|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
25-275 |
3.62e-94 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
:
Pssm-ID: 214532 Cd Length: 238 Bit Score: 305.05 E-value: 3.62e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 25 QQRGLFPAILNLATNAHISANATCGEKGPEMFCKLVehvpGRPVRHAQCRVCDgnSTNPRERHPITHAIDGTN----NWW 100
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLV----GHTEQGKKCDYCD--ARNPRRSHPAENLTDGNNpnnpTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 101 QSPSIQNGReyHWVTVTLDLRQVFQVAYVIIKAAnAPRPGNWILERSVDGVKFRPWQYYAvsdTECLTRYKITPRRGPPT 180
Cdd:smart00136 77 QSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 181 YrADNEVICTSYYSKLVPLEHGEIHTSLINGRPSADDP--SPQLLEFTSARYIRLRLQRIRTLNADLMtlshrdlrDLDP 258
Cdd:smart00136 151 G-NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 312147379 259 IVTRRYYYSIKDISVGG 275
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_I super family |
cl26988 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1582-1825 |
2.90e-85 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
The actual alignment was detected with superfamily member pfam06008:
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 280.45 E-value: 2.90e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1582 VLSLN-LAGVSLAPYGTLENLENTTKYFQGYLLEENAKKVQAEI---QLGGIEEQTENLQKELARVLRSHQQVNTAMERT 1657
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEIlekELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1658 SNRSQALATFLEQLHRNIKEITEKVATLNQttgEDFQPPVSALQSLHQNISSLLALIKKRNFTEMRQNATLELKAAKDLL 1737
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1738 SRIQKRFQKPQEKLKALKEA-SSLLSNHIADLQAAEELLREAGSKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKL 1816
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANAlRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
....*....
gi 312147379 1817 IAQGREWVD 1825
Cdd:pfam06008 238 LKTARDSLD 246
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2018-2152 |
3.77e-53 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
:
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 183.46 E-value: 3.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2018 VKELAVAANETAARTLEDMLGLSLRVFNTSEDLSRVNATVQETKDLLHNSTMTTILAGRKMRDMEMQANLLFDRLKPLKM 2097
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 2098 LEEN---LSRNLSEIKLLISRARKQAASIKVAVSADRDCIRAYQPQISSTNYNTLLLN 2152
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1225-1367 |
8.44e-49 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 170.91 E-value: 8.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1225 YWRLPKQFQGDQLLAYGGKLQYTVAFYSTLGTGTSNYEPQVLIKGGRTRKHIIYMDAPAPENGVRQDYEVGMKEEFWKYf 1304
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312147379 1305 nsVSEKHVTHSDFMSVLSNIEYILIKASYGQGLQQSRIANISMEVGRkavePAPEGKVALQLE 1367
Cdd:pfam00052 80 --SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAV----PGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
572-702 |
8.02e-46 |
|
Laminin B domain;
:
Pssm-ID: 214597 Cd Length: 127 Bit Score: 162.05 E-value: 8.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 572 SPYYWAAPEAYLGNKLTAFGGFLKYTVSYDIPvetVDSNLMSHADVIIKGNGLTISTRAEGlSLQPYEEYFNVVRLVPEN 651
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGR---RGGTHVSAPDVILEGNGLRISHPAEG-PPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 652 FRDFNtRREIDRDQLMTVLANVTHLLIRANYnSAKMALYRLDSVSLDIASP 702
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATY-SQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2751-2880 |
8.00e-43 |
|
Laminin G domain;
:
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 153.63 E-value: 8.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2751 IRTFASSGLIYYVAHQNQMDYAVLQLHEGRLNFMFDLGKGRTKVSHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSVT 2830
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 2831 -VVGNATTLDVERKLYLGGLPAHYRARSIGTITHSIPACIGDVTVNSQQLD 2880
Cdd:pfam00054 81 sPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2314-2470 |
4.34e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
:
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 137.93 E-value: 4.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2314 SFHFDGSGYAVVE-KALRPTVTQIIILFSTFSPNGLLFYLASNGTKDFLSIELLRGRVKVMVDLGSGPLTLMTDRRYNNG 2392
Cdd:cd00110 1 GVSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 2393 TWYKIAFQRNRKQGLLAVfdaydtsDKEtKQGETPGAASDLNRLEKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2470
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV-------DGE-RVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2900-3053 |
4.60e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
:
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 137.93 E-value: 4.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2900 GTFFEGSGYAALVKEGYKvRLDLNITLEFRTSSKNGVLLGISSA-KVDAIGLEIVDGKVSFHVNNGAGRITATYKPRatr 2978
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 2979 tLCDGKWHTLHAHKSRHRIVLTVDGDAVRAESPHTHSTSADTNDPIYVGGYPAHVKQNCLSSRASFRGCVRNLEL 3053
Cdd:cd00110 77 -LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2495-2659 |
6.49e-30 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
:
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 117.52 E-value: 6.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2495 SVSFLKGGYMEMPPKSL-SPESSLLATFATKNSSGVILAAlgkdaekagASQAHVPFFSILLIEGRIEVHINSGDGTslr 2573
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYA---------GSQNGGDFLALELEDGRLVLRYDLGSGS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2574 kALLHAPTgSYSDGQEHSISVVRNRRVITVQLDENSPVEMKLGPLTEGRTINiSNLYIGGLPEGKGTPMIRMRTSFHGCI 2653
Cdd:cd00110 69 -LVLSSKT-PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLD-GPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 312147379 2654 KNVVID 2659
Cdd:cd00110 146 RDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2136-2285 |
1.10e-27 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
:
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 110.97 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2136 AYQPQISSTNYNTLLLNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKAAFLWDLGSGSTRLEfPDVSINNDKWHSIYITR 2215
Cdd:cd00110 11 RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQWHSVSVER 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2216 FGNMGSLSVKeasaaEDPPVRTSKSPGLAnvlDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLN 2285
Cdd:cd00110 90 NGRSVTLSVD-----GERVVESGSPGGSA---LLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
909-955 |
1.56e-15 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 72.77 E-value: 1.56e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 909 CNCHENGSLSGICHLETGLCDCKPYVTGQQCDQCLPGYYGLDTGLGC 955
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
404-463 |
1.22e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.68 E-value: 1.22e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 404 CDCDPVGSLSSVCIKddlhadlangkWPGQCPCRKGYAGDKCDRCQFGYRGFPNCVPCDC 463
Cdd:pfam00053 1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1051-1099 |
3.29e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.14 E-value: 3.29e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 1051 CNCSVVGSTSPQCDVLSGQCSCKEGFGGQSCHQCSLGYRSFPDCVPCDC 1099
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1516-1553 |
3.70e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.14 E-value: 3.70e-12
10 20 30
....*....|....*....|....*....|....*...
gi 312147379 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEECLPRH 1553
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1410-1456 |
3.03e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.03e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 1410 CNCNNH---SDVCDPETGKCLnCRDHTAGDHCELCTAGYYGKVIGLPGDC 1456
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1097-1154 |
5.13e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 5.13e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 1097 CDCDLRGTLADTCDLEQGlcsctedsgTCSCKENVLGPQCDKCRAGTFALRADNPLGC 1154
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG---------QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
461-507 |
1.04e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.04e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 461 CDCSTVGSVNE--DPCTEPCLCKKNVEGENCDRCKPGFYNLKERNPEGC 507
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
958-1005 |
1.83e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 1.83e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 958 CNCSGEGSISDNCTEE-GQCHCVPGVSGKQCDQCSHGFYAFQNGGCTPC 1005
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
748-796 |
3.47e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 3.47e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 312147379 748 PCECHGHSS---ECD-IHGICSgCTHNTTGDHCEQCLPGFYGTPSRgtPGDCQ 796
Cdd:cd00055 1 PCDCNGHGSlsgQCDpGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
855-907 |
1.46e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.82 E-value: 1.46e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 312147379 855 PCNCSGNVDplEAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVTAKNCR 907
Cdd:cd00055 1 PCDCNGHGS--LSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1004-1049 |
6.66e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 6.66e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 1004 PCDC---AHTQNNCDPDSGECLCPPHTHGLKCEQCEEAFWGLDPE-QGCQ 1049
Cdd:cd00055 1 PCDCnghGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| Laminin_I super family |
cl26988 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1838-2092 |
1.40e-08 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
The actual alignment was detected with superfamily member pfam06008:
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 58.58 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1838 LTQLEHHRDELLLWASKIRSHVDDlvMQMSKRRARDLvhraEQHASELQSAAEALDRDLENVRNVSLNATSavhvhtNIQ 1917
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQ--IEILEKELSSL----AQETEELQKKATQTLAKAQQVNAESERTLG------HAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1918 TLTEEAESLAADAHKTANKTSLISE--SLAPRGK--AVLQRSSRFVKE--SVSTRKKQQGITLKLDELKNLTSQFQERVD 1991
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLGEndFALPSSDlsRMLAEAQRMLGEirSRDFGTQLQNAEAELKAAQDLLSRIQTWFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1992 NITRQANDSLTVLRESpggMREKSRKVKELAVAANETAARTlEDMLGLSLRVFNTSEDLSRVNATVQETKDLLHNstmtT 2071
Cdd:pfam06008 166 SPQEENKALANALRDS---LAEYEAKLSDLRELLREAAAKT-RDANRLNLANQANLREFQRKKEEVSEQKNQLEE----T 237
|
250 260
....*....|....*....|.
gi 312147379 2072 ILAGrkmRDMEMQANLLFDRL 2092
Cdd:pfam06008 238 LKTA---RDSLDAANLLLQEI 255
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
277-324 |
4.96e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 4.96e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 277 CICSGHAS---SCpwdeEAKQLQCQCEHNTCGESCDRCCPGFHQQPWRPGT 324
Cdd:cd00055 2 CDCNGHGSlsgQC----DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
798-853 |
1.07e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.43 E-value: 1.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 312147379 798 CACPLSIDSnnfSPTChltDREEVVCdQCAPGYSGAWCERCADGYYGNPTVPGGTC 853
Cdd:pfam00053 1 CDCNPHGSL---SDTC---DPETGQC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1459-1513 |
1.93e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.96 E-value: 1.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 1459 CTCPHHPpfSFSPTCVLEGdsgFWCDaCLPGYEGQYCERCSAGYHGNPRAAGGSC 1513
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
715-739 |
5.78e-03 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 5.78e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
25-275 |
3.62e-94 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 305.05 E-value: 3.62e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 25 QQRGLFPAILNLATNAHISANATCGEKGPEMFCKLVehvpGRPVRHAQCRVCDgnSTNPRERHPITHAIDGTN----NWW 100
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLV----GHTEQGKKCDYCD--ARNPRRSHPAENLTDGNNpnnpTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 101 QSPSIQNGReyHWVTVTLDLRQVFQVAYVIIKAAnAPRPGNWILERSVDGVKFRPWQYYAvsdTECLTRYKITPRRGPPT 180
Cdd:smart00136 77 QSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 181 YrADNEVICTSYYSKLVPLEHGEIHTSLINGRPSADDP--SPQLLEFTSARYIRLRLQRIRTLNADLMtlshrdlrDLDP 258
Cdd:smart00136 151 G-NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 312147379 259 IVTRRYYYSIKDISVGG 275
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1582-1825 |
2.90e-85 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 280.45 E-value: 2.90e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1582 VLSLN-LAGVSLAPYGTLENLENTTKYFQGYLLEENAKKVQAEI---QLGGIEEQTENLQKELARVLRSHQQVNTAMERT 1657
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEIlekELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1658 SNRSQALATFLEQLHRNIKEITEKVATLNQttgEDFQPPVSALQSLHQNISSLLALIKKRNFTEMRQNATLELKAAKDLL 1737
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1738 SRIQKRFQKPQEKLKALKEA-SSLLSNHIADLQAAEELLREAGSKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKL 1816
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANAlRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
....*....
gi 312147379 1817 IAQGREWVD 1825
Cdd:pfam06008 238 LKTARDSLD 246
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
29-275 |
3.51e-85 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 279.08 E-value: 3.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 29 LFPAILNLATNAHISANATCGEKGPEMFCKLVEHVPGRpvrhaQCRVCDgnSTNPRERHPITHAIDGTNN----WWQSPS 104
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNGtnetWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 105 IQngREYHWVTVTLDLRQVFQVAYVIIKAAnAPRPGNWILERSVD-GVKFRPWQYYAvsdTECLTRYKITPRrgPPTYRA 183
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPSG--PSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 184 DNEVICTSYYSKLVPLEHGEIHTSLINGRPSA--DDPSPQLLEFTSARYIRLRLQRIRTLNADLMTlshrdlrdlDPIVT 261
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLGDELLD---------DPSVL 216
|
250
....*....|....
