|
Name |
Accession |
Description |
Interval |
E-value |
| CysPc |
cd00044 |
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ... |
147-471 |
1.65e-105 |
|
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction.
:
Pssm-ID: 238004 [Multi-domain] Cd Length: 315 Bit Score: 325.06 E-value: 1.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 147 TTSKINGIEYVPFMNVDLRERFAYPMPFCdrwgklPLSPKQKTTFSKWVRPEDLTNN-----PTMIY-TVSSFSIKQTIV 220
Cdd:cd00044 1 TLLQICLLSGVLFEDPDFPPNDSSLGFDD------SLSNGQPKKVIEWKRPSEIFADdgnsnPRLFVnGASPSDVCQGIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 221 SDCSFVASLAISAAYErrfnkKLITGIIYPqnkDGEPEYNPCGKYMVKLHLNGVPRKVIIDDQLPVDHkGELLCSYSNNK 300
Cdd:cd00044 75 GDCWFLAALAALAERP-----ELLKRVIPP---DQSFEENYAGIYHFRFWKNGEWVEVVIDDRLPTSN-GGLLFMHSRDR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 301 SELWVSLIEKAYMKVMGGYDF-PGSNSNIDLHALTGWIPERIAMHSDSQTFSKDNSFRMLYqRFHKGDVLITASTGMMTE 379
Cdd:cd00044 146 NELWVALLEKAYAKLHGSYEAlVGGNTAEALEDLTGGPTERIDLKSADASSGDNDLFALLL-SFLQGGSLIGCSTGSRSE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 380 AEGEK-WGLVPTHAYAVLDIREFK--GLRFIQLKNPWSHLRWKGRYSENDVKNWTPELQkylnFDPRTAQKIDNGIFWIS 456
Cdd:cd00044 225 EEARTaNGLVKGHAYSVLDVREVQeeGLRLLRLRNPWGVGEWWGGWSDDSSEWWVIDAE----RKKLLLSGKDDGEFWMS 300
|
330
....*....|....*
gi 1774221924 457 WDDLCQYYDVIYLSW 471
Cdd:cd00044 301 FEDFLRNFDGLYVCN 315
|
|
| MIT super family |
cl00299 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ... |
85-149 |
6.34e-39 |
|
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.
The actual alignment was detected with superfamily member cd02680:
Pssm-ID: 469712 Cd Length: 75 Bit Score: 138.21 E-value: 6.34e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774221924 85 LDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRTTS 149
Cdd:cd02680 1 LDLERAHFLVTQAFDEDEKGNAEEAIELYTEAVELCINTSNETMDQALQTKLKQLARQALDRAEA 65
|
|
| calpain_III |
smart00720 |
calpain_III domain; |
620-743 |
6.83e-38 |
|
calpain_III domain;
:
Pssm-ID: 214786 Cd Length: 143 Bit Score: 137.88 E-value: 6.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 620 TLSKRINGKWS-GQSAGGCGNFQETHKNNPIYQFHIEKTGP----LLIEL----------RGPRQYSVGFEVVTV----S 680
Cdd:smart00720 1 WHTKSVQGSWTrGQTAGGCRNYPATFWTNPQFRITLEEPDDddctVLIALmqknrrrlrrKGADFLTIGFAVYKVpkelH 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774221924 681 TLGDPGPHGFLRKSSGDYRCGFCYLELENIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKIT 743
Cdd:smart00720 81 LRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
|
|
| MIT_calpain7_1 |
cd02681 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
5-76 |
1.61e-36 |
|
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear.
:
Pssm-ID: 239144 Cd Length: 76 Bit Score: 131.56 E-value: 1.61e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774221924 5 ALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYAEMAG----SSLENIQEKITEYLERVQALHSAVQSKSA 76
Cdd:cd02681 1 ALERDAVQFARLAVQRDQEGRYSEAVFYYKEAAQLLIYAEMAGtlndSHLKTIQEKSNEYLDRAQALHQLVQGQQG 76
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysPc |
cd00044 |
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ... |
147-471 |
1.65e-105 |
|
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction.
