|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1582-1837 |
3.54e-101 |
|
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: 326.29 E-value: 3.54e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1582 VLSLN-LTGVSPAPYGILENLENTTKYFQRYLIKENAKKIRAEI---QLEGIAEQTENLQKELTRVLARHQKVNAEMERT 1657
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEIlekELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1658 SNGTQALATFIEQLHANIKEITEKVATLNQtarKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLL 1737
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1738 SRIQKRFQKPQEKLKALKEA-NSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSEL 1816
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANAlRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 1431906468 1817 IAKGREWVDAAGTHTAAAQDT 1837
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
25-275 |
2.56e-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: 305.44 E-value: 2.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 25 QQRGLFPAILNLATNAHISANATCGEKGPEMFCKLVehvpGRPVRHAQCRVCDgnSTNPRERHPISHAIDGTN----NWW 100
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLV----GHTEQGKKCDYCD--ARNPRRSHPAENLTDGNNpnnpTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 101 QSPSIQNGReyHWVTVTLDLRQVFQVAYIIIKAAnAPRPGNWILERSVDGVKFKPWQYYAvsdTECLTRYKITPRRGPPT 180
Cdd:smart00136 77 QSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 181 YrADNEVICTSYYSKLVPLEHGEIHTSLINGRPSADDP--SPQLLEFTSARYIRLRLQRIRTLNADLMtlshrdlrDLDP 258
Cdd:smart00136 151 G-NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 1431906468 259 IVTRRYYYSIKDISVGG 275
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2018-2152 |
7.89e-55 |
|
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: 188.08 E-value: 7.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2018 ARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKT 2097
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431906468 2098 LEEN---LSRNLSEIKLLISRARKQVASIKVAVSADRDCIRAYQPQTSSTNYNTLILN 2152
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1225-1367 |
5.41e-49 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 171.30 E-value: 5.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1225 YWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGTGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQDYEVRMKEEFWKYf 1304
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 1305 nsVSEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGRKAvelpAEGEAALLLE 1367
Cdd:pfam00052 80 --SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG----GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
575-714 |
7.52e-44 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 156.66 E-value: 7.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 575 YWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETvdSDLMSHADIIIKGNGLTISTRAEG-LSLQPYEEYFNVVRLVPENFR 653
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG--GSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 654 DfDTRREIDRDQLMTVLANVTHLLIRANYNSaKMALYRLDSVSLDIASPNAIDLaVAADVE 714
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYST-GSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2751-2880 |
3.33e-42 |
|
Laminin G domain;
:
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 151.70 E-value: 3.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2751 IRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSVT 2830
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 2831 -VVGNATTLDVERKLYLGGLPSHYRARNIGTITHSIPACIGEIMVNGQQLD 2880
Cdd:pfam00054 81 sPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2900-3053 |
3.50e-38 |
|
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: 141.02 E-value: 3.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2900 GTFFEGSGYAALVKEGYKvRLDLNITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRaar 2978
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 2979 aLCDGKWHTLQAHKSKHRIVLTVDGNSVRAESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 3053
Cdd:cd00110 77 -LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2314-2470 |
3.79e-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: 138.32 E-value: 3.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2314 SFHFDGSGYAMVEKTLRPTV-TQIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNG 2392
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTrLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431906468 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 ... |
2495-2659 |
7.26e-32 |
|
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: 122.91 E-value: 7.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2495 SVSFLRGGYVEMPPKSL-SPESSLLATFATKNSSGILLVAlgkdaeeagGAQAHVPFFSIMLLEGRIEVHVNSGDGTslr 2573
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYA---------GSQNGGDFLALELEDGRLVLRYDLGSGS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2574 kALLHAPTgSYSDGQEHSISLVRNRRVITIQVDENSPVEMKLgPLTEGKTIDISNLYIGGLPEDKATPMLKMRTSFHGCI 2653
Cdd:cd00110 69 -LVLSSKT-PLNDGQWHSVSVERNGRSVTLSVDGERVVESGS-PGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 1431906468 2654 KNVVLD 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 |
2.88e-29 |
|
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: 115.59 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2136 AYQPQTSSTNYNTLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEfPEVSINNNRWHSIYITR 2215
Cdd:cd00110 11 RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQWHSVSVER 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2216 FGNMGSLSVKeasaaENPPVRTSKSPGPskvLDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLN 2285
Cdd:cd00110 90 NGRSVTLSVD-----GERVVESGSPGGS---ALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
909-955 |
3.12e-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: 72.00 E-value: 3.12e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 909 CDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGLDTGLGC 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 |
1.78e-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: 63.91 E-value: 1.78e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 404 CNCDPVGSLSSVCIKddrhadlangkWPGQCPCRKGYAGDKCDRCQFGYRGFPNCIPCDC 463
Cdd:pfam00053 1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1516-1553 |
5.09e-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: 5.09e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1431906468 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1553
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1410-1456 |
1.23e-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: 61.60 E-value: 1.23e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1410 CNCNNH---SDVCDPETGKCLsCRDHTSGDHCELCASGYYGKVTGLPGDC 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. |
1051-1099 |
1.35e-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: 61.60 E-value: 1.35e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1431906468 1051 CNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGYRSFPDCVPCGC 1099
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
748-796 |
1.45e-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: 58.52 E-value: 1.45e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 748 PCECHGHAS---ECD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRgtPGDCQ 796
Cdd:cd00055 1 PCDCNGHGSlsgQCDpGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1097-1154 |
1.98e-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: 58.13 E-value: 1.98e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431906468 1097 CGCDLRGTLPDTCDLEqglcscsedGGTCSCKENAVGPQCSKCQAGTFALRGDNPQGC 1154
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
958-1002 |
3.54e-10 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 3.54e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1431906468 958 CNCSVEGSVSDNC-TEEGQCHCGPGVSGKQCDRCSHGFYAFQDGGC 1002
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
855-907 |
1.37e-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: 1.37e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 855 PCNCSGNVDplEAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVTAKNCR 907
Cdd:cd00055 1 PCDCNGHGS--LSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
461-507 |
3.28e-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: 54.67 E-value: 3.28e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 461 CDCRTVGSLNeDPCIE---PCLCKKNVEGKNCDRCKPGFYNLKERNPEGC 507
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1004-1049 |
1.69e-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: 52.74 E-value: 1.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1004 PCDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGLDPE-QGCQ 1049
Cdd:cd00055 1 PCDCnghGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
798-853 |
2.97e-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: 2.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1431906468 798 CACPLSIDSnnfSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGGTC 853
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETG---QC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
277-324 |
3.56e-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: 51.97 E-value: 3.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 277 CICYGHAS---SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPGT 324
Cdd:cd00055 2 CDCNGHGSlsgQC----DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1711-2035 |
6.56e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
:
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1711 LGLIKERNFTEMQQNATLE-LKAAKDLLSRIQKRFQKPQEKLKALKE----ANSLLSNHSEKLQAAEELLKEAGSKTQES 1785
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEqLRKALFELDKLQEELEQLREELEQAREeleqLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1786 NLLLLLVKANLKEFQEKKLRVQEEqnvtseliakgrewvdaagthtaaaqdtLTQLEHHRDELLLWARKIRSHVDDLVMQ 1865
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEE----------------------------LEELQKERQDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1866 MSKRRARdlvhraeqhASELQSRAGALDRDLENVRNvSLNATSAAHVHSNIQTLTEEAEMLAADAHKTANKTDLISESLA 1945
Cdd:COG4372 145 IAEREEE---------LKELEEQLESLQEELAALEQ-ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1946 SRGKAVLQRSSRFLKESVSTRRKQQGITMKLDELKNLTSQFQESMDNIMKQANDSLA-MLRESPGGMREKGRKARELAAA 2024
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKdTEEEELEIAALELEALEEAALE 294
|
330
....*....|.
gi 1431906468 2025 ANESAVKTLED 2035
Cdd:COG4372 295 LKLLALLLNLA 305
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1459-1513 |
2.28e-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: 46.58 E-value: 2.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 1459 CTCPHHPpfSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGSC 1513
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
715-739 |
5.45e-03 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 5.45e-03
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1582-1837 |
3.54e-101 |
|
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: 326.29 E-value: 3.54e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1582 VLSLN-LTGVSPAPYGILENLENTTKYFQRYLIKENAKKIRAEI---QLEGIAEQTENLQKELTRVLARHQKVNAEMERT 1657
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEIlekELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1658 SNGTQALATFIEQLHANIKEITEKVATLNQtarKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLL 1737
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1738 SRIQKRFQKPQEKLKALKEA-NSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSEL 1816
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANAlRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 1431906468 1817 IAKGREWVDAAGTHTAAAQDT 1837
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
25-275 |
2.56e-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: 305.44 E-value: 2.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 25 QQRGLFPAILNLATNAHISANATCGEKGPEMFCKLVehvpGRPVRHAQCRVCDgnSTNPRERHPISHAIDGTN----NWW 100
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLV----GHTEQGKKCDYCD--ARNPRRSHPAENLTDGNNpnnpTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 101 QSPSIQNGReyHWVTVTLDLRQVFQVAYIIIKAAnAPRPGNWILERSVDGVKFKPWQYYAvsdTECLTRYKITPRRGPPT 180
Cdd:smart00136 77 QSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 181 YrADNEVICTSYYSKLVPLEHGEIHTSLINGRPSADDP--SPQLLEFTSARYIRLRLQRIRTLNADLMtlshrdlrDLDP 258
Cdd:smart00136 151 G-NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 1431906468 259 IVTRRYYYSIKDISVGG 275
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
29-275 |
4.74e-86 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 281.39 E-value: 4.74e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 29 LFPAILNLATNAHISANATCGEKGPEMFCKLVEHVPGRpvrhaQCRVCDgnSTNPRERHPISHAIDGTNN----WWQSPS 104
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNGtnetWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 105 IQngREYHWVTVTLDLRQVFQVAYIIIKAAnAPRPGNWILERSVD-GVKFKPWQYYAvsdTECLTRYKITPRrgPPTYRA 183
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPSG--PSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 184 DNEVICTSYYSKLVPLEHGEIHTSLINGRPSA--DDPSPQLLEFTSARYIRLRLQRIRTLNADLMTlshrdlrdlDPIVT 261
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLGDELLD---------DPSVL 216
|
250
....*....|....
