|
Name |
Accession |
Description |
Interval |
E-value |
| CysPc |
cd00044 |
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ... |
214-538 |
1.12e-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: 324.67 E-value: 1.12e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 214 TTSKINGIEYVPFMNVDLRERFAYPMPFCdrwgklPLSPKQKTTFSKWVRPEDLTNN-----PTMIY-TVSSFSIKQTIV 287
Cdd:cd00044 1 TLLQICLLSGVLFEDPDFPPNDSSLGFDD------SLSNGQPKKVIEWKRPSEIFADdgnsnPRLFVnGASPSDVCQGIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 288 SDCSFVASLAISAAYErrfnkKLITGIIYPqnkDGEPEYNPCGKYMVKLHLNGVPRKVIIDDQLPVDHkGELLCSYSNNK 367
Cdd:cd00044 75 GDCWFLAALAALAERP-----ELLKRVIPP---DQSFEENYAGIYHFRFWKNGEWVEVVIDDRLPTSN-GGLLFMHSRDR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 368 SELWVSLIEKAYMKVMGGYDF-PGSNSNIDLHALTGWIPERIAMHSDSQTFSKDNSFRMLYqRFHKGDVLITASTGMMTE 446
Cdd:cd00044 146 NELWVALLEKAYAKLHGSYEAlVGGNTAEALEDLTGGPTERIDLKSADASSGDNDLFALLL-SFLQGGSLIGCSTGSRSE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 447 AEGEK-WGLVPTHAYAVLDIREFK--GLRFIQLKNPWSHLRWKGRYSENDVKNWTPELQkylnFDPRTAQKIDNGIFWIS 523
Cdd:cd00044 225 EEARTaNGLVKGHAYSVLDVREVQeeGLRLLRLRNPWGVGEWWGGWSDDSSEWWVIDAE----RKKLLLSGKDDGEFWMS 300
|
330
....*....|....*
gi 1774222183 524 WDDLCQYYDVIYLSW 538
Cdd:cd00044 301 FEDFLRNFDGLYVCN 315
|
|
| MIT super family |
cl00299 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ... |
85-159 |
1.47e-45 |
|
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: 156.70 E-value: 1.47e-45
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774222183 85 LDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEALSEPLTKPVG 159
Cdd:cd02680 1 LDLERAHFLVTQAFDEDEKGNAEEAIELYTEAVELCINTSNETMDQALQTKLKQLARQALDRAEALKESMSKASS 75
|
|
| calpain_III |
smart00720 |
calpain_III domain; |
593-716 |
6.93e-38 |
|
calpain_III domain;
:
Pssm-ID: 214786 Cd Length: 143 Bit Score: 137.88 E-value: 6.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 593 TLSKRINGKWS-GQSAGGCGNFQETHKNNPIYQFHIEKTGP----LLIEL----------RGPRQYSVGFEVVTV----S 653
Cdd:smart00720 1 WHTKSVQGSWTrGQTAGGCRNYPATFWTNPQFRITLEEPDDddctVLIALmqknrrrlrrKGADFLTIGFAVYKVpkelH 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774222183 654 TLGDPGPHGFLRKSSGDYRCGFCYLELENIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKIT 716
Cdd:smart00720 81 LRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
|
|
| MIT_calpain7_1 |
cd02681 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
5-76 |
1.49e-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: 1.49e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774222183 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. ... |
214-538 |
1.12e-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: 324.67 E-value: 1.12e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 214 TTSKINGIEYVPFMNVDLRERFAYPMPFCdrwgklPLSPKQKTTFSKWVRPEDLTNN-----PTMIY-TVSSFSIKQTIV 287
Cdd:cd00044 1 TLLQICLLSGVLFEDPDFPPNDSSLGFDD------SLSNGQPKKVIEWKRPSEIFADdgnsnPRLFVnGASPSDVCQGIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 288 SDCSFVASLAISAAYErrfnkKLITGIIYPqnkDGEPEYNPCGKYMVKLHLNGVPRKVIIDDQLPVDHkGELLCSYSNNK 367