gi 312147379 262 RRYYYSIKDISVGG 275
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2018-2152 |
3.77e-53 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 183.46 E-value: 3.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2018 VKELAVAANETAARTLEDMLGLSLRVFNTSEDLSRVNATVQETKDLLHNSTMTTILAGRKMRDMEMQANLLFDRLKPLKM 2097
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 2098 LEEN---LSRNLSEIKLLISRARKQAASIKVAVSADRDCIRAYQPQISSTNYNTLLLN 2152
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1225-1367 |
8.44e-49 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 170.91 E-value: 8.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1225 YWRLPKQFQGDQLLAYGGKLQYTVAFYSTLGTGTSNYEPQVLIKGGRTRKHIIYMDAPAPENGVRQDYEVGMKEEFWKYf 1304
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312147379 1305 nsVSEKHVTHSDFMSVLSNIEYILIKASYGQGLQQSRIANISMEVGRkavePAPEGKVALQLE 1367
Cdd:pfam00052 80 --SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAV----PGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
572-702 |
8.02e-46 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 162.05 E-value: 8.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 572 SPYYWAAPEAYLGNKLTAFGGFLKYTVSYDIPvetVDSNLMSHADVIIKGNGLTISTRAEGlSLQPYEEYFNVVRLVPEN 651
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGR---RGGTHVSAPDVILEGNGLRISHPAEG-PPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 652 FRDFNtRREIDRDQLMTVLANVTHLLIRANYnSAKMALYRLDSVSLDIASP 702
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATY-SQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
575-714 |
1.69e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 158.59 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 575 YWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETvdSNLMSHADVIIKGNGLTISTRAEG-LSLQPYEEYFNVVRLVPENFR 653
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG--GSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312147379 654 DfNTRREIDRDQLMTVLANVTHLLIRANYNSaKMALYRLDSVSLDIASPNAIDLvVAADVE 714
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYST-GSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2751-2880 |
8.00e-43 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 153.63 E-value: 8.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2751 IRTFASSGLIYYVAHQNQMDYAVLQLHEGRLNFMFDLGKGRTKVSHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSVT 2830
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 2831 -VVGNATTLDVERKLYLGGLPAHYRARSIGTITHSIPACIGDVTVNSQQLD 2880
Cdd:pfam00054 81 sPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
1221-1351 |
8.07e-39 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 142.01 E-value: 8.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1221 AEPFYWRLPKQFQGDQLLAYGGKLQYTVAFYSTLGtGTSNYEPQVLIKGGRTRKHIIYMDAPAPENGVRQDYEvgMKEEF 1300
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVR--FREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 1301 WKYFNsvsEKHVTHSDFMSVLSNIEYILIKASYGQGLQQSRIANISMEVGR 1351
Cdd:smart00281 79 WQYYG---GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAV 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2314-2470 |
4.34e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 137.93 E-value: 4.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2314 SFHFDGSGYAVVE-KALRPTVTQIIILFSTFSPNGLLFYLASNGTKDFLSIELLRGRVKVMVDLGSGPLTLMTDRRYNNG 2392
Cdd:cd00110 1 GVSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 2393 TWYKIAFQRNRKQGLLAVfdaydtsDKEtKQGETPGAASDLNRLEKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2470
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV-------DGE-RVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2900-3053 |
4.60e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 137.93 E-value: 4.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2900 GTFFEGSGYAALVKEGYKvRLDLNITLEFRTSSKNGVLLGISSA-KVDAIGLEIVDGKVSFHVNNGAGRITATYKPRatr 2978
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 2979 tLCDGKWHTLHAHKSRHRIVLTVDGDAVRAESPHTHSTSADTNDPIYVGGYPAHVKQNCLSSRASFRGCVRNLEL 3053
Cdd:cd00110 77 -LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2724-2875 |
6.06e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 131.77 E-value: 6.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2724 FGLSQNSHLVLPfNQSDVRKRLQVQLNIRTFASSGLIYYVAHQNQMDYAVLQLHEGRLNFMFDLGKGRTKVSHPALLSDG 2803
Cdd:cd00110 2 VSFSGSSYVRLP-TLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312147379 2804 KWHTVKTEYIKRKAFMTVDGQESPSVTVVGNATTLDVERKLYLGGLPAHYRARSIgTITHSIPACIGDVTVN 2875
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2923-3055 |
1.02e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 127.46 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2923 NITLEFRTSSKNGVLLGISSA-KVDAIGLEIVDGKVSFHVNNGAGRITATYKPRatrTLCDGKWHTLHAHKSRHRIVLTV 3001
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKgGGDYLALELRDGRLVLRYDLGSGPARLTSDPT---PLNDGQWHRVAVERNGRSVTLSV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 3002 DG-DAVRAESPHTHsTSADTNDPIYVGGYPAHVKQNCLSSRASFRGCVRNLELSR 3055
Cdd:smart00282 78 DGgNRVSGESPGGL-TILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2746-2877 |
7.24e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 125.14 E-value: 7.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2746 QVQLNIRTFASSGLIYYVAHQNQMDYAVLQLHEGRLNFMFDLGKGRTKVSHPAL-LSDGKWHTVKTEYIKRKAFMTVDGQ 2824
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 312147379 2825 ESPSVTVVGNATTLDVERKLYLGGLPAHYRaRSIGTITHSIPACIGDVTVNSQ 2877
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDLK-LPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2335-2472 |
1.51e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 124.37 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2335 QIIILFSTFSPNGLLFYLASNGTKDFLSIELLRGRVKVMVDLGSGPLTLM-TDRRYNNGTWYKIAFQRNRKQGLLAVfda 2413
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTsDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2414 ydtsDKETKQ-GETPGAASDLNRleKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEISR 2472
Cdd:smart00282 78 ----DGGNRVsGESPGGLTILNL--DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2495-2659 |
6.49e-30 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 117.52 E-value: 6.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2495 SVSFLKGGYMEMPPKSL-SPESSLLATFATKNSSGVILAAlgkdaekagASQAHVPFFSILLIEGRIEVHINSGDGTslr 2573
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYA---------GSQNGGDFLALELEDGRLVLRYDLGSGS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2574 kALLHAPTgSYSDGQEHSISVVRNRRVITVQLDENSPVEMKLGPLTEGRTINiSNLYIGGLPEGKGTPMIRMRTSFHGCI 2653
Cdd:cd00110 69 -LVLSSKT-PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLD-GPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 312147379 2654 KNVVID 2659
Cdd:cd00110 146 RDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2928-3053 |
6.62e-30 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 116.37 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2928 FRTSSKNGVLLGISSAKVDAIGLEIVDGKVSFHVNNGAGRITATYKpraTRTLCDGKWHTLHAHKSRHRIVLTVDGDAVR 3007
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSS---GKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 312147379 3008 AESPHTHSTSADTNDPIYVGGYPAHVKQNCLSSRASFRGCVRNLEL 3053
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2340-2472 |
5.03e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 114.34 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2340 FSTFSPNGLLFYLASNGTKDFLSIELLRGRVKVMVDLGSGPLTLMTDRRYNNGTWYKIAFQRNRKQGLLAVfdaydtSDK 2419
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSV------DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 2420 ETKQGETP-GAASDLNrlEKDLIYVGGLPHSKAVRK-GVSSRSYVGCIKNLEISR 2472
Cdd:pfam00054 75 ARPTGESPlGATTDLD--VDGPLYVGGLPSLGVKKRrLAISPSFDGCIRDVIVNG 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2136-2285 |
1.10e-27 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 110.97 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2136 AYQPQISSTNYNTLLLNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKAAFLWDLGSGSTRLEfPDVSINNDKWHSIYITR 2215
Cdd:cd00110 11 RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQWHSVSVER 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2216 FGNMGSLSVKeasaaEDPPVRTSKSPGLAnvlDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLN 2285
Cdd:cd00110 90 NGRSVTLSVD-----GERVVESGSPGGSA---LLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2148-2287 |
3.47e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.97 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2148 TLLLNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKAAFLWDLGSGSTRLEFPDVSINNDKWHSIYITRFGNMGSLSVkea 2227
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2228 saaEDPPVRTSKSPGLANVLDINnsTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLNGK 2287
Cdd:smart00282 78 ---DGGNRVSGESPGGLTILNLD--GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2153-2290 |
3.18e-26 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 106.25 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2153 VKTQEPDNLLFYLGSSSSSDFLAVEMRRGKAAFLWDLGSGSTRLEFPDVsINNDKWHSIYITRFGNMGSLSVkeasAAED 2232
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK-LNDGKWHSVELERNGRSGTLSV----DGEA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 312147379 2233 PPVRTSKSPGLAnvlDINNSTLMFVGGLGGQI-KKSPAVKVTHFKGCMGEAFLNGKSIG 2290
Cdd:pfam00054 76 RPTGESPLGATT---DLDVDGPLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2520-2659 |
3.59e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 105.88 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2520 TFATKNSSGVILAALGKDaekagasqaHVPFFSILLIEGRIEVHINSGDGTslrkALLHAPTGSYSDGQEHSISVVRNRR 2599
Cdd:smart00282 5 SFRTTSPNGLLLYAGSKG---------GGDYLALELRDGRLVLRYDLGSGP----ARLTSDPTPLNDGQWHRVAVERNGR 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2600 VITVQLDENSPVEMKLGPLTEGRTINiSNLYIGGLPEGKGTPMIRMRTSFHGCIKNVVID 2659
Cdd:smart00282 72 SVTLSVDGGNRVSGESPGGLTILNLD-GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2521-2664 |
4.13e-26 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 105.86 E-value: 4.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2521 FATKNSSGVILAalgkdaekaGASQAHVPFFSILLIEGRIEVHINSGDGtslrKALLHAPTGsYSDGQEHSISVVRNRRV 2600
Cdd:pfam00054 1 FRTTEPSGLLLY---------NGTQTERDFLALELRDGRLEVSYDLGSG----AAVVRSGDK-LNDGKWHSVELERNGRS 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 2601 ITVQLDENSPV--EMKLGPLTegrTINISN-LYIGGLPE-GKGTPMIRMRTSFHGCIKNVVIDAQLLD 2664
Cdd:pfam00054 67 GTLSVDGEARPtgESPLGATT---DLDVDGpLYVGGLPSlGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
909-955 |
1.56e-15 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 72.77 E-value: 1.56e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 909 CNCHENGSLSGICHLETGLCDCKPYVTGQQCDQCLPGYYGLDTGLGC 955
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
908-956 |
1.84e-14 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 69.69 E-value: 1.84e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 908 ACNCHENGSLSGICHLETGLCDCKPYVTGQQCDQCLPGYYGLDT-GLGCV 956
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
909-955 |
6.72e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.11 E-value: 6.72e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 909 CNCHENGSLSGICHLETGLCDCKPYVTGQQCDQCLPGYYGlDTGLGC 955
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
404-463 |
1.22e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.68 E-value: 1.22e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 404 CDCDPVGSLSSVCIKddlhadlangkWPGQCPCRKGYAGDKCDRCQFGYRGFPNCVPCDC 463
Cdd:pfam00053 1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1051-1099 |
3.29e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.14 E-value: 3.29e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 1051 CNCSVVGSTSPQCDVLSGQCSCKEGFGGQSCHQCSLGYRSFPDCVPCDC 1099
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1516-1553 |
3.70e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.14 E-value: 3.70e-12
10 20 30
....*....|....*....|....*....|....*...
gi 312147379 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEECLPRH 1553
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1516-1553 |
4.99e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.76 E-value: 4.99e-12
10 20 30
....*....|....*....|....*....|....*...
gi 312147379 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEECLPRH 1553
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1598-2129 |
8.23e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1598 LENLENTTKYFQGYLLEENAKKVQAEIQLGGIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKE 1677
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1678 ITEKVATLN------QTTGEDFQppvSALQSLHQNISSLLALIKKRNFTEMRQNATLELKAAKDL----------LSRIQ 1741
Cdd:TIGR02168 391 LELQIASLNneierlEARLERLE---DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELqeelerleeaLEELR 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1742 KRFQKPQEKLKALKEASSLLSNHIADLQAAEELLREAGsktqesslllLLVKANLKDFREKKLHVqeeqNLTSKLIAQGR 1821
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS----------EGVKALLKNQSGLSGIL----GVLSELISVDE 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1822 EW---------------VDAARTHAAAAQDTLTQLEHHRDELL----LWASKIRSHVDDLVMQMS--KRRARDLVHRAEQ 1880
Cdd:TIGR02168 534 GYeaaieaalggrlqavVVENLNAAKKAIAFLKQNELGRVTFLpldsIKGTEIQGNDREILKNIEgfLGVAKDLVKFDPK 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1881 H-------------ASELQSAAEALDRDLENVRNVSLN-----------------ATSAVHVHTNIQTLTEEAESLAADA 1930
Cdd:TIGR02168 614 LrkalsyllggvlvVDDLDNALELAKKLRPGYRIVTLDgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKI 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1931 HKTANKTsliseslaprgKAVLQRSSRFVKESVSTRKKQQGITLKLDELKNLTSQFQERVDNIT---RQANDSLTVLRES 2007
Cdd:TIGR02168 694 AELEKAL-----------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEeriAQLSKELTELEAE 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2008 PGGMREKSRKVKELAVAANETAARTLEDMLGLSLRVFNTSEDLSRVNATVQETKDLLHNSTMTTILAGRKMRDMEMQANL 2087
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 312147379 2088 LFDRLKPLKMLEENLSRNLSEIKLLISRARKQAASIKVAVSA 2129
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1516-1553 |
1.09e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.56 E-value: 1.09e-11
10 20 30
....*....|....*....|....*....|....*...
gi 312147379 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEECLPRH 1553
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1613-2021 |
1.31e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1613 LEENAKKVQAeiqlggIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKEITEKVATLNQTtged 1692
Cdd:TIGR02168 679 IEELEEKIEE------LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1693 fqppvsaLQSLHQNISSLLALIKKRNftEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSnhiADLQAAE 1772
Cdd:TIGR02168 749 -------IAQLSKELTELEAEIEELE--ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1773 ELLREAGSKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREwvdaartHAAAAQDTLTQLEHHRDELLLWA 1852
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE-------LIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1853 SKIRSHVDDLVMQMskRRARDLVHRAEQHASELQSAAEALDRDLENVRnvslnatsaVHVHTNIQTLTEEAESLAADAhk 1932
Cdd:TIGR02168 890 ALLRSELEELSEEL--RELESKRSELRRELEELREKLAQLELRLEGLE---------VRIDNLQERLSEEYSLTLEEA-- 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1933 tanktslisESLAPRGKAVLQRSSRFVKEsvstrkkqqgITLKLDELK--NLTS-----QFQERVDNITRQAND---SLT 2002
Cdd:TIGR02168 957 ---------EALENKIEDDEEEARRRLKR----------LENKIKELGpvNLAAieeyeELKERYDFLTAQKEDlteAKE 1017
|
410
....*....|....*....
gi 312147379 2003 VLRESpggMREKSRKVKEL 2021
Cdd:TIGR02168 1018 TLEEA---IEEIDREARER 1033
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1410-1456 |
3.03e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.03e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 1410 CNCNNH---SDVCDPETGKCLnCRDHTAGDHCELCTAGYYGKVIGLPGDC 1456
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1097-1154 |
5.13e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 5.13e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 1097 CDCDLRGTLADTCDLEQGlcsctedsgTCSCKENVLGPQCDKCRAGTFALRADNPLGC 1154
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG---------QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
461-507 |
1.04e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.04e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 461 CDCSTVGSVNE--DPCTEPCLCKKNVEGENCDRCKPGFYNLKERNPEGC 507
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
958-1005 |
1.83e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 1.83e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 958 CNCSGEGSISDNCTEE-GQCHCVPGVSGKQCDQCSHGFYAFQNGGCTPC 1005
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
958-1002 |
2.42e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.09 E-value: 2.42e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 312147379 958 CNCSGEGSISDNC-TEEGQCHCVPGVSGKQCDQCSHGFYAFQNGGC 1002
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1614-2132 |
3.20e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1614 EENAKKVQAEIQLGGIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKEITEKVATLNQTTGEDF 1693
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1694 QppvsALQSLHQNISSLLAlikkrnftEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAAEE 1773
Cdd:COG1196 344 E----ELEEAEEELEEAEA--------ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1774 LLREAGSKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREwvdaARTHAAAAQDTLTQLEHHRDELLLWAS 1853
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLELLAELLEEAALLEAALAELLEELA 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1854 KIRSHVDDLVMQMSKRRARDLVHRAEQHASELQSAAEALD---RDLENVRNVSLNATSAVHVHtnIQTLTEEAESLAADA 1930
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvliGVEAAYEAALEAALAAALQN--IVVEDDEVAAAAIEY 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1931 HKTANK---TSLISESLAPRGKAVLQRSSRFVKESVStrkkqqGITLKLDELKNLTSQFQERVDNITRQANDSLTVLRES 2007
Cdd:COG1196 566 LKAAKAgraTFLPLDKIRARAALAAALARGAIGAAVD------LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2008 pGGMREKSRKVKELAVAANETAARTLEDMLGLSLRVFNTSEDLSRVNATVQETKDLLHNSTMTTILAGRKMRDMEMQANL 2087
Cdd:COG1196 640 -VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 312147379 2088 LFDRLKPLKMLEENLSRNLSEIKLLISRARKQAASIKVAVSADRD 2132
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
748-796 |
3.47e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 3.47e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 312147379 748 PCECHGHSS---ECD-IHGICSgCTHNTTGDHCEQCLPGFYGTPSRgtPGDCQ 796
Cdd:cd00055 1 PCDCNGHGSlsgQCDpGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
403-456 |
6.18e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 6.18e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 312147379 403 PCDCDPVGSLSSVCIKDDlhadlangkwpGQCPCRKGYAGDKCDRCQFGYRGFP 456
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT-----------GQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1050-1093 |
6.95e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 6.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 312147379 1050 ACNCSVVGSTSPQCDVLSGQCSCKEGFGGQSCHQCSLGYRSFPD 1093
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1409-1447 |
1.14e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.21 E-value: 1.14e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 312147379 1409 PCNCNNHSDV---CDPETGKCLnCRDHTAGDHCELCTAGYYG 1447
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1051-1094 |
1.19e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 1.19e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 312147379 1051 CNCSVVGSTSPQCDVLSGQCSCKEGFGGQSCHQCSLGY--RSFPDC 1094
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
855-907 |
1.46e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.82 E-value: 1.46e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 312147379 855 PCNCSGNVDplEAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVTAKNCR 907
Cdd:cd00055 1 PCDCNGHGS--LSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
957-1003 |
1.81e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.44 E-value: 1.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 957 PCNCSGEGSISDNCTEE-GQCHCVPGVSGKQCDQCSHGFY--AFQNGGCT 1003
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYglPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
856-902 |
2.37e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 2.37e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 856 CNCSGNVDPleAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVT 902
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
460-507 |
6.60e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 6.60e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 460 PCDCSTVGSVNE--DPCTEPCLCKKNVEGENCDRCKPGFYNLKERnPEGC 507
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ-GGGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1004-1049 |
6.66e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 6.66e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 1004 PCDC---AHTQNNCDPDSGECLCPPHTHGLKCEQCEEAFWGLDPE-QGCQ 1049
Cdd:cd00055 1 PCDCnghGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
461-507 |
8.76e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 8.76e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 461 CDCSTVGSVNE--DPCTEPCLCKKNVEGENCDRCKPGFYNlkeRNPEGC 507
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
749-795 |
1.20e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 1.20e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 749 CECHGHSS---ECDIH-GICSgCTHNTTGDHCEQCLPGFYGTPSrGTPGDC 795
Cdd:pfam00053 1 CDCNPHGSlsdTCDPEtGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
404-458 |
1.28e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.28e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 312147379 404 CDCDPVGSLSSVCIKDDlhadlangkwpGQCPCRKGYAGDKCDRCQFGYRG--FPNC 458
Cdd:smart00180 1 CDCDPGGSASGTCDPDT-----------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1838-2092 |
1.40e-08 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 58.58 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1838 LTQLEHHRDELLLWASKIRSHVDDlvMQMSKRRARDLvhraEQHASELQSAAEALDRDLENVRNVSLNATSavhvhtNIQ 1917
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQ--IEILEKELSSL----AQETEELQKKATQTLAKAQQVNAESERTLG------HAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1918 TLTEEAESLAADAHKTANKTSLISE--SLAPRGK--AVLQRSSRFVKE--SVSTRKKQQGITLKLDELKNLTSQFQERVD 1991
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLGEndFALPSSDlsRMLAEAQRMLGEirSRDFGTQLQNAEAELKAAQDLLSRIQTWFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1992 NITRQANDSLTVLRESpggMREKSRKVKELAVAANETAARTlEDMLGLSLRVFNTSEDLSRVNATVQETKDLLHNstmtT 2071
Cdd:pfam06008 166 SPQEENKALANALRDS---LAEYEAKLSDLRELLREAAAKT-RDANRLNLANQANLREFQRKKEEVSEQKNQLEE----T 237
|
250 260
....*....|....*....|.