gi 1431906468 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 |
7.89e-55 |
|
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: 188.08 E-value: 7.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2018 ARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKT 2097
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431906468 2098 LEEN---LSRNLSEIKLLISRARKQVASIKVAVSADRDCIRAYQPQTSSTNYNTLILN 2152
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1225-1367 |
5.41e-49 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 171.30 E-value: 5.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1225 YWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGTGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQDYEVRMKEEFWKYf 1304
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 1305 nsVSEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGRKAvelpAEGEAALLLE 1367
Cdd:pfam00052 80 --SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG----GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
575-714 |
7.52e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 156.66 E-value: 7.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 575 YWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETvdSDLMSHADIIIKGNGLTISTRAEG-LSLQPYEEYFNVVRLVPENFR 653
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG--GSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 654 DfDTRREIDRDQLMTVLANVTHLLIRANYNSaKMALYRLDSVSLDIASPNAIDLaVAADVE 714
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYST-GSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
572-702 |
1.46e-43 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 155.50 E-value: 1.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 572 STYYWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETVdsdLMSHADIIIKGNGLTISTRAEGlSLQPYEEYFNVVRLVPEN 651
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGT---HVSAPDVILEGNGLRISHPAEG-PPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 652 FRDFDtRREIDRDQLMTVLANVTHLLIRANYnSAKMALYRLDSVSLDIASP 702
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATY-SQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2751-2880 |
3.33e-42 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 151.70 E-value: 3.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2751 IRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSVT 2830
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 2831 -VVGNATTLDVERKLYLGGLPSHYRARNIGTITHSIPACIGEIMVNGQQLD 2880
Cdd:pfam00054 81 sPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
1221-1351 |
6.55e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 145.10 E-value: 6.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1221 AEPFYWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGtGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQdyEVRMKEEF 1300
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGNGLRISHPAEGPPLPDELTTV--EVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 1301 WKYFNsvsEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGR 1351
Cdd:smart00281 79 WQYYG---GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAV 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2900-3053 |
3.50e-38 |
|
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: 141.02 E-value: 3.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2900 GTFFEGSGYAALVKEGYKvRLDLNITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRaar 2978
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 2979 aLCDGKWHTLQAHKSKHRIVLTVDGNSVRAESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 3053
Cdd:cd00110 77 -LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2314-2470 |
3.79e-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: 138.32 E-value: 3.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2314 SFHFDGSGYAMVEKTLRPTV-TQIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNG 2392
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTrLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431906468 2393 TWYKIAFQRNRKQGLLAVfdaydtsDKEtKQGETPGAASDLNRLEKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2470
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV-------DGE-RVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2923-3055 |
2.22e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 132.46 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2923 NITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRAaraLCDGKWHTLQAHKSKHRIVLTV 3001
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKgGGDYLALELRDGRLVLRYDLGSGPARLTSDPTP---LNDGQWHRVAVERNGRSVTLSV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 3002 DG-NSVRAESPHTHsTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRLSR 3055
Cdd:smart00282 78 DGgNRVSGESPGGL-TILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2724-2875 |
7.50e-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: 7.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2724 FGLSQNSHLVLPlNQSDVRKRLQVQLSIRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDG 2803
Cdd:cd00110 2 VSFSGSSYVRLP-TLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431906468 2804 KWHTVKTEYIKRKAFMTVDGQESPSVTVVGNATTLDVERKLYLGGLPSHYRARnIGTITHSIPACIGEIMVN 2875
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP-GLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2746-2877 |
1.97e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 126.69 E-value: 1.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2746 QVQLSIRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPAL-LSDGKWHTVKTEYIKRKAFMTVDGQ 2824
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 2825 ESPSVTVVGNATTLDVERKLYLGGLPSHYRARnIGTITHSIPACIGEIMVNGQ 2877
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLP-PLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2335-2472 |
7.75e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 125.14 E-value: 7.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2335 QIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLM-TDRRYNNGTWYKIAFQRNRKQGLLAVfda 2413
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTsDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 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 |
7.26e-32 |
|
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: 122.91 E-value: 7.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2495 SVSFLRGGYVEMPPKSL-SPESSLLATFATKNSSGILLVAlgkdaeeagGAQAHVPFFSIMLLEGRIEVHVNSGDGTslr 2573
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYA---------GSQNGGDFLALELEDGRLVLRYDLGSGS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2574 kALLHAPTgSYSDGQEHSISLVRNRRVITIQVDENSPVEMKLgPLTEGKTIDISNLYIGGLPEDKATPMLKMRTSFHGCI 2653
Cdd:cd00110 69 -LVLSSKT-PLNDGQWHSVSVERNGRSVTLSVDGERVVESGS-PGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 1431906468 2654 KNVVLD 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 |
1.02e-29 |
|
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: 115.98 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2928 FRTTSKNGVLLGISSAKVDAIGLEIVDGKVLFHVNNGAGRITATYQPRAaraLCDGKWHTLQAHKSKHRIVLTVDGNSVR 3007
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKN---LNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1431906468 3008 AESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 3053
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2340-2472 |
1.22e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 115.88 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2340 FSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNGTWYKIAFQRNRKQGLLAVfdaydtSDK 2419
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSV------DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 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 |
2.88e-29 |
|
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: 115.59 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2136 AYQPQTSSTNYNTLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEfPEVSINNNRWHSIYITR 2215
Cdd:cd00110 11 RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQWHSVSVER 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2216 FGNMGSLSVKeasaaENPPVRTSKSPGPskvLDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLN 2285
Cdd:cd00110 90 NGRSVTLSVD-----GERVVESGSPGGS---ALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2148-2287 |
3.60e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 114.74 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2148 TLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVSINNNRWHSIYITRFGNMGSLSVkea 2227
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2228 saaENPPVRTSKSPGPSKVLDINnsTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLNGK 2287
Cdd:smart00282 78 ---DGGNRVSGESPGGLTILNLD--GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2153-2290 |
1.70e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 109.71 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2153 VKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVsINNNRWHSIYITRFGNMGSLSVkeasaAEN 2232
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK-LNDGKWHSVELERNGRSGTLSV-----DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431906468 2233 PPVRTSKSPGPSKVLDINnsTLMFVGGLGGQI-KKSPAVKVTHFKGCMGEAFLNGKSIG 2290
Cdd:pfam00054 75 ARPTGESPLGATTDLDVD--GPLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2520-2659 |
1.94e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 109.74 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2520 TFATKNSSGILLVALGKDaeeaggaqaHVPFFSIMLLEGRIEVHVNSGDGTslrkALLHAPTGSYSDGQEHSISLVRNRR 2599
Cdd:smart00282 5 SFRTTSPNGLLLYAGSKG---------GGDYLALELRDGRLVLRYDLGSGP----ARLTSDPTPLNDGQWHRVAVERNGR 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2600 VITIQVDENSPVEMKLGPLTEGKTIDiSNLYIGGLPEDKATPMLKMRTSFHGCIKNVVLD 2659
Cdd:smart00282 72 SVTLSVDGGNRVSGESPGGLTILNLD-GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2521-2664 |
3.26e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 108.94 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2521 FATKNSSGILLValgkdaeeaGGAQAHVPFFSIMLLEGRIEVHVNSGDGtslrKALLHAPTGsYSDGQEHSISLVRNRRV 2600
Cdd:pfam00054 1 FRTTEPSGLLLY---------NGTQTERDFLALELRDGRLEVSYDLGSG----AAVVRSGDK-LNDGKWHSVELERNGRS 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431906468 2601 ITIQVDENSPV--EMKLGPLTEGKTIDisNLYIGGLPEDKATPMLK-MRTSFHGCIKNVVLDAQLLD 2664
Cdd:pfam00054 67 GTLSVDGEARPtgESPLGATTDLDVDG--PLYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
909-955 |
3.12e-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: 72.00 E-value: 3.12e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 909 CDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGLDTGLGC 955
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1598-2129 |
4.44e-15 |
|
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: 82.41 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1598 LENLENTTKYFQRYLIKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKE 1677
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1678 ITEKVATLN---QTARKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLlsriQKRFQKPQEKLKAL 1754
Cdd:TIGR02168 391 LELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL----QEELERLEEALEEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1755 KEANSLLsnhSEKLQAAEELLKEAGSKTqesnLLLLLVKANLKEFQEKKLRVQEEQN-------VTSELIAKGREW---V 1824
Cdd:TIGR02168 467 REELEEA---EQALDAAERELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSglsgilgVLSELISVDEGYeaaI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1825 DAA-GTHTAA-----------AQDTLTQLEHHRDELL----LWARKIRShvDDLVMQMSKRRARDLVHRAEQHASELQ-- 1886
Cdd:TIGR02168 540 EAAlGGRLQAvvvenlnaakkAIAFLKQNELGRVTFLpldsIKGTEIQG--NDREILKNIEGFLGVAKDLVKFDPKLRka 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1887 ------------SRAGALD---RDLENVRNVSLN-----------------ATSAAHVHSNIQTLTEEAEMLAADAHKTA 1934
Cdd:TIGR02168 618 lsyllggvlvvdDLDNALElakKLRPGYRIVTLDgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1935 NKTDLISESLASRGKAVLQRssrfLKESVSTRRKQQGITMKLDELKNLTSQFQESMDnimkQANDSLAMLRESPGGMREK 2014
Cdd:TIGR02168 698 KALAELRKELEELEEELEQL----RKELEELSRQISALRKDLARLEAEVEQLEERIA----QLSKELTELEAEIEELEER 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2015 GRKARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKP 2094
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
570 580 590
....*....|....*....|....*....|....*
gi 1431906468 2095 LKTLEENLSRNLSEIKLLISRARKQVASIKVAVSA 2129
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
908-956 |
1.22e-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: 70.08 E-value: 1.22e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 908 ACDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGLDT-GLGCV 956
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
909-955 |
3.02e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.88 E-value: 3.02e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 909 CDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGlDTGLGC 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 |
1.78e-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: 63.91 E-value: 1.78e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 404 CNCDPVGSLSSVCIKddrhadlangkWPGQCPCRKGYAGDKCDRCQFGYRGFPNCIPCDC 463
Cdd:pfam00053 1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1516-1553 |
5.09e-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: 5.09e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1431906468 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1553
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1516-1553 |
7.20e-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: 62.37 E-value: 7.20e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1431906468 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1553
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1516-1553 |
8.79e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 8.79e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1431906468 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1553
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1410-1456 |
1.23e-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: 61.60 E-value: 1.23e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1410 CNCNNH---SDVCDPETGKCLsCRDHTSGDHCELCASGYYGKVTGLPGDC 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. |
1051-1099 |
1.35e-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: 61.60 E-value: 1.35e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1431906468 1051 CNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGYRSFPDCVPCGC 1099
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
748-796 |
1.45e-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: 58.52 E-value: 1.45e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 748 PCECHGHAS---ECD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRgtPGDCQ 796
Cdd:cd00055 1 PCDCNGHGSlsgQCDpGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1097-1154 |
1.98e-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: 58.13 E-value: 1.98e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431906468 1097 CGCDLRGTLPDTCDLEqglcscsedGGTCSCKENAVGPQCSKCQAGTFALRGDNPQGC 1154
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
958-1002 |
3.54e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 3.54e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1431906468 958 CNCSVEGSVSDNC-TEEGQCHCGPGVSGKQCDRCSHGFYAFQDGGC 1002
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1409-1457 |
3.94e-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: 57.36 E-value: 3.94e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1431906468 1409 PCNCNNHSDV---CDPETGKCLsCRDHTSGDHCELCASGYYGkVTGLPGDCT 1457
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1598-2124 |
4.68e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1598 LENLENTTKYFQRYLIKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNG-------TQALATFIEQ 1670
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiarleerRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1671 LHANIKEITEKVATLNQTARkdfqppvsALQSMHQNISSLLGLIKErnftEMQQNATLELKAAKDLLSRIQKRFQKPQEK 1750
Cdd:COG1196 321 LEEELAELEEELEELEEELE--------ELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1751 LKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREwvdaAGTH 1830
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1831 TAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQHASELQ--SRAGALDRDLENVRNVSLnATS 1908
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEAAL-EAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1909 AAHVHSNIQTLTEEAEMLAADAHKTANK---TDLISESLASRGKAVLQRSSRFLKESV----STRRKQQGITMKLDELKN 1981
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAVdlvaSDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1982 LTSQFQESMDNIMKQAND--------SLAMLRESPGGMREKGRKARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRV 2053
Cdd:COG1196 624 GRTLVAARLEAALRRAVTlagrlrevTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 2054 NATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIkLLISRARKQVASIK 2124
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELERELERLE 773
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
403-456 |
6.88e-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: 6.88e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1431906468 403 PCNCDPVGSLSSVCIKDDrhadlangkwpGQCPCRKGYAGDKCDRCQFGYRGFP 456
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT-----------GQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
958-1005 |
7.34e-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: 56.59 E-value: 7.34e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1431906468 958 CNCSVEGSVSDNCTEE-GQCHCGPGVSGKQCDRCSHGFYAFQDGGCTPC 1005
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
855-907 |
1.37e-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: 1.37e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 855 PCNCSGNVDplEAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVTAKNCR 907
Cdd:cd00055 1 PCDCNGHGS--LSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
856-902 |
2.28e-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: 55.44 E-value: 2.28e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 856 CNCSGNVDPleAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVT 902
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
461-507 |
3.28e-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: 54.67 E-value: 3.28e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 461 CDCRTVGSLNeDPCIE---PCLCKKNVEGKNCDRCKPGFYNLKERNPEGC 507
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1050-1093 |
5.32e-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: 54.28 E-value: 5.32e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1431906468 1050 ACNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGYRSFPD 1093
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
749-795 |
7.24e-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: 53.90 E-value: 7.24e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 749 CECHGHAS---ECDIH-GICsVCTHNTTGDHCEQCLPGFYGTPSrGTPGDC 795
Cdd:pfam00053 1 CDCNPHGSlsdTCDPEtGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
957-1003 |
1.01e-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: 53.51 E-value: 1.01e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 957 PCNCSVEGSVSDNCTEE-GQCHCGPGVSGKQCDRCSHGFY--AFQDGGCT 1003
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYglPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1051-1094 |
1.26e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.26e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1431906468 1051 CNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGY--RSFPDC 1094
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1410-1456 |
1.33e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.33e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1410 CNCN---NHSDVCDPETGKCLsCRDHTSGDHCELCASGYYGKVtglPGDC 1456
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
404-458 |
1.36e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1431906468 404 CNCDPVGSLSSVCIKDDrhadlangkwpGQCPCRKGYAGDKCDRCQFGYRG--FPNC 458
Cdd:smart00180 1 CDCDPGGSASGTCDPDT-----------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1613-2138 |
1.60e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1613 IKENAKKIRAEIQ-LEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITE--KVATLNQTA 1689
Cdd:PRK03918 219 LREELEKLEKEVKeLEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1690 RKDFQPPVSALQSMHQNISSLLGLIK--ERNFTEmqqnatLELKAAKdlLSRIQKRFQKPQEKLKALKEANSLLSNHSEK 1767
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINgiEERIKE------LEEKEER--LEELKKKLKELEKRLEELEERHELYEEAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1768 LQAAEELLKEAGSKTQESnlllllVKANLKEFQEKKLRVQEEqnvTSELIAKGREWVDAAGTHTAA------AQDT---- 1837
Cdd:PRK03918 371 KEELERLKKRLTGLTPEK------LEKELEELEKAKEEIEEE---ISKITARIGELKKEIKELKKAieelkkAKGKcpvc 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1838 ---LTqlEHHRDELLlwarkirshvddlvmqmskRRARDLVHRAEQHASELQSRAGALDRDLENVRNVslnatsaahvhs 1914
Cdd:PRK03918 442 greLT--EEHRKELL-------------------EEYTAELKRIEKELKEIEEKERKLRKELRELEKV------------ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1915 niqtLTEEAEMLAadAHKTANKTDLISESLASRGKAVLQRSS---RFLKESVSTRRKQQGITM----KLDELKNLTSQFQ 1987
Cdd:PRK03918 489 ----LKKESELIK--LKELAEQLKELEEKLKKYNLEELEKKAeeyEKLKEKLIKLKGEIKSLKkeleKLEELKKKLAELE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1988 ESMDNIMKQANDSLAMLRE-SPGGMREKGRKARELAAAANE-----SAVKTLEDVL----ALSLRVFNTSEDLSRVNATV 2057
Cdd:PRK03918 563 KKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEylelkDAEKELEREEkelkKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2058 QET----NDLLHN-STMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIKL---LISRARKQVASIKVA--- 2126
Cdd:PRK03918 643 EELrkelEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEeleEREKAKKELEKLEKAler 722
|
570
....*....|..
gi 1431906468 2127 VSADRDCIRAYQ 2138
Cdd:PRK03918 723 VEELREKVKKYK 734
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1004-1049 |
1.69e-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: 52.74 E-value: 1.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1004 PCDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGLDPE-QGCQ 1049
Cdd:cd00055 1 PCDCnghGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
798-853 |
2.97e-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: 2.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1431906468 798 CACPLSIDSnnfSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGGTC 853
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETG---QC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1097-1154 |
3.13e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431906468 1097 CGCDLRGTLPDTCDLeqglcscseDGGTCSCKENAVGPQCSKCQAGTFalrGDNPQGC 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 |
3.54e-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: 3.54e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1431906468 1005 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGL--DPEQGC 1048
Cdd:pfam00053 1 CDCnphGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
277-324 |
3.56e-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: 51.97 E-value: 3.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 277 CICYGHAS---SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPGT 324
Cdd:cd00055 2 CDCNGHGSlsgQC----DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1005-1048 |
6.92e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 6.92e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 1005 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGlDPEQGC 1048
Cdd:smart00180 1 CDCdpgGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
460-507 |
1.12e-07 |
|
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: 50.43 E-value: 1.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 460 PCDCRTVGSLNEDpCIEP---CLCKKNVEGKNCDRCKPGFYNLKERnPEGC 507
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGtgqCECKPNTTGRRCDRCAPGYYGLPSQ-GGGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1096-1154 |
6.10e-07 |
|
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: 48.50 E-value: 6.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431906468 1096 PCGCDLRGTLPDTCDLEqglcscsedGGTCSCKENAVGPQCSKCQAGTFALRgDNPQGC 1154
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1711-2035 |
6.56e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1711 LGLIKERNFTEMQQNATLE-LKAAKDLLSRIQKRFQKPQEKLKALKE----ANSLLSNHSEKLQAAEELLKEAGSKTQES 1785
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEqLRKALFELDKLQEELEQLREELEQAREeleqLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1786 NLLLLLVKANLKEFQEKKLRVQEEqnvtseliakgrewvdaagthtaaaqdtLTQLEHHRDELLLWARKIRSHVDDLVMQ 1865
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEE----------------------------LEELQKERQDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1866 MSKRRARdlvhraeqhASELQSRAGALDRDLENVRNvSLNATSAAHVHSNIQTLTEEAEMLAADAHKTANKTDLISESLA 1945
Cdd:COG4372 145 IAEREEE---------LKELEEQLESLQEELAALEQ-ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1946 SRGKAVLQRSSRFLKESVSTRRKQQGITMKLDELKNLTSQFQESMDNIMKQANDSLA-MLRESPGGMREKGRKARELAAA 2024
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKdTEEEELEIAALELEALEEAALE 294
|
330
....*....|.