Cdd:cd00044 75 GDCWFLAALAALAERP-----ELLKRVIPP---DQSFEENYAGIYHFRFWKNGEWVEVVIDDRLPTSN-GGLLFMHSRDR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 368 SELWVSLIEKAYMKVMGGYDF-PGSNSNIDLHALTGWIPERIAMHSDSQTFSKDNSFRMLYqRFHKGDVLITASTGMMTE 446
Cdd:cd00044 146 NELWVALLEKAYAKLHGSYEAlVGGNTAEALEDLTGGPTERIDLKSADASSGDNDLFALLL-SFLQGGSLIGCSTGSRSE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 447 AEGEK-WGLVPTHAYAVLDIREFK--GLRFIQLKNPWSHLRWKGRYSENDVKNWTPELQkylnFDPRTAQKIDNGIFWIS 523
Cdd:cd00044 225 EEARTaNGLVKGHAYSVLDVREVQeeGLRLLRLRNPWGVGEWWGGWSDDSSEWWVIDAE----RKKLLLSGKDDGEFWMS 300
|
330
....*....|....*
gi 1774222183 524 WDDLCQYYDVIYLSW 538
Cdd:cd00044 301 FEDFLRNFDGLYVCN 315
|
|
| CysPc |
smart00230 |
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ... |
223-545 |
2.07e-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: 2.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 223 YVPFMNVDLRERFAYPMP-FCDRWGKLPLSPKQKTtFSKWVRPEDLTNNPTMIY-TVSSFSIKQTIVSDCSFVASLAISA 300
Cdd:smart00230 1 YEALRQYCKESGTLFEDPlFPANNGSLFFSQRQRK-FVVWKRPHEIFENPPFIVgGASRTDICQGVLGDCWLLAALASLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 301 AYErrfnkKLITgIIYPQNKDGEPeyNPCGKYMVKLHLNGVPRKVIIDDQLPVDhKGELLCSYSNNKSELWVSLIEKAYM 380
Cdd:smart00230 80 LRE-----KLLD-RVIPHDQEFSE--NYAGIFHFRFWRFGKWVDVVIDDRLPTY-NGELVFMHSNSRNEFWSALLEKAYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 381 KVMGGYDFPGSNSNID-LHALTGWIPERIAMHSDSQTfsKDNSFRMLYQRFHKGdVLITASTGMMTEAEGE---KWGLVP 456
Cdd:smart00230 151 KLNGCYEALKGGSTTEaLEDLTGGVAESIDLKEASKD--PDNLFEDLFKAFERG-SLMGCSIGAGTAVEEEeqkDCGLVK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 457 THAYAVLDIRE--FKGLRFIQLKNPWSHLRWKGRYSEnDVKNWT---PELQKYLNFDPRtaqkiDNGIFWISWDDLCQYY 531
Cdd:smart00230 228 GHAYSVTDVREvqGRRQELLRLRNPWGQVEWNGPWSD-DSPEWRsvsASEKKNLGLTFD-----DDGEFWMSFEDFLRHF 301
|
330
....*....|....*
gi 1774222183 532 -DVIYLSWNPGLFKE 545
Cdd:smart00230 302 dKVEICNLNPDSLEE 316
|
|
| Peptidase_C2 |
pfam00648 |
Calpain family cysteine protease; |
249-532 |
3.98e-48 |
|
Calpain family cysteine protease;
Pssm-ID: 459889 [Multi-domain] Cd Length: 295 Bit Score: 171.53 E-value: 3.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 249 PLSPKQKTTFsKWVRPEDLTNNPTMI-YTVSSFSIKQTIVSDCSFVASLAISAAYERRFNKklitgIIYPqnkDGEPEYN 327
Cdd:pfam00648 16 PPSPPPPRGV-EWKRPKEICSNPQFIvDGASRFDICQGELGDCWLLAAIASLTLNPKLLER-----VVPP---DQSFEEN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 328 PCGKYMVKLHLNGVPRKVIIDDQLPVdHKGELLCSYSNNKSELWVSLIEKAYMKVMGGY-DFPGSNSNIDLHALTGWIPE 406
Cdd:pfam00648 87 YAGIFHFRFWRFGEWVDVVIDDRLPT-RNGKLLFVHSRDKNEFWSALLEKAYAKLHGSYeALKGGSTSEALEDFTGGVAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 407 RIAMHSdsqtfSKDNSFRMLyQRFHKGDVLITASTGMMTEAEGEKW---GLVPTHAYAVLDIRE----FKGLRFIQLKNP 479
Cdd:pfam00648 166 SYDLKE-----PPPNLFEIL-LKALERGSLMGCSIDATSAAEEEARtpnGLVKGHAYSVTGVRKvnlkGGKVRLIRLRNP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1774222183 480 WSHLRWKGRYSENDvKNW---TPELQKYLNFdprtaQKIDNGIFWISWDDLCQYYD 532
Cdd:pfam00648 240 WGEVEWNGAWSDGS-PEWqtvSPEEKEELGL-----TKKDDGEFWMSFEDFLKYFT 289
|
|
| MIT_calpain7_2 |
cd02680 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
85-159 |
1.47e-45 |
|
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: 156.70 E-value: 1.47e-45
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774222183 85 LDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEALSEPLTKPVG 159