Pssm-ID: 238004 [Multi-domain] Cd Length: 315 Bit Score: 325.06 E-value: 1.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 147 TTSKINGIEYVPFMNVDLRERFAYPMPFCdrwgklPLSPKQKTTFSKWVRPEDLTNN-----PTMIY-TVSSFSIKQTIV 220
Cdd:cd00044 1 TLLQICLLSGVLFEDPDFPPNDSSLGFDD------SLSNGQPKKVIEWKRPSEIFADdgnsnPRLFVnGASPSDVCQGIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 221 SDCSFVASLAISAAYErrfnkKLITGIIYPqnkDGEPEYNPCGKYMVKLHLNGVPRKVIIDDQLPVDHkGELLCSYSNNK 300
Cdd:cd00044 75 GDCWFLAALAALAERP-----ELLKRVIPP---DQSFEENYAGIYHFRFWKNGEWVEVVIDDRLPTSN-GGLLFMHSRDR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 301 SELWVSLIEKAYMKVMGGYDF-PGSNSNIDLHALTGWIPERIAMHSDSQTFSKDNSFRMLYqRFHKGDVLITASTGMMTE 379
Cdd:cd00044 146 NELWVALLEKAYAKLHGSYEAlVGGNTAEALEDLTGGPTERIDLKSADASSGDNDLFALLL-SFLQGGSLIGCSTGSRSE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 380 AEGEK-WGLVPTHAYAVLDIREFK--GLRFIQLKNPWSHLRWKGRYSENDVKNWTPELQkylnFDPRTAQKIDNGIFWIS 456
Cdd:cd00044 225 EEARTaNGLVKGHAYSVLDVREVQeeGLRLLRLRNPWGVGEWWGGWSDDSSEWWVIDAE----RKKLLLSGKDDGEFWMS 300
|
330
....*....|....*
gi 1774221924 457 WDDLCQYYDVIYLSW 471
Cdd:cd00044 301 FEDFLRNFDGLYVCN 315
|
|
| CysPc |
smart00230 |
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ... |
156-478 |
2.81e-85 |
|
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). Calcium activated neutral protease (large subunit).
Pssm-ID: 128526 Cd Length: 318 Bit Score: 272.28 E-value: 2.81e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 156 YVPFMNVDLRERFAYPMP-FCDRWGKLPLSPKQKTtFSKWVRPEDLTNNPTMIY-TVSSFSIKQTIVSDCSFVASLAISA 233
Cdd:smart00230 1 YEALRQYCKESGTLFEDPlFPANNGSLFFSQRQRK-FVVWKRPHEIFENPPFIVgGASRTDICQGVLGDCWLLAALASLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 234 AYErrfnkKLITgIIYPQNKDGEPeyNPCGKYMVKLHLNGVPRKVIIDDQLPVDhKGELLCSYSNNKSELWVSLIEKAYM 313
Cdd:smart00230 80 LRE-----KLLD-RVIPHDQEFSE--NYAGIFHFRFWRFGKWVDVVIDDRLPTY-NGELVFMHSNSRNEFWSALLEKAYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 314 KVMGGYDFPGSNSNID-LHALTGWIPERIAMHSDSQTfsKDNSFRMLYQRFHKGdVLITASTGMMTEAEGE---KWGLVP 389
Cdd:smart00230 151 KLNGCYEALKGGSTTEaLEDLTGGVAESIDLKEASKD--PDNLFEDLFKAFERG-SLMGCSIGAGTAVEEEeqkDCGLVK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 390 THAYAVLDIRE--FKGLRFIQLKNPWSHLRWKGRYSEnDVKNWT---PELQKYLNFDPRtaqkiDNGIFWISWDDLCQYY 464
Cdd:smart00230 228 GHAYSVTDVREvqGRRQELLRLRNPWGQVEWNGPWSD-DSPEWRsvsASEKKNLGLTFD-----DDGEFWMSFEDFLRHF 301
|
330
....*....|....*
gi 1774221924 465 -DVIYLSWNPGLFKE 478
Cdd:smart00230 302 dKVEICNLNPDSLEE 316
|
|
| Peptidase_C2 |
pfam00648 |
Calpain family cysteine protease; |
182-465 |
3.81e-48 |
|
Calpain family cysteine protease;
