAVDNHYGGLSGGHYTAYARNFANNGWYLFDDSRITEVD 805
|
|
| MATH_HAUSP |
cd03772 |
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, ... |
56-179 |
4.00e-15 |
|
Herpesvirus-associated ubiquitin-specific protease (HAUSP, also known as USP7) family, N-terminal MATH (TRAF-like) domain; composed of proteins similar to human HAUSP, an enzyme that specifically catalyzes the deubiquitylation of p53 and MDM2, hence playing an important role in the p53-MDM2 pathway. It contains an N-terminal TRAF-like domain and a C-terminal catalytic protease (C19 family) domain. The tumor suppressor p53 protein is a transcription factor that responds to many cellular stress signals and is regulated primarily through ubiquitylation and subsequent degradation. MDM2 is a RING-finger E3 ubiquitin ligase that promotes p53 ubiquitinylation. p53 and MDM2 bind to the same site in the N-terminal TRAF-like domain of HAUSP in a mutually exclusive manner. HAUSP also interacts with the Epstein-Barr nuclear antigen 1 (EBNA1) protein of the Epstein-Barr virus (EBV), which efficiently immortalizes infected cells predisposing the host to a variety of cancers. EBNA1 plays several important roles in EBV latent infection and cellular transformation. It binds the same pocket as p53 in the HAUSP TRAF-like domain. Through interactions with p53, MDM2 and EBNA1, HAUSP plays a role in cell proliferation, apoptosis and EBV-mediated immortalization.
Pssm-ID: 239741 Cd Length: 137 Bit Score: 73.26 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 56 KFTWTIPNFSRQNTRKHYSDVFVvGGYKWRILIFPKGNNVDH-----LSMYLDVsDAASLPYGWSRYAQFSLAVVNQIHT 130
Cdd:cd03772 4 TFSFTVERFSRLSESVLSPPCFV-RNLPWKIMVMPRNYPDRNphqksVGFFLQC-NAESDSTSWSCHAQAVLRIINYKDD 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 18415260 131 RYTVRKETQHQFNARESDWGFTSFMPLSELYDPSRGYLVNDTVLVEAEV 179
Cdd:cd03772 82 EPSFSRRISHLFFSKENDWGFSNFMTWSEVTDPEKGFIEDDTITLEVYV 130
|
|
| Peptidase_C19B |
cd02658 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
200-476 |
8.67e-15 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239123 [Multi-domain] Cd Length: 311 Bit Score: 76.59 E-value: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 200 GLKNQGATCYMNSLLQTLYHIPYFRK---AVYHMPTTENDAPTASIPLALQSLFYKLQYNDTSVATKELTK--------- 267
Cdd:cd02658 1 GLRNLGNSCYLNSVLQVLFSIPSFQWrydDLENKFPSDVVDPANDLNCQLIKLADGLLSGRYSKPASLKSEndpyqvgik 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 268 --SF------GWDTYDSFMQHDVQELNRVLCEKLEDKMKGTVVEgTIQQLFEGHHMNYIECINVDFKSTRKESFYDLQLD 339
Cdd:cd02658 81 psMFkaligkGHPEFSTMRQQDALEFLLHLIDKLDRESFKNLGL-NPNDLFKFMIEDRLECLSCKKVKYTSELSEILSLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 340 VKG--------CKDVY------ASFDKYVEVERLEGDNKYHAEGHGlqdAKKGVLFIDFPPVLQLQLKRFEYDfMRDTMV 405
Cdd:cd02658 160 VPKdeatekeeGELVYepvpleDCLKAYFAPETIEDFCSTCKEKTT---ATKTTGFKTFPDYLVINMKRFQLL-ENWVPK 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18415260 406 KINdryeFPLELDLDREDGKYlspdadrsvrnlyTLHSVLVHSG-GVHGGHYYAFIR--PTLSDQWYKFDDERV 476