Cdd:cd02680 1 LDLERAHFLVTQAFDEDEKGNAEEAIELYTEAVELCINTSNETMDQALQTKLKQLARQALDRAEALKESMSKASS 75
|
|
| calpain_III |
smart00720 |
calpain_III domain; |
593-716 |
6.93e-38 |
|
calpain_III domain;
Pssm-ID: 214786 Cd Length: 143 Bit Score: 137.88 E-value: 6.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 593 TLSKRINGKWS-GQSAGGCGNFQETHKNNPIYQFHIEKTGP----LLIEL----------RGPRQYSVGFEVVTV----S 653
Cdd:smart00720 1 WHTKSVQGSWTrGQTAGGCRNYPATFWTNPQFRITLEEPDDddctVLIALmqknrrrlrrKGADFLTIGFAVYKVpkelH 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774222183 654 TLGDPGPHGFLRKSSGDYRCGFCYLELENIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKIT 716
Cdd:smart00720 81 LRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
|
|
| MIT_calpain7_1 |
cd02681 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
5-76 |
1.49e-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: 1.49e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774222183 5 ALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYAEMAG----SSLENIQEKITEYLERVQALHSAVQSKSA 76
Cdd:cd02681 1 ALERDAVQFARLAVQRDQEGRYSEAVFYYKEAAQLLIYAEMAGtlndSHLKTIQEKSNEYLDRAQALHQLVQGQQG 76
|
|
| Calpain_III |
cd00214 |
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ... |
591-718 |
1.87e-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: 131.27 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 591 PYTLSKRINGKWS-GQSAGGCGNFQETHKNNPIYQFHIEKTG------PLLIELR----------GPRQYSVGFEVVTVS 653
Cdd:cd00214 1 RKWHTKSFNGEWRrGQTAGGCRNNPDTFWTNPQFRIRVPEPDddegkcTVLIALMqknrrhlrkkGLDLLTIGFHVYKVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774222183 654 T-LGDPGPHGFLRK-----SSGDYRCGFCYLELEnIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKITQL 718
Cdd:cd00214 81 GeNRHLRRDFFLHKaprarSSTFINTREVSLRFR-LPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
|
|
| MIT |
smart00745 |
Microtubule Interacting and Trafficking molecule domain; |
87-155 |
1.71e-16 |
|
Microtubule Interacting and Trafficking molecule domain;
Pssm-ID: 197854 Cd Length: 77 Bit Score: 74.65 E-value: 1.71e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774222183 87 LERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEALSEPLT 155
Cdd:smart00745 5 LSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLL 73
|
|
| MIT |
pfam04212 |
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ... |
87-152 |
5.97e-15 |
|
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: 69.88 E-value: 5.97e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774222183 87 LERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEALSE 152
Cdd:pfam04212 1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
|
|
| MIT |
pfam04212 |
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ... |
10-69 |
5.69e-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: 55.62 E-value: 5.69e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774222183 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. ... |
599-705 |
3.96e-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: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 599 NGKW-SGQSAGGCGNFQETHKNNPIYQFHIEKTGP--------LLIEL----------RGPRQYSVGFEV--VTVSTLGD 657