Pssm-ID: 459889 [Multi-domain] Cd Length: 295 Bit Score: 171.92 E-value: 3.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 182 PLSPKQKTTFsKWVRPEDLTNNPTMI-YTVSSFSIKQTIVSDCSFVASLAISAAYERRFNKklitgIIYPqnkDGEPEYN 260
Cdd:pfam00648 16 PPSPPPPRGV-EWKRPKEICSNPQFIvDGASRFDICQGELGDCWLLAAIASLTLNPKLLER-----VVPP---DQSFEEN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 261 PCGKYMVKLHLNGVPRKVIIDDQLPVdHKGELLCSYSNNKSELWVSLIEKAYMKVMGGY-DFPGSNSNIDLHALTGWIPE 339
Cdd:pfam00648 87 YAGIFHFRFWRFGEWVDVVIDDRLPT-RNGKLLFVHSRDKNEFWSALLEKAYAKLHGSYeALKGGSTSEALEDFTGGVAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 340 RIAMHSdsqtfSKDNSFRMLyQRFHKGDVLITASTGMMTEAEGEKW---GLVPTHAYAVLDIRE----FKGLRFIQLKNP 412
Cdd:pfam00648 166 SYDLKE-----PPPNLFEIL-LKALERGSLMGCSIDATSAAEEEARtpnGLVKGHAYSVTGVRKvnlkGGKVRLIRLRNP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1774221924 413 WSHLRWKGRYSENDvKNW---TPELQKYLNFdprtaQKIDNGIFWISWDDLCQYYD 465
Cdd:pfam00648 240 WGEVEWNGAWSDGS-PEWqtvSPEEKEELGL-----TKKDDGEFWMSFEDFLKYFT 289
|
|
| MIT_calpain7_2 |
cd02680 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
85-149 |
6.34e-39 |
|
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear.
Pssm-ID: 239143 Cd Length: 75 Bit Score: 138.21 E-value: 6.34e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774221924 85 LDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRTTS 149
Cdd:cd02680 1 LDLERAHFLVTQAFDEDEKGNAEEAIELYTEAVELCINTSNETMDQALQTKLKQLARQALDRAEA 65
|
|
| calpain_III |
smart00720 |
calpain_III domain; |
620-743 |
6.83e-38 |
|
calpain_III domain;
Pssm-ID: 214786 Cd Length: 143 Bit Score: 137.88 E-value: 6.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 620 TLSKRINGKWS-GQSAGGCGNFQETHKNNPIYQFHIEKTGP----LLIEL----------RGPRQYSVGFEVVTV----S 680
Cdd:smart00720 1 WHTKSVQGSWTrGQTAGGCRNYPATFWTNPQFRITLEEPDDddctVLIALmqknrrrlrrKGADFLTIGFAVYKVpkelH 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774221924 681 TLGDPGPHGFLRKSSGDYRCGFCYLELENIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKIT 743
Cdd:smart00720 81 LRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
|
|
| MIT_calpain7_1 |
cd02681 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
5-76 |
1.61e-36 |
|
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear.
Pssm-ID: 239144 Cd Length: 76 Bit Score: 131.56 E-value: 1.61e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774221924 5 ALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYAEMAG----SSLENIQEKITEYLERVQALHSAVQSKSA 76
Cdd:cd02681 1 ALERDAVQFARLAVQRDQEGRYSEAVFYYKEAAQLLIYAEMAGtlndSHLKTIQEKSNEYLDRAQALHQLVQGQQG 76
|
|
| Calpain_III |
cd00214 |
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ... |
618-745 |
1.46e-35 |
|
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains.