gi 1431906468 2025 ANESAVKTLED 2035
Cdd:COG4372 295 LKLLALLLNLA 305
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
749-790 |
7.34e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 7.34e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1431906468 749 CECH--GHASE-CD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRG 790
Cdd:smart00180 1 CDCDpgGSASGtCDpDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
461-507 |
1.01e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.69 E-value: 1.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 461 CDCRTVGSLNeDPCIEP---CLCKKNVEGKNCDRCKPGFYNlkeRNPEGC 507
Cdd:smart00180 1 CDCDPGGSAS-GTCDPDtgqCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
855-899 |
1.84e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 1.84e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1431906468 855 PCNCSGNVDPleagHCDSVTGECLkCLWNTDGAHCERCADGFYGD 899
Cdd:smart00180 2 DCDPGGSASG----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1601-2133 |
1.98e-06 |
|
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: 53.90 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1601 LENTTKYFQ-RYLIKENAKKiraeiQLEGIAEQT-ENLQKELTRVLARHQKVNAEMERTSNGTQALatfIEQLHANIKEI 1678
Cdd:TIGR00606 267 LDNEIKALKsRKKQMEKDNS-----ELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1679 T-EKVATLNQTARKDFQPPVSALQSMHQNISSL-LGLIKERNFTEMQQNATLELKAAKDLLSRIQKRfqkpqeklKAlKE 1756
Cdd:TIGR00606 339 NqEKTELLVEQGRLQLQADRHQEHIRARDSLIQsLATRLELDGFERGPFSERQIKNFHTLVIERQED--------EA-KT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1757 ANSLLSNhsekLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKlrVQEEQNVTSELiakgrewvdaagthtaaaqd 1836
Cdd:TIGR00606 410 AAQLCAD----LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK--QEELKFVIKEL-------------------- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1837 tlTQLEHHRDELLLWARKIRSHVDDLvmqmSKRRARDLVHRAEQHASELQSRAGALDRDL--ENVRNVSLNAtsaaHVHS 1914
Cdd:TIGR00606 464 --QQLEGSSDRILELDQELRKAEREL----SKAEKNSLTETLKKEVKSLQNEKADLDRKLrkLDQEMEQLNH----HTTT 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1915 NIQTLTEEAEMLAADAHKTANK----------------TDLISESLASRGKAVLQRSSRFLKESVSTRRKQQGITMKLDE 1978
Cdd:TIGR00606 534 RTQMEMLTKDKMDKDEQIRKIKsrhsdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1979 LKNLTSQFQESMDNIMK----QANDS-LAMLRESpggmREKGRKARE-LAAAAN--ESAVKTLED----VLALSLRVFNT 2046
Cdd:TIGR00606 614 LESKEEQLSSYEDKLFDvcgsQDEESdLERLKEE----IEKSSKQRAmLAGATAvySQFITQLTDenqsCCPVCQRVFQT 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2047 SEDLSRVNATVQETNDLL---HNSTMTTLLAGRKMKD-----MEMQANLLLDRLKPLKTLEE---NLSRNLSEIKLLISR 2115
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLApdkLKSTESELKKKEKRRDemlglAPGRQSIIDLKEKEIPELRNklqKVNRDIQRLKNDIEE 769
|
570
....*....|....*...
gi 1431906468 2116 ARKQVASIKVAVSADRDC 2133
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVC 787
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1459-1513 |
2.28e-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: 46.58 E-value: 2.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 1459 CTCPHHPpfSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGSC 1513
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
797-851 |
6.11e-06 |
|
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: 45.42 E-value: 6.11e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 797 PCACPLSIDSNnfsPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGG 851
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTG---QC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1838-2092 |
6.18e-06 |
|
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: 50.49 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1838 LTQLEHHRDELLLWARKIRSHVDDlvMQMSKRRARDLvhraEQHASELQSRAGALDRDLENVRNVSlNATSaahvhSNIQ 1917
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQ--IEILEKELSSL----AQETEELQKKATQTLAKAQQVNAES-ERTL-----GHAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1918 TLTEEAEMLAADAHKTANKTDLISE--SLASRGK--AVLQRSSRFLKE--SVSTRRKQQGITMKLDELKNLTSQFQESMD 1991
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLGEndFALPSSDlsRMLAEAQRMLGEirSRDFGTQLQNAEAELKAAQDLLSRIQTWFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1992 NIMKQANDSLAMLRESPGGMREKGRKARELaaaANESAVKTlEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNstmtT 2071
Cdd:pfam06008 166 SPQEENKALANALRDSLAEYEAKLSDLREL---LREAAAKT-RDANRLNLANQANLREFQRKKEEVSEQKNQLEE----T 237
|
250 260
....*....|....*....|.
gi 1431906468 2072 LLAGRkmkDMEMQANLLLDRL 2092
Cdd:pfam06008 238 LKTAR---DSLDAANLLLQEI 255
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1458-1514 |
1.65e-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: 44.27 E-value: 1.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1431906468 1458 PCTCPHHPpfSFSPTCVVEgdsDFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGsCQ 1514
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
716-910 |
2.42e-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: 46.91 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 716 CECPQGY---TGTSCEACLPGyyrvdgilfggicqpcechghasecdiHGICSVCTHNTTGdhCEQCLPGFYGTPSRGTP 792
Cdd:cd13416 1 EACPSGQytsSGECCEQCPPG---------------------------EGVARPCGDNQTV--CEPCLDGVTFSDVVSHT 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 793 GDCQPCA-CPLSIdsnnfSPTCHLTDGEEVVCdqcapgysgswceRCADGYYgnPTVPGGTCVPCNCsgnvdpleaghCD 871
Cdd:cd13416 52 EPCQPCTrCPGLM-----SMRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCEPCTV-----------CP 100
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1431906468 872 SVTGECLKCLWNTDgAHCERCADGFYGDAVTAKN----CRACD 910
Cdd:cd13416 101 PGQGVVQSCGPNQD-TVCEACPEGTYSDEDSSTDpclpCTVCE 142
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
798-846 |
3.76e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.07 E-value: 3.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1431906468 798 CACPLSidsNNFSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNP 846
Cdd:smart00180 1 CDCDPG---GSASGTCDPDTG---QC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
277-320 |
1.01e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 1.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 277 CICY--GHAS-SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPW 320
Cdd:smart00180 1 CDCDpgGSASgTC----DPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1459-1506 |
1.23e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1431906468 1459 CTCphHPPFSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNP 1506
Cdd:smart00180 1 CDC--DPGGSASGTCDPDT---GQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
277-323 |
2.31e-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: 38.10 E-value: 2.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 277 CICYGHASSCPwDEEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPG 323
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
715-739 |
5.45e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 5.45e-03
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
715-747 |
9.03e-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: 9.03e-03
10 20 30
....*....|....*....|....*....|...
gi 1431906468 715 HCECPQGYTGTSCEACLPGYYRVDGILFGgiCQ 747
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1582-1837 |
3.54e-101 |
|
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: 326.29 E-value: 3.54e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1582 VLSLN-LTGVSPAPYGILENLENTTKYFQRYLIKENAKKIRAEI---QLEGIAEQTENLQKELTRVLARHQKVNAEMERT 1657
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEIlekELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1658 SNGTQALATFIEQLHANIKEITEKVATLNQtarKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLL 1737
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1738 SRIQKRFQKPQEKLKALKEA-NSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSEL 1816
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANAlRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 1431906468 1817 IAKGREWVDAAGTHTAAAQDT 1837
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
25-275 |
2.56e-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: 305.44 E-value: 2.56e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 25 QQRGLFPAILNLATNAHISANATCGEKGPEMFCKLVehvpGRPVRHAQCRVCDgnSTNPRERHPISHAIDGTN----NWW 100
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGEPGPERYCKLV----GHTEQGKKCDYCD--ARNPRRSHPAENLTDGNNpnnpTWW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 101 QSPSIQNGReyHWVTVTLDLRQVFQVAYIIIKAAnAPRPGNWILERSVDGVKFKPWQYYAvsdTECLTRYKITPRRGPPT 180
Cdd:smart00136 77 QSEPLSNGP--QNVNLTLDLGKEFHVTYVILKFC-SPRPSLWILERSDFGKTWQPWQYFS---SDCRRTFGRPPRGPITK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 181 YrADNEVICTSYYSKLVPLEHGEIHTSLINGRPSADDP--SPQLLEFTSARYIRLRLQRIRTLNADLMtlshrdlrDLDP 258
Cdd:smart00136 151 G-NEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFdnSPVLQEWVTATNIRVRLTRLRTLGDELM--------DDRP 221
|
250
....*....|....*..
gi 1431906468 259 IVTRRYYYSIKDISVGG 275
Cdd:smart00136 222 EVTRRYYYAISDIAVGG 238
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
29-275 |
4.74e-86 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 281.39 E-value: 4.74e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 29 LFPAILNLATNAHISANATCGEKGPEMFCKLVEHVPGRpvrhaQCRVCDgnSTNPRERHPISHAIDGTNN----WWQSPS 104
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPERYCILSGLEGGK-----KCFICD--SRDPHNSHPPSNLTDSNNGtnetWWQSET 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 105 IQngREYHWVTVTLDLRQVFQVAYIIIKAAnAPRPGNWILERSVD-GVKFKPWQYYAvsdTECLTRYKITPRrgPPTYRA 183
Cdd:pfam00055 74 GV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDfGKTWQPYQYFA---SDCRRTFGRPSG--PSRGIK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 184 DNEVICTSYYSKLVPLEHGEIHTSLINGRPSA--DDPSPQLLEFTSARYIRLRLQRIRTLNADLMTlshrdlrdlDPIVT 261
Cdd:pfam00055 146 DDEVICTSEYSDISPLTGGEVIFSTLEGRPSAniFDYSPELQDWLTATNIRIRLLRLHTLGDELLD---------DPSVL 216
|
250
....*....|....