Cdd:pfam01067 2 EGRWvRGSTAGGCRNYPDTFWTNPQYRFTLTEPDDdddegectVLVSLmqknrrkqrrLGENLLTIGFAIykVPVELNRK 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1774222183 658 PGPHGFLRKS----SGDY---RCGFCYLELeniPSGIFNIIPSTFLPKQEGPFFL 705
Cdd:pfam01067 82 LRKHFFLTNQpvarSSTYinsREVSLRFRL---PPGEYVIVPSTFEPNEEGEFLL 133
|
|
| MIT |
smart00745 |
Microtubule Interacting and Trafficking molecule domain; |
4-74 |
4.75e-06 |
|
Microtubule Interacting and Trafficking molecule domain;
Pssm-ID: 197854 Cd Length: 77 Bit Score: 44.99 E-value: 4.75e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774222183 4 TALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQAL---IYAEMAGSSLENIQEKITEYLERVQALHSAVQSK 74
Cdd:smart00745 2 RDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLlegIKVESDSKRREALKAKAAEYLDRAEEIKKSLLER 75
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
5-150 |
1.07e-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: 44.72 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 5 ALERDAVQF-ARLAVQRDH--EGRYSEAVFYYKEAAQALIYAEMAGSSLENIQEKITEYLERVQALHSAVQsksadplks 81
Cdd:COG2956 68 LLERDPDRAeALLELAQDYlkAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLK--------- 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774222183 82 khqLDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDL---CLKTSYETADKVLQNKLKQLARQALDRAEAL 150
Cdd:COG2956 139 ---LGPENAHAYCELAELYLEQGDYDEAIEALEKALKLdpdCARALLLLAELYLEQGDYEEAIAALERALEQ 207
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysPc |
cd00044 |
Calpains, domains IIa, IIb; calcium-dependent cytoplasmic cysteine proteinases, papain-like. ... |
214-538 |
1.12e-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: 324.67 E-value: 1.12e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 214 TTSKINGIEYVPFMNVDLRERFAYPMPFCdrwgklPLSPKQKTTFSKWVRPEDLTNN-----PTMIY-TVSSFSIKQTIV 287
Cdd:cd00044 1 TLLQICLLSGVLFEDPDFPPNDSSLGFDD------SLSNGQPKKVIEWKRPSEIFADdgnsnPRLFVnGASPSDVCQGIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 288 SDCSFVASLAISAAYErrfnkKLITGIIYPqnkDGEPEYNPCGKYMVKLHLNGVPRKVIIDDQLPVDHkGELLCSYSNNK 367
Cdd:cd00044 75 GDCWFLAALAALAERP-----ELLKRVIPP---DQSFEENYAGIYHFRFWKNGEWVEVVIDDRLPTSN-GGLLFMHSRDR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 368 SELWVSLIEKAYMKVMGGYDF-PGSNSNIDLHALTGWIPERIAMHSDSQTFSKDNSFRMLYqRFHKGDVLITASTGMMTE 446
Cdd:cd00044 146 NELWVALLEKAYAKLHGSYEAlVGGNTAEALEDLTGGPTERIDLKSADASSGDNDLFALLL-SFLQGGSLIGCSTGSRSE 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 447 AEGEK-WGLVPTHAYAVLDIREFK--GLRFIQLKNPWSHLRWKGRYSENDVKNWTPELQkylnFDPRTAQKIDNGIFWIS 523
Cdd:cd00044 225 EEARTaNGLVKGHAYSVLDVREVQeeGLRLLRLRNPWGVGEWWGGWSDDSSEWWVIDAE----RKKLLLSGKDDGEFWMS 300
|
330
....*....|....*
gi 1774222183 524 WDDLCQYYDVIYLSW 538
Cdd:cd00044 301 FEDFLRNFDGLYVCN 315
|
|
| CysPc |
smart00230 |
Calpain-like thiol protease family; Calpain-like thiol protease family (peptidase family C2). ... |
223-545 |
2.07e-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: 2.07e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 223 YVPFMNVDLRERFAYPMP-FCDRWGKLPLSPKQKTtFSKWVRPEDLTNNPTMIY-TVSSFSIKQTIVSDCSFVASLAISA 300
Cdd:smart00230 1 YEALRQYCKESGTLFEDPlFPANNGSLFFSQRQRK-FVVWKRPHEIFENPPFIVgGASRTDICQGVLGDCWLLAALASLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 301 AYErrfnkKLITgIIYPQNKDGEPeyNPCGKYMVKLHLNGVPRKVIIDDQLPVDhKGELLCSYSNNKSELWVSLIEKAYM 380