Pssm-ID: 238132 Cd Length: 150 Bit Score: 131.65 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 618 PYTLSKRINGKWS-GQSAGGCGNFQETHKNNPIYQFHIEKTG------PLLIELR----------GPRQYSVGFEVVTVS 680
Cdd:cd00214 1 RKWHTKSFNGEWRrGQTAGGCRNNPDTFWTNPQFRIRVPEPDddegkcTVLIALMqknrrhlrkkGLDLLTIGFHVYKVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774221924 681 T-LGDPGPHGFLRK-----SSGDYRCGFCYLELEnIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKITQL 745
Cdd:cd00214 81 GeNRHLRRDFFLHKaprarSSTFINTREVSLRFR-LPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
|
|
| MIT |
smart00745 |
Microtubule Interacting and Trafficking molecule domain; |
83-146 |
6.56e-14 |
|
Microtubule Interacting and Trafficking molecule domain;
Pssm-ID: 197854 Cd Length: 77 Bit Score: 67.33 E-value: 6.56e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774221924 83 HQLDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDR 146
Cdd:smart00745 1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDR 64
|
|
| MIT |
pfam04212 |
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ... |
87-146 |
1.98e-12 |
|
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.
Pssm-ID: 461228 Cd Length: 66 Bit Score: 62.56 E-value: 1.98e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 87 LERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDR 146
Cdd:pfam04212 1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLER 60
|
|
| MIT |
pfam04212 |
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ... |
10-69 |
4.86e-10 |
|
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.
Pssm-ID: 461228 Cd Length: 66 Bit Score: 56.01 E-value: 4.86e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774221924 10 AVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYA---EMAGSSLENIQEKITEYLERVQALHS 69
Cdd:pfam04212 4 ALELVKKAVEEDNAGNYEEALELYKEALDYLLLAlkeTKNEERRELLRAKIAEYLERAEELKE 66
|
|
| Calpain_III |
pfam01067 |
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ... |
626-732 |
3.64e-09 |
|
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions.
Pssm-ID: 460050 Cd Length: 136 Bit Score: 55.63 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 626 NGKW-SGQSAGGCGNFQETHKNNPIYQFHIEKTGP--------LLIEL----------RGPRQYSVGFEV--VTVSTLGD 684
Cdd:pfam01067 2 EGRWvRGSTAGGCRNYPDTFWTNPQYRFTLTEPDDdddegectVLVSLmqknrrkqrrLGENLLTIGFAIykVPVELNRK 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1774221924 685 PGPHGFLRKS----SGDY---RCGFCYLELeniPSGIFNIIPSTFLPKQEGPFFL 732
Cdd:pfam01067 82 LRKHFFLTNQpvarSSTYinsREVSLRFRL---PPGEYVIVPSTFEPNEEGEFLL 133
|
|
| MIT |
smart00745 |
Microtubule Interacting and Trafficking molecule domain; |
4-74 |
4.43e-06 |
|
Microtubule Interacting and Trafficking molecule domain;
Pssm-ID: 197854 Cd Length: 77 Bit Score: 44.99 E-value: 4.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774221924 4 TALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQAL---IYAEMAGSSLENIQEKITEYLERVQALHSAVQSK 74
Cdd:smart00745 2 RDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLlegIKVESDSKRREALKAKAAEYLDRAEEIKKSLLER 75
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
5-146 |
6.03e-04 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 42.41 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 5 ALERDAVQF-ARLAVQRDH--EGRYSEAVFYYKEAAQALIYAEMAGSSLENIQEKITEYLERVQALHSAVQsksadplks 81
Cdd:COG2956 68 LLERDPDRAeALLELAQDYlkAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLK--------- 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774221924 82 khqLDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDL---CLKTSYETADKVLQNKLKQLARQALDR 146
Cdd:COG2956 139 ---LGPENAHAYCELAELYLEQGDYDEAIEALEKALKLdpdCARALLLLAELYLEQGDYEEAIAALER 203
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysPc |
cd00044 |
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ... |
147-471 |
1.65e-105 |
|
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. Functions in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction.