Cdd:cd02658 236 KLD----VPIDVPEELGPGKY-------------ELIAFISHKGtSVHSGHYVAHIKkeIDGEGKWVLFNDEKV 292
|
|
| UCH_1 |
pfam13423 |
Ubiquitin carboxyl-terminal hydrolase; |
199-473 |
5.80e-13 |
|
Ubiquitin carboxyl-terminal hydrolase;
Pssm-ID: 463872 [Multi-domain] Cd Length: 305 Bit Score: 71.15 E-value: 5.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 199 VGLKNQGATCYMNSLLQTLYHIPYFRK-AVYHmpTTENDAPTASIPLALQSLFYKLQ---------------YNDTSVAT 262
Cdd:pfam13423 1 SGLETHIPNSYTNSLLQLLRFIPPLRNlALSH--LATECLKEHCLLCELGFLFDMLEkakgkncqasnflraLSSIPEAS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 263 K-----ELTKSFGWDTYdsfmQHDVQELNRVLCEKLED-----KMKGTVVEGTIQQLFEGHHMNYIECINVDFKSTRKES 332
Cdd:pfam13423 79 AlglldEDRETNSAISL----SSLIQSFNRFLLDQLSSeenstPPNPSPAESPLEQLFGIDAETTIRCSNCGHESVRESS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 333 FYDLQLDV------KGCKDVYASFDKYVE--VERlEGDNKYHAEG-HGLQDAKKGVLFIDFPPVLQLQLKRFEYDFMRDt 403
Cdd:pfam13423 155 THVLDLIYprkpssNNKKPPNQTFSSILKssLER-ETTTKAWCEKcKRYQPLESRRTVRNLPPVLSLNAALTNEEWRQL- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18415260 404 mvkINDRYEFPLELDLDREDGKYLSPDAdrsvrNLYTLHSVLVH-SGGVHGGHYYAFIR-------PTLSDQWYKFDD 473
Cdd:pfam13423 233 ---WKTPGWLPPEIGLTLSDDLQGDNEI-----VKYELRGVVVHiGDSGTSGHLVSFVKvadseleDPTESQWYLFND 302
|
|
| Peptidase_C19J |
cd02666 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
199-522 |
4.21e-11 |
|
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl group of the C-terminal Gly residue of ubiquitin. The purpose of the de-ubiquitination is thought to be editing of the ubiquitin conjugates, which could rescue them from degradation, as well as recycling of the ubiquitin. The ubiquitin/proteasome system is responsible for most protein turnover in the mammalian cell, and with over 50 members, family C19 is one of the largest families of peptidases in the human genome.
Pssm-ID: 239131 [Multi-domain] Cd Length: 343 Bit Score: 65.98 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 199 VGLKNQGATCYMNSLLQTLYHIPYFRKAV-----------YHMPTT----ENDAPTASIPLALQ------SLFYKLQYND 257
Cdd:cd02666 2 AGLDNIGNTCYLNSLLQYFFTIKPLRDLVlnfdeskaelaSDYPTErrigGREVSRSELQRSNQfvyelrSLFNDLIHSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 258 TSVAT--KELTksfgwdtYDSFMQHDVQE-LNRVLCEkLE-------------DKMKGTVVEGTIQQLFEGHHMNYI-EC 320
Cdd:cd02666 82 TRSVTpsKELA-------YLALRQQDVTEcIDNVLFQ-LEvalepisnafagpDTEDDKEQSDLIKRLFSGKTKQQLvPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 321 INVDFKSTR--KESFYDLQLDV----------KGCKDVYASFDKYVEVERLEgdnkyhaeghglqdakkgvlfiDFPPVL 388
Cdd:cd02666 154 SMGNQPSVRtkTERFLSLLVDVgkkgreivvlLEPKDLYDALDRYFDYDSLT----------------------KLPQRS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 389 QLQLKRF-----EYDFMRDTMVKINDRYEFPLELDLDREDGKyLSPDADRSVRNL---------------YTLHSVLVHS 448
Cdd:cd02666 212 QVQAQLAqplqrELISMDRYELPSSIDDIDELIREAIQSESS-LVRQAQNELAELkheiekqfddlksygYRLHAVFIHR 290
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18415260 449 GGVHGGHYYAFIRPTLSDQWYKFDDERVTKEDlkraleeqyggEEELPQTNPGFNNNPpfkftkysnaYMLVYI 522