Cdd:smart00230 80 LRE-----KLLD-RVIPHDQEFSE--NYAGIFHFRFWRFGKWVDVVIDDRLPTY-NGELVFMHSNSRNEFWSALLEKAYA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 381 KVMGGYDFPGSNSNID-LHALTGWIPERIAMHSDSQTfsKDNSFRMLYQRFHKGdVLITASTGMMTEAEGE---KWGLVP 456
Cdd:smart00230 151 KLNGCYEALKGGSTTEaLEDLTGGVAESIDLKEASKD--PDNLFEDLFKAFERG-SLMGCSIGAGTAVEEEeqkDCGLVK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 457 THAYAVLDIRE--FKGLRFIQLKNPWSHLRWKGRYSEnDVKNWT---PELQKYLNFDPRtaqkiDNGIFWISWDDLCQYY 531
Cdd:smart00230 228 GHAYSVTDVREvqGRRQELLRLRNPWGQVEWNGPWSD-DSPEWRsvsASEKKNLGLTFD-----DDGEFWMSFEDFLRHF 301
|
330
....*....|....*
gi 1774222183 532 -DVIYLSWNPGLFKE 545
Cdd:smart00230 302 dKVEICNLNPDSLEE 316
|
|
| Peptidase_C2 |
pfam00648 |
Calpain family cysteine protease; |
249-532 |
3.98e-48 |
|
Calpain family cysteine protease;
Pssm-ID: 459889 [Multi-domain] Cd Length: 295 Bit Score: 171.53 E-value: 3.98e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 249 PLSPKQKTTFsKWVRPEDLTNNPTMI-YTVSSFSIKQTIVSDCSFVASLAISAAYERRFNKklitgIIYPqnkDGEPEYN 327
Cdd:pfam00648 16 PPSPPPPRGV-EWKRPKEICSNPQFIvDGASRFDICQGELGDCWLLAAIASLTLNPKLLER-----VVPP---DQSFEEN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 328 PCGKYMVKLHLNGVPRKVIIDDQLPVdHKGELLCSYSNNKSELWVSLIEKAYMKVMGGY-DFPGSNSNIDLHALTGWIPE 406
Cdd:pfam00648 87 YAGIFHFRFWRFGEWVDVVIDDRLPT-RNGKLLFVHSRDKNEFWSALLEKAYAKLHGSYeALKGGSTSEALEDFTGGVAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 407 RIAMHSdsqtfSKDNSFRMLyQRFHKGDVLITASTGMMTEAEGEKW---GLVPTHAYAVLDIRE----FKGLRFIQLKNP 479
Cdd:pfam00648 166 SYDLKE-----PPPNLFEIL-LKALERGSLMGCSIDATSAAEEEARtpnGLVKGHAYSVTGVRKvnlkGGKVRLIRLRNP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1774222183 480 WSHLRWKGRYSENDvKNW---TPELQKYLNFdprtaQKIDNGIFWISWDDLCQYYD 532
Cdd:pfam00648 240 WGEVEWNGAWSDGS-PEWqtvSPEEKEELGL-----TKKDDGEFWMSFEDFLKYFT 289
|
|
| MIT_calpain7_2 |
cd02680 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
85-159 |
1.47e-45 |
|
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: 156.70 E-value: 1.47e-45
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774222183 85 LDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEALSEPLTKPVG 159
Cdd:cd02680 1 LDLERAHFLVTQAFDEDEKGNAEEAIELYTEAVELCINTSNETMDQALQTKLKQLARQALDRAEALKESMSKASS 75
|
|
| calpain_III |
smart00720 |
calpain_III domain; |
593-716 |
6.93e-38 |
|
calpain_III domain;
Pssm-ID: 214786 Cd Length: 143 Bit Score: 137.88 E-value: 6.93e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 593 TLSKRINGKWS-GQSAGGCGNFQETHKNNPIYQFHIEKTGP----LLIEL----------RGPRQYSVGFEVVTV----S 653
Cdd:smart00720 1 WHTKSVQGSWTrGQTAGGCRNYPATFWTNPQFRITLEEPDDddctVLIALmqknrrrlrrKGADFLTIGFAVYKVpkelH 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774222183 654 TLGDPGPHGFLRKSSGDYRCGFCYLELENIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKIT 716
Cdd:smart00720 81 LRRDFFLSNAPRASSGDYINGREVSERFRLPPGEYVIVPSTFEPNQEGDFLLRVFSEGPFKLT 143
|
|
| MIT_calpain7_1 |
cd02681 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
5-76 |
1.49e-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: 1.49e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774222183 5 ALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYAEMAG----SSLENIQEKITEYLERVQALHSAVQSKSA 76