Pssm-ID: 238004 [Multi-domain] Cd Length: 315 Bit Score: 325.06 E-value: 1.65e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 147 TTSKINGIEYVPFMNVDLRERFAYPMPFCdrwgklPLSPKQKTTFSKWVRPEDLTNN-----PTMIY-TVSSFSIKQTIV 220
Cdd:cd00044 1 TLLQICLLSGVLFEDPDFPPNDSSLGFDD------SLSNGQPKKVIEWKRPSEIFADdgnsnPRLFVnGASPSDVCQGIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 221 SDCSFVASLAISAAYErrfnkKLITGIIYPqnkDGEPEYNPCGKYMVKLHLNGVPRKVIIDDQLPVDHkGELLCSYSNNK 300
Cdd:cd00044 75 GDCWFLAALAALAERP-----ELLKRVIPP---DQSFEENYAGIYHFRFWKNGEWVEVVIDDRLPTSN-GGLLFMHSRDR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 301 SELWVSLIEKAYMKVMGGYDF-PGSNSNIDLHALTGWIPERIAMHSDSQTFSKDNSFRMLYqRFHKGDVLITASTGMMTE 379
Cdd:cd00044 146 NELWVALLEKAYAKLHGSYEAlVGGNTAEALEDLTGGPTERIDLKSADASSGDNDLFALLL-SFLQGGSLIGCSTGSRSE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 380 AEGEK-WGLVPTHAYAVLDIREFK--GLRFIQLKNPWSHLRWKGRYSENDVKNWTPELQkylnFDPRTAQKIDNGIFWIS 456
Cdd:cd00044 225 EEARTaNGLVKGHAYSVLDVREVQeeGLRLLRLRNPWGVGEWWGGWSDDSSEWWVIDAE----RKKLLLSGKDDGEFWMS 300
|
330
....*....|....*
gi 1774221924 457 WDDLCQYYDVIYLSW 471
Cdd:cd00044 301 FEDFLRNFDGLYVCN 315
|
|
| CysPc |
smart00230 |
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ... |
156-478 |
2.81e-85 |
|
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). Calcium activated neutral protease (large subunit).
Pssm-ID: 128526 Cd Length: 318 Bit Score: 272.28 E-value: 2.81e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 156 YVPFMNVDLRERFAYPMP-FCDRWGKLPLSPKQKTtFSKWVRPEDLTNNPTMIY-TVSSFSIKQTIVSDCSFVASLAISA 233
Cdd:smart00230 1 YEALRQYCKESGTLFEDPlFPANNGSLFFSQRQRK-FVVWKRPHEIFENPPFIVgGASRTDICQGVLGDCWLLAALASLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 234 AYErrfnkKLITgIIYPQNKDGEPeyNPCGKYMVKLHLNGVPRKVIIDDQLPVDhKGELLCSYSNNKSELWVSLIEKAYM 313
Cdd:smart00230 80 LRE-----KLLD-RVIPHDQEFSE--NYAGIFHFRFWRFGKWVDVVIDDRLPTY-NGELVFMHSNSRNEFWSALLEKAYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 314 KVMGGYDFPGSNSNID-LHALTGWIPERIAMHSDSQTfsKDNSFRMLYQRFHKGdVLITASTGMMTEAEGE---KWGLVP 389
Cdd:smart00230 151 KLNGCYEALKGGSTTEaLEDLTGGVAESIDLKEASKD--PDNLFEDLFKAFERG-SLMGCSIGAGTAVEEEeqkDCGLVK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 390 THAYAVLDIRE--FKGLRFIQLKNPWSHLRWKGRYSEnDVKNWT---PELQKYLNFDPRtaqkiDNGIFWISWDDLCQYY 464
Cdd:smart00230 228 GHAYSVTDVREvqGRRQELLRLRNPWGQVEWNGPWSD-DSPEWRsvsASEKKNLGLTFD-----DDGEFWMSFEDFLRHF 301
|
330
....*....|....*
gi 1774221924 465 -DVIYLSWNPGLFKE 478
Cdd:smart00230 302 dKVEICNLNPDSLEE 316
|
|
| Peptidase_C2 |
pfam00648 |
Calpain family cysteine protease; |
182-465 |
3.81e-48 |
|
Calpain family cysteine protease;
Pssm-ID: 459889 [Multi-domain] Cd Length: 295 Bit Score: 171.92 E-value: 3.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 182 PLSPKQKTTFsKWVRPEDLTNNPTMI-YTVSSFSIKQTIVSDCSFVASLAISAAYERRFNKklitgIIYPqnkDGEPEYN 260
Cdd:pfam00648 16 PPSPPPPRGV-EWKRPKEICSNPQFIvDGASRFDICQGELGDCWLLAAIASLTLNPKLLER-----VVPP---DQSFEEN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 261 PCGKYMVKLHLNGVPRKVIIDDQLPVdHKGELLCSYSNNKSELWVSLIEKAYMKVMGGY-DFPGSNSNIDLHALTGWIPE 339