gi 312147379 2072 ILAGrkmRDMEMQANLLFDRL 2092
Cdd:pfam06008 238 LKTA---RDSLDAANLLLQEI 255
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1096-1154 |
2.14e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 312147379 1096 PCDCDLRGTLADTCDLEqglcsctedSGTCSCKENVLGPQCDKCRAGTFALrADNPLGC 1154
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1005-1048 |
2.24e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.24e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 1005 CDC---AHTQNNCDPDSGECLCPPHTHGLKCEQCEEAFWGlDPEQGC 1048
Cdd:smart00180 1 CDCdpgGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1097-1154 |
3.28e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.28e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 1097 CDCDLRGTLADTCDLeqglcscteDSGTCSCKENVLGPQCDKCRAGTFalrADNPLGC 1154
Cdd:smart00180 1 CDCDPGGSASGTCDP---------DTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1005-1048 |
3.72e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 3.72e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 1005 CDC---AHTQNNCDPDSGECLCPPHTHGLKCEQCEEAFWGL--DPEQGC 1048
Cdd:pfam00053 1 CDCnphGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
277-324 |
4.96e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 4.96e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 277 CICSGHAS---SCpwdeEAKQLQCQCEHNTCGESCDRCCPGFHQQPWRPGT 324
Cdd:cd00055 2 CDCNGHGSlsgQC----DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1410-1456 |
5.63e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 5.63e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 1410 CNCN---NHSDVCDPETGKCLnCRDHTAGDHCELCTAGYYGKViglPGDC 1456
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1612-1825 |
6.05e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.60 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1612 LLEENAKKVQAEIQlgGIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKEITEKVATLNQTtge 1691
Cdd:COG4372 28 ALSEQLRKALFELD--KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1692 dfqppvsaLQSLHQNISSLLALIKKRNfTEmRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAA 1771
Cdd:COG4372 103 --------LESLQEEAEELQEELEELQ-KE-RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312147379 1772 EELLREAGSKTQesslllllVKANLKDFREKKLHVQEEQNLTSKLIAQGREWVD 1825
Cdd:COG4372 173 LQALSEAEAEQA--------LDELLKEANRNAEKEEELAEAEKLIESLPRELAE 218
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
798-853 |
1.07e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.43 E-value: 1.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 312147379 798 CACPLSIDSnnfSPTChltDREEVVCdQCAPGYSGAWCERCADGYYGNPTVPGGTC 853
Cdd:pfam00053 1 CDCNPHGSL---SDTC---DPETGQC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
749-790 |
1.50e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.50e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 312147379 749 CECH--GHSSE-CD-IHGICSgCTHNTTGDHCEQCLPGFYGTPSRG 790
Cdd:smart00180 1 CDCDpgGSASGtCDpDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1459-1513 |
1.93e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.96 E-value: 1.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 1459 CTCPHHPpfSFSPTCVLEGdsgFWCDaCLPGYEGQYCERCSAGYHGNPRAAGGSC 1513
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
855-899 |
2.01e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 2.01e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 312147379 855 PCNCSGNVDPleagHCDSVTGECLkCLWNTDGAHCERCADGFYGD 899
Cdd:smart00180 2 DCDPGGSASG----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
716-914 |
2.25e-05 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 47.30 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 716 CECPQGY---TGTSCEACLPGyyrvdgilfggicqpcechghssecdiHGICSGCTHNTTGdhCEQCLPGFYGTPSRGTP 792
Cdd:cd13416 1 EACPSGQytsSGECCEQCPPG---------------------------EGVARPCGDNQTV--CEPCLDGVTFSDVVSHT 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 793 GDCQPCA-CPLSIdsnnfSPTCHLTDREEVVCdqcapgysgawceRCADGYYgnPTVPGGTCVPCNCsgnvdpleaghCD 871
Cdd:cd13416 52 EPCQPCTrCPGLM-----SMRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCEPCTV-----------CP 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 312147379 872 SVTGECLKCLWNTDgAHCERCADGFYGDAVTAKN-CRACN-CHEN 914
Cdd:cd13416 101 PGQGVVQSCGPNQD-TVCEACPEGTYSDEDSSTDpCLPCTvCEDG 144
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1699-2026 |
2.48e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1699 ALQSLHQNISSLLALIKKRNFTEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAAEELLREA 1778
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1779 GSKTQesslllllvkanlkdfREKKLHVQEEQNLTSKLIAQGREwvdaarthaaaAQDTLTQLEHHRDELLLWASKIRSH 1858
Cdd:COG1196 297 LARLE----------------QDIARLEERRRELEERLEELEEE-----------LAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1859 vddlvmQMSKRRARDLVHRAEQHASELQSAAEALDRDLENVRNVSLNATSAVHVHTN-IQTLTEEAESLAADAHKTANKT 1937
Cdd:COG1196 350 ------EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1938 SLISESLAPRGKAVLQRSSRFVKESVSTRKKQQ---GITLKLDELKNLTSQFQERVDNITRQANDS---LTVLRESPGGM 2011
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEeeeALLELLAELLEEAALLEAALAELLEELAEAaarLLLLLEAEADY 503
|
330
....*....|....*
gi 312147379 2012 REKSRKVKELAVAAN 2026
Cdd:COG1196 504 EGFLEGVKAALLLAG 518
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
797-851 |
2.77e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.88 E-value: 2.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 797 PCACPLSIDSNnfsPTChltDREEVVCdQCAPGYSGAWCERCADGYYGNPTVPGG 851
Cdd:cd00055 1 PCDCNGHGSLS---GQC---DPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1458-1514 |
4.71e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.11 E-value: 4.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 312147379 1458 PCTCPHHPpfSFSPTCVLEgdSGFwCDaCLPGYEGQYCERCSAGYHGNPRAAGGsCQ 1514
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPG--TGQ-CE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1613-2124 |
5.21e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1613 LEENAKKVQaEIQlgGIEEQTENLQKELARVLRSHQQVNTAMERTSNRsqalatfLEQLHRNIKEITEKVATLNQTTG-- 1690
Cdd:PRK03918 278 LEEKVKELK-ELK--EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE-------INGIEERIKELEEKEERLEELKKkl 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1691 EDFQPPVSALQSLHQNISSLLALIK-KRNFTEMRQNATLElKAAKDLLSrIQKRFQKPQEKLKALKEASSLLSNHIADLQ 1769
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKAKKEeLERLKKRLTGLTPE-KLEKELEE-LEKAKEEIEEEISKITARIGELKKEIKELK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1770 AAEELLREAGSK--------TQESSLL-LLLVKANLKDFREKKlhvQEEQNLTSKLIAQGREwvdaaRTHAAAAQDTLTQ 1840
Cdd:PRK03918 426 KAIEELKKAKGKcpvcgrelTEEHRKElLEEYTAELKRIEKEL---KEIEEKERKLRKELRE-----LEKVLKKESELIK 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1841 LEHHRDELLLWASKIRSH-VDDLvmqmsKRRARDLvHRAEQHASELQSAAEALDRDLEnvRNVSLNATSAVhVHTNIQTL 1919
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYnLEEL-----EKKAEEY-EKLKEKLIKLKGEIKSLKKELE--KLEELKKKLAE-LEKKLDEL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1920 TEEAESLaadAHKTANKTSLISESLAPRgkavLQRSSRFVKESVSTRKKQQGITLKLDELKNLTSQFQERVDNITRQAND 1999
Cdd:PRK03918 569 EEELAEL---LKELEELGFESVEELEER----LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2000 sltvlrespggMREKSRKVKELAVAANETAARTLED-MLGLSLRVFNTSEDLSRVNATVQETKDLLHNstmttilagrkm 2078
Cdd:PRK03918 642 -----------LEELRKELEELEKKYSEEEYEELREeYLELSRELAGLRAELEELEKRREEIKKTLEK------------ 698
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 312147379 2079 rdmeMQANLlfDRLKPLKMLEENLSRNLSEIKLLISRARKQAASIK 2124
Cdd:PRK03918 699 ----LKEEL--EEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
798-846 |
1.43e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 1.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 798 CACPLSidsNNFSPTChltDREEVVCdQCAPGYSGAWCERCADGYYGNP 846
Cdd:smart00180 1 CDCDPG---GSASGTC---DPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
277-320 |
1.53e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 1.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 277 CICS--GHAS-SCpwdeEAKQLQCQCEHNTCGESCDRCCPGFHQQPW 320
Cdd:smart00180 1 CDCDpgGSASgTC----DPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1613-1861 |
2.24e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 45.13 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1613 LEENAKKVQAEiQLGGIEEQTENLQKElarvlrsHQQVNTAMERTSNRSQALA----TFLEQLHRNIKEITEKVATLNQt 1688
Cdd:cd00176 16 LSEKEELLSST-DYGDDLESVEALLKK-------HEALEAELAAHEERVEALNelgeQLIEEGHPDAEEIQERLEELNQ- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1689 tgedfqppvsalqsLHQNISSLLALIKKRnftemrqnatleLKAAKDLlsriQKRFQKPQEKLKALKEASSLLSN--HIA 1766
Cdd:cd00176 87 --------------RWEELRELAEERRQR------------LEEALDL----QQFFRDADDLEQWLEEKEAALASedLGK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1767 DLQAAEELLREagsktqesslllllvkanLKDFREKklhVQEEQNLTSKLIAQGRE-WVDAARTHAAAAQDTLTQLEHHR 1845
Cdd:cd00176 137 DLESVEELLKK------------------HKELEEE---LEAHEPRLKSLNELAEElLEEGHPDADEEIEEKLEELNERW 195
|
250
....*....|....*.
gi 312147379 1846 DELLLWASKIRSHVDD 1861
Cdd:cd00176 196 EELLELAEERQKKLEE 211
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1598-1900 |
1.38e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1598 LENLENTTKYFQGYLLEENAKKVQA-EIQLGGIEEQTENLQKELarvlrshqqvntamertsNRSQALATFLEQLHRNIK 1676
Cdd:PRK03918 505 LKELEEKLKKYNLEELEKKAEEYEKlKEKLIKLKGEIKSLKKEL------------------EKLEELKKKLAELEKKLD 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1677 EITEKVATLNQTTGE-DFqppvSALQSLHQNISSLLALIKKrnftemrqnaTLELKAAKDLLSRIQKRFQKPQEKlkaLK 1755
Cdd:PRK03918 567 ELEEELAELLKELEElGF----ESVEELEERLKELEPFYNE----------YLELKDAEKELEREEKELKKLEEE---LD 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1756 EASSLLSNHIADLQAAEELLREAGSKTQEsslllllvkanlKDFREKKLHVQEEQNLTSKLIAQgrewvdaarthaaaaq 1835
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKYSE------------EEYEELREEYLELSRELAGLRAE---------------- 681
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 1836 dtLTQLEHHRDElllwaskIRSHVDDLVMQMSKRrardlvhraEQHASELQSAAEALDRdLENVR 1900
Cdd:PRK03918 682 --LEELEKRREE-------IKKTLEKLKEELEER---------EKAKKELEKLEKALER-VEELR 727
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
277-323 |
1.40e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.87 E-value: 1.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 277 CICSGHASSCPwDEEAKQLQCQCEHNTCGESCDRCCPGFHQQPWRPG 323
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1711-1999 |
1.58e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1711 LALIKKRNFTEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAA-----------EELLREAG 1779
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaneisrlEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1780 SKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREWVDAARTHAAAAQDTLTQLEHHRDELLLWASKIRSHV 1859
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1860 DDLVMQMSK-----RRARDLVHRAEQHASELQSAAEALDRDLENVRnvslnatsAVHVHTNIQTLTEEAESLAADAHKTA 1934
Cdd:TIGR02168 389 AQLELQIASlnneiERLEARLERLEDRRERLQQEIEELLKKLEEAE--------LKELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 1935 NKTSLISESLAPRGKAVLQRSSRFvkESVSTRKKQqgitlkLDELKNLTSQFQERVDNITRQAND 1999
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAEREL--AQLQARLDS------LERLQENLEGFSEGVKALLKNQSG 517
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1459-1506 |
5.51e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 5.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 312147379 1459 CTCphHPPFSFSPTCVLegDSGFwCDaCLPGYEGQYCERCSAGYHGNP 1506
Cdd:smart00180 1 CDC--DPGGSASGTCDP--DTGQ-CE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
715-739 |
5.78e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 5.78e-03
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
715-747 |
9.48e-03 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 36.56 E-value: 9.48e-03
10 20 30
....*....|....*....|....*....|...