Cdd:cd02681 1 ALERDAVQFARLAVQRDQEGRYSEAVFYYKEAAQLLIYAEMAGtlndSHLKTIQEKSNEYLDRAQALHQLVQGQQG 76
|
|
| Calpain_III |
cd00214 |
Calpain, subdomain III. Calpains are calcium-activated cytoplasmic cysteine proteinases, ... |
591-718 |
1.87e-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: 131.27 E-value: 1.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 591 PYTLSKRINGKWS-GQSAGGCGNFQETHKNNPIYQFHIEKTG------PLLIELR----------GPRQYSVGFEVVTVS 653
Cdd:cd00214 1 RKWHTKSFNGEWRrGQTAGGCRNNPDTFWTNPQFRIRVPEPDddegkcTVLIALMqknrrhlrkkGLDLLTIGFHVYKVP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774222183 654 T-LGDPGPHGFLRK-----SSGDYRCGFCYLELEnIPSGIFNIIPSTFLPKQEGPFFLDFNSIIPIKITQL 718
Cdd:cd00214 81 GeNRHLRRDFFLHKaprarSSTFINTREVSLRFR-LPPGEYVIVPSTFEPGEEGEFLLRVFSEKSIKSSEL 150
|
|
| MIT |
cd02656 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ... |
86-157 |
2.40e-19 |
|
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: 82.74 E-value: 2.40e-19
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774222183 86 DLERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEALSEPLTKP 157
Cdd:cd02656 2 LLQQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEPKLRKLLRKKVKEYLDRAEFLKELLKKQ 73
|
|
| MIT |
smart00745 |
Microtubule Interacting and Trafficking molecule domain; |
87-155 |
1.71e-16 |
|
Microtubule Interacting and Trafficking molecule domain;
Pssm-ID: 197854 Cd Length: 77 Bit Score: 74.65 E-value: 1.71e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1774222183 87 LERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEALSEPLT 155
Cdd:smart00745 5 LSKAKELISKALKADEAGNYEEALELYKKAIEYLLEGIKVESDSKRREALKAKAAEYLDRAEEIKKSLL 73
|
|
| MIT |
pfam04212 |
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ... |
87-152 |
5.97e-15 |
|
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: 69.88 E-value: 5.97e-15
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774222183 87 LERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEALSE 152
Cdd:pfam04212 1 LSKALELVKKAVEEDNAGNYEEALELYKEALDYLLLALKETKNEERRELLRAKIAEYLERAEELKE 66
|
|
| MIT |
cd02656 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. The MIT domain ... |
5-76 |
1.09e-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: 1.09e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774222183 5 ALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYAEMAGSS---LENIQEKITEYLERVQALHSAVQSKSA 76
Cdd:cd02656 1 ELLQQAKELIKQAVKEDEDGNYEEALELYKEALDYLLQALKAEKEpklRKLLRKKVKEYLDRAEFLKELLKKQKQ 75
|
|
| MIT |
pfam04212 |
MIT (microtubule interacting and transport) domain; The MIT domain forms an asymmetric ... |
10-69 |
5.69e-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: 55.62 E-value: 5.69e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774222183 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. ... |
599-705 |
3.96e-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: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 599 NGKW-SGQSAGGCGNFQETHKNNPIYQFHIEKTGP--------LLIEL----------RGPRQYSVGFEV--VTVSTLGD 657