Cdd:pfam00648 87 YAGIFHFRFWRFGEWVDVVIDDRLPT-RNGKLLFVHSRDKNEFWSALLEKAYAKLHGSYeALKGGSTSEALEDFTGGVAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 340 RIAMHSdsqtfSKDNSFRMLyQRFHKGDVLITASTGMMTEAEGEKW---GLVPTHAYAVLDIRE----FKGLRFIQLKNP 412
Cdd:pfam00648 166 SYDLKE-----PPPNLFEIL-LKALERGSLMGCSIDATSAAEEEARtpnGLVKGHAYSVTGVRKvnlkGGKVRLIRLRNP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1774221924 413 WSHLRWKGRYSENDvKNW---TPELQKYLNFdprtaQKIDNGIFWISWDDLCQYYD 465
Cdd:pfam00648 240 WGEVEWNGAWSDGS-PEWqtvSPEEKEELGL-----TKKDDGEFWMSFEDFLKYFT 289
|
|
| MIT_calpain7_2 |
cd02680 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
85-149 |
6.34e-39 |
|
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear.
Pssm-ID: 239143 Cd Length: 75 Bit Score: 138.21 E-value: 6.34e-39
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774221924 85 LDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRTTS 149
Cdd:cd02680 1 LDLERAHFLVTQAFDEDEKGNAEEAIELYTEAVELCINTSNETMDQALQTKLKQLARQALDRAEA 65
|
|
| calpain_III |
smart00720 |
calpain_III domain; |
620-743 |
6.83e-38 |
|
calpain_III domain;
Pssm-ID: 214786 Cd Length: 143 Bit Score: 137.88 E-value: 6.83e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 620 TLSKRINGKWS-GQSAGGCGNFQETHKNNPIYQFHIEKTGP----LLIEL----------RGPRQYSVGFEVVTV----S 680
Cdd:smart00720 1 WHTKSVQGSWTrGQTAGGCRNYPATFWTNPQFRITLEEPDDddctVLIALmqknrrrlrrKGADFLTIGFAVYKVpkelH 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774221924 681 TLGDPGPHGFLRKSSGDYRCGFCYLELENIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKIT 743
Cdd:smart00720 81 LRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
|
|
| MIT_calpain7_1 |
cd02681 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
5-76 |
1.61e-36 |
|
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in the nuclear thiol protease PalBH. The molecular function of the MIT domain is unclear.
Pssm-ID: 239144 Cd Length: 76 Bit Score: 131.56 E-value: 1.61e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774221924 5 ALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYAEMAG----SSLENIQEKITEYLERVQALHSAVQSKSA 76
Cdd:cd02681 1 ALERDAVQFARLAVQRDQEGRYSEAVFYYKEAAQLLIYAEMAGtlndSHLKTIQEKSNEYLDRAQALHQLVQGQQG 76
|
|
| Calpain_III |
cd00214 |
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ... |
618-745 |
1.46e-35 |
|
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, participate in cytoskeletal remodeling processes, cell differentiation, apoptosis and signal transduction. Catalytic domain and the two calmodulin-like domains are separated by C2-like domain III. Domain III plays an important role in calcium-induced activation of calpain involving electrostatic interactions with subdomain II. Proposed to mediate calpain's interaction with phospholipids and translocation to cytoplasmic/nuclear membranes. CD includes subdomain III of typical and atypical calpains.