gi 312147379 715 HCECPQGYTGTSCEACLPGYYRVDGILFGgiCQ 747
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
25-275 |
3.62e-94 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 305.05 E-value: 3.62e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 25 QQRGLFPAILNLATNAHISANATCGEKGPEMFCKLVehvpGRPVRHAQCRVCDgnSTNPRERHPITHAIDGTN----NWW 100
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLV----GHTEQGKKCDYCD--ARNPRRSHPAENLTDGNNpnnpTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 101 QSPSIQNGReyHWVTVTLDLRQVFQVAYVIIKAAnAPRPGNWILERSVDGVKFRPWQYYAvsdTECLTRYKITPRRGPPT 180
Cdd:smart00136 77 QSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 181 YrADNEVICTSYYSKLVPLEHGEIHTSLINGRPSADDP--SPQLLEFTSARYIRLRLQRIRTLNADLMtlshrdlrDLDP 258
Cdd:smart00136 151 G-NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 312147379 259 IVTRRYYYSIKDISVGG 275
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1582-1825 |
2.90e-85 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 280.45 E-value: 2.90e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1582 VLSLN-LAGVSLAPYGTLENLENTTKYFQGYLLEENAKKVQAEI---QLGGIEEQTENLQKELARVLRSHQQVNTAMERT 1657
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEIlekELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1658 SNRSQALATFLEQLHRNIKEITEKVATLNQttgEDFQPPVSALQSLHQNISSLLALIKKRNFTEMRQNATLELKAAKDLL 1737
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1738 SRIQKRFQKPQEKLKALKEA-SSLLSNHIADLQAAEELLREAGSKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKL 1816
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANAlRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
....*....
gi 312147379 1817 IAQGREWVD 1825
Cdd:pfam06008 238 LKTARDSLD 246
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
29-275 |
3.51e-85 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 279.08 E-value: 3.51e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 29 LFPAILNLATNAHISANATCGEKGPEMFCKLVEHVPGRpvrhaQCRVCDgnSTNPRERHPITHAIDGTNN----WWQSPS 104
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNGtnetWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 105 IQngREYHWVTVTLDLRQVFQVAYVIIKAAnAPRPGNWILERSVD-GVKFRPWQYYAvsdTECLTRYKITPRrgPPTYRA 183
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPSG--PSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 184 DNEVICTSYYSKLVPLEHGEIHTSLINGRPSA--DDPSPQLLEFTSARYIRLRLQRIRTLNADLMTlshrdlrdlDPIVT 261
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLGDELLD---------DPSVL 216
|
250
....*....|....
gi 312147379 262 RRYYYSIKDISVGG 275
Cdd:pfam00055 217 RKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2018-2152 |
3.77e-53 |
|
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 183.46 E-value: 3.77e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2018 VKELAVAANETAARTLEDMLGLSLRVFNTSEDLSRVNATVQETKDLLHNSTMTTILAGRKMRDMEMQANLLFDRLKPLKM 2097
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 2098 LEEN---LSRNLSEIKLLISRARKQAASIKVAVSADRDCIRAYQPQISSTNYNTLLLN 2152
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1225-1367 |
8.44e-49 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 170.91 E-value: 8.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1225 YWRLPKQFQGDQLLAYGGKLQYTVAFYSTLGTGTSNYEPQVLIKGGRTRKHIIYMDAPAPENGVRQDYEVGMKEEFWKYf 1304
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 312147379 1305 nsVSEKHVTHSDFMSVLSNIEYILIKASYGQGLQQSRIANISMEVGRkavePAPEGKVALQLE 1367
Cdd:pfam00052 80 --SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAV----PGGSGPPASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
572-702 |
8.02e-46 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 162.05 E-value: 8.02e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 572 SPYYWAAPEAYLGNKLTAFGGFLKYTVSYDIPvetVDSNLMSHADVIIKGNGLTISTRAEGlSLQPYEEYFNVVRLVPEN 651
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGR---RGGTHVSAPDVILEGNGLRISHPAEG-PPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 652 FRDFNtRREIDRDQLMTVLANVTHLLIRANYnSAKMALYRLDSVSLDIASP 702
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATY-SQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
575-714 |
1.69e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 158.59 E-value: 1.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 575 YWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETvdSNLMSHADVIIKGNGLTISTRAEG-LSLQPYEEYFNVVRLVPENFR 653
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG--GSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312147379 654 DfNTRREIDRDQLMTVLANVTHLLIRANYNSaKMALYRLDSVSLDIASPNAIDLvVAADVE 714
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYST-GSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2751-2880 |
8.00e-43 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 153.63 E-value: 8.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2751 IRTFASSGLIYYVAHQNQMDYAVLQLHEGRLNFMFDLGKGRTKVSHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSVT 2830
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 2831 -VVGNATTLDVERKLYLGGLPAHYRARSIGTITHSIPACIGDVTVNSQQLD 2880
Cdd:pfam00054 81 sPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
1221-1351 |
8.07e-39 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 142.01 E-value: 8.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1221 AEPFYWRLPKQFQGDQLLAYGGKLQYTVAFYSTLGtGTSNYEPQVLIKGGRTRKHIIYMDAPAPENGVRQDYEvgMKEEF 1300
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVR--FREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 1301 WKYFNsvsEKHVTHSDFMSVLSNIEYILIKASYGQGLQQSRIANISMEVGR 1351
Cdd:smart00281 79 WQYYG---GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAV 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2314-2470 |
4.34e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 137.93 E-value: 4.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2314 SFHFDGSGYAVVE-KALRPTVTQIIILFSTFSPNGLLFYLASNGTKDFLSIELLRGRVKVMVDLGSGPLTLMTDRRYNNG 2392
Cdd:cd00110 1 GVSFSGSSYVRLPtLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 2393 TWYKIAFQRNRKQGLLAVfdaydtsDKEtKQGETPGAASDLNRLEKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2470
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV-------DGE-RVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2900-3053 |
4.60e-37 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 137.93 E-value: 4.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2900 GTFFEGSGYAALVKEGYKvRLDLNITLEFRTSSKNGVLLGISSA-KVDAIGLEIVDGKVSFHVNNGAGRITATYKPRatr 2978
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 2979 tLCDGKWHTLHAHKSRHRIVLTVDGDAVRAESPHTHSTSADTNDPIYVGGYPAHVKQNCLSSRASFRGCVRNLEL 3053
Cdd:cd00110 77 -LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2724-2875 |
6.06e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 131.77 E-value: 6.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2724 FGLSQNSHLVLPfNQSDVRKRLQVQLNIRTFASSGLIYYVAHQNQMDYAVLQLHEGRLNFMFDLGKGRTKVSHPALLSDG 2803
Cdd:cd00110 2 VSFSGSSYVRLP-TLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 312147379 2804 KWHTVKTEYIKRKAFMTVDGQESPSVTVVGNATTLDVERKLYLGGLPAHYRARSIgTITHSIPACIGDVTVN 2875
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL-PVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2923-3055 |
1.02e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 127.46 E-value: 1.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2923 NITLEFRTSSKNGVLLGISSA-KVDAIGLEIVDGKVSFHVNNGAGRITATYKPRatrTLCDGKWHTLHAHKSRHRIVLTV 3001
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKgGGDYLALELRDGRLVLRYDLGSGPARLTSDPT---PLNDGQWHRVAVERNGRSVTLSV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 3002 DG-DAVRAESPHTHsTSADTNDPIYVGGYPAHVKQNCLSSRASFRGCVRNLELSR 3055
Cdd:smart00282 78 DGgNRVSGESPGGL-TILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2746-2877 |
7.24e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 125.14 E-value: 7.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2746 QVQLNIRTFASSGLIYYVAHQNQMDYAVLQLHEGRLNFMFDLGKGRTKVSHPAL-LSDGKWHTVKTEYIKRKAFMTVDGQ 2824
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 312147379 2825 ESPSVTVVGNATTLDVERKLYLGGLPAHYRaRSIGTITHSIPACIGDVTVNSQ 2877
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDLK-LPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2335-2472 |
1.51e-32 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 124.37 E-value: 1.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2335 QIIILFSTFSPNGLLFYLASNGTKDFLSIELLRGRVKVMVDLGSGPLTLM-TDRRYNNGTWYKIAFQRNRKQGLLAVfda 2413
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTsDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2414 ydtsDKETKQ-GETPGAASDLNRleKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEISR 2472
Cdd:smart00282 78 ----DGGNRVsGESPGGLTILNL--DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2495-2659 |
6.49e-30 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 117.52 E-value: 6.49e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2495 SVSFLKGGYMEMPPKSL-SPESSLLATFATKNSSGVILAAlgkdaekagASQAHVPFFSILLIEGRIEVHINSGDGTslr 2573
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYA---------GSQNGGDFLALELEDGRLVLRYDLGSGS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2574 kALLHAPTgSYSDGQEHSISVVRNRRVITVQLDENSPVEMKLGPLTEGRTINiSNLYIGGLPEGKGTPMIRMRTSFHGCI 2653
Cdd:cd00110 69 -LVLSSKT-PLNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLD-GPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 312147379 2654 KNVVID 2659
Cdd:cd00110 146 RDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2928-3053 |
6.62e-30 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 116.37 E-value: 6.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2928 FRTSSKNGVLLGISSAKVDAIGLEIVDGKVSFHVNNGAGRITATYKpraTRTLCDGKWHTLHAHKSRHRIVLTVDGDAVR 3007
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSS---GKNLNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 312147379 3008 AESPHTHSTSADTNDPIYVGGYPAHVKQNCLSSRASFRGCVRNLEL 3053
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2928-3058 |
1.87e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 115.49 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2928 FRTSSKNGVLL-GISSAKVDAIGLEIVDGKVSFHVNNGAGRITATYKPRatrtLCDGKWHTLHAHKSRHRIVLTVDG-DA 3005
Cdd:pfam00054 1 FRTTEPSGLLLyNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK----LNDGKWHSVELERNGRSGTLSVDGeAR 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 312147379 3006 VRAESPHTHSTSADTNDPIYVGGYPAHVKQN-CLSSRASFRGCVRNLELSRGSQ 3058
Cdd:pfam00054 77 PTGESPLGATTDLDVDGPLYVGGLPSLGVKKrRLAISPSFDGCIRDVIVNGKPL 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2340-2472 |
5.03e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 114.34 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2340 FSTFSPNGLLFYLASNGTKDFLSIELLRGRVKVMVDLGSGPLTLMTDRRYNNGTWYKIAFQRNRKQGLLAVfdaydtSDK 2419
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSV------DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 2420 ETKQGETP-GAASDLNrlEKDLIYVGGLPHSKAVRK-GVSSRSYVGCIKNLEISR 2472
Cdd:pfam00054 75 ARPTGESPlGATTDLD--VDGPLYVGGLPSLGVKKRrLAISPSFDGCIRDVIVNG 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2136-2285 |
1.10e-27 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 110.97 E-value: 1.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2136 AYQPQISSTNYNTLLLNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKAAFLWDLGSGSTRLEfPDVSINNDKWHSIYITR 2215
Cdd:cd00110 11 RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQWHSVSVER 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2216 FGNMGSLSVKeasaaEDPPVRTSKSPGLAnvlDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLN 2285
Cdd:cd00110 90 NGRSVTLSVD-----GERVVESGSPGGSA---LLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2148-2287 |
3.47e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 108.97 E-value: 3.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2148 TLLLNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKAAFLWDLGSGSTRLEFPDVSINNDKWHSIYITRFGNMGSLSVkea 2227
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2228 saaEDPPVRTSKSPGLANVLDINnsTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLNGK 2287
Cdd:smart00282 78 ---DGGNRVSGESPGGLTILNLD--GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2340-2470 |
3.12e-26 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 105.96 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2340 FSTFSPNGLLFYlASNGTKDFLSIELLRGRVKVMVDLGSGPLTLM-TDRRYNNGTWYKIAFQRNRKQGLLAVfdaydtsD 2418
Cdd:pfam02210 1 FRTRQPNGLLLY-AGGGGSDFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTLSV-------D 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 312147379 2419 KETKQGETPGAASDLNRLEKDLiYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2470
Cdd:pfam02210 73 GQTVVSSLPPGESLLLNLNGPL-YLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2153-2290 |
3.18e-26 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 106.25 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2153 VKTQEPDNLLFYLGSSSSSDFLAVEMRRGKAAFLWDLGSGSTRLEFPDVsINNDKWHSIYITRFGNMGSLSVkeasAAED 2232
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK-LNDGKWHSVELERNGRSGTLSV----DGEA 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 312147379 2233 PPVRTSKSPGLAnvlDINNSTLMFVGGLGGQI-KKSPAVKVTHFKGCMGEAFLNGKSIG 2290
Cdd:pfam00054 76 RPTGESPLGATT---DLDVDGPLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2520-2659 |
3.59e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 105.88 E-value: 3.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2520 TFATKNSSGVILAALGKDaekagasqaHVPFFSILLIEGRIEVHINSGDGTslrkALLHAPTGSYSDGQEHSISVVRNRR 2599
Cdd:smart00282 5 SFRTTSPNGLLLYAGSKG---------GGDYLALELRDGRLVLRYDLGSGP----ARLTSDPTPLNDGQWHRVAVERNGR 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2600 VITVQLDENSPVEMKLGPLTEGRTINiSNLYIGGLPEGKGTPMIRMRTSFHGCIKNVVID 2659
Cdd:smart00282 72 SVTLSVDGGNRVSGESPGGLTILNLD-GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2521-2664 |
4.13e-26 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 105.86 E-value: 4.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2521 FATKNSSGVILAalgkdaekaGASQAHVPFFSILLIEGRIEVHINSGDGtslrKALLHAPTGsYSDGQEHSISVVRNRRV 2600
Cdd:pfam00054 1 FRTTEPSGLLLY---------NGTQTERDFLALELRDGRLEVSYDLGSG----AAVVRSGDK-LNDGKWHSVELERNGRS 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 2601 ITVQLDENSPV--EMKLGPLTegrTINISN-LYIGGLPE-GKGTPMIRMRTSFHGCIKNVVIDAQLLD 2664
Cdd:pfam00054 67 GTLSVDGEARPtgESPLGATT---DLDVDGpLYVGGLPSlGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2521-2661 |
7.02e-22 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 93.64 E-value: 7.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2521 FATKNSSGVILAALGKDAEkagasqahvpFFSILLIEGRIEVHINSGDGTslrkALLHAPTGSYSDGQEHSISVVRNRRV 2600
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSD----------FLALELVNGRLVLRYDLGSGP----ESLLSSGKNLNDGQWHSVRVERNGNT 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 312147379 2601 ITVQLDENSPVEMKLGPLTEGRTINiSNLYIGGLPEGKGTPMIRMRTSFHGCIKNVVIDAQ 2661
Cdd:pfam02210 67 LTLSVDGQTVVSSLPPGESLLLNLN-GPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2751-2877 |
2.48e-21 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 92.10 E-value: 2.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2751 IRTFASSGLIYYVAHQNQmDYAVLQLHEGRLNFMFDLGKGRTKV-SHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSV 2829
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLlSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 312147379 2830 TVVGNATTLDVERKLYLGGLPAHYRARSIGTiTHSIPACIGDVTVNSQ 2877
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPV-RAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2153-2287 |
3.15e-20 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 89.02 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2153 VKTQEPDNLLFYLGSSSSsDFLAVEMRRGKAAFLWDLGSGSTRLEFPDVSINNDKWHSIYITRFGNMGSLSVkeasaaED 2232
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSV------DG 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 2233 PPVRTSKSPGLANVLDINNStlMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLNGK 2287
Cdd:pfam02210 74 QTVVSSLPPGESLLLNLNGP--LYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
909-955 |
1.56e-15 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 72.77 E-value: 1.56e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 909 CNCHENGSLSGICHLETGLCDCKPYVTGQQCDQCLPGYYGLDTGLGC 955
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
908-956 |
1.84e-14 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 69.69 E-value: 1.84e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 908 ACNCHENGSLSGICHLETGLCDCKPYVTGQQCDQCLPGYYGLDT-GLGCV 956
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
909-955 |
6.72e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.11 E-value: 6.72e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 909 CNCHENGSLSGICHLETGLCDCKPYVTGQQCDQCLPGYYGlDTGLGC 955
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1618-2161 |
9.28e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 74.83 E-value: 9.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1618 KKVQAEIQLGGIEEQTENLQKE---LARVLRSHQQV-NTAME---RTSNRSQALATFL--------------EQLHRNIK 1676
Cdd:pfam01576 20 RQQKAESELKELEKKHQQLCEEknaLQEQLQAETELcAEAEEmraRLAARKQELEEILhelesrleeeeersQQLQNEKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1677 EITEKVATLNQTTGEDfqppVSALQSLHQNISSLLALIKK---RNFTEMRQNATL--ELKAAKDLLSRIQKRFQKPQEKL 1751
Cdd:pfam01576 100 KMQQHIQDLEEQLDEE----EAARQKLQLEKVTTEAKIKKleeDILLLEDQNSKLskERKLLEERISEFTSNLAEEEEKA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1752 KALKEASSLLSNHIADLQaaEELLREAGSKtQESSLLLLLVKANLKDFREKklhVQEEQNLTSKLIAQgrewvdaARTHA 1831
Cdd:pfam01576 176 KSLSKLKNKHEAMISDLE--ERLKKEEKGR-QELEKAKRKLEGESTDLQEQ---IAELQAQIAELRAQ-------LAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1832 AAAQDTLTQLEH---HRDELLLWASKIRSHVDDLVMQM-SKRRARDlvhRAEQHASELQSAAEALDRDLENvrnvSLNAT 1907
Cdd:pfam01576 243 EELQAALARLEEetaQKNNALKKIRELEAQISELQEDLeSERAARN---KAEKQRRDLGEELEALKTELED----TLDTT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1908 SA---------VHVHTNIQTLTEEAESLAADAHKTANKTSLISESL------APRGKAVLQRS-----SRFVKESVSTRK 1967
Cdd:pfam01576 316 AAqqelrskreQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELteqleqAKRNKANLEKAkqaleSENAELQAELRT 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1968 KQQGITLKLDELKNLTSQFQE---RVDNITRQANDsltvlrespggMREKSRKVK-ELavaanETAARTLEDMLGLSLRV 2043
Cdd:pfam01576 396 LQQAKQDSEHKRKKLEGQLQElqaRLSESERQRAE-----------LAEKLSKLQsEL-----ESVSSLLNEAEGKNIKL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2044 fntSEDLSRVNATVQETKDLLHNSTMTTILAGRKMRDMEMQANLLFDRLKPLKMLEENLSRNLSEIKLLISRARKQAASI 2123
Cdd:pfam01576 460 ---SKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
|
570 580 590
....*....|....*....|....*....|....*...