Cdd:pfam01067 2 EGRWvRGSTAGGCRNYPDTFWTNPQYRFTLTEPDDdddegectVLVSLmqknrrkqrrLGENLLTIGFAIykVPVELNRK 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1774222183 658 PGPHGFLRKS----SGDY---RCGFCYLELeniPSGIFNIIPSTFLPKQEGPFFL 705
Cdd:pfam01067 82 LRKHFFLTNQpvarSSTYinsREVSLRFRL---PPGEYVIVPSTFEPNEEGEFLL 133
|
|
| MIT_VPS4 |
cd02678 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
87-156 |
2.42e-07 |
|
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: 48.42 E-value: 2.42e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774222183 87 LERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKT-SYETadkvlQNKLKQLAR----QALDRAEALSEPLTK 156
Cdd:cd02678 3 LQKAIELVKKAIEEDNAGNYEEALRLYQHALEYFMHAlKYEK-----NPKSKESIRakctEYLDRAEKLKEYLAK 72
|
|
| MIT |
smart00745 |
Microtubule Interacting and Trafficking molecule domain; |
4-74 |
4.75e-06 |
|
Microtubule Interacting and Trafficking molecule domain;
Pssm-ID: 197854 Cd Length: 77 Bit Score: 44.99 E-value: 4.75e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774222183 4 TALERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQAL---IYAEMAGSSLENIQEKITEYLERVQALHSAVQSK 74
Cdd:smart00745 2 RDYLSKAKELISKALKADEAGNYEEALELYKKAIEYLlegIKVESDSKRREALKAKAAEYLDRAEEIKKSLLER 75
|
|
| MIT_VPS4 |
cd02678 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
10-76 |
7.89e-06 |
|
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: 7.89e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 10 AVQFARLAVQRDHEGRYSEAVFYYKEAAQALIYA---EMAGSSLENIQEKITEYLERVQALHSAVQSKSA 76
Cdd:cd02678 6 AIELVKKAIEEDNAGNYEEALRLYQHALEYFMHAlkyEKNPKSKESIRAKCTEYLDRAEKLKEYLAKKEK 75
|
|
| LapB |
COG2956 |
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ... |
5-150 |
1.07e-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: 44.72 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774222183 5 ALERDAVQF-ARLAVQRDH--EGRYSEAVFYYKEAAQALIYAEMAGSSLENIQEKITEYLERVQALHSAVQsksadplks 81
Cdd:COG2956 68 LLERDPDRAeALLELAQDYlkAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLK--------- 138
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1774222183 82 khqLDLERAHFLVTQAFDEDEKENVEDAIELYTEAVDL---CLKTSYETADKVLQNKLKQLARQALDRAEAL 150
Cdd:COG2956 139 ---LGPENAHAYCELAELYLEQGDYDEAIEALEKALKLdpdCARALLLLAELYLEQGDYEEAIAALERALEQ 207
|
|
| MIT_AAA_Arch |
cd02682 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
6-76 |
2.24e-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: 2.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774222183 6 LERDAVQFARLAVQRDHEGRYSEAVFYYKEAAQAL---IYAEMAGSSLENIQEKITEYLERVQALHSAVQSKSA 76
Cdd:cd02682 2 LEEMARKYAINAVKAEKEGNAEDAITNYKKAIEVLsqiVKNYPDSPTRLIYEQMINEYKRRIEVLEKQNPASSA 75
|
|
| MIT_2 |
cd02684 |
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This ... |
87-150 |
1.33e-03 |
|
MIT: domain contained within Microtubule Interacting and Trafficking molecules. This sub-family of MIT domains is found in proteins with an n-terminal serine/threonine kinase domain. The molecular function of the MIT domain is unclear.
Pssm-ID: 239147 Cd Length: 75 Bit Score: 37.88 E-value: 1.33e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774222183 87 LERAHFLVTQAFDEDEKENVEDAIELYTEAVDLCLKTSYETADKVLQNKLKQLARQALDRAEAL 150
Cdd:cd02684 3 LEKAIALVVQAVKKDQRGDAAAALSLYCSALQYFVPALHYETDAQRKEALRQKVLQYVSRAEEL 66
|
|
| |