gi 1431906468 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 |
7.89e-55 |
|
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: 188.08 E-value: 7.89e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2018 ARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKT 2097
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431906468 2098 LEEN---LSRNLSEIKLLISRARKQVASIKVAVSADRDCIRAYQPQTSSTNYNTLILN 2152
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1225-1367 |
5.41e-49 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 171.30 E-value: 5.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1225 YWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGTGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQDYEVRMKEEFWKYf 1304
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 1305 nsVSEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGRKAvelpAEGEAALLLE 1367
Cdd:pfam00052 80 --SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG----GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
575-714 |
7.52e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 156.66 E-value: 7.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 575 YWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETvdSDLMSHADIIIKGNGLTISTRAEG-LSLQPYEEYFNVVRLVPENFR 653
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG--GSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 654 DfDTRREIDRDQLMTVLANVTHLLIRANYNSaKMALYRLDSVSLDIASPNAIDLaVAADVE 714
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYST-GSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
572-702 |
1.46e-43 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 155.50 E-value: 1.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 572 STYYWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETVdsdLMSHADIIIKGNGLTISTRAEGlSLQPYEEYFNVVRLVPEN 651
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGT---HVSAPDVILEGNGLRISHPAEG-PPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 652 FRDFDtRREIDRDQLMTVLANVTHLLIRANYnSAKMALYRLDSVSLDIASP 702
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATY-SQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2751-2880 |
3.33e-42 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 151.70 E-value: 3.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2751 IRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSVT 2830
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 2831 -VVGNATTLDVERKLYLGGLPSHYRARNIGTITHSIPACIGEIMVNGQQLD 2880
Cdd:pfam00054 81 sPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
1221-1351 |
6.55e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 145.10 E-value: 6.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1221 AEPFYWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGtGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQdyEVRMKEEF 1300
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGNGLRISHPAEGPPLPDELTTV--EVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 1301 WKYFNsvsEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGR 1351
Cdd:smart00281 79 WQYYG---GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAV 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2900-3053 |
3.50e-38 |
|
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: 141.02 E-value: 3.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2900 GTFFEGSGYAALVKEGYKvRLDLNITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRaar 2978
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 2979 aLCDGKWHTLQAHKSKHRIVLTVDGNSVRAESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 3053
Cdd:cd00110 77 -LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2314-2470 |
3.79e-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: 138.32 E-value: 3.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2314 SFHFDGSGYAMVEKTLRPTV-TQIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNG 2392
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTrLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1431906468 2393 TWYKIAFQRNRKQGLLAVfdaydtsDKEtKQGETPGAASDLNRLEKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2470
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV-------DGE-RVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2923-3055 |
2.22e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 132.46 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2923 NITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRAaraLCDGKWHTLQAHKSKHRIVLTV 3001
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKgGGDYLALELRDGRLVLRYDLGSGPARLTSDPTP---LNDGQWHRVAVERNGRSVTLSV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 3002 DG-NSVRAESPHTHsTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRLSR 3055
Cdd:smart00282 78 DGgNRVSGESPGGL-TILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2724-2875 |
7.50e-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: 7.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2724 FGLSQNSHLVLPlNQSDVRKRLQVQLSIRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDG 2803
Cdd:cd00110 2 VSFSGSSYVRLP-TLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1431906468 2804 KWHTVKTEYIKRKAFMTVDGQESPSVTVVGNATTLDVERKLYLGGLPSHYRARnIGTITHSIPACIGEIMVN 2875
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP-GLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2746-2877 |
1.97e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 126.69 E-value: 1.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2746 QVQLSIRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPAL-LSDGKWHTVKTEYIKRKAFMTVDGQ 2824
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 2825 ESPSVTVVGNATTLDVERKLYLGGLPSHYRARnIGTITHSIPACIGEIMVNGQ 2877
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLP-PLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2335-2472 |
7.75e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 125.14 E-value: 7.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2335 QIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLM-TDRRYNNGTWYKIAFQRNRKQGLLAVfda 2413
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTsDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 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 |
7.26e-32 |
|
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: 122.91 E-value: 7.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2495 SVSFLRGGYVEMPPKSL-SPESSLLATFATKNSSGILLVAlgkdaeeagGAQAHVPFFSIMLLEGRIEVHVNSGDGTslr 2573
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYA---------GSQNGGDFLALELEDGRLVLRYDLGSGS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2574 kALLHAPTgSYSDGQEHSISLVRNRRVITIQVDENSPVEMKLgPLTEGKTIDISNLYIGGLPEDKATPMLKMRTSFHGCI 2653
Cdd:cd00110 69 -LVLSSKT-PLNDGQWHSVSVERNGRSVTLSVDGERVVESGS-PGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 1431906468 2654 KNVVLD 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 |
1.02e-29 |
|
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: 115.98 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2928 FRTTSKNGVLLGISSAKVDAIGLEIVDGKVLFHVNNGAGRITATYQPRAaraLCDGKWHTLQAHKSKHRIVLTVDGNSVR 3007
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKN---LNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1431906468 3008 AESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 3053
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2340-2472 |
1.22e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 115.88 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2340 FSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNGTWYKIAFQRNRKQGLLAVfdaydtSDK 2419
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSV------DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 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 |
2.88e-29 |
|
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: 115.59 E-value: 2.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2136 AYQPQTSSTNYNTLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEfPEVSINNNRWHSIYITR 2215
Cdd:cd00110 11 RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQWHSVSVER 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2216 FGNMGSLSVKeasaaENPPVRTSKSPGPskvLDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLN 2285
Cdd:cd00110 90 NGRSVTLSVD-----GERVVESGSPGGS---ALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2148-2287 |
3.60e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 114.74 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2148 TLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVSINNNRWHSIYITRFGNMGSLSVkea 2227
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2228 saaENPPVRTSKSPGPSKVLDINnsTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLNGK 2287
Cdd:smart00282 78 ---DGGNRVSGESPGGLTILNLD--GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2928-3058 |
9.83e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 113.18 E-value: 9.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2928 FRTTSKNGVLL-GISSAKVDAIGLEIVDGKVLFHVNNGAGRITATYQPRaaraLCDGKWHTLQAHKSKHRIVLTVDGN-S 3005
Cdd:pfam00054 1 FRTTEPSGLLLyNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK----LNDGKWHSVELERNGRSGTLSVDGEaR 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1431906468 3006 VRAESPHTHSTSADTNDPIYVGGYPAHIKQN-CLSSRASFRGCVRNLRLSRGSQ 3058
Cdd:pfam00054 77 PTGESPLGATTDLDVDGPLYVGGLPSLGVKKrRLAISPSFDGCIRDVIVNGKPL 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2153-2290 |
1.70e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 109.71 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2153 VKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVsINNNRWHSIYITRFGNMGSLSVkeasaAEN 2232
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK-LNDGKWHSVELERNGRSGTLSV-----DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431906468 2233 PPVRTSKSPGPSKVLDINnsTLMFVGGLGGQI-KKSPAVKVTHFKGCMGEAFLNGKSIG 2290
Cdd:pfam00054 75 ARPTGESPLGATTDLDVD--GPLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2520-2659 |
1.94e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 109.74 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2520 TFATKNSSGILLVALGKDaeeaggaqaHVPFFSIMLLEGRIEVHVNSGDGTslrkALLHAPTGSYSDGQEHSISLVRNRR 2599
Cdd:smart00282 5 SFRTTSPNGLLLYAGSKG---------GGDYLALELRDGRLVLRYDLGSGP----ARLTSDPTPLNDGQWHRVAVERNGR 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2600 VITIQVDENSPVEMKLGPLTEGKTIDiSNLYIGGLPEDKATPMLKMRTSFHGCIKNVVLD 2659
Cdd:smart00282 72 SVTLSVDGGNRVSGESPGGLTILNLD-GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2521-2664 |
3.26e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 108.94 E-value: 3.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2521 FATKNSSGILLValgkdaeeaGGAQAHVPFFSIMLLEGRIEVHVNSGDGtslrKALLHAPTGsYSDGQEHSISLVRNRRV 2600
Cdd:pfam00054 1 FRTTEPSGLLLY---------NGTQTERDFLALELRDGRLEVSYDLGSG----AAVVRSGDK-LNDGKWHSVELERNGRS 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431906468 2601 ITIQVDENSPV--EMKLGPLTEGKTIDisNLYIGGLPEDKATPMLK-MRTSFHGCIKNVVLDAQLLD 2664
Cdd:pfam00054 67 GTLSVDGEARPtgESPLGATTDLDVDG--PLYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2340-2470 |
1.55e-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: 106.74 E-value: 1.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2340 FSTFSPNGLLFYlASNGTKDFLSIELVRGRVKVMVDLGSGPLTLM-TDRRYNNGTWYKIAFQRNRKQGLLAVfdaydtsD 2418
Cdd:pfam02210 1 FRTRQPNGLLLY-AGGGGSDFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTLSV-------D 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1431906468 2419 KETKQGETPGAASDLNRLEKDLiYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2470
Cdd:pfam02210 73 GQTVVSSLPPGESLLLNLNGPL-YLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2521-2661 |
9.61e-23 |
|
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: 95.95 E-value: 9.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2521 FATKNSSGILLVALGKDAEeaggaqahvpFFSIMLLEGRIEVHVNSGDGTslrkALLHAPTGSYSDGQEHSISLVRNRRV 2600
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSD----------FLALELVNGRLVLRYDLGSGP----ESLLSSGKNLNDGQWHSVRVERNGNT 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 2601 ITIQVDENSPVEMKLGPLTEGKTIDiSNLYIGGLPEDKATPMLKMRTSFHGCIKNVVLDAQ 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 ... |
2153-2287 |
1.74e-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: 95.18 E-value: 1.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2153 VKTQEPDNLLFYLGSSSSsDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVSINNNRWHSIYITRFGNMGSLSVKEasaaen 2232
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDG------ 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 2233 ppVRTSKSPGPSKVLDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLNGK 2287
Cdd:pfam02210 74 --QTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2751-2877 |
2.29e-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: 2.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2751 IRTFASSGLIYYVAHQNQmDYATLQLQEGRLHFMFDLGKGRTKV-SHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSV 2829
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLlSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1431906468 2830 TVVGNATTLDVERKLYLGGLPSHYRARNIGTiTHSIPACIGEIMVNGQ 2877
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPV-RAGFVGCIRDVRVNGE 126
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
909-955 |
3.12e-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: 72.00 E-value: 3.12e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 909 CDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGLDTGLGC 955
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1598-2129 |
4.44e-15 |
|
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: 82.41 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1598 LENLENTTKYFQRYLIKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKE 1677
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1678 ITEKVATLN---QTARKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLlsriQKRFQKPQEKLKAL 1754
Cdd:TIGR02168 391 LELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL----QEELERLEEALEEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1755 KEANSLLsnhSEKLQAAEELLKEAGSKTqesnLLLLLVKANLKEFQEKKLRVQEEQN-------VTSELIAKGREW---V 1824
Cdd:TIGR02168 467 REELEEA---EQALDAAERELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSglsgilgVLSELISVDEGYeaaI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1825 DAA-GTHTAA-----------AQDTLTQLEHHRDELL----LWARKIRShvDDLVMQMSKRRARDLVHRAEQHASELQ-- 1886
Cdd:TIGR02168 540 EAAlGGRLQAvvvenlnaakkAIAFLKQNELGRVTFLpldsIKGTEIQG--NDREILKNIEGFLGVAKDLVKFDPKLRka 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1887 ------------SRAGALD---RDLENVRNVSLN-----------------ATSAAHVHSNIQTLTEEAEMLAADAHKTA 1934
Cdd:TIGR02168 618 lsyllggvlvvdDLDNALElakKLRPGYRIVTLDgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1935 NKTDLISESLASRGKAVLQRssrfLKESVSTRRKQQGITMKLDELKNLTSQFQESMDnimkQANDSLAMLRESPGGMREK 2014
Cdd:TIGR02168 698 KALAELRKELEELEEELEQL----RKELEELSRQISALRKDLARLEAEVEQLEERIA----QLSKELTELEAEIEELEER 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2015 GRKARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKP 2094
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
570 580 590
....*....|....*....|....*....|....*
gi 1431906468 2095 LKTLEENLSRNLSEIKLLISRARKQVASIKVAVSA 2129
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
908-956 |
1.22e-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: 70.08 E-value: 1.22e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 908 ACDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGLDT-GLGCV 956
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
909-955 |
3.02e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.88 E-value: 3.02e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 909 CDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGlDTGLGC 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 ... |
1612-2161 |
5.21e-14 |
|
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: 78.68 E-value: 5.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1612 LIKENAKKIRAEIQLEGIAEQTENLQKE---LTRVLARHQKVNAEME----RTSNGTQALATFIEQLHANIKEITEKVAT 1684
Cdd:pfam01576 14 LQKVKERQQKAESELKELEKKHQQLCEEknaLQEQLQAETELCAEAEemraRLAARKQELEEILHELESRLEEEEERSQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1685 LnQTARKDFQPPV-----------SALQSMHQNISSLLGLIK---ERNFTEMQQNATL--ELKAAKDLLSRIQKRFQKPQ 1748
Cdd:pfam01576 94 L-QNEKKKMQQHIqdleeqldeeeAARQKLQLEKVTTEAKIKkleEDILLLEDQNSKLskERKLLEERISEFTSNLAEEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1749 EKLKALkeaNSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEK--KLRVQEEQnVTSELIAKGREwvda 1826
Cdd:pfam01576 173 EKAKSL---SKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQiaELQAQIAE-LRAQLAKKEEE---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1827 agthTAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQM-SKRRARDlvhRAEQHASELQSRAGALDRDLENvrnvSLN 1905
Cdd:pfam01576 245 ----LQAALARLEEETAQKNNALKKIRELEAQISELQEDLeSERAARN---KAEKQRRDLGEELEALKTELED----TLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1906 ATSA---------AHVHSNIQTLTEEAEM----LAADAHKTANKTDLISESL--ASRGKAVLQRSSRFLKE-----SVST 1965
Cdd:pfam01576 314 TTAAqqelrskreQEVTELKKALEEETRSheaqLQEMRQKHTQALEELTEQLeqAKRNKANLEKAKQALESenaelQAEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1966 RRKQQGITMKLDELKNLTSQFQEsmdnIMKQANDSlamlrespggMREKGRKARELAAAANE--SAVKTLEDVLALSLRV 2043
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKLEGQLQE----LQARLSES----------ERQRAELAEKLSKLQSEleSVSSLLNEAEGKNIKL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2044 fntSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIKLLISRARKQVASI 2123
Cdd:pfam01576 460 ---SKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
|
570 580 590
....*....|....*....|....*....|....*...