gi 312147379 2124 KVAVSADRDCIRAYQPQISSTnynTLLLNVKTQEPDNL 2161
Cdd:pfam01576 537 AGTLEALEEGKKRLQRELEAL---TQQLEEKAAAYDKL 571
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
404-463 |
1.22e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.68 E-value: 1.22e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 404 CDCDPVGSLSSVCIKddlhadlangkWPGQCPCRKGYAGDKCDRCQFGYRGFPNCVPCDC 463
Cdd:pfam00053 1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1051-1099 |
3.29e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.14 E-value: 3.29e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 1051 CNCSVVGSTSPQCDVLSGQCSCKEGFGGQSCHQCSLGYRSFPDCVPCDC 1099
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1516-1553 |
3.70e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 63.14 E-value: 3.70e-12
10 20 30
....*....|....*....|....*....|....*...
gi 312147379 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEECLPRH 1553
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1516-1553 |
4.99e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.76 E-value: 4.99e-12
10 20 30
....*....|....*....|....*....|....*...
gi 312147379 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEECLPRH 1553
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1598-2129 |
8.23e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 8.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1598 LENLENTTKYFQGYLLEENAKKVQAEIQLGGIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKE 1677
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1678 ITEKVATLN------QTTGEDFQppvSALQSLHQNISSLLALIKKRNFTEMRQNATLELKAAKDL----------LSRIQ 1741
Cdd:TIGR02168 391 LELQIASLNneierlEARLERLE---DRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELqeelerleeaLEELR 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1742 KRFQKPQEKLKALKEASSLLSNHIADLQAAEELLREAGsktqesslllLLVKANLKDFREKKLHVqeeqNLTSKLIAQGR 1821
Cdd:TIGR02168 468 EELEEAEQALDAAERELAQLQARLDSLERLQENLEGFS----------EGVKALLKNQSGLSGIL----GVLSELISVDE 533
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1822 EW---------------VDAARTHAAAAQDTLTQLEHHRDELL----LWASKIRSHVDDLVMQMS--KRRARDLVHRAEQ 1880
Cdd:TIGR02168 534 GYeaaieaalggrlqavVVENLNAAKKAIAFLKQNELGRVTFLpldsIKGTEIQGNDREILKNIEgfLGVAKDLVKFDPK 613
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1881 H-------------ASELQSAAEALDRDLENVRNVSLN-----------------ATSAVHVHTNIQTLTEEAESLAADA 1930
Cdd:TIGR02168 614 LrkalsyllggvlvVDDLDNALELAKKLRPGYRIVTLDgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKI 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1931 HKTANKTsliseslaprgKAVLQRSSRFVKESVSTRKKQQGITLKLDELKNLTSQFQERVDNIT---RQANDSLTVLRES 2007
Cdd:TIGR02168 694 AELEKAL-----------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEeriAQLSKELTELEAE 762
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2008 PGGMREKSRKVKELAVAANETAARTLEDMLGLSLRVFNTSEDLSRVNATVQETKDLLHNSTMTTILAGRKMRDMEMQANL 2087
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLED 842
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 312147379 2088 LFDRLKPLKMLEENLSRNLSEIKLLISRARKQAASIKVAVSA 2129
Cdd:TIGR02168 843 LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1516-1553 |
1.09e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.56 E-value: 1.09e-11
10 20 30
....*....|....*....|....*....|....*...
gi 312147379 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEECLPRH 1553
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1613-2021 |
1.31e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 70.86 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1613 LEENAKKVQAeiqlggIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKEITEKVATLNQTtged 1692
Cdd:TIGR02168 679 IEELEEKIEE------LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER---- 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1693 fqppvsaLQSLHQNISSLLALIKKRNftEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSnhiADLQAAE 1772
Cdd:TIGR02168 749 -------IAQLSKELTELEAEIEELE--ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR---AELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1773 ELLREAGSKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREwvdaartHAAAAQDTLTQLEHHRDELLLWA 1852
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEE-------LIEELESELEALLNERASLEEAL 889
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1853 SKIRSHVDDLVMQMskRRARDLVHRAEQHASELQSAAEALDRDLENVRnvslnatsaVHVHTNIQTLTEEAESLAADAhk 1932
Cdd:TIGR02168 890 ALLRSELEELSEEL--RELESKRSELRRELEELREKLAQLELRLEGLE---------VRIDNLQERLSEEYSLTLEEA-- 956
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1933 tanktslisESLAPRGKAVLQRSSRFVKEsvstrkkqqgITLKLDELK--NLTS-----QFQERVDNITRQAND---SLT 2002
Cdd:TIGR02168 957 ---------EALENKIEDDEEEARRRLKR----------LENKIKELGpvNLAAieeyeELKERYDFLTAQKEDlteAKE 1017
|
410
....*....|....*....
gi 312147379 2003 VLRESpggMREKSRKVKEL 2021
Cdd:TIGR02168 1018 TLEEA---IEEIDREARER 1033
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1410-1456 |
3.03e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.44 E-value: 3.03e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 1410 CNCNNH---SDVCDPETGKCLnCRDHTAGDHCELCTAGYYGKVIGLPGDC 1456
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1097-1154 |
5.13e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.06 E-value: 5.13e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 1097 CDCDLRGTLADTCDLEQGlcsctedsgTCSCKENVLGPQCDKCRAGTFALRADNPLGC 1154
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG---------QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
461-507 |
1.04e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.04e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 461 CDCSTVGSVNE--DPCTEPCLCKKNVEGENCDRCKPGFYNLKERNPEGC 507
Cdd:pfam00053 1 CDCNPHGSLSDtcDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
958-1005 |
1.83e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 1.83e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 958 CNCSGEGSISDNCTEE-GQCHCVPGVSGKQCDQCSHGFYAFQNGGCTPC 1005
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
958-1002 |
2.42e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.09 E-value: 2.42e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 312147379 958 CNCSGEGSISDNC-TEEGQCHCVPGVSGKQCDQCSHGFYAFQNGGC 1002
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1614-2132 |
3.20e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 3.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1614 EENAKKVQAEIQLGGIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKEITEKVATLNQTTGEDF 1693
Cdd:COG1196 264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1694 QppvsALQSLHQNISSLLAlikkrnftEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAAEE 1773
Cdd:COG1196 344 E----ELEEAEEELEEAEA--------ELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1774 LLREAGSKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREwvdaARTHAAAAQDTLTQLEHHRDELLLWAS 1853
Cdd:COG1196 412 LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLELLAELLEEAALLEAALAELLEELA 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1854 KIRSHVDDLVMQMSKRRARDLVHRAEQHASELQSAAEALD---RDLENVRNVSLNATSAVHVHtnIQTLTEEAESLAADA 1930
Cdd:COG1196 488 EAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAvliGVEAAYEAALEAALAAALQN--IVVEDDEVAAAAIEY 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1931 HKTANK---TSLISESLAPRGKAVLQRSSRFVKESVStrkkqqGITLKLDELKNLTSQFQERVDNITRQANDSLTVLRES 2007
Cdd:COG1196 566 LKAAKAgraTFLPLDKIRARAALAAALARGAIGAAVD------LVASDLREADARYYVLGDTLLGRTLVAARLEAALRRA 639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2008 pGGMREKSRKVKELAVAANETAARTLEDMLGLSLRVFNTSEDLSRVNATVQETKDLLHNSTMTTILAGRKMRDMEMQANL 2087
Cdd:COG1196 640 -VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLE 718
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 312147379 2088 LFDRLKPLKMLEENLSRNLSEIKLLISRARKQAASIKVAVSADRD 2132
Cdd:COG1196 719 EELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLE 763
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
748-796 |
3.47e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 3.47e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 312147379 748 PCECHGHSS---ECD-IHGICSgCTHNTTGDHCEQCLPGFYGTPSRgtPGDCQ 796
Cdd:cd00055 1 PCDCNGHGSlsgQCDpGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
403-456 |
6.18e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 6.18e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 312147379 403 PCDCDPVGSLSSVCIKDDlhadlangkwpGQCPCRKGYAGDKCDRCQFGYRGFP 456
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT-----------GQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1050-1093 |
6.95e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.59 E-value: 6.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 312147379 1050 ACNCSVVGSTSPQCDVLSGQCSCKEGFGGQSCHQCSLGYRSFPD 1093
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1409-1447 |
1.14e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.21 E-value: 1.14e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 312147379 1409 PCNCNNHSDV---CDPETGKCLnCRDHTAGDHCELCTAGYYG 1447
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYG 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1051-1094 |
1.19e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 55.78 E-value: 1.19e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 312147379 1051 CNCSVVGSTSPQCDVLSGQCSCKEGFGGQSCHQCSLGY--RSFPDC 1094
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
855-907 |
1.46e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.82 E-value: 1.46e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 312147379 855 PCNCSGNVDplEAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVTAKNCR 907
Cdd:cd00055 1 PCDCNGHGS--LSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
957-1003 |
1.81e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.44 E-value: 1.81e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 957 PCNCSGEGSISDNCTEE-GQCHCVPGVSGKQCDQCSHGFY--AFQNGGCT 1003
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYglPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
856-902 |
2.37e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 55.05 E-value: 2.37e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 856 CNCSGNVDPleAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVT 902
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
460-507 |
6.60e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 6.60e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 460 PCDCSTVGSVNE--DPCTEPCLCKKNVEGENCDRCKPGFYNLKERnPEGC 507
Cdd:cd00055 1 PCDCNGHGSLSGqcDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ-GGGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1004-1049 |
6.66e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 6.66e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 1004 PCDC---AHTQNNCDPDSGECLCPPHTHGLKCEQCEEAFWGLDPE-QGCQ 1049
Cdd:cd00055 1 PCDCnghGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
461-507 |
8.76e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 8.76e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 461 CDCSTVGSVNE--DPCTEPCLCKKNVEGENCDRCKPGFYNlkeRNPEGC 507
Cdd:smart00180 1 CDCDPGGSASGtcDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
749-795 |
1.20e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 1.20e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 749 CECHGHSS---ECDIH-GICSgCTHNTTGDHCEQCLPGFYGTPSrGTPGDC 795
Cdd:pfam00053 1 CDCNPHGSlsdTCDPEtGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
404-458 |
1.28e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.28e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 312147379 404 CDCDPVGSLSSVCIKDDlhadlangkwpGQCPCRKGYAGDKCDRCQFGYRG--FPNC 458
Cdd:smart00180 1 CDCDPGGSASGTCDPDT-----------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1838-2092 |
1.40e-08 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 58.58 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1838 LTQLEHHRDELLLWASKIRSHVDDlvMQMSKRRARDLvhraEQHASELQSAAEALDRDLENVRNVSLNATSavhvhtNIQ 1917
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQ--IEILEKELSSL----AQETEELQKKATQTLAKAQQVNAESERTLG------HAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1918 TLTEEAESLAADAHKTANKTSLISE--SLAPRGK--AVLQRSSRFVKE--SVSTRKKQQGITLKLDELKNLTSQFQERVD 1991
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLGEndFALPSSDlsRMLAEAQRMLGEirSRDFGTQLQNAEAELKAAQDLLSRIQTWFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1992 NITRQANDSLTVLRESpggMREKSRKVKELAVAANETAARTlEDMLGLSLRVFNTSEDLSRVNATVQETKDLLHNstmtT 2071
Cdd:pfam06008 166 SPQEENKALANALRDS---LAEYEAKLSDLRELLREAAAKT-RDANRLNLANQANLREFQRKKEEVSEQKNQLEE----T 237
|
250 260
....*....|....*....|.