Cdd:cd02666 291 GEASSGHYWVYIKDFEENVWRKYNDETVTVVP-----------ASEVFLFTLGNTATP----------YFLVYV 343
|
|
| MATH_TRIM37 |
cd03773 |
Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal ... |
52-174 |
1.56e-10 |
|
Tripartite motif containing protein 37 (TRIM37) family, MATH domain; TRIM37 is a peroxisomal protein and is a member of the tripartite motif (TRIM) protein subfamily, also known as the RING-B-box-coiled-coil (RBCC) subfamily of zinc-finger proteins. Mutations in the human TRIM37 gene (also known as MUL) cause Mulibrey (muscle-liver-brain-eye) nanism, a rare growth disorder of prenatal onset characterized by dysmorphic features, pericardial constriction and hepatomegaly. TRIM37, similar to other TRIMs, contains a cysteine-rich, zinc-binding RING-finger domain followed by another cysteine-rich zinc-binding domain, the B-box, and a coiled-coil domain. TRIM37 is autoubiquitinated in a RING domain-dependent manner, indicating that it functions as an ubiquitin E3 ligase. In addition to the tripartite motif, TRIM37 also contains a MATH domain C-terminal to the coiled-coil domain. The MATH domain of TRIM37 has been shown to interact with the TRAF domain of six known TRAFs in vitro, however, it is unclear whether this is physiologically relevant. Eleven TRIM37 mutations have been associated with Mulibrey nanism so far. One mutation, Gly322Val, is located in the MATH domain and is the only mutation that does not affect the length of the protein. It results in the incorrect subcellular localization of TRIM37.
Pssm-ID: 239742 Cd Length: 132 Bit Score: 60.12 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 52 PPTLKFTWTIPNFS--RQNTRKHYSDVFVVGGYKWRILIFPKGNNV---DHLSMYLDVSDAASLPygwSRYaQFSLAVVN 126
Cdd:cd03773 2 PPYDSATFTLENFStlRQSADPVYSDPLNVDGLCWRLKVYPDGNGEvrgNFLSVFLELCSGLGEA---SKY-EYRVEMVH 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 18415260 127 QIHTRYTVRKETQHQFNARESdWGFTSFMPLSELYDpsRGYLV--NDTVL 174
Cdd:cd03773 78 QANPTKNIKREFASDFEVGEC-WGYNRFFRLDLLIN--EGYLLpeNDTLI 124
|
|
| UBP12 |
COG5560 |
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones]; |
133-338 |
7.74e-07 |
|
Ubiquitin C-terminal hydrolase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227847 [Multi-domain] Cd Length: 823 Bit Score: 53.35 E-value: 7.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 133 TVRKETQHQFNARESDWGFTSFMPLSELyDPSRGYLVNDTVLVEAEVAVRKVLDYWSYDSKKETGFVGLKNQGATCYMNS 212
Cdd:COG5560 201 LGLDSFFRRYRVLASDGRVLHPLTRLEL-FEDRSVLLLSKITRNPDWLVDSIVDDHNRSINKEAGTCGLRNLGNTCYMNS 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 213 LLQTLYHIP----YFRKAVYHMPTTEND--APTASIPLALQSLFYKL-QYNDTSVATKELTKSFG--WDTYDSFMQHDVQ 283
Cdd:COG5560 280 ALQCLMHTWelrdYFLSDEYEESINEENplGMHGSVASAYADLIKQLyDGNLHAFTPSGFKKTIGsfNEEFSGYDQQDSQ 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 284 E------------LNRV----------LCEKLEDKMKGTVVE----------GTIQQLFEGHHMNYIECINVDFKSTRKE 331
Cdd:COG5560 360 EfiaflldglhedLNRIikkpytskpdLSPGDDVVVKKKAKEcwwehlkrndSIITDLFQGMYKSTLTCPGCGSVSITFD 439
|
....*..