gi 1431906468 2124 KVAVSADRDCIRAYQPQTSSTnynTLILNVKTQEPDNL 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 |
1.78e-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: 63.91 E-value: 1.78e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 404 CNCDPVGSLSSVCIKddrhadlangkWPGQCPCRKGYAGDKCDRCQFGYRGFPNCIPCDC 463
Cdd:pfam00053 1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1516-1553 |
5.09e-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: 5.09e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1431906468 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1553
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1516-1553 |
7.20e-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: 62.37 E-value: 7.20e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1431906468 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1553
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1516-1553 |
8.79e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 8.79e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1431906468 1516 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1553
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1410-1456 |
1.23e-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: 61.60 E-value: 1.23e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1410 CNCNNH---SDVCDPETGKCLsCRDHTSGDHCELCASGYYGKVTGLPGDC 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. |
1051-1099 |
1.35e-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: 61.60 E-value: 1.35e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1431906468 1051 CNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGYRSFPDCVPCGC 1099
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
748-796 |
1.45e-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: 58.52 E-value: 1.45e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 748 PCECHGHAS---ECD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRgtPGDCQ 796
Cdd:cd00055 1 PCDCNGHGSlsgQCDpGTGQC-ECKPNTTGRRCDRCAPGYYGLPSQ--GGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1097-1154 |
1.98e-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: 58.13 E-value: 1.98e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431906468 1097 CGCDLRGTLPDTCDLEqglcscsedGGTCSCKENAVGPQCSKCQAGTFALRGDNPQGC 1154
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
958-1002 |
3.54e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 3.54e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1431906468 958 CNCSVEGSVSDNC-TEEGQCHCGPGVSGKQCDRCSHGFYAFQDGGC 1002
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1409-1457 |
3.94e-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: 57.36 E-value: 3.94e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1431906468 1409 PCNCNNHSDV---CDPETGKCLsCRDHTSGDHCELCASGYYGkVTGLPGDCT 1457
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1598-2124 |
4.68e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 4.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1598 LENLENTTKYFQRYLIKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNG-------TQALATFIEQ 1670
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiarleerRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1671 LHANIKEITEKVATLNQTARkdfqppvsALQSMHQNISSLLGLIKErnftEMQQNATLELKAAKDLLSRIQKRFQKPQEK 1750
Cdd:COG1196 321 LEEELAELEEELEELEEELE--------ELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1751 LKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREwvdaAGTH 1830
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1831 TAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQHASELQ--SRAGALDRDLENVRNVSLnATS 1908
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEAAL-EAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1909 AAHVHSNIQTLTEEAEMLAADAHKTANK---TDLISESLASRGKAVLQRSSRFLKESV----STRRKQQGITMKLDELKN 1981
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAVdlvaSDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1982 LTSQFQESMDNIMKQAND--------SLAMLRESPGGMREKGRKARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRV 2053
Cdd:COG1196 624 GRTLVAARLEAALRRAVTlagrlrevTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 2054 NATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIkLLISRARKQVASIK 2124
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELERELERLE 773
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
403-456 |
6.88e-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: 6.88e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1431906468 403 PCNCDPVGSLSSVCIKDDrhadlangkwpGQCPCRKGYAGDKCDRCQFGYRGFP 456
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGT-----------GQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
958-1005 |
7.34e-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: 56.59 E-value: 7.34e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1431906468 958 CNCSVEGSVSDNCTEE-GQCHCGPGVSGKQCDRCSHGFYAFQDGGCTPC 1005
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
855-907 |
1.37e-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: 1.37e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 855 PCNCSGNVDplEAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVTAKNCR 907
Cdd:cd00055 1 PCDCNGHGS--LSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
856-902 |
2.28e-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: 55.44 E-value: 2.28e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 856 CNCSGNVDPleAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVT 902
Cdd:pfam00053 1 CDCNPHGSL--SDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
461-507 |
3.28e-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: 54.67 E-value: 3.28e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 461 CDCRTVGSLNeDPCIE---PCLCKKNVEGKNCDRCKPGFYNLKERNPEGC 507
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1050-1093 |
5.32e-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: 54.28 E-value: 5.32e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1431906468 1050 ACNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGYRSFPD 1093
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1622-1827 |
5.76e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1622 AEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLNQ---TARKDFQPPVS 1698
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1699 ALQSMHQNISSLLGLIKERNFTEMQQNATL---ELKAAKDLLSRIQKRfqkpQEKLKALK-EANSLLSNHSEKLQAAEEL 1774
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFSDFLDRLSAlskIADADADLLEELKAD----KAELEAKKaELEAKLAELEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 1775 LKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVDAA 1827
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
749-795 |
7.24e-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: 53.90 E-value: 7.24e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 749 CECHGHAS---ECDIH-GICsVCTHNTTGDHCEQCLPGFYGTPSrGTPGDC 795
Cdd:pfam00053 1 CDCNPHGSlsdTCDPEtGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1655-2021 |
7.80e-09 |
|
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: 61.61 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1655 ERTSNGTQALATFIEQLHANIKEITEKVATLNQTarkdfqppVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAK 1734
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKA--------LAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1735 dLLSRIQKRFQKPQEKLKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTS 1814
Cdd:TIGR02168 738 -LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1815 ELIAKGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKRRAR-----DLVHRAEQHASELQSRA 1889
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleallNERASLEEALALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1890 GALDRDLENVRNvslnatsaaHVHSNIQTLTEEAEMLAA---DAHKTANKTDLISESLASRGK----AVLQRSSRFLKES 1962
Cdd:TIGR02168 897 EELSEELRELES---------KRSELRRELEELREKLAQlelRLEGLEVRIDNLQERLSEEYSltleEAEALENKIEDDE 967
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1431906468 1963 VSTRRKQQGITMKLDELK--NLTS-----QFQESMDNIMKQAND---SLAMLRESpggMREKGRKAREL 2021
Cdd:TIGR02168 968 EEARRRLKRLENKIKELGpvNLAAieeyeELKERYDFLTAQKEDlteAKETLEEA---IEEIDREARER 1033
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1598-2130 |
9.20e-09 |
|
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: 61.39 E-value: 9.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1598 LENLENTTKYFQryliKENAKKIRAEI-QLEGIAEQTENLQKELTRVLARHQKVNAEME-RTSNGTQALATFIEQLHANI 1675
Cdd:pfam12128 324 LEALEDQHGAFL----DADIETAAADQeQLPSWQSELENLEERLKALTGKHQDVTAKYNrRRSKIKEQNNRDIAGIKDKL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1676 KEITEKVATLNQTARKDFQPPVSALQSMHQ----NISSLLGLIKER----NFTEMQQNATLELK---AAKDLL-----SR 1739
Cdd:pfam12128 400 AKIREARDRQLAVAEDDLQALESELREQLEagklEFNEEEYRLKSRlgelKLRLNQATATPELLlqlENFDERierarEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1740 IQKRFQKPQEKLKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFqekkLRVQeeqnvtseliAK 1819
Cdd:pfam12128 480 QEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF----LRKE----------AP 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1820 GreWVDAAGTHTAAAQDTLTQL------EHHRDELLLWARKIR----SHVDDLVMQMSKRRARDLVHRAEQHASELQSRA 1889
Cdd:pfam12128 546 D--WEQSIGKVISPELLHRTDLdpevwdGSVGGELNLYGVKLDlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAA 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1890 ----GALDRDLENV-RNVSLNATSAAHVHSNIQTLTEEAEMLAadahktanktDLISESLASRGKAVLQRSSRFLKESVS 1964
Cdd:pfam12128 624 eeqlVQANGELEKAsREETFARTALKNARLDLRRLFDEKQSEK----------DKKNKALAERKDSANERLNSLEAQLKQ 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1965 TRRKQQGITMKLDE-LKNLTSQFQESMDNIMKQANDSLAMLRESPGGmREKGRKA----------RELAA--------AA 2025
Cdd:pfam12128 694 LDKKHQAWLEEQKEqKREARTEKQAYWQVVEGALDAQLALLKAAIAA-RRSGAKAelkaletwykRDLASlgvdpdviAK 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2026 NESAVKTLEDVL---------ALSLRVF----------NTSEDLSRVNATVQETNDLLhnstmttllaGRKMKDMEMQAN 2086
Cdd:pfam12128 773 LKREIRTLERKIeriavrrqeVLRYFDWyqetwlqrrpRLATQLSNIERAISELQQQL----------ARLIADTKLRRA 842
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1431906468 2087 LLLDRLKPLKTLEENLSRNLSEIKLLISRarkqVASIKVAVSAD 2130
Cdd:pfam12128 843 KLEMERKASEKQQVRLSENLRGLRCEMSK----LATLKEDANSE 882
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1620-1957 |
9.48e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 9.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1620 IRAEI--QLEGIAEQTEnlqkeltrVLARHQKVNAEMERTSNgtQALATFIEQLHANIKEITEKVATLNQTARkdfqppv 1697
Cdd:COG1196 194 ILGELerQLEPLERQAE--------KAERYRELKEELKELEA--ELLLLKLRELEAELEELEAELEELEAELE------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1698 sALQSMHQNISSLLGLIKERnftemQQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEansllsnhseKLQAAEELLKE 1777
Cdd:COG1196 257 -ELEAELAELEAELEELRLE-----LEELELELEEAQAEEYELLAELARLEQDIARLEE----------RRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1778 AGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRS 1857
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1858 HVDDLvmqmsKRRARDLVHRAEQHASELQSRAGALDRDLENVRNVSLNATSAAHVHSNIQTLTEEAE-MLAADAHKTANK 1936
Cdd:COG1196 401 QLEEL-----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLeLLAELLEEAALL 475
|
330 340
....*....|....*....|.
gi 1431906468 1937 TDLISESLASRGKAVLQRSSR 1957
Cdd:COG1196 476 EAALAELLEELAEAAARLLLL 496
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
957-1003 |
1.01e-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: 53.51 E-value: 1.01e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 957 PCNCSVEGSVSDNCTEE-GQCHCGPGVSGKQCDRCSHGFY--AFQDGGCT 1003
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYglPSQGGGCQ 50
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1597-2006 |
1.06e-08 |
|
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: 61.22 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1597 ILENLENTTKYF---QRYLIKENAKKIRAEIQLEGIAEQTENL----QKELTRVLARHQKVNAEMERTSNGTQALATFIE 1669
Cdd:TIGR00606 696 FISDLQSKLRLApdkLKSTESELKKKEKRRDEMLGLAPGRQSIidlkEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1670 QLHAniKEITEKVATLNQTARKDFQPPVSALQ-SMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLLSRI---QKRFQ 1745
Cdd:TIGR00606 776 TIMP--EEESAKVCLTDVTIMERFQMELKDVErKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIelnRKLIQ 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1746 KPQEKLKALKEANSLLSnhSEKLQAAEElLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVD 1825
Cdd:TIGR00606 854 DQQEQIQHLKSKTNELK--SEKLQIGTN-LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1826 AAGTHTAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQhASELQSRAGALDRDLENVRnvsln 1905
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQ-LEECEKHQEKINEDMRLMR----- 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1906 atsaahvhSNIQTlTEEAEMLAADAHKTANKTDLISEslasrgkavlqrssrfLKESVSTRRKQQGiTMKLDELKNLTSQ 1985
Cdd:TIGR00606 1005 --------QDIDT-QKIQERWLQDNLTLRKRENELKE----------------VEEELKQHLKEMG-QMQVLQMKQEHQK 1058
|
410 420
....*....|....*....|.
gi 1431906468 1986 FQESMDNIMKQANDSLAMLRE 2006
Cdd:TIGR00606 1059 LEENIDLIKRNHVLALGRQKG 1079
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1051-1094 |
1.26e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.26e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1431906468 1051 CNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGY--RSFPDC 1094
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1410-1456 |
1.33e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.33e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1410 CNCN---NHSDVCDPETGKCLsCRDHTSGDHCELCASGYYGKVtglPGDC 1456
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
404-458 |
1.36e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.08 E-value: 1.36e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1431906468 404 CNCDPVGSLSSVCIKDDrhadlangkwpGQCPCRKGYAGDKCDRCQFGYRG--FPNC 458
Cdd:smart00180 1 CDCDPGGSASGTCDPDT-----------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1613-2138 |
1.60e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1613 IKENAKKIRAEIQ-LEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITE--KVATLNQTA 1689
Cdd:PRK03918 219 LREELEKLEKEVKeLEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1690 RKDFQPPVSALQSMHQNISSLLGLIK--ERNFTEmqqnatLELKAAKdlLSRIQKRFQKPQEKLKALKEANSLLSNHSEK 1767
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINgiEERIKE------LEEKEER--LEELKKKLKELEKRLEELEERHELYEEAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1768 LQAAEELLKEAGSKTQESnlllllVKANLKEFQEKKLRVQEEqnvTSELIAKGREWVDAAGTHTAA------AQDT---- 1837
Cdd:PRK03918 371 KEELERLKKRLTGLTPEK------LEKELEELEKAKEEIEEE---ISKITARIGELKKEIKELKKAieelkkAKGKcpvc 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1838 ---LTqlEHHRDELLlwarkirshvddlvmqmskRRARDLVHRAEQHASELQSRAGALDRDLENVRNVslnatsaahvhs 1914
Cdd:PRK03918 442 greLT--EEHRKELL-------------------EEYTAELKRIEKELKEIEEKERKLRKELRELEKV------------ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1915 niqtLTEEAEMLAadAHKTANKTDLISESLASRGKAVLQRSS---RFLKESVSTRRKQQGITM----KLDELKNLTSQFQ 1987
Cdd:PRK03918 489 ----LKKESELIK--LKELAEQLKELEEKLKKYNLEELEKKAeeyEKLKEKLIKLKGEIKSLKkeleKLEELKKKLAELE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1988 ESMDNIMKQANDSLAMLRE-SPGGMREKGRKARELAAAANE-----SAVKTLEDVL----ALSLRVFNTSEDLSRVNATV 2057
Cdd:PRK03918 563 KKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEylelkDAEKELEREEkelkKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2058 QET----NDLLHN-STMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIKL---LISRARKQVASIKVA--- 2126
Cdd:PRK03918 643 EELrkelEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEeleEREKAKKELEKLEKAler 722
|
570
....*....|..
gi 1431906468 2127 VSADRDCIRAYQ 2138
Cdd:PRK03918 723 VEELREKVKKYK 734
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1004-1049 |
1.69e-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: 52.74 E-value: 1.69e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1004 PCDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGLDPE-QGCQ 1049
Cdd:cd00055 1 PCDCnghGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
798-853 |
2.97e-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: 2.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1431906468 798 CACPLSIDSnnfSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGGTC 853
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETG---QC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1097-1154 |
3.13e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.93 E-value: 3.13e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1431906468 1097 CGCDLRGTLPDTCDLeqglcscseDGGTCSCKENAVGPQCSKCQAGTFalrGDNPQGC 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 |
3.54e-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: 3.54e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1431906468 1005 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGL--DPEQGC 1048
Cdd:pfam00053 1 CDCnphGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
277-324 |
3.56e-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: 51.97 E-value: 3.56e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 277 CICYGHAS---SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPGT 324
Cdd:cd00055 2 CDCNGHGSlsgQC----DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1005-1048 |
6.92e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 6.92e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 1005 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGlDPEQGC 1048
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 ... |
1615-2131 |
7.56e-08 |
|
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: 58.65 E-value: 7.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1615 ENAKKIRAEIQLEGIAEQTEN--LQKELtRVLARhQKVNAEMERTSNGTQalatfIEQLHANIKEiTEKvatlnqtARKD 1692
Cdd:pfam01576 366 EQAKRNKANLEKAKQALESENaeLQAEL-RTLQQ-AKQDSEHKRKKLEGQ-----LQELQARLSE-SER-------QRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1693 FQPPVSALQSMHQNISSLLGLIKERNftemqqnatleLKAAKDLlSRIQKRFQKPQE--------------KLKALK-EA 1757
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKN-----------IKLSKDV-SSLESQLQDTQEllqeetrqklnlstRLRQLEdER 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1758 NSLLsnhsEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEF-------QEKKLRVQEE-QNVTSELIAKGREWVDAAGT 1829
Cdd:pfam01576 499 NSLQ----EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDagtlealEEGKKRLQRElEALTQQLEEKAAAYDKLEKT 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1830 HTAAAQ---DTLTQLEHHRdELLLWARKIRSHVDDLVMQ---MSKRRA--RDlvhRAEQHASELQSRAGALDRDLENVR- 1900
Cdd:pfam01576 575 KNRLQQeldDLLVDLDHQR-QLVSNLEKKQKKFDQMLAEekaISARYAeeRD---RAEAEAREKETRALSLARALEEALe 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1901 --------NVSLNA------TSAAHVHSNI-----------QTLTE--------EAEMLAAD-----------AHKTANK 1936
Cdd:pfam01576 651 akeelertNKQLRAemedlvSSKDDVGKNVhelerskraleQQVEEmktqleelEDELQATEdaklrlevnmqALKAQFE 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1937 TDLIS-ESLASRGKAVLQRSSRFLKESVSTRRKQQGITM----KLD-ELKNLTSQfqesMDNIMKQANDSLAMLRESPGG 2010
Cdd:pfam01576 731 RDLQArDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVaakkKLElDLKELEAQ----IDAANKGREEAVKQLKKLQAQ 806
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2011 MREKGRKARELAAA---------ANESAVKTLE-DVLALslrvfntSEDLS---RVNATVQETNDLLHNStmttLLAGRK 2077
Cdd:pfam01576 807 MKDLQRELEEARASrdeilaqskESEKKLKNLEaELLQL-------QEDLAaseRARRQAQQERDELADE----IASGAS 875
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 2078 MKdmemqaNLLLDRLKPLKT----LEENLSRNLSEIKLLISRARK---QVASIKVAVSADR 2131
Cdd:pfam01576 876 GK------SALQDEKRRLEAriaqLEEELEEEQSNTELLNDRLRKstlQVEQLTTELAAER 930
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1668-1999 |
9.21e-08 |
|
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: 58.14 E-value: 9.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1668 IEQLHANIKEITEKVATLNQTARK--DFQPPVSALQSMHqnISSLLGLIKERNftEMQQNATLELKAAKDLLSRIQKRFQ 1745
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKaeRYKELKAELRELE--LALLVLRLEELR--EELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1746 KPQEKL------------------KALKEANSLLSN-------HSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQ 1800
Cdd:TIGR02168 264 ELEEKLeelrlevseleeeieelqKELYALANEISRleqqkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1801 EKKLRVQEEQNVTSELIAKGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRSHVddlvmqmskRRARDLVHRAEQ 1880
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI---------ERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1881 HASELQSRAGALDRDLENVRnvslnatsAAHVHSNIQTLTEEAEMLAADAHKTANKTDLISESLASRGKAVLQRSSRFlk 1960
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAE--------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL-- 484
|
330 340 350
....*....|....*....|....*....|....*....