gi 312147379 2072 ILAGrkmRDMEMQANLLFDRL 2092
Cdd:pfam06008 238 LKTA---RDSLDAANLLLQEI 255
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1096-1154 |
2.14e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.14e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 312147379 1096 PCDCDLRGTLADTCDLEqglcsctedSGTCSCKENVLGPQCDKCRAGTFALrADNPLGC 1154
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGL-PSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1005-1048 |
2.24e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.24e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 1005 CDC---AHTQNNCDPDSGECLCPPHTHGLKCEQCEEAFWGlDPEQGC 1048
Cdd:smart00180 1 CDCdpgGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1097-1154 |
3.28e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.28e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 1097 CDCDLRGTLADTCDLeqglcscteDSGTCSCKENVLGPQCDKCRAGTFalrADNPLGC 1154
Cdd:smart00180 1 CDCDPGGSASGTCDP---------DTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1005-1048 |
3.72e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 51.97 E-value: 3.72e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 1005 CDC---AHTQNNCDPDSGECLCPPHTHGLKCEQCEEAFWGL--DPEQGC 1048
Cdd:pfam00053 1 CDCnphGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
277-324 |
4.96e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 4.96e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 312147379 277 CICSGHAS---SCpwdeEAKQLQCQCEHNTCGESCDRCCPGFHQQPWRPGT 324
Cdd:cd00055 2 CDCNGHGSlsgQC----DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1410-1456 |
5.63e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.16 E-value: 5.63e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 312147379 1410 CNCN---NHSDVCDPETGKCLnCRDHTAGDHCELCTAGYYGKViglPGDC 1456
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1602-2023 |
5.85e-08 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 58.58 E-value: 5.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1602 ENTTKYFQgYLLEENAKKVQaeiQLggiEEQT----ENLQKELAR---VLRSHQQVNTAMERTSNRSQALATFLEQLHRN 1674
Cdd:pfam05483 253 ENKMKDLT-FLLEESRDKAN---QL---EEKTklqdENLKELIEKkdhLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1675 IKEITEKVAT----LNQT-TGEDFQppVSALQSLHQNISSLLALIKKR--NFTEMRQNATLELKAAKDLLSRIQKRFQKP 1747
Cdd:pfam05483 326 ICQLTEEKEAqmeeLNKAkAAHSFV--VTEFEATTCSLEELLRTEQQRleKNEDQLKIITMELQKKSSELEEMTKFKNNK 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1748 QEKLKALK----EASSLLSNHiadlQAAEELLREAGSKTQESSLllllvkanLKDFREKKLHVQEEQnLTSKLIAQGREW 1823
Cdd:pfam05483 404 EVELEELKkilaEDEKLLDEK----KQFEKIAEELKGKEQELIF--------LLQAREKEIHDLEIQ-LTAIKTSEEHYL 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1824 VDAARTHAAAAQDTL--TQLEHHRDELLLWASKIRSHVDDLVMQMsKRRARDLVHRAEQ------HASELQSAAEALDRD 1895
Cdd:pfam05483 471 KEVEDLKTELEKEKLknIELTAHCDKLLLENKELTQEASDMTLEL-KKHQEDIINCKKQeermlkQIENLEEKEMNLRDE 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1896 LENVRNVSLNATSAVHV-----HTNIQTLTEEAESLAADAHKTANKTSLISESLAPRGKAV--LQRSSRFVKESVSTRKK 1968
Cdd:pfam05483 550 LESVREEFIQKGDEVKCkldksEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIeeLHQENKALKKKGSAENK 629
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1969 QQGI-TLKLD----ELKNLTSQFQERVDNITRQANDSlTVLRESPGGMREKSRKVKELAV 2023
Cdd:pfam05483 630 QLNAyEIKVNklelELASAKQKFEEIIDNYQKEIEDK-KISEEKLLEEVEKAKAIADEAV 688
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1612-1825 |
6.05e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.60 E-value: 6.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1612 LLEENAKKVQAEIQlgGIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKEITEKVATLNQTtge 1691
Cdd:COG4372 28 ALSEQLRKALFELD--KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEE--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1692 dfqppvsaLQSLHQNISSLLALIKKRNfTEmRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAA 1771
Cdd:COG4372 103 --------LESLQEEAEELQEELEELQ-KE-RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 312147379 1772 EELLREAGSKTQesslllllVKANLKDFREKKLHVQEEQNLTSKLIAQGREWVD 1825
Cdd:COG4372 173 LQALSEAEAEQA--------LDELLKEANRNAEKEEELAEAEKLIESLPRELAE 218
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
798-853 |
1.07e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.43 E-value: 1.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 312147379 798 CACPLSIDSnnfSPTChltDREEVVCdQCAPGYSGAWCERCADGYYGNPTVPGGTC 853
Cdd:pfam00053 1 CDCNPHGSL---SDTC---DPETGQC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1612-1778 |
2.19e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.93 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1612 LLEENAKKVQAEIQlgGIEEQTENLQKELARVLRSHQQVNTA-----------MERTSNRSQALATFLEQLHRNIKEITE 1680
Cdd:COG4942 80 ALEAELAELEKEIA--ELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARREQAEELRA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1681 KVATLNQTTGEdfqppvsaLQSLHQNISSLLALIKKRnftemRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSL 1760
Cdd:COG4942 158 DLAELAALRAE--------LEAERAELEALLAELEEE-----RAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
170
....*....|....*...
gi 312147379 1761 LSNHIADLQAAEELLREA 1778
Cdd:COG4942 225 LEALIARLEAEAAAAAER 242
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1600-2072 |
6.40e-07 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 55.44 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1600 NLENTTKYFQGYL--LEENAKKVQ--AEIQLGGIEEQTENLQ---KELARVLRSHQQVNTAMERTSNRSQALATFLEQLh 1672
Cdd:TIGR00606 699 DLQSKLRLAPDKLksTESELKKKEkrRDEMLGLAPGRQSIIDlkeKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTI- 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1673 rNIKEITEKVATLNQTTGEDFQPPVSALQ-SLHQNISSLLALIKKRNFTEMRQNATLELKAAKDLLSRI---QKRFQKPQ 1748
Cdd:TIGR00606 778 -MPEEESAKVCLTDVTIMERFQMELKDVErKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIelnRKLIQDQQ 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1749 EKLKALKEASSLLSNHiaDLQAAEELLReAGSKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREWVDAAR 1828
Cdd:TIGR00606 857 EQIQHLKSKTNELKSE--KLQIGTNLQR-RQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKE 933
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1829 THAAAAQDTLTQLEHHRDELLLWASKIRSHVDDLVMQMSKRRARDLVHRAEQhASELQSAAEALDRDLENVRNvslnats 1908
Cdd:TIGR00606 934 TSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQ-LEECEKHQEKINEDMRLMRQ------- 1005
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1909 avhvhtNIQTlTEEAESLAADahktaNKTSLISESlaprgkavlqrSSRFVKESVSTRKKQQGiTLKLDELKNLTSQFQE 1988
Cdd:TIGR00606 1006 ------DIDT-QKIQERWLQD-----NLTLRKREN-----------ELKEVEEELKQHLKEMG-QMQVLQMKQEHQKLEE 1061
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1989 RVDNITRQANDSLTVLRESPggmREKSRKVKELAVAANETAARTLEDMLgLSLRVFNTS-EDLSRVNATVQETKDLLHNS 2067
Cdd:TIGR00606 1062 NIDLIKRNHVLALGRQKGYE---KEIKHFKKELREPQFRDAEEKYREMM-IVMRTTELVnKDLDIYYKTLDQAIMKFHSM 1137
|
....*
gi 312147379 2068 TMTTI 2072
Cdd:TIGR00606 1138 KMEEI 1142
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1613-1822 |
7.58e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.38 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1613 LEENAKKVQAEIQLggIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKEITEKVATLNQ---TT 1689
Cdd:COG4942 25 AEAELEQLQQEIAE--LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAeleAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1690 GEDFQPPVSALQSLHQNiSSLLALIKKRNFTEMRQNATLE---LKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIA 1766
Cdd:COG4942 103 KEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQYLkylAPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 312147379 1767 DLQAA-EELLREAGSKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGRE 1822
Cdd:COG4942 182 ELEEErAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1598-2055 |
1.23e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.46 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1598 LENLENTTKYFQgyllEENAKKVQAEI-QLGGIEEQTENLQKELARVLRSHQQVNTAME-RTSNRSQALATFLEQLHRNI 1675
Cdd:pfam12128 324 LEALEDQHGAFL----DADIETAAADQeQLPSWQSELENLEERLKALTGKHQDVTAKYNrRRSKIKEQNNRDIAGIKDKL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1676 KEITEKVATLNQTTGEDFQPPVSALQSLHQ------NISSLL--------------------ALIKKRNFTEM------- 1722
Cdd:pfam12128 400 AKIREARDRQLAVAEDDLQALESELREQLEagklefNEEEYRlksrlgelklrlnqatatpeLLLQLENFDERieraree 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1723 -------RQNATLELKAAK-------DLLSRIQKRFQKPQEKLKALKE-----ASSLL----------SNHIADLQAAEE 1773
Cdd:pfam12128 480 qeaanaeVERLQSELRQARkrrdqasEALRQASRRLEERQSALDELELqlfpqAGTLLhflrkeapdwEQSIGKVISPEL 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1774 LLR-------EAGSKTQESS-----------------LLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREWVDaarT 1829
Cdd:pfam12128 560 LHRtdldpevWDGSVGGELNlygvkldlkridvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELE---K 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1830 HAAAAQDTLTQLEHHRDELLLWASKIRSHVDDLVMQMSKR------RARDLVHRAEQHASELQSAAEALDRDLENVRNVS 1903
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERkdsaneRLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEK 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1904 LNATSAVHVHTNIQ----TLTEEAESLAADAH----KTANKTSLIS----------------------ESLAPRGKAVLq 1953
Cdd:pfam12128 717 QAYWQVVEGALDAQlallKAAIAARRSGAKAElkalETWYKRDLASlgvdpdviaklkreirtlerkiERIAVRRQEVL- 795
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1954 RSSRFVKESVSTRKKQQGITL-----KLDELK-NLTSQFQE---RVDNITRQ--ANDSLTV-LRESPGGMREKSRKVKEL 2021
Cdd:pfam12128 796 RYFDWYQETWLQRRPRLATQLsnierAISELQqQLARLIADtklRRAKLEMErkASEKQQVrLSENLRGLRCEMSKLATL 875
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 312147379 2022 AVAANETAA--------RTLEDML----GLSLRVFNTSEDLSRVNA 2055
Cdd:pfam12128 876 KEDANSEQAqgsigerlAQLEDLKlkrdYLSESVKKYVEHFKNVIA 921
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
749-790 |
1.50e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.50e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 312147379 749 CECH--GHSSE-CD-IHGICSgCTHNTTGDHCEQCLPGFYGTPSRG 790
Cdd:smart00180 1 CDCDpgGSASGtCDpDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1459-1513 |
1.93e-06 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 46.96 E-value: 1.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 1459 CTCPHHPpfSFSPTCVLEGdsgFWCDaCLPGYEGQYCERCSAGYHGNPRAAGGSC 1513
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
855-899 |
2.01e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 2.01e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 312147379 855 PCNCSGNVDPleagHCDSVTGECLkCLWNTDGAHCERCADGFYGD 899
Cdd:smart00180 2 DCDPGGSASG----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
727-1098 |
2.48e-06 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 52.66 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 727 CEACLPGYyrvdGILFGGICQPCechghSSECDIHGiCSGCThNTTGDHCEQCLPGFYGTPSRGTPGDCQPCAcplsids 806
Cdd:pfam03302 1 CDECKPGY----ELSADKTKCTS-----SAPCKTEN-CKACS-NDKREVCEECNSNNYLTPTSQCIDDCAKIG------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 807 NNFSPTChltDREEVVCDQCAPGY-----SGAWCERCADGYYGNptvpGGTCVPCNCSgnvdpleaghCDSVTGECLkcl 881
Cdd:pfam03302 63 NYYYTTN---ANNKKICKECTVANcktceDQGQCQACNDGFYKS----GDACSPCHES----------CKTCSGGTA--- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 882 wntdgAHCERCADGF---YGDAVTAKNCRAcNCHEnGSLSGICHLETGLCDCKPYvtgqqCDQClpgyygldTGLGCVPC 958
Cdd:pfam03302 123 -----SDCTECLTGKalrYGNDGTKGTCGE-GCTT-GTGAGACKTCGLTIDGTSY-----CSEC--------ATETEYPQ 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 959 NcsgeGSISDNCTEEGQCHCVPGVSGKQCDQCSHGFYAfQNGGCTPCDCAHTQNNCDPDSGECLCPPHTHGLKCEQ---- 1034
Cdd:pfam03302 183 N----GVCTSTAARATATCKASSVANGMCSSCANGYFR-MNGGCYETTKFPGKSVCEEANSGGTCQKEAPGYKLNNgdlv 257
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312147379 1035 -CEEAFWGLDPEQGCQACNCSVVGSTS--PQCDvlsgqCSCKEGFGG-QSCHQCSLG-YRSFPDCVPCD 1098
Cdd:pfam03302 258 tCSPGCKTCTSNTVCTTCMDGYVKTSDscTKCD-----SSCETCTGAtTTCKTCATGyYKSGTGCVSCT 321
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1602-2131 |
3.48e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.87 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1602 ENTTKYFQGYLLEENAKKVQAEIQLGGIEEQTENLQKELARVLRShqqVNTAMERTSNRSQALATFLEQLHrNIKEI--T 1679
Cdd:pfam01576 404 EHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSL---LNEAEGKNIKLSKDVSSLESQLQ-DTQELlqE 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1680 EKVATLNQTTgedfqppvsALQSLHQNISSLLALIKKRnfTEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASS 1759
Cdd:pfam01576 480 ETRQKLNLST---------RLRQLEDERNSLQEQLEEE--EEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKK 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1760 LLSNHIADL--------QAAEELLREAGSKTQE------SSLLLLLVKANLKDfREKKLH--VQEEQNLTSKLI------ 1817
Cdd:pfam01576 549 RLQRELEALtqqleekaAAYDKLEKTKNRLQQElddllvDLDHQRQLVSNLEK-KQKKFDqmLAEEKAISARYAeerdra 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1818 -AQGREwvdaarthaaaaQDT--------LTQLEHHRDELLLWASKIRSHVDDLVmqMSKRRARDLVH------RA-EQH 1881
Cdd:pfam01576 628 eAEARE------------KETralslaraLEEALEAKEELERTNKQLRAEMEDLV--SSKDDVGKNVHelerskRAlEQQ 693
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1882 ASELQSAAEALDRDL---ENVR---NVSLNATSAVHvHTNIQTLTEEAEslaaDAHKTANKTslISESLAPRGKAVLQRS 1955
Cdd:pfam01576 694 VEEMKTQLEELEDELqatEDAKlrlEVNMQALKAQF-ERDLQARDEQGE----EKRRQLVKQ--VRELEAELEDERKQRA 766
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1956 srfvkESVSTRKKqqgitLKLDeLKNLTSQfqerVDNITRQANDSLTVLRESPGGMREKSRKVKELAVAANE--TAARTL 2033
Cdd:pfam01576 767 -----QAVAAKKK-----LELD-LKELEAQ----IDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEilAQSKES 831
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2034 EDML-GLSLRVFNTSEDLS---RVNATVQETKD-----LLHNSTMTTILAGRKMRdmemqanlLFDRlkpLKMLEENLSR 2104
Cdd:pfam01576 832 EKKLkNLEAELLQLQEDLAaseRARRQAQQERDeladeIASGASGKSALQDEKRR--------LEAR---IAQLEEELEE 900
|
570 580 590
....*....|....*....|....*....|
gi 312147379 2105 NLSEIKLLISRARK---QAASIKVAVSADR 2131
Cdd:pfam01576 901 EQSNTELLNDRLRKstlQVEQLTTELAAER 930
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1612-2063 |
4.54e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 52.63 E-value: 4.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1612 LLEENAKKVQAEIQLGGIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKEITEKVATLNQTTGE 1691
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1692 DfqppVSALQSLHQNISSLLALIKKRNftEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAA 1771
Cdd:COG1196 398 L----AAQLEELEEAEEALLERLERLE--EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1772 EELLREAGSKTQESSLLLLLVKANLKDFRE---------KKLHVQEEQNLTSKLIAQGREWVDAARTHAAAAQDTLTQLE 1842
Cdd:COG1196 472 AALLEAALAELLEELAEAAARLLLLLEAEAdyegflegvKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1843 HHRDEllLWASKIRSHVDDLV------MQMSKRRARDLVHRAEQHASELQsAAEALDRDLENVRNVSLNATSAVHVHTNI 1916
Cdd:COG1196 552 VVEDD--EVAAAAIEYLKAAKagratfLPLDKIRARAALAAALARGAIGA-AVDLVASDLREADARYYVLGDTLLGRTLV 628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1917 QTLTEEAESLAADAHKTANKTSLISESLAPRGKAVLQRSSRFVKESVSTRKKQQGITLKLD-ELKNLTSQFQERVDNITR 1995
Cdd:COG1196 629 AARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAeEELELEEALLAEEEEERE 708
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312147379 1996 QANDSLTVLRESpggmREKSRKVKELAVAANETAARTLEDMLGLSLRVFNTSEDLSRVNATVQETKDL 2063
Cdd:COG1196 709 LAEAEEERLEEE----LEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERL 772
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1618-1822 |
5.62e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 5.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1618 KKVQAEIQLGGIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKEITEKVATLNQTTGEDfqppV 1697
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----A 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1698 SALQSLHQNISSLLALIKKRNFTEMRQNATL---ELKAAKDLLSRIQKRfqkpQEKLKALK-EASSLLSNHIADLQAAEE 1773
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLDRLSAlskIADADADLLEELKAD----KAELEAKKaELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 312147379 1774 LLREAGSKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGRE 1822
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1613-1786 |
7.18e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 7.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1613 LEENAKkvQAEIQLGGIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALAT--FLEQLHRNIKEITEKVATLNQTTG 1690
Cdd:COG3206 210 LSEEAK--LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYT 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1691 EDfQPPVsalQSLHQNISSLLALIKKRNfTEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQA 1770
Cdd:COG3206 288 PN-HPDV---IALRAQIAALRAQLQQEA-QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362
|
170
....*....|....*.