gi 18415260 332 SFYDLQL 338
Cdd:COG5560 440 PFMDLTL 446
|
|
| MATH_SPOP |
cd03774 |
Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to ... |
55-181 |
6.12e-06 |
|
Speckle-type POZ protein (SPOP) family, MATH domain; composed of proteins with similarity to human SPOP. SPOP was isolated as a novel antigen recognized by serum from a scleroderma patient, whose overexpression in COS cells results in a discrete speckled pattern in the nuclei. It contains an N-terminal MATH domain and a C-terminal BTB (also called POZ) domain. Together with Cul3, SPOP constitutes an ubiquitin E3 ligase which is able to ubiquitinate the PcG protein BMI1, the variant histone macroH2A1 and the death domain-associated protein Daxx. Therefore, SPOP may be involved in the regulation of these proteins and may play a role in transcriptional regulation, apoptosis and X-chromosome inactivation. Cul3 binds to the BTB domain of SPOP whereas Daxx and the macroH2A1 nonhistone region have been shown to bind to the MATH domain. Both MATH and BTB domains are necessary for the nuclear speckled accumulation of SPOP. There are many proteins, mostly uncharacterized, containing both MATH and BTB domains from C. elegans and plants which are excluded from this family.
Pssm-ID: 239743 Cd Length: 139 Bit Score: 47.16 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 55 LKFTWTIPNFS--RQNTRKHY-SDVFVVGG---YKWRILIFPKG---NNVDHLSMYLDVSDAASLPYgwsrYAQFSLAVV 125
Cdd:cd03774 5 FCYMWTISNFSfcREEMGEVIkSSTFSSGAndkLKWCLRVNPKGldeESKDYLSLYLLLVSCPKSEV----RAKFKFSIL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 18415260 126 NQIHTRYTVRKETQHQFNARESDWGFTSFMPLSELYDPSRGYLVNDTVLVEAEVAV 181
Cdd:cd03774 81 NAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSV 136
|
|
| Peptidase_C19M |
cd02669 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
197-478 |
8.62e-05 |
|
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: 46.54 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 197 GFVGLKNQGATCYMNSLLQTLYHIPYFRK--AVYHMPTTENDAPTAsIPLALQSLFYKLqYNDT------------SVAT 262
Cdd:cd02669 118 GFVGLNNIKNNDYANVIIQALSHVKPIRNffLLYENYENIKDRKSE-LVKRLSELIRKI-WNPRnfkghvsphellQAVS 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 263 KELTKSFGWDTydsfmQHDVQE-----LNRvLCEKLEDKMKGtvVEGTIQQLFEGH----------HMNYIECINVDFKS 327
Cdd:cd02669 196 KVSKKKFSITE-----QSDPVEflswlLNT-LHKDLGGSKKP--NSSIIHDCFQGKvqietqkikpHAEEEGSKDKFFKD 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 328 TRKES-----FYDLQLDVKG-----------------CKDVYASFDKYVEVErlegdnkyhaeghgLQDAKKGVLFIDFP 385
Cdd:cd02669 268 SRVKKtsvspFLLLTLDLPPpplfkdgneeniipqvpLKQLLKKYDGKTETE--------------LKDSLKRYLISRLP 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 386 PVLQLQLKRFEY-DFMRD---TMVkindryEFPLELDldrEDGKYLSPDADRSVRNL-YTLHSVLVHSGGVHG-GHYYAF 459
Cdd:cd02669 334 KYLIFHIKRFSKnNFFKEknpTIV------NFPIKNL---DLSDYVHFDKPSLNLSTkYNLVANIVHEGTPQEdGTWRVQ 404
|
330
....*....|....*....
gi 18415260 460 IRPTLSDQWYKFDDERVTK 478
Cdd:cd02669 405 LRHKSTNKWFEIQDLNVKE 423
|
|
| Peptidase_C19N |
cd02670 |
A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are ... |
385-521 |
8.54e-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: 42.51 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 385 PPVLQLQLKRFEYDFMRDtmVKINDRYEFPLELDLDR--EDGKYLSPDADRSVRNLYT--------------LHSVLVHS 448
Cdd:cd02670 99 PSCLIICLKRYGKTEGKA--QKMFKKILIPDEIDIPDfvADDPRACSKCQLECRVCYDdkdfsptcgkfklsLCSAVCHR 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18415260 449 G-GVHGGHYYAFIR-----------PTLSDQWYKFDDervtkedlkraLEEQYGGEEelpqtnpGFNNNPPFKFtkySNA 516
Cdd:cd02670 177 GtSLETGHYVAFVRygsysltetdnEAYNAQWVFFDD-----------MADRDGVSN-------GFNIPAARLL---EDP 235
|
....*
gi 18415260 517 YMLVY 521
Cdd:cd02670 236 YMLFY 240
|
|
| |