gi 1431906468 1961 esvstRRKQQGITMkLDELKNLTSQFQESMDNIMKQAND 1999
Cdd:TIGR02168 485 -----AQLQARLDS-LERLQENLEGFSEGVKALLKNQSG 517
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1609-1834 |
9.87e-08 |
|
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: 57.08 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1609 QRYLIKENAKKIRA-EIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLNQ 1687
Cdd:COG4942 18 QADAAAEAEAELEQlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1688 ---TARKDFQPPVSALQSMHQNiSSLLGLIKERNFTEMQQNATLelkaAKDLLSRIQKRFQKPQEKLKALKEANSLLSNH 1764
Cdd:COG4942 98 eleAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQY----LKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431906468 1765 SEKLQAA----EELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVDAAGTHTAAA 1834
Cdd:COG4942 173 RAELEALlaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
460-507 |
1.12e-07 |
|
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: 50.43 E-value: 1.12e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 460 PCDCRTVGSLNEDpCIEP---CLCKKNVEGKNCDRCKPGFYNLKERnPEGC 507
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGtgqCECKPNTTGRRCDRCAPGYYGLPSQ-GGGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1612-1931 |
1.56e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1612 LIKENAKKIRAEI-QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLN---- 1686
Cdd:COG4372 25 LIAALSEQLRKALfELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeele 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1687 --QTARKDFQPPVSALQSMHQNissllgLIKERNFTEMQQNATLELKAAKD-LLSRIQKRFQKPQEKLKALKEANSLLSN 1763
Cdd:COG4372 105 slQEEAEELQEELEELQKERQD------LEQQRKQLEAQIAELQSEIAEREeELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1764 HsEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSEliakGREWVDAAGTHTAAAQDTLTQLEH 1843
Cdd:COG4372 179 A-EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA----KLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1844 HRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQHASELQSRAGALDRDLENVRNVSLNATSAAHVHSNIQTLTEEA 1923
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
....*...
gi 1431906468 1924 EMLAADAH 1931
Cdd:COG4372 334 ILLAELAD 341
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1617-1893 |
1.92e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1617 AKKIRAEIQLEGIAEQTENLQKEL----TRVLARHQKVNA-EMERTSNGTQALA-----TFIEQLHANIKEITEKVATLN 1686
Cdd:PRK04863 383 ARAEAAEEEVDELKSQLADYQQALdvqqTRAIQYQQAVQAlERAKQLCGLPDLTadnaeDWLEEFQAKEQEATEELLSLE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1687 Q------TARKDFQ----------PPVSALQSMHQNISSLLGLIKERNftEMQQNATLELKaakdlLSRIQKRFQKPQEK 1750
Cdd:PRK04863 463 QklsvaqAAHSQFEqayqlvrkiaGEVSRSEAWDVARELLRRLREQRH--LAEQLQQLRMR-----LSELEQRLRQQQRA 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1751 LKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNllllLVKANLKEfQEKKLRVQEEQ--NVTSELIAKGREWVdaag 1828
Cdd:PRK04863 536 ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS----ESVSEARE-RRMALRQQLEQlqARIQRLAARAPAWL---- 606
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1829 thtaAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQM-SKRRARDLVHRA----EQHASELQSRAGALD 1893
Cdd:PRK04863 607 ----AAQDALARLREQSGEEFEDSQDVTEYMQQLLERErELTVERDELAARkqalDEEIERLSQPGGSED 672
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1729-2119 |
2.37e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1729 ELKAAKDLLSRIQKRfqKPQEKLKALKEANSLLS-------------NHSEKLQAAEELLKEAGSKTQESNLLLLLVKAN 1795
Cdd:COG4717 50 RLEKEADELFKPQGR--KPELNLKELKELEEELKeaeekeeeyaelqEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1796 ---LKEFQEKKLRVQEEQNVTSELIAKGREWVDAAgTHTAAAQDTLTQLEHHRDELL-LWARKIRSHVDDLVMQMSKRRA 1871
Cdd:COG4717 128 lplYQELEALEAELAELPERLEELEERLEELRELE-EELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1872 RdlVHRAEQHASELQSRAGALDRDLENVRNVSLNATSAAHVHSNIQTLTEEAEM--LAADAHKTANKTDLISESLASRGK 1949
Cdd:COG4717 207 R--LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlaLLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1950 AVLQRSSRFLKESVSTRRKQQGITmKLDELKNLTSQ-FQESMDNIMKQANDSLAMLRESPGGMREKGRKARELAAAANES 2028
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQ-ALPALEELEEEeLEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2029 AVKTLEDVLALSLRVFNTS---------EDLSRVNATVQETNDL-----LHNSTMTTLLAGRKMKDMEMQANLLLDRLKP 2094
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEdeeelraalEQAEEYQELKEELEELeeqleELLGELEELLEALDEEELEEELEELEEELEE 443
|
410 420
....*....|....*....|....*
gi 1431906468 2095 LKTLEENLSRNLSEIKLLISRARKQ 2119
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEED 468
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1617-2033 |
2.93e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 2.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1617 AKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVatlnQTARKDFQPP 1696
Cdd:PRK02224 265 ETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL----EECRVAAQAH 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1697 VSALQSMHQNISSLlgliKERNFTEMQQNATLE--LKAAKDLLSRIQKRFQKPQEKLKALKEAnslLSNHSEKLQAAEEL 1774
Cdd:PRK02224 341 NEEAESLREDADDL----EERAEELREEAAELEseLEEAREAVEDRREEIEELEEEIEELRER---FGDAPVDLGNAEDF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1775 LKEAGSKTQESNLLLLLVKANLKEFQEkklRVQEEQnvtsELIAKGR-----EWVDAAGtHTAAAQDTLTQLEHHRDELL 1849
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARE---RVEEAE----ALLEAGKcpecgQPVEGSP-HVETIEEDRERVEELEAELE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1850 lwarKIRSHVDDLvmqmSKR--RARDLVhRAEQHASELQSRAGALDRDLENVRNvSLNATSAAhvhsnIQTLTEEAEMLA 1927
Cdd:PRK02224 486 ----DLEEEVEEV----EERleRAEDLV-EAEDRIERLEERREDLEELIAERRE-TIEEKRER-----AEELRERAAELE 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1928 ADA---HKTANKTDLISESLASRGKAVLQRssrfLKESVSTRRKQQGITMKLDELKNLTSQFQ------ESMDNIMKQAN 1998
Cdd:PRK02224 551 AEAeekREAAAEAEEEAEEAREEVAELNSK----LAELKERIESLERIRTLLAAIADAEDEIErlrekrEALAELNDERR 626
|
410 420 430
....*....|....*....|....*....|....*
gi 1431906468 1999 DSLAMLREspggmrekgRKaRELAAAANESAVKTL 2033
Cdd:PRK02224 627 ERLAEKRE---------RK-RELEAEFDEARIEEA 651
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1701-2121 |
4.54e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1701 QSMhqnISSLLGLIKERNFTEMQQNATLelkAAKDLLSRIQKRFQKPQEKLKAlKEANSLlsnHsEKLQAAEELLKEags 1780
Cdd:PRK02224 152 QDM---IDDLLQLGKLEEYRERASDARL---GVERVLSDQRGSLDQLKAQIEE-KEEKDL---H-ERLNGLESELAE--- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1781 ktqesnlllllVKANLKEFQEKKLRVQEEQNVTSELIA---KGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRS 1857
Cdd:PRK02224 218 -----------LDEEIERYEEQREQARETRDEADEVLEeheERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1858 HVDDLVMQMSKRRARDLVHRA-----EQHASELQSRAGALDRDLENVRnvslnaTSAAHVHSNIQTLTEEAEMLAADAHK 1932
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDAdaeavEARREELEDRDEELRDRLEECR------VAAQAHNEEAESLREDADDLEERAEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1933 TANKTDLISESLASRGKAVLQRSSRF--LKESVSTRRKQ-QGITMKLDELKNLTSQFQESMDNIMKQANDSLAMLREspg 2009
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIeeLEEEIEELRERfGDAPVDLGNAEDFLEELREERDELREREAELEATLRT--- 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2010 gMREKGRKARELAAAAN----------ESAVKTLED----VLALSLRVFNTSEDLSRVNATVQETNDLlhnstmttllag 2075
Cdd:PRK02224 438 -ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdrerVEELEAELEDLEEEVEEVEERLERAEDL------------ 504
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1431906468 2076 rkmKDMEMQANLLLDRLKPLKTLEENLSRNLSEIKLLISRARKQVA 2121
Cdd:PRK02224 505 ---VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1599-1877 |
4.91e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1599 ENLENTTKYFQRylIKENAKKIRAEI-----QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHA 1673
Cdd:COG4372 80 EELEELNEQLQA--AQAELAQAQEELeslqeEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1674 NIKEITEKVATLNQTARKdfqppvsalQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLLSRIQKRFQKPQEKLKA 1753
Cdd:COG4372 158 QLESLQEELAALEQELQA---------LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1754 LKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAkgrEWVDAAGTHTAA 1833
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL---ELKLLALLLNLA 305
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1431906468 1834 AQDTLTQLEHHRDELLLW-ARKIRSHVDDLVMQMSKRRARDLVHR 1877
Cdd:COG4372 306 ALSLIGALEDALLAALLElAKKLELALAILLAELADLLQLLLVGL 350
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1096-1154 |
6.10e-07 |
|
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: 48.50 E-value: 6.10e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431906468 1096 PCGCDLRGTLPDTCDLEqglcscsedGGTCSCKENAVGPQCSKCQAGTFALRgDNPQGC 1154
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1711-2035 |
6.56e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 6.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1711 LGLIKERNFTEMQQNATLE-LKAAKDLLSRIQKRFQKPQEKLKALKE----ANSLLSNHSEKLQAAEELLKEAGSKTQES 1785
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEqLRKALFELDKLQEELEQLREELEQAREeleqLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1786 NLLLLLVKANLKEFQEKKLRVQEEqnvtseliakgrewvdaagthtaaaqdtLTQLEHHRDELLLWARKIRSHVDDLVMQ 1865
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEE----------------------------LEELQKERQDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1866 MSKRRARdlvhraeqhASELQSRAGALDRDLENVRNvSLNATSAAHVHSNIQTLTEEAEMLAADAHKTANKTDLISESLA 1945
Cdd:COG4372 145 IAEREEE---------LKELEEQLESLQEELAALEQ-ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1946 SRGKAVLQRSSRFLKESVSTRRKQQGITMKLDELKNLTSQFQESMDNIMKQANDSLA-MLRESPGGMREKGRKARELAAA 2024
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKdTEEEELEIAALELEALEEAALE 294
|
330
....*....|.