Pssm-ID: 238132 Cd Length: 150 Bit Score: 131.65 E-value: 1.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 618 PYTLSKRINGKWS-GQSAGGCGNFQETHKNNPIYQFHIEKTG------PLLIELR----------GPRQYSVGFEVVTVS 680
Cdd:cd00214 1 RKWHTKSFNGEWRrGQTAGGCRNNPDTFWTNPQFRIRVPEPDddegkcTVLIALMqknrrhlrkkGLDLLTIGFHVYKVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774221924 681 T-LGDPGPHGFLRK-----SSGDYRCGFCYLELEnIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKITQL 745
Cdd:cd00214 81 GeNRHLRRDFFLHKaprarSSTFINTREVSLRFR-LPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
|
|
| MIT |
cd02656 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ... |
86-146 |
9.74e-16 |
|
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.
Pssm-ID: 239121 Cd Length: 75 Bit Score: 72.34 E-value: 9.74e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774221924 86 DLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDR 146
Cdd:cd02656 2 LLQQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKLLRKKVKEYLDR 62
|
|
| MIT |
smart00745 |
Microtubule Interacting and Trafficking molecule domain; |
83-146 |
6.56e-14 |
|
Microtubule Interacting and Trafficking molecule domain;
Pssm-ID: 197854 Cd Length: 77 Bit Score: 67.33 E-value: 6.56e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774221924 83 HQLDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDR 146
Cdd:smart00745 1 TRDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDR 64
|
|
| MIT |
cd02656 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ... |
5-76 |
1.01e-12 |
|
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain is found in sorting nexins, the nuclear thiol protease PalBH, the AAA protein spastin and archaebacterial proteins with similar domain architecture, vacuolar sorting proteins and others. The molecular function of the MIT domain is unclear.
Pssm-ID: 239121 Cd Length: 75 Bit Score: 63.87 E-value: 1.01e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774221924 5 ALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYAEMAGSS---LENIQEKITEYLERVQALHSAVQSKSA 76
Cdd:cd02656 1 ELLQQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEpklRKLLRKKVKEYLDRAEFLKELLKKQKQ 75
|
|
| MIT |
pfam04212 |
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ... |
87-146 |
1.98e-12 |
|
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.
Pssm-ID: 461228 Cd Length: 66 Bit Score: 62.56 E-value: 1.98e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 87 LERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDR 146
Cdd:pfam04212 1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLER 60
|
|
| MIT |
pfam04212 |
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ... |
10-69 |
4.86e-10 |
|
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric three-helix bundle and binds ESCRT-III (endosomal sorting complexes required for transport) substrates.
Pssm-ID: 461228 Cd Length: 66 Bit Score: 56.01 E-value: 4.86e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774221924 10 AVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYA---EMAGSSLENIQEKITEYLERVQALHS 69
Cdd:pfam04212 4 ALELVKKAVEEDNAGNYEEALELYKEALDYLLLAlkeTKNEERRELLRAKIAEYLERAEELKE 66
|
|
| Calpain_III |
pfam01067 |
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. ... |
626-732 |
3.64e-09 |
|
Calpain large subunit, domain III; The function of the domain III and I are currently unknown. Domain II is a cysteine protease and domain IV is a calcium binding domain. Calpains are believed to participate in intracellular signaling pathways mediated by calcium ions.