gi 312147379 1771 AEELLREAGSKTQESS 1786
Cdd:COG3206 363 ARELYESLLQRLEEAR 378
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1609-2064 |
7.83e-06 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 51.89 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1609 QGYLL----EENAKKVQAEIQLGGIEEQT------ENLQKELARVLRSH----QQVNTAMERTSNRSQALATFLEQLHRN 1674
Cdd:TIGR00618 423 QGQLAhakkQQELQQRYAELCAAAITCTAqcekleKIHLQESAQSLKEReqqlQTKEQIHLQETRKKAVVLARLLELQEE 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1675 IKEITEKVATLNQTTGEDFQPPV--SALQSLHQNISSLLALIKKrnfteMRQNATLELKAAKDL---LSRIQKRFQKPQE 1749
Cdd:TIGR00618 503 PCPLCGSCIHPNPARQDIDNPGPltRRMQRGEQTYAQLETSEED-----VYHQLTSERKQRASLkeqMQEIQQSFSILTQ 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1750 KLKALKEASSLLSNHIADLQA-AEELLREAGSKTQESslLLLLVKANLK-DFREKKLHVQE-EQNLTSKLIAQGREwvda 1826
Cdd:TIGR00618 578 CDNRSKEDIPNLQNITVRLQDlTEKLSEAEDMLACEQ--HALLRKLQPEqDLQDVRLHLQQcSQELALKLTALHAL---- 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1827 arthaaaaQDTLTQ--LEHH-----RDELLLWA----------SKIRSHVDDLVM------------------------- 1864
Cdd:TIGR00618 652 --------QLTLTQerVREHalsirVLPKELLAsrqlalqkmqSEKEQLTYWKEMlaqcqtllrelethieeydrefnei 723
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1865 -QMSKRRARDLVHRAEQHASELQSAAEALDRDLENVRNVSLNATSAVHVhtNIQTLTEEAE----------SLAADAHKT 1933
Cdd:TIGR00618 724 eNASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTA--ALQTGAELSHlaaeiqffnrLREEDTHLL 801
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1934 ANKTSLISESLAPRGKAVLQRSSRFVKESVSTRKKQQGITLKLDELKNLTSQFQERVDNITRQANDS--LTVLRESPGGM 2011
Cdd:TIGR00618 802 KTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQakIIQLSDKLNGI 881
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 2012 REKSRKVKE--LAVAANETAARTLEDMLGLSLRVFNTSEDLSRVNATVQETKDLL 2064
Cdd:TIGR00618 882 NQIKIQFDGdaLIKFLHEITLYANVRLANQSEGRFHGRYADSHVNARKYQGLALL 936
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1613-1897 |
1.34e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.09 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1613 LEENAKKVQAEIQLGGIEEqtenLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKEITEKVAtlnqttged 1692
Cdd:COG1196 218 LKEELKELEAELLLLKLRE----LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE--------- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1693 fqppvSALQSLHQNISSLLALIKKRNF-TEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSnhiADLQAA 1771
Cdd:COG1196 285 -----EAQAEEYELLAELARLEQDIARlEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE---EELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1772 EELLREAGSKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREwvdaarthaaAAQDTLTQLEHHRDELLLW 1851
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE----------AEEALLERLERLEEELEEL 426
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 312147379 1852 ASKIRSHVDDLVMQmsKRRARDLVHRAEQHASELQSAAEALDRDLE 1897
Cdd:COG1196 427 EEALAELEEEEEEE--EEALEEAAEEEAELEEEEEALLELLAELLE 470
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
716-914 |
2.25e-05 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 47.30 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 716 CECPQGY---TGTSCEACLPGyyrvdgilfggicqpcechghssecdiHGICSGCTHNTTGdhCEQCLPGFYGTPSRGTP 792
Cdd:cd13416 1 EACPSGQytsSGECCEQCPPG---------------------------EGVARPCGDNQTV--CEPCLDGVTFSDVVSHT 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 793 GDCQPCA-CPLSIdsnnfSPTCHLTDREEVVCdqcapgysgawceRCADGYYgnPTVPGGTCVPCNCsgnvdpleaghCD 871
Cdd:cd13416 52 EPCQPCTrCPGLM-----SMRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCEPCTV-----------CP 100
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 312147379 872 SVTGECLKCLWNTDgAHCERCADGFYGDAVTAKN-CRACN-CHEN 914
Cdd:cd13416 101 PGQGVVQSCGPNQD-TVCEACPEGTYSDEDSSTDpCLPCTvCEDG 144
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1613-1900 |
2.43e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.52 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1613 LEENAKKVQAEIQlgGIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKEITEKVATLNQTTGEd 1692
Cdd:COG4372 99 AQEELESLQEEAE--ELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1693 fqppvsalQSLHQNISSLLALIKKRNFTEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAAE 1772
Cdd:COG4372 176 --------LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEED 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1773 ELLREAGSKTQEsslLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREWVDAARTHAAAAQDTLTQLEHHRDELLLWA 1852
Cdd:COG4372 248 KEELLEEVILKE---IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 312147379 1853 SKirsHVDDLVMQMSKRRARDLVHRAEQHASELQSAAEALDRDLENVR 1900
Cdd:COG4372 325 AK---KLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1613-2037 |
2.46e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1613 LEENAKKVQAEIQ-LGGIEEQTENLQKELARV------LRSHQQVNTAMERTSNRSQALATF---LEQLHRNIKEITEKV 1682
Cdd:COG4717 83 AEEKEEEYAELQEeLEELEEELEELEAELEELreelekLEKLLQLLPLYQELEALEAELAELperLEELEERLEELRELE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1683 ATLNQTTGEdfqppvsaLQSLHQNISSLLALIKKRNFTEMRQNATlELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLS 1762
Cdd:COG4717 163 EELEELEAE--------LAELQEELEELLEQLSLATEEELQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1763 NHIADLQAAEELLREAGSKTQESSllLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREWVDAARTHAAAAQDTLTQLE 1842
Cdd:COG4717 234 NELEAAALEERLKEARLLLLIAAA--LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1843 HHRD----ELLLWASKIR-------SHVDDLVMQMskRRARDLVHRAEQHASELQSAaealdrDLENVRNVSLNATSAvh 1911
Cdd:COG4717 312 ALEEleeeELEELLAALGlppdlspEELLELLDRI--EELQELLREAEELEEELQLE------ELEQEIAALLAEAGV-- 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1912 vhTNIQTLTEEAEsLAADAHKTANKTSLISESLAPRGKAVLQRSSRFVKESVSTRKKQqgITLKLDELKNLTSQFQERVD 1991
Cdd:COG4717 382 --EDEEELRAALE-QAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE--LEEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 312147379 1992 NITRQ-----ANDSLTVLRESpggMREKSRKVKELA--VAANETAARTLEDML 2037
Cdd:COG4717 457 ELEAEleqleEDGELAELLQE---LEELKAELRELAeeWAALKLALELLEEAR 506
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1699-2026 |
2.48e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1699 ALQSLHQNISSLLALIKKRNFTEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAAEELLREA 1778
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1779 GSKTQesslllllvkanlkdfREKKLHVQEEQNLTSKLIAQGREwvdaarthaaaAQDTLTQLEHHRDELLLWASKIRSH 1858
Cdd:COG1196 297 LARLE----------------QDIARLEERRRELEERLEELEEE-----------LAELEEELEELEEELEELEEELEEA 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1859 vddlvmQMSKRRARDLVHRAEQHASELQSAAEALDRDLENVRNVSLNATSAVHVHTN-IQTLTEEAESLAADAHKTANKT 1937
Cdd:COG1196 350 ------EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAqLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1938 SLISESLAPRGKAVLQRSSRFVKESVSTRKKQQ---GITLKLDELKNLTSQFQERVDNITRQANDS---LTVLRESPGGM 2011
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEeeeALLELLAELLEEAALLEAALAELLEELAEAaarLLLLLEAEADY 503
|
330
....*....|....*
gi 312147379 2012 REKSRKVKELAVAAN 2026
Cdd:COG1196 504 EGFLEGVKAALLLAG 518
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
797-851 |
2.77e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.88 E-value: 2.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 797 PCACPLSIDSNnfsPTChltDREEVVCdQCAPGYSGAWCERCADGYYGNPTVPGG 851
Cdd:cd00055 1 PCDCNGHGSLS---GQC---DPGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1458-1514 |
4.71e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.11 E-value: 4.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 312147379 1458 PCTCPHHPpfSFSPTCVLEgdSGFwCDaCLPGYEGQYCERCSAGYHGNPRAAGGsCQ 1514
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPG--TGQ-CE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1613-2124 |
5.21e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1613 LEENAKKVQaEIQlgGIEEQTENLQKELARVLRSHQQVNTAMERTSNRsqalatfLEQLHRNIKEITEKVATLNQTTG-- 1690
Cdd:PRK03918 278 LEEKVKELK-ELK--EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE-------INGIEERIKELEEKEERLEELKKkl 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1691 EDFQPPVSALQSLHQNISSLLALIK-KRNFTEMRQNATLElKAAKDLLSrIQKRFQKPQEKLKALKEASSLLSNHIADLQ 1769
Cdd:PRK03918 348 KELEKRLEELEERHELYEEAKAKKEeLERLKKRLTGLTPE-KLEKELEE-LEKAKEEIEEEISKITARIGELKKEIKELK 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1770 AAEELLREAGSK--------TQESSLL-LLLVKANLKDFREKKlhvQEEQNLTSKLIAQGREwvdaaRTHAAAAQDTLTQ 1840
Cdd:PRK03918 426 KAIEELKKAKGKcpvcgrelTEEHRKElLEEYTAELKRIEKEL---KEIEEKERKLRKELRE-----LEKVLKKESELIK 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1841 LEHHRDELLLWASKIRSH-VDDLvmqmsKRRARDLvHRAEQHASELQSAAEALDRDLEnvRNVSLNATSAVhVHTNIQTL 1919
Cdd:PRK03918 498 LKELAEQLKELEEKLKKYnLEEL-----EKKAEEY-EKLKEKLIKLKGEIKSLKKELE--KLEELKKKLAE-LEKKLDEL 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1920 TEEAESLaadAHKTANKTSLISESLAPRgkavLQRSSRFVKESVSTRKKQQGITLKLDELKNLTSQFQERVDNITRQAND 1999
Cdd:PRK03918 569 EEELAEL---LKELEELGFESVEELEER----LKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2000 sltvlrespggMREKSRKVKELAVAANETAARTLED-MLGLSLRVFNTSEDLSRVNATVQETKDLLHNstmttilagrkm 2078
Cdd:PRK03918 642 -----------LEELRKELEELEKKYSEEEYEELREeYLELSRELAGLRAELEELEKRREEIKKTLEK------------ 698
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 312147379 2079 rdmeMQANLlfDRLKPLKMLEENLSRNLSEIKLLISRARKQAASIK 2124
Cdd:PRK03918 699 ----LKEEL--EEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1852-2007 |
7.14e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 46.10 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1852 ASKIRSHVDDLVMQMSkRRARDLVHRAEQhasELQSAAEALDRDLENVRNVSLNATSAVH--VHTNIQTLTEEAESLAAD 1929
Cdd:pfam01442 6 LDELSTYAEELQEQLG-PVAQELVDRLEK---ETEALRERLQKDLEEVRAKLEPYLEELQakLGQNVEELRQRLEPYTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1930 AHKTAN-KTSLISESLAPRG---KAVLQRSSRFVKESVSTRKKQ--QGITLKLDELKnltSQFQERVDNITRQANDSLTV 2003
Cdd:pfam01442 82 LRKRLNaDAEELQEKLAPYGeelRERLEQNVDALRARLAPYAEElrQKLAERLEELK---ESLAPYAEEVQAQLSQRLQE 158
|
....
gi 312147379 2004 LRES 2007
Cdd:pfam01442 159 LREK 162
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1702-2121 |
7.47e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1702 SLHQNISSLL--ALIKKRN--FTEMRQNATLELKAAKDLLSRIQKRFQKPQEkLKALKEASSLLSNHIADLQAAEELLRE 1777
Cdd:COG4717 38 TLLAFIRAMLleRLEKEADelFKPQGRKPELNLKELKELEEELKEAEEKEEE-YAELQEELEELEEELEELEAELEELRE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1778 AgsktQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREWVDAARTHAAAAQDtLTQLEHHRDELLLWAS-KIR 1856
Cdd:COG4717 117 E----LEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE-LAELQEELEELLEQLSlATE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1857 SHVDDLVMQMSKRRARdlVHRAEQHASELQSAAEALDRDLENVRNVSLNATSAVHVHTNIQTLTEEAE--SLAADAHKTA 1934
Cdd:COG4717 192 EELQDLAEELEELQQR--LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAAllALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1935 NKTSLISESLAPRGKAVLQRSSRFVKESVSTRKKQQGI-------TLKLDELKNLTSQFQERVDNITRQANDSLTVLRES 2007
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELqalpaleELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2008 PGGMREKSRKVKELAVAANETAARTL--------EDMLGLSLRVFNTSEDLsrvNATVQETKDLL--HNSTMTTILAGRK 2077
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAALlaeagvedEEELRAALEQAEEYQEL---KEELEELEEQLeeLLGELEELLEALD 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 312147379 2078 MRDMEMQANLLFDRLKPLKMLEENLSRNLSEIKLLISRARKQAA 2121
Cdd:COG4717 427 EEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGE 470
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1629-1888 |
1.08e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.58 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1629 IEEQTENLQKELARVLRSHQQVNTAMERTSNRSQalaTFLEQLHRNIKEITEKVATLNQttgedfqppvsALQSLHQNIS 1708
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYK---RDREQWERQRRELESRVAELKE-----------ELRQSREKHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1709 SLLALIKKRnftemrQNATLELKAAKDLLSRIQkrfQKPQEKLKALKEASSLLSNHIADLQAAEELLREagsKTQESSLL 1788
Cdd:pfam07888 98 ELEEKYKEL------SASSEELSEEKDALLAQR---AAHEARIRELEEDIKTLTQRVLERETELERMKE---RAKKAGAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1789 LLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREWVDAARTHAAAAQDTLTQLEH-----HRDELLLWASK--IRSHVDD 1861
Cdd:pfam07888 166 RKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQklttaHRKEAENEALLeeLRSLQER 245
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 312147379 1862 LVmqMSKRRA-------------RDLVHrAEQHASELQSA 1888
Cdd:pfam07888 246 LN--ASERKVeglgeelssmaaqRDRTQ-AELHQARLQAA 282
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
798-846 |
1.43e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 1.43e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 312147379 798 CACPLSidsNNFSPTChltDREEVVCdQCAPGYSGAWCERCADGYYGNP 846
Cdd:smart00180 1 CDCDPG---GSASGTC---DPDTGQC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
277-320 |
1.53e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 1.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 277 CICS--GHAS-SCpwdeEAKQLQCQCEHNTCGESCDRCCPGFHQQPW 320
Cdd:smart00180 1 CDCDpgGSASgTC----DPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1598-1929 |
2.11e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1598 LENLENTTKYFQGYL--LEENAKKVQAEIQLGGIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQAlatfLEQLHRni 1675
Cdd:COG4717 104 LEELEAELEELREELekLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAE----LAELQE-- 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1676 kEITEKVATLNQTTGEDFQPPVSALQSLHQNISSLLALIKKRNFTEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALK 1755
Cdd:COG4717 178 -ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAA 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1756 EASSLLSN---------HIADLQAA---------------EELLREAGSKTQESSLLLLLVKANLKDFReKKLHVQEEQN 1811
Cdd:COG4717 257 ALLALLGLggsllslilTIAGVLFLvlgllallflllareKASLGKEAEELQALPALEELEEEELEELL-AALGLPPDLS 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1812 LTS--KLIAQGREWVDAARTHAAAAQD-TLTQLEHHRDELLlwaskIRSHVDDLvmqmskrraRDLVHRAEQH--ASELQ 1886
Cdd:COG4717 336 PEEllELLDRIEELQELLREAEELEEElQLEELEQEIAALL-----AEAGVEDE---------EELRAALEQAeeYQELK 401
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 312147379 1887 SAAEALDRDLEN---VRNVSLNATSAVHVHTNIQTLTEEAESLAAD 1929
Cdd:COG4717 402 EELEELEEQLEEllgELEELLEALDEEELEEELEELEEELEELEEE 447
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1613-1861 |
2.24e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 45.13 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1613 LEENAKKVQAEiQLGGIEEQTENLQKElarvlrsHQQVNTAMERTSNRSQALA----TFLEQLHRNIKEITEKVATLNQt 1688
Cdd:cd00176 16 LSEKEELLSST-DYGDDLESVEALLKK-------HEALEAELAAHEERVEALNelgeQLIEEGHPDAEEIQERLEELNQ- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1689 tgedfqppvsalqsLHQNISSLLALIKKRnftemrqnatleLKAAKDLlsriQKRFQKPQEKLKALKEASSLLSN--HIA 1766
Cdd:cd00176 87 --------------RWEELRELAEERRQR------------LEEALDL----QQFFRDADDLEQWLEEKEAALASedLGK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1767 DLQAAEELLREagsktqesslllllvkanLKDFREKklhVQEEQNLTSKLIAQGRE-WVDAARTHAAAAQDTLTQLEHHR 1845
Cdd:cd00176 137 DLESVEELLKK------------------HKELEEE---LEAHEPRLKSLNELAEElLEEGHPDADEEIEEKLEELNERW 195
|
250
....*....|....*.