gi 1431906468 2025 ANESAVKTLED 2035
Cdd:COG4372 295 LKLLALLLNLA 305
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
749-790 |
7.34e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 7.34e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1431906468 749 CECH--GHASE-CD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRG 790
Cdd:smart00180 1 CDCDpgGSASGtCDpDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
461-507 |
1.01e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.69 E-value: 1.01e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1431906468 461 CDCRTVGSLNeDPCIEP---CLCKKNVEGKNCDRCKPGFYNlkeRNPEGC 507
Cdd:smart00180 1 CDCDPGGSAS-GTCDPDtgqCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1617-1898 |
1.34e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.57 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1617 AKKIRAEIQLEGIAEQTENLQKEL----TRVLARHQKVNAeMERTSNGTQA-------LATFIEQLHANIKEITEKVATL 1685
Cdd:COG3096 382 ARLEAAEEEVDSLKSQLADYQQALdvqqTRAIQYQQAVQA-LEKARALCGLpdltpenAEDYLAAFRAKEQQATEEVLEL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1686 NQ------TARKDFQPPVSALQSM---------HQNISSLLglikeRNFTEmQQNATLELKAAKDLLSRIQKRFQKpQEK 1750
Cdd:COG3096 461 EQklsvadAARRQFEKAYELVCKIageversqaWQTARELL-----RRYRS-QQALAQRLQQLRAQLAELEQRLRQ-QQN 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1751 LKALkeANSLLSNHSEKLQAAEEL--LKEAGSKTQESnlllllVKANLKEFQEKK--LRVQEEQNVT--SELIAKGREWV 1824
Cdd:COG3096 534 AERL--LEEFCQRIGQQLDAAEELeeLLAELEAQLEE------LEEQAAEAVEQRseLRQQLEQLRAriKELAARAPAWL 605
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1431906468 1825 daagthtaAAQDTLTQLEHHRDELLLWARKIRSHvddlvMQMSKRRARDlvhrAEQHASELQSRAGALDRDLEN 1898
Cdd:COG3096 606 --------AAQDALERLREQSGEALADSQEVTAA-----MQQLLERERE----ATVERDELAARKQALESQIER 662
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
855-899 |
1.84e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 1.84e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1431906468 855 PCNCSGNVDPleagHCDSVTGECLkCLWNTDGAHCERCADGFYGD 899
Cdd:smart00180 2 DCDPGGSASG----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1601-2133 |
1.98e-06 |
|
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: 53.90 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1601 LENTTKYFQ-RYLIKENAKKiraeiQLEGIAEQT-ENLQKELTRVLARHQKVNAEMERTSNGTQALatfIEQLHANIKEI 1678
Cdd:TIGR00606 267 LDNEIKALKsRKKQMEKDNS-----ELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1679 T-EKVATLNQTARKDFQPPVSALQSMHQNISSL-LGLIKERNFTEMQQNATLELKAAKDLLSRIQKRfqkpqeklKAlKE 1756
Cdd:TIGR00606 339 NqEKTELLVEQGRLQLQADRHQEHIRARDSLIQsLATRLELDGFERGPFSERQIKNFHTLVIERQED--------EA-KT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1757 ANSLLSNhsekLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKlrVQEEQNVTSELiakgrewvdaagthtaaaqd 1836
Cdd:TIGR00606 410 AAQLCAD----LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK--QEELKFVIKEL-------------------- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1837 tlTQLEHHRDELLLWARKIRSHVDDLvmqmSKRRARDLVHRAEQHASELQSRAGALDRDL--ENVRNVSLNAtsaaHVHS 1914
Cdd:TIGR00606 464 --QQLEGSSDRILELDQELRKAEREL----SKAEKNSLTETLKKEVKSLQNEKADLDRKLrkLDQEMEQLNH----HTTT 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1915 NIQTLTEEAEMLAADAHKTANK----------------TDLISESLASRGKAVLQRSSRFLKESVSTRRKQQGITMKLDE 1978
Cdd:TIGR00606 534 RTQMEMLTKDKMDKDEQIRKIKsrhsdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1979 LKNLTSQFQESMDNIMK----QANDS-LAMLRESpggmREKGRKARE-LAAAAN--ESAVKTLED----VLALSLRVFNT 2046
Cdd:TIGR00606 614 LESKEEQLSSYEDKLFDvcgsQDEESdLERLKEE----IEKSSKQRAmLAGATAvySQFITQLTDenqsCCPVCQRVFQT 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2047 SEDLSRVNATVQETNDLL---HNSTMTTLLAGRKMKD-----MEMQANLLLDRLKPLKTLEE---NLSRNLSEIKLLISR 2115
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLApdkLKSTESELKKKEKRRDemlglAPGRQSIIDLKEKEIPELRNklqKVNRDIQRLKNDIEE 769
|
570
....*....|....*...
gi 1431906468 2116 ARKQVASIKVAVSADRDC 2133
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVC 787
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1459-1513 |
2.28e-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: 46.58 E-value: 2.28e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 1459 CTCPHHPpfSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGSC 1513
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1614-2059 |
3.57e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1614 KENAKKIRAEIQ-LEGIAEQTENLQKELTRVLARHQKVN---------AEMERTSNGTQALATFIEQLHANIKEITEKVA 1683
Cdd:COG4717 84 EEKEEEYAELQEeLEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1684 TLNQTARKdfqppvsaLQSMHQNISSLLGLIKERNFTEMQQNATlELKAAKDLLSRIQKRFQKPQEKLKALKEANSLLSN 1763
Cdd:COG4717 164 ELEELEAE--------LAELQEELEELLEQLSLATEEELQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1764 HSEKLQAAEELLKEAGSKTQESnlLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVDAAGTHTAAAQDTLTQLEH 1843
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAA--ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1844 HRDellLWARKIRSHVDDLVM--QMSKRRARDLVHRAEQhASELQSRAGALDRDL-----ENVRNVSLNATSAahvhSNI 1916
Cdd:COG4717 313 LEE---LEEEELEELLAALGLppDLSPEELLELLDRIEE-LQELLREAEELEEELqleelEQEIAALLAEAGV----EDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1917 QTLTEEAEmLAADAHKTANKTDLISESLASRGKAVLQRSSRFLKESVSTRRKQqgITMKLDELKNLTSQFQESM---DNI 1993
Cdd:COG4717 385 EELRAALE-QAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE--LEEELEELEEELEELREELaelEAE 461
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1431906468 1994 MKQA--NDSLAMLREspggmrEKGRKARELAAAANE-SAVKTLEDVLALSLRVFnTSEDLSRVNATVQE 2059
Cdd:COG4717 462 LEQLeeDGELAELLQ------ELEELKAELRELAEEwAALKLALELLEEAREEY-REERLPPVLERASE 523
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
797-851 |
6.11e-06 |
|
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: 45.42 E-value: 6.11e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 797 PCACPLSIDSNnfsPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGG 851
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTG---QC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1838-2092 |
6.18e-06 |
|
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: 50.49 E-value: 6.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1838 LTQLEHHRDELLLWARKIRSHVDDlvMQMSKRRARDLvhraEQHASELQSRAGALDRDLENVRNVSlNATSaahvhSNIQ 1917
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQ--IEILEKELSSL----AQETEELQKKATQTLAKAQQVNAES-ERTL-----GHAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1918 TLTEEAEMLAADAHKTANKTDLISE--SLASRGK--AVLQRSSRFLKE--SVSTRRKQQGITMKLDELKNLTSQFQESMD 1991
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLGEndFALPSSDlsRMLAEAQRMLGEirSRDFGTQLQNAEAELKAAQDLLSRIQTWFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1992 NIMKQANDSLAMLRESPGGMREKGRKARELaaaANESAVKTlEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNstmtT 2071
Cdd:pfam06008 166 SPQEENKALANALRDSLAEYEAKLSDLREL---LREAAAKT-RDANRLNLANQANLREFQRKKEEVSEQKNQLEE----T 237
|
250 260
....*....|....*....|.
gi 1431906468 2072 LLAGRkmkDMEMQANLLLDRL 2092
Cdd:pfam06008 238 LKTAR---DSLDAANLLLQEI 255
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1597-2110 |
9.43e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.56 E-value: 9.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1597 ILENLENTTKYFQRYLIKEN-AKKIRAEIQleGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFI------- 1668
Cdd:TIGR04523 133 KKENKKNIDKFLTEIKKKEKeLEKLNNKYN--DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkki 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1669 ---EQLHANIKEITEKVATLNQTARK---DFQPPVSALQSMHQNISSLLGLiKERNFTEMQQNaTLELKAAKDLLSRIQK 1742
Cdd:TIGR04523 211 qknKSLESQISELKKQNNQLKDNIEKkqqEINEKTTEISNTQTQLNQLKDE-QNKIKKQLSEK-QKELEQNNKKIKELEK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1743 RFQKPQEKLKAL---KEANsLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLvkanLKEfQEKKLRvQEEQNVTSELIAK 1819
Cdd:TIGR04523 289 QLNQLKSEISDLnnqKEQD-WNKELKSELKNQEKKLEEIQNQISQNNKIISQ----LNE-QISQLK-KELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1820 GREwvdaagthTAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKrrARDLVHRAEQHASELQSRAGALDRDLENV 1899
Cdd:TIGR04523 362 QRE--------LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN--QEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1900 R--NVSLNATsaahvhsnIQTLTEEaemlaaDAHKtanktDLISESLASRGKAVLQRSSRFLKESVSTRR----KQQGIT 1973
Cdd:TIGR04523 432 KetIIKNNSE--------IKDLTNQ------DSVK-----ELIIKNLDNTRESLETQLKVLSRSINKIKQnleqKQKELK 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1974 MKLDELKNLTSQFQESMDNImKQANDSLAMLREspggmrekgrKARELAAAAN--ESAVKTLEDVLaLSLRVFNTSEDLS 2051
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKV-KDLTKKISSLKE----------KIEKLESEKKekESKISDLEDEL-NKDDFELKKENLE 560
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 2052 RVNATVQETNDLLHNsTMTTLLAGRKMKDmEMQANLLLDRLKPLKTLEE------NLSRNLSEIK 2110
Cdd:TIGR04523 561 KEIDEKNKEIEELKQ-TQKSLKKKQEEKQ-ELIDQKEKEKKDLIKEIEEkekkisSLEKELEKAK 623
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1598-2121 |
1.31e-05 |
|
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: 51.12 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1598 LENLENTTKYFQRYLIKENAKKiraeiQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNG------TQALATFIEQL 1671
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEQL-----KKQQLLKQLRARIEELRAQEAVLEETQERINRARKAaplaahIKAVTQIEQQA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1672 HANIKEITEKVATLNQtARKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLLSRIQKRFQKPQEKL 1751
Cdd:TIGR00618 310 QRIHTELQSKMRSRAK-LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1752 KALKEANSLLSNHSEKLQaaEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEE---QNVTSELIAKGREWVDAAG 1828
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQ--REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAaaiTCTAQCEKLEKIHLQESAQ 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1829 THTAAAQ-----DTLTQ-------------LEHHRDELLLWARKIRSH---VDDLVMQMSKRRARDLVHRAEQHASELQS 1887
Cdd:TIGR00618 467 SLKEREQqlqtkEQIHLqetrkkavvlarlLELQEEPCPLCGSCIHPNparQDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1888 RAGALDRDLENVRNVSLNATSAAHvhsNIQTLTEEAEMLAADAHKTANKTDLI-----SESLASRGKAVLQRSS-RFLKE 1961
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQ---SFSILTQCDNRSKEDIPNLQNITVRLqdlteKLSEAEDMLACEQHALlRKLQP 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1962 SVSTRRKQQGITMKLDEL-KNLTSQFQESMDNIMKQANDSLAMLRESPggMREKGRKARELAAAANE------------- 2027
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELaLKLTALHALQLTLTQERVREHALSIRVLP--KELLASRQLALQKMQSEkeqltywkemlaq 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 2028 --SAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKdmeMQANLLLD-RLKPLKTLEENLSR 2104
Cdd:TIGR00618 702 cqTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTV---LKARTEAHfNNNEEVTAALQTGA 778
|
570
....*....|....*..
gi 1431906468 2105 NLSEIKLLISRARKQVA 2121
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLRE 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1609-1899 |
1.54e-05 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1609 QRYLIKENAKKIRA-EIQLEGIAEQTENLQKELTRVLARHQKVNAEMERtsngtqalatfIEQLhanIKEITEKVATLNQ 1687
Cdd:TIGR02169 221 REYEGYELLKEKEAlERQKEAIERQLASLEEELEKLTEEISELEKRLEE-----------IEQL---LEELNKKIKDLGE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1688 TARKDFQppvSALQSMHQNISSLLGLIKERNftEMQQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEANSLLSNHSEK 1767
Cdd:TIGR02169 287 EEQLRVK---EKIGELEAEIASLERSIAEKE--RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1768 LQAAEELLKeagSKTQESNLLLLLVKANLKEFQEKKLRVQEEQN----VTSELIAKGREWVDAAGTHTAA---AQDTLTQ 1840
Cdd:TIGR02169 362 LKEELEDLR---AELEEVDKEFAETRDELKDYREKLEKLKREINelkrELDRLQEELQRLSEELADLNAAiagIEAKINE 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431906468 1841 LEHHRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQhaSELQSRAGALDRDLENV 1899
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY--DRVEKELSKLQRELAEA 495
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1458-1514 |
1.65e-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: 44.27 E-value: 1.65e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1431906468 1458 PCTCPHHPpfSFSPTCVVEgdsDFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGsCQ 1514
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
716-910 |
2.42e-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: 46.91 E-value: 2.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 716 CECPQGY---TGTSCEACLPGyyrvdgilfggicqpcechghasecdiHGICSVCTHNTTGdhCEQCLPGFYGTPSRGTP 792
Cdd:cd13416 1 EACPSGQytsSGECCEQCPPG---------------------------EGVARPCGDNQTV--CEPCLDGVTFSDVVSHT 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 793 GDCQPCA-CPLSIdsnnfSPTCHLTDGEEVVCdqcapgysgswceRCADGYYgnPTVPGGTCVPCNCsgnvdpleaghCD 871
Cdd:cd13416 52 EPCQPCTrCPGLM-----SMRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCEPCTV-----------CP 100
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1431906468 872 SVTGECLKCLWNTDgAHCERCADGFYGDAVTAKN----CRACD 910
Cdd:cd13416 101 PGQGVVQSCGPNQD-TVCEACPEGTYSDEDSSTDpclpCTVCE 142
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
823-1097 |
2.95e-05 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 49.20 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 823 CDQCAPGYSGSwCERCADGYYGNPTvpgGTCVP-CNCSGNVDPLEAGHCDSVTGECL--KCLWNTDGAHCERCADGFY-- 897
Cdd:pfam03302 28 CKACSNDKREV-CEECNSNNYLTPT---SQCIDdCAKIGNYYYTTNANNKKICKECTvaNCKTCEDQGQCQACNDGFYks 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 898 GDAVTA--KNCRAC------DCHE--NGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGLDTGLGCVPCNCSVEGSVS 967