Pssm-ID: 460050 Cd Length: 136 Bit Score: 55.63 E-value: 3.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 626 NGKW-SGQSAGGCGNFQETHKNNPIYQFHIEKTGP--------LLIEL----------RGPRQYSVGFEV--VTVSTLGD 684
Cdd:pfam01067 2 EGRWvRGSTAGGCRNYPDTFWTNPQYRFTLTEPDDdddegectVLVSLmqknrrkqrrLGENLLTIGFAIykVPVELNRK 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1774221924 685 PGPHGFLRKS----SGDY---RCGFCYLELeniPSGIFNIIPSTFLPKQEGPFFL 732
Cdd:pfam01067 82 LRKHFFLTNQpvarSSTYinsREVSLRFRL---PPGEYVIVPSTFEPNEEGEFLL 133
|
|
| MIT |
smart00745 |
Microtubule Interacting and Trafficking molecule domain; |
4-74 |
4.43e-06 |
|
Microtubule Interacting and Trafficking molecule domain;
Pssm-ID: 197854 Cd Length: 77 Bit Score: 44.99 E-value: 4.43e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774221924 4 TALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQAL---IYAEMAGSSLENIQEKITEYLERVQALHSAVQSK 74
Cdd:smart00745 2 RDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLlegIKVESDSKRREALKAKAAEYLDRAEEIKKSLLER 75
|
|
| MIT_VPS4 |
cd02678 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
10-76 |
1.01e-05 |
|
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.
Pssm-ID: 239141 Cd Length: 75 Bit Score: 44.18 E-value: 1.01e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 10 AVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYA---EMAGSSLENIQEKITEYLERVQALHSAVQSKSA 76
Cdd:cd02678 6 AIELVKKAIEEDNAGNYEEALRLYQHALEYFMHAlkyEKNPKSKESIRAKCTEYLDRAEKLKEYLAKKEK 75
|
|
| MIT_VPS4 |
cd02678 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
87-146 |
2.19e-04 |
|
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in intracellular protein transport proteins of the AAA-ATPase family. The molecular function of the MIT domain is unclear.
Pssm-ID: 239141 Cd Length: 75 Bit Score: 40.33 E-value: 2.19e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774221924 87 LERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKT-SYETadkvlQNKLKQLAR----QALDR 146
Cdd:cd02678 3 LQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHAlKYEK-----NPKSKESIRakctEYLDR 62
|
|
| MIT_AAA_Arch |
cd02682 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
6-76 |
2.35e-04 |
|
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in mostly archaebacterial AAA-ATPases. The molecular function of the MIT domain is unclear.
Pssm-ID: 239145 Cd Length: 75 Bit Score: 40.20 E-value: 2.35e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774221924 6 LERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQAL---IYAEMAGSSLENIQEKITEYLERVQALHSAVQSKSA 76
Cdd:cd02682 2 LEEMARKYAINAVKAEKEGNAEDAITNYKKAIEVLsqiVKNYPDSPTRLIYEQMINEYKRRIEVLEKQNPASSA 75
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
5-146 |
6.03e-04 |
|
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442196 [Multi-domain] Cd Length: 275 Bit Score: 42.41 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 5 ALERDAVQF-ARLAVQRDH--EGRYSEAVFYYKEAAQALIYAEMAGSSLENIQEKITEYLERVQALHSAVQsksadplks 81
Cdd:COG2956 68 LLERDPDRAeALLELAQDYlkAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLK--------- 138
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774221924 82 khqLDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDL---CLKTSYETADKVLQNKLKQLARQALDR 146
Cdd:COG2956 139 ---LGPENAHAYCELAELYLEQGDYDEAIEALEKALKLdpdCARALLLLAELYLEQGDYEEAIAALER 203
|
|
| TOPEUc |
smart00435 |
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ... |
47-155 |
7.80e-03 |
|
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras
Pssm-ID: 214661 [Multi-domain] Cd Length: 391 Bit Score: 39.25 E-value: 7.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774221924 47 GSSLENIQEKITEYLE-----RVQALHSAVQSKSADPLKSKHQLDLERAHFLVTQAFDEDEKENVEdaielyteavdlcl 121
Cdd:smart00435 276 EKSMEKLQEKIKALKYqlkrlKKMILLFEMISDLKRKLKSKFERDNEKLDAEVKEKKKEKKKEEKK-------------- 341
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1774221924 122 KTSYETadkvLQNKLKQLARQALDR--------TTSKINGIE 155
Cdd:smart00435 342 KKQIER----LEERIEKLEVQATDKeenktvalGTSKINYID 379
|
|
| |