gi 312147379 1846 DELLLWASKIRSHVDD 1861
Cdd:cd00176 196 EELLELAEERQKKLEE 211
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1625-1778 |
3.69e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.92 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1625 QLGGIEEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRNIKEITEKVATLNQ-----TTGEDFQppvsA 1699
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgnvRNNKEYE----A 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312147379 1700 LQslHQnISSLLALIKKRNFTEMRQNATLElkAAKDLLSRIQKRFQKPQEKLKALKEAsslLSNHIADLQAAEELLREA 1778
Cdd:COG1579 94 LQ--KE-IESLKRRISDLEDEILELMERIE--ELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAE 164
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1601-2133 |
4.78e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.19 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1601 LENTTKYFQGYLLEENAKKVQAEIQLggiEEQTENLQKELARVLRSHQQVNTAMERTsnrsqalatfLEQLHRNIKEITE 1680
Cdd:TIGR00606 267 LDNEIKALKSRKKQMEKDNSELELKM---EKVFQGTDEQLNDLYHNHQRTVREKERE----------LVDCQRELEKLNK 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1681 KVATLNQTTGEdFQPPVSALQ---SLHQnissllALIKKRNfTEMRQNAT-LELKA-AKDLLSRIQ-KRFQKPqeKLKAL 1754
Cdd:TIGR00606 334 ERRLLNQEKTE-LLVEQGRLQlqaDRHQ------EHIRARD-SLIQSLATrLELDGfERGPFSERQiKNFHTL--VIERQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1755 KEASSLLSNHIADLQAAEELLREAGSKTQESSLLLLLVKANlkdfreKKLHVQEEQNLTSKLIAQGRewvdaarthaaaa 1834
Cdd:TIGR00606 404 EDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIEL------KKEILEKKQEELKFVIKELQ------------- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1835 qdtltQLEHHRDELLLWASKIRSHVDDLvmqmSKRRARDLVHRAEQHASELQSAAEALDRDL--ENVRNVSLNAtsavHV 1912
Cdd:TIGR00606 465 -----QLEGSSDRILELDQELRKAEREL----SKAEKNSLTETLKKEVKSLQNEKADLDRKLrkLDQEMEQLNH----HT 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1913 HTNIQTLTEEAESLAADAHKTANK----------------TSLISESLAPRGKAVLQRSSRFVKESVSTRKKQQGITLKL 1976
Cdd:TIGR00606 532 TTRTQMEMLTKDKMDKDEQIRKIKsrhsdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1977 DELKNLTSQFQERVDNI----TRQANDS-LTVLRESpggmREKSRKVKELAVAANETAARTLEDMLG-------LSLRVF 2044
Cdd:TIGR00606 612 NELESKEEQLSSYEDKLfdvcGSQDEESdLERLKEE----IEKSSKQRAMLAGATAVYSQFITQLTDenqsccpVCQRVF 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 2045 NTSEDLSRVNATVQETKDLL---HNSTMTTILAGRKMRD-----MEMQANLLFDRLKPLKMLEE---NLSRNLSEIKLLI 2113
Cdd:TIGR00606 688 QTEAELQEFISDLQSKLRLApdkLKSTESELKKKEKRRDemlglAPGRQSIIDLKEKEIPELRNklqKVNRDIQRLKNDI 767
|
570 580
....*....|....*....|
gi 312147379 2114 SRARKQAASIKVAVSADRDC 2133
Cdd:TIGR00606 768 EEQETLLGTIMPEEESAKVC 787
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1598-1900 |
1.38e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1598 LENLENTTKYFQGYLLEENAKKVQA-EIQLGGIEEQTENLQKELarvlrshqqvntamertsNRSQALATFLEQLHRNIK 1676
Cdd:PRK03918 505 LKELEEKLKKYNLEELEKKAEEYEKlKEKLIKLKGEIKSLKKEL------------------EKLEELKKKLAELEKKLD 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1677 EITEKVATLNQTTGE-DFqppvSALQSLHQNISSLLALIKKrnftemrqnaTLELKAAKDLLSRIQKRFQKPQEKlkaLK 1755
Cdd:PRK03918 567 ELEEELAELLKELEElGF----ESVEELEERLKELEPFYNE----------YLELKDAEKELEREEKELKKLEEE---LD 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1756 EASSLLSNHIADLQAAEELLREAGSKTQEsslllllvkanlKDFREKKLHVQEEQNLTSKLIAQgrewvdaarthaaaaq 1835
Cdd:PRK03918 630 KAFEELAETEKRLEELRKELEELEKKYSE------------EEYEELREEYLELSRELAGLRAE---------------- 681
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 1836 dtLTQLEHHRDElllwaskIRSHVDDLVMQMSKRrardlvhraEQHASELQSAAEALDRdLENVR 1900
Cdd:PRK03918 682 --LEELEKRREE-------IKKTLEKLKEELEER---------EKAKKELEKLEKALER-VEELR 727
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
277-323 |
1.40e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.87 E-value: 1.40e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 312147379 277 CICSGHASSCPwDEEAKQLQCQCEHNTCGESCDRCCPGFHQQPWRPG 323
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1711-1999 |
1.58e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1711 LALIKKRNFTEMRQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAA-----------EELLREAG 1779
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyalaneisrlEQQKQILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1780 SKTQESSLLLLLVKANLKDFREKKLHVQEEQNLTSKLIAQGREWVDAARTHAAAAQDTLTQLEHHRDELLLWASKIRSHV 1859
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1860 DDLVMQMSK-----RRARDLVHRAEQHASELQSAAEALDRDLENVRnvslnatsAVHVHTNIQTLTEEAESLAADAHKTA 1934
Cdd:TIGR02168 389 AQLELQIASlnneiERLEARLERLEDRRERLQQEIEELLKKLEEAE--------LKELQAELEELEEELEELQEELERLE 460
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312147379 1935 NKTSLISESLAPRGKAVLQRSSRFvkESVSTRKKQqgitlkLDELKNLTSQFQERVDNITRQAND 1999
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAEREL--AQLQARLDS------LERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1570-1762 |
2.17e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1570 ALLNDLDSIGDAVLSLNLAGVSLApyGTLENLENTTKYFQGYLLEENAKKVQAEIQLGGIEEQTENLQKELArvlrshQQ 1649
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELS--EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS------EE 948
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1650 VNTAMERTSNRSQALATFLEQLHRNIKEITEKVATL---NQTTGEDFQPP--------------VSALQSLHQNISSLLA 1712
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELgpvNLAAIEEYEELkerydfltaqkedlTEAKETLEEAIEEIDR 1028
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312147379 1713 LIKKR----------NFTEMRQ------NATLELKAAKDLL-SRIQKRFQKPQEKLKALkeasSLLS 1762
Cdd:TIGR02168 1029 EARERfkdtfdqvneNFQRVFPklfgggEAELRLTDPEDLLeAGIEIFAQPPGKKNQNL----SLLS 1091
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1628-1776 |
4.48e-03 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 42.37 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1628 GIEEQTENLQKELARVLRSHQQVNTAMERTsnrsqalatfLEQLhRNIK------EITEKVATLnqttgEDFqppVS--A 1699
Cdd:pfam04108 53 GLEKVLNELKKDFKQLLKDLDAALERLEET----------LDKL-RNTPvepalpPGEEKQKTL-----LDF---IDedS 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 312147379 1700 LQSLHQNISSLLALIKKRnFTEMRQNatleLKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAAEELLR 1776
Cdd:pfam04108 114 VEILRDALKELIDELQAA-QESLDSD----LKRFDDDLRDLQKELESLSSPSESISLIPTLLKELESLEEEMASLLE 185
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1624-1900 |
4.94e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1624 IQLGGIEEQTENLQKelARVlrshqQVNTAMERTSNRsqalatfLEQLHRNIKEITEKvatlnqttgedfqPPVSALQSL 1703
Cdd:PRK02224 159 LQLGKLEEYRERASD--ARL-----GVERVLSDQRGS-------LDQLKAQIEEKEEK-------------DLHERLNGL 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1704 HQNISSLLALIKKrnFTEMRQNATLELKAAKDLLSRIQKRfqkpQEKLKALKEAssllsnhIADLQAAeelLREAGSKTQ 1783
Cdd:PRK02224 212 ESELAELDEEIER--YEEQREQARETRDEADEVLEEHEER----REELETLEAE-------IEDLRET---IAETERERE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1784 ESSLLLLLVKANLKDFREKKLHVQEEQNLTS---KLIAQGREWVDaarthaaaaqdtlTQLEHHRDELLLWASKIRSHVD 1860
Cdd:PRK02224 276 ELAEEVRDLRERLEELEEERDDLLAEAGLDDadaEAVEARREELE-------------DRDEELRDRLEECRVAAQAHNE 342
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 312147379 1861 DLvmqmskRRARDLVHRAEQHASELQSAAEALDRDLENVR 1900
Cdd:PRK02224 343 EA------ESLREDADDLEERAEELREEAAELESELEEAR 376
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1459-1506 |
5.51e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 5.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 312147379 1459 CTCphHPPFSFSPTCVLegDSGFwCDaCLPGYEGQYCERCSAGYHGNP 1506
Cdd:smart00180 1 CDC--DPGGSASGTCDP--DTGQ-CE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
1716-2065 |
5.77e-03 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 42.41 E-value: 5.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1716 KRNFTEMRQNatLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAAEELLREAGSKTQESSLLLLLVKAN 1795
Cdd:COG2770 271 ARAFNRMADS--LRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALLLLLLLAA 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1796 LKDFREKKLHVQEEQNLTSKLIAQGREWVDAARTHAAAAQDTLTQLEHHRDELLLWASKIRSHVDDLVMQMSKRRARDLV 1875
Cdd:COG2770 349 DLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALALLALAAAA 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1876 HRAEQHASELQSAAEALDRDLENVRNVSLNATSAVHVHTNIQTLTEEAESLAADAHKTANKTSLISESLAPRGKAVLQRS 1955
Cdd:COG2770 429 AAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAAAEELAEE 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1956 SRFVKESVSTRKKQQGITLKLDELKNLTSQFQERVDNITRQANDSLTVLRESPGGMREKSRKVKELAVAANETAARTLED 2035
Cdd:COG2770 509 LLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLLAALLLAAVAALLELAALLLL 588
|
330 340 350
....*....|....*....|....*....|
gi 312147379 2036 MLGLSLRVFNTSEDLSRVNATVQETKDLLH 2065
Cdd:COG2770 589 LLAAAEALAALELELAAAAEAALAEAELLE 618
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
715-739 |
5.78e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 5.78e-03
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1630-1778 |
7.62e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 7.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1630 EEQTENLQKELARVLRSHQQVNTAMERTSNRSQALATFLEQLHRnIKEITEkvatlnqtTGEDFQPPVSALQSLHQNISS 1709
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQR-LAEYSW--------DEIDVASAEREIAELEAELER 679
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 312147379 1710 LLAlikkrnftemrqnATLELKAAKDLLSRIQKRFQKPQEKLKALKEASSLLSNHIADLQAAEELLREA 1778
Cdd:COG4913 680 LDA-------------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1622-1898 |
9.17e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.87 E-value: 9.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1622 AEIQLGGIEEQTENLQKELA-RVLRSHQQVNTAMERT-SNRSQALATF-------------LEQ---LHRNIKEITEKVA 1683
Cdd:PRK04863 400 ADYQQALDVQQTRAIQYQQAvQALERAKQLCGLPDLTaDNAEDWLEEFqakeqeateellsLEQklsVAQAAHSQFEQAY 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1684 TLNQTTGedfqPPVSALQSLHQNISSLLALIKKRNFTEMRQnatlELKAAkdlLSRIQKRFQKPQEKLKALKEASSLLSN 1763
Cdd:PRK04863 480 QLVRKIA----GEVSRSEAWDVARELLRRLREQRHLAEQLQ----QLRMR---LSELEQRLRQQQRAERLLAEFCKRLGK 548
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312147379 1764 HIADLQAAEELLREAGSKTQESSllllLVKANLKDFREKKLHVQEE-QNLTSKLIAQGREWVdaarthaaAAQDTLTQLE 1842
Cdd:PRK04863 549 NLDDEDELEQLQEELEARLESLS----ESVSEARERRMALRQQLEQlQARIQRLAARAPAWL--------AAQDALARLR 616
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 312147379 1843 HHRDELLLwaskIRSHVDDLvMQMSKRRARDLvhraEQHASELQSAAEALDRDLEN 1898
Cdd:PRK04863 617 EQSGEEFE----DSQDVTEY-MQQLLEREREL----TVERDELAARKQALDEEIER 663
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
715-747 |
9.48e-03 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 36.56 E-value: 9.48e-03
10 20 30
....*....|....*....|....*....|...
gi 312147379 715 HCECPQGYTGTSCEACLPGYYRVDGILFGgiCQ 747
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| |