Cdd:pfam03302 104 GDACSPchESCKTCsggtasDCTEclTGKALRYGNDGTKGTCGEGCTTGTGAGACKTCGLTIDGTSYCSECATETEYPQN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 968 DNCTEEGQ-----CHCGPGVSGKqCDRCSHGFYAfQDGGCTPCDCAHTQNNCDPASGECLCPPHTQGLKCEE-----CEE 1037
Cdd:pfam03302 184 GVCTSTAAratatCKASSVANGM-CSSCANGYFR-MNGGCYETTKFPGKSVCEEANSGGTCQKEAPGYKLNNgdlvtCSP 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 1038 AYWGLDPEQGCQACNCSAVGSTSAqCDVLSGHCPCKKGfGGQSCHQCSLG-YRSFPDCVPC 1097
Cdd:pfam03302 262 GCKTCTSNTVCTTCMDGYVKTSDS-CTKCDSSCETCTG-ATTTCKTCATGyYKSGTGCVSC 320
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
798-846 |
3.76e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 43.07 E-value: 3.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1431906468 798 CACPLSidsNNFSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNP 846
Cdd:smart00180 1 CDCDPG---GSASGTCDPDTG---QC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
727-1068 |
4.63e-05 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 48.81 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 727 CEACLPGYyrvdGILFGGICQPCechghASECDIHGiCSVCThNTTGDHCEQCLPGFYGTPSRGTPGDCQPCAcplsids 806
Cdd:pfam03302 1 CDECKPGY----ELSADKTKCTS-----SAPCKTEN-CKACS-NDKREVCEECNSNNYLTPTSQCIDDCAKIG------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 807 NNFSPTChltDGEEVVCDQCAPGY-----SGSWCERCADGYYGNptvpGGTCVPC--NCSGNVDPLEAGHCDSVTGECLK 879
Cdd:pfam03302 63 NYYYTTN---ANNKKICKECTVANcktceDQGQCQACNDGFYKS----GDACSPCheSCKTCSGGTASDCTECLTGKALR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 880 -------------CLWNTDGAHCERCADGFYGdavtAKNCRACDCHENGSLSGICH----LETGLCDCKPHVTGqQCDQC 942
Cdd:pfam03302 136 ygndgtkgtcgegCTTGTGAGACKTCGLTIDG----TSYCSECATETEYPQNGVCTstaaRATATCKASSVANG-MCSSC 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 943 LSGYYGLDTGL----------------GCVPCNCSVEGSVSDNCT-EEGQCHCGPGVSGKQCDRCSHGfYAFQDGGCTPC 1005
Cdd:pfam03302 211 ANGYFRMNGGCyettkfpgksvceeanSGGTCQKEAPGYKLNNGDlVTCSPGCKTCTSNTVCTTCMDG-YVKTSDSCTKC 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431906468 1006 DCA-HTQNNCDPASGECLCPPHTQGLKCEECE--EAYWGLDPEQGCQACNCSAVGSTSAQCDVLSG 1068
Cdd:pfam03302 290 DSScETCTGATTTCKTCATGYYKSGTGCVSCTssESDNGITGVKGCLNCAPPSNNKGSVLCYLIKD 355
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
277-320 |
1.01e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.91 E-value: 1.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 277 CICY--GHAS-SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPW 320
Cdd:smart00180 1 CDCDpgGSASgTC----DPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1599-1819 |
2.41e-04 |
|
chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.98 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1599 ENLENttkyfQRYLIKENAKKIRAEI-----QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHA 1673
Cdd:TIGR02169 836 QELQE-----QRIDLKEQIKSIEKEIenlngKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1674 NIKEITEKVATLNQTarkdfqppvsaLQSMHQNISSLlglikERNFTEMQQNATLELKAAKdllsrIQKRFQKPQEKLKA 1753
Cdd:TIGR02169 911 QIEKKRKRLSELKAK-----------LEALEEELSEI-----EDPKGEDEEIPEEELSLED-----VQAELQRVEEEIRA 969
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1431906468 1754 LKEANSLlsnhseklqaAEELLKEagsktqesnlllllVKANLKEFQEKKLRVQEEQNVTSELIAK 1819
Cdd:TIGR02169 970 LEPVNML----------AIQEYEE--------------VLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1597-1811 |
4.45e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 46.17 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1597 ILENLENTTKYFQRYLikenaKKIRAEIQlegIAEQT-ENLQKELTRVLARHQKVNAEmertsngtqalatfIEQLHANI 1675
Cdd:TIGR04523 455 IIKNLDNTRESLETQL-----KVLSRSIN---KIKQNlEQKQKELKSKEKELKKLNEE--------------KKELEEKV 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1676 KEITEKVATLNQTARKdfqppvsaLQS----MHQNISSLlglikERNFTEMQQNATLELkaakdllsrIQKRFQKPQEKL 1751
Cdd:TIGR04523 513 KDLTKKISSLKEKIEK--------LESekkeKESKISDL-----EDELNKDDFELKKEN---------LEKEIDEKNKEI 570
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1431906468 1752 KALKEAN-SLLSNHSEKlqaaEELLKEagsKTQESNLLLLLV--KANLKEFQEKKLRVQEEQN 1811
Cdd:TIGR04523 571 EELKQTQkSLKKKQEEK----QELIDQ---KEKEKKDLIKEIeeKEKKISSLEKELEKAKKEN 626
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1598-1870 |
5.64e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1598 LENLENTTKYFQRYL--IKENAKKIRAE-------IQLEGIAEQTENLQKELTRV-LARHQKVNAEMERTSNGTQALATF 1667
Cdd:PRK03918 461 LKRIEKELKEIEEKErkLRKELRELEKVlkkeselIKLKELAEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1668 IEQLHANIKEITE---KVATLNqtarkdfqppvSALQSMHQNISSLLGLIKERNFTEMQQ------------NATLELKA 1732
Cdd:PRK03918 541 IKSLKKELEKLEElkkKLAELE-----------KKLDELEEELAELLKELEELGFESVEEleerlkelepfyNEYLELKD 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1733 AKDLLSRIQKRFQKPQEKL-KALKEANsllsnhsEKLQAAEELLKEagsktqesnlllllvkanLKEFqEKKLRVQEEQN 1811
Cdd:PRK03918 610 AEKELEREEKELKKLEEELdKAFEELA-------ETEKRLEELRKE------------------LEEL-EKKYSEEEYEE 663
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1431906468 1812 VTSELIAKGREWvdaagthtAAAQDTLTQLEHHRDElllwarkIRSHVDDLVMQMSKRR 1870
Cdd:PRK03918 664 LREEYLELSREL--------AGLRAELEELEKRREE-------IKKTLEKLKEELEERE 707
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1916-2037 |
8.35e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 45.04 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1916 IQTLTEEAEMLAADAHKTANKTDLIS---ESLASRGKAVLQRSSRFLKESVSTRRKQ----QGITMKLDELKNLTSQFQE 1988
Cdd:pfam10168 577 LQSLEEERKSLSERAEKLAEKYEEIKdkqEKLMRRCKKVLQRLNSQLPVLSDAEREMkkelETINEQLKHLANAIKQAKK 656
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1431906468 1989 SMDnimKQAndslamlRESPGGMREKGRKARELaaaaNESAVKTLEDVL 2037
Cdd:pfam10168 657 KMN---YQR-------YQIAKSQSIRKKSSLSL----SEKQRKTIKEIL 691
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1597-1937 |
1.12e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.82 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1597 ILENLENTTKYFQRYLIKENAKKIRAEI-QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQ------ALATFIE 1669
Cdd:PTZ00440 1155 TLNEVNEIEIEYERILIDHIVEQINNEAkKSKTIMEEIESYKKDIDQVKKNMSKERNDHLTTFEYNAyydkatASYENIE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1670 QL--HAN--------------IKEITEKVATLNQTARKDFQPPVSALQSMHqNISSLLGLIKERNFTE-----MQQNATL 1728
Cdd:PTZ00440 1235 ELttEAKglkgeanrstnvdeLKEIKLQVFSYLQQVIKENNKMENALHEIK-NMYEFLISIDSEKILKeilnsTKKAEEF 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1729 ELKAAKDL--LSRIQKRFQKPQEKLKALKEANSLLSNHS---EKLQAAEELLKEAGSKTQESNLLLLLVKANlKEFQEKK 1803
Cdd:PTZ00440 1314 SNDAKKELekTDNLIKQVEAKIEQAKEHKNKIYGSLEDKqidDEIKKIEQIKEEISNKRKEINKYLSNIKSN-KEKCDLH 1392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1804 LRV---------------QEEQNVTSEL-IAKGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRSHVDD-LVMQM 1866
Cdd:PTZ00440 1393 VRNasrgkdkidflnkheAIEPSNSKEVnIIKITDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNILNNsSILGK 1472
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1431906468 1867 S------KRRARDLVHRAEQHASELQSRAGALDRDLENVRNvslnatsaahvHSNIqtlTEEAEMLAADAHKTANKT 1937
Cdd:PTZ00440 1473 KtklekkKKEATNIMDDINGEHSIIKTKLTKSSEKLNQLNE-----------QPNI---KREGDVLNNDKSTIAYET 1535
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1459-1506 |
1.23e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.83 E-value: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1431906468 1459 CTCphHPPFSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNP 1506
Cdd:smart00180 1 CDC--DPGGSASGTCDPDT---GQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
277-323 |
2.31e-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: 38.10 E-value: 2.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1431906468 277 CICYGHASSCPwDEEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPG 323
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1629-1900 |
2.59e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1629 IAEQTENLQKELTRVLARHQkvnaEMERTSNGTQALATfIEQLHANIKEITEKVATLNQTArkdfqppvSALQsmHQNIS 1708
Cdd:COG4913 223 TFEAADALVEHFDDLERAHE----ALEDAREQIELLEP-IRELAERYAAARERLAELEYLR--------AALR--LWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1709 SLLGLIKERnftemQQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEAnsLLSNHSEKLQAAEELLKEAGSKTQEsnll 1788
Cdd:COG4913 288 RRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEAQ--IRGNGGDRLEQLEREIERLERELEE---- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1789 lllVKANLKEFQEKkLRVQEEQNVTSEliakgREWVDAAgthtAAAQDTLTQLEHHRDELllwarkiRSHVDDLvmqmsK 1868
Cdd:COG4913 357 ---RERRRARLEAL-LAALGLPLPASA-----EEFAALR----AEAAALLEALEEELEAL-------EEALAEA-----E 411
|
250 260 270
....*....|....*....|....*....|....*
gi 1431906468 1869 RRARDLVHRAEQHASE---LQSRAGALDRDLENVR 1900
Cdd:COG4913 412 AALRDLRRELRELEAEiasLERRKSNIPARLLALR 446
|
|
| F-BAR_Rgd1 |
cd07652 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ... |
1614-1786 |
2.60e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho GTPase activating protein Rgd1 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Saccharomyces cerevisiae Rgd1 is a GTPase activating protein (GAP) with activity towards Rho3p and Rho4p, which are involved in bud growth and cytokinesis, respectively. At low pH, S. cerevisiae Rgd1 is required for cell survival and the activation of the protein kinase C pathway, which is important in cell integrity and the maintenance of cell shape. It contains an N-terminal F-BAR domain and a C-terminal Rho GAP domain. The F-BAR domain of S. cerevisiae Rgd1 binds to phosphoinositides and plays an important role in the localization of the protein to the bud tip/neck during the cell cycle. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153336 [Multi-domain] Cd Length: 234 Bit Score: 42.33 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1614 KENAK--KIRAEIQLEGIaeqtENLQKeltrvLARHQKvnaEMERTSNGTQAlaTFIEQLHANIkEITEKVATLNQTArk 1691
Cdd:cd07652 22 KEFATflKKRAAIEEEHA----RGLKK-----LARTTL---DTYKRPDHKQG--SFSNAYHSSL-EFHEKLADNGLRF-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1692 dfqppVSALQSMHQNISSLL-------------GLIKERNFTEMQQ---NATLELKAAKDLLSRIqkRFQKPQEKLKALK 1755
Cdd:cd07652 85 -----AKALNEMSDELSSLAktveksrksiketGKRAEKKVQDAEAaaeKAKARYDSLADDLERV--KTGDPGKKLKFGL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1431906468 1756 EANSLLSNHSE----KLQAAEELLKeagSKTQESN 1786
Cdd:cd07652 158 KGNKSAAQHEDellrKVQAADQDYA---SKVNAAQ 189
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1766-1981 |
3.13e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 3.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1766 EKLQA-AEELLKEAGSKTqesnlllllvKANLKEFQEKKLRVQEEQNVTSELiakgrewvdaagthtAAAQDTLTQLEHH 1844
Cdd:COG4717 49 ERLEKeADELFKPQGRKP----------ELNLKELKELEEELKEAEEKEEEY---------------AELQEELEELEEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1845 RDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQHASELQSRAGALDRDLENVRNvslnatsaahVHSNIQTLTEEAE 1924
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE----------LEEELEELEAELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1431906468 1925 MLAADAHKTANKTDLISE----SLASRGKAVLQRSSRFLKESVSTRRKQQGITMKLDELKN 1981
Cdd:COG4717 174 ELQEELEELLEQLSLATEeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1609-1808 |
5.29e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1609 QRYLIKENAKKIRAEIqlEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLNQT 1688
Cdd:COG1340 30 KRDELNEELKELAEKR--DELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1689 arkdfQPPVSALQSMhqnISSLLglikernftEMQQNATLELKAAKDLLSRIQKRfqkpQEKLKALKEANSLLSNHSEKL 1768
Cdd:COG1340 108 -----GGSIDKLRKE---IERLE---------WRQQTEVLSPEEEKELVEKIKEL----EKELEKAKKALEKNEKLKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1431906468 1769 QAAEELLKEAGSKTQEsnlllllVKANLKEFQEKKLRVQE 1808
Cdd:COG1340 167 AELKELRKEAEEIHKK-------IKELAEEAQELHEEMIE 199
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
715-739 |
5.45e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.29 E-value: 5.45e-03
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1625-1778 |
6.66e-03 |
|
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: 41.06 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1625 QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLNQ---TAR--KDFQppvsA 1699
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgNVRnnKEYE----A 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1431906468 1700 LQsmHQnISSLLGLIKERNFTEMQQNATLElkAAKDLLSRIQKRFQKPQEKLKALKEAnslLSNHSEKLQAAEELLKEA 1778
Cdd:COG1579 94 LQ--KE-IESLKRRISDLEDEILELMERIE--ELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAE 164
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
715-747 |
9.03e-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: 9.03e-03
10 20 30
....*....|....*....|....*....|...
gi 1431906468 715 HCECPQGYTGTSCEACLPGYYRVDGILFGgiCQ 747
Cdd:cd00055 20 QCECKPNTTGRRCDRCAPGYYGLPSQGGG--CQ 50
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1625-1840 |
9.57e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.36 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1625 QLEGIAEQTEN------LQKELTRVLARHQKVNAEMERtsngTQALATFIEQLHANIKEITEKVATLNQTARKDFQP--- 1695
Cdd:pfam12795 1 KLDELEKAKLDeaakkkLLQDLQQALSLLDKIDASKQR----AAAYQKALDDAPAELRELRQELAALQAKAEAAPKEila 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431906468 1696 --PVSALQSMHQNISSLLGLIKERNFTEMQQNATLE--LKAAKDLLSRIQKRFQKPQEKLKALKEANSLLSNHSEKLQAA 1771
Cdd:pfam12795 77 slSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQtrPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1431906468 1772 EELLKEAGSKTQE-----SNLLLLLVKANLKEFQEKKLRVQEEQNVTSELI-AKGREWVDAAgthtAAAQDTLTQ 1840
Cdd:pfam12795 157 ELAALKAQIDMLEqellsNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLnEKRLQEAEQA----VAQTEQLAE 227
|
|
| |
