|
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 ... |
1337-1592 |
3.21e-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: 3.21e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1337 VLSLN-LTGVSPAPYGILENLENTTKYFQRYLIKENAKKIRAEI---QLEGIAEQTENLQKELTRVLARHQKVNAEMERT 1412
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEIlekELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1413 SNGTQALATFIEQLHANIKEITEKVATLNQtarKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLL 1492
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1493 SRIQKRFQKPQEKLKALKEA-NSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSEL 1571
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANAlRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 1720389100 1572 IAKGREWVDAAGTHTAAAQDT 1592
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
1773-1907 |
7.25e-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: 7.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1773 ARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKT 1852
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389100 1853 LEEN---LSRNLSEIKLLISRARKQVASIKVAVSADRDCIRAYQPQTSSTNYNTLILN 1907
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
980-1122 |
4.97e-49 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 171.30 E-value: 4.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 980 YWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGTGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQDYEVRMKEEFWKYf 1059
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 1060 nsVSEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGRKAvelpAEGEAALLLE 1122
Cdd:pfam00052 80 --SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG----GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
330-469 |
6.91e-44 |
|
Laminin B (Domain IV);
:
Pssm-ID: 459652 Cd Length: 136 Bit Score: 156.66 E-value: 6.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 330 YWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETvdSDLMSHADIIIKGNGLTISTRAEG-LSLQPYEEYFNVVRLVPENFR 408
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG--GSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 409 DfDTRREIDRDQLMTVLANVTHLLIRANYNSaKMALYRLDSVSLDIASPNAIDLaVAADVE 469
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYST-GSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2506-2635 |
3.06e-42 |
|
Laminin G domain;
:
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 151.70 E-value: 3.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2506 IRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSVT 2585
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 2586 -VVGNATTLDVERKLYLGGLPSHYRARNIGTITHSIPACIGEIMVNGQQLD 2635
Cdd:pfam00054 81 sPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2655-2808 |
3.21e-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: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2655 GTFFEGSGYAALVKEGYKvRLDLNITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRaar 2733
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 2734 aLCDGKWHTLQAHKSKHRIVLTVDGNSVRAESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 2808
Cdd:cd00110 77 -LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2069-2225 |
3.48e-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: 3.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2069 SFHFDGSGYAMVEKTLRPTV-TQIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNG 2147
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTrLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389100 2148 TWYKIAFQRNRKQGLLAVfdaydtsDKEtKQGETPGAASDLNRLEKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2225
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV-------DGE-RVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2250-2414 |
6.67e-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: 6.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2250 SVSFLRGGYVEMPPKSL-SPESSLLATFATKNSSGILLVAlgkdaeeagGAQAHVPFFSIMLLEGRIEVHVNSGDGTslr 2328
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYA---------GSQNGGDFLALELEDGRLVLRYDLGSGS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2329 kALLHAPTgSYSDGQEHSISLVRNRRVITIQVDENSPVEMKLgPLTEGKTIDISNLYIGGLPEDKATPMLKMRTSFHGCI 2408
Cdd:cd00110 69 -LVLSSKT-PLNDGQWHSVSVERNGRSVTLSVDGERVVESGS-PGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 1720389100 2409 KNVVLD 2414
Cdd:cd00110 146 RDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1891-2040 |
2.65e-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: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1891 AYQPQTSSTNYNTLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEfPEVSINNNRWHSIYITR 1970
Cdd:cd00110 11 RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQWHSVSVER 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1971 FGNMGSLSVKeasaaENPPVRTSKSPGPskvLDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLN 2040
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. |
664-710 |
4.42e-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: 71.23 E-value: 4.42e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 664 CDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGLDTGLGC 710
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
159-218 |
2.45e-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: 63.53 E-value: 2.45e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 159 CNCDPVGSLSSVCIKddrhadlangkWPGQCPCRKGYAGDKCDRCQFGYRGFPNCIPCDC 218
Cdd:pfam00053 1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1271-1308 |
6.72e-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: 62.37 E-value: 6.72e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1720389100 1271 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1308
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
806-854 |
1.71e-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: 61.22 E-value: 1.71e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720389100 806 CNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGYRSFPDCVPCGC 854
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1165-1211 |
1.76e-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: 61.22 E-value: 1.76e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1165 CNCNNH---SDVCDPETGKCLsCRDHTSGDHCELCASGYYGKVTGLPGDC 1211
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
503-551 |
2.16e-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: 58.13 E-value: 2.16e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 503 PCECHGHAS---ECD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRgtPGDCQ 551
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. |
852-909 |
2.61e-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: 57.75 E-value: 2.61e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389100 852 CGCDLRGTLPDTCDLEqglcscsedGGTCSCKENAVGPQCSKCQAGTFALRGDNPQGC 909
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
713-757 |
5.21e-10 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1720389100 713 CNCSVEGSVSDNC-TEEGQCHCGPGVSGKQCDRCSHGFYAFQDGGC 757
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
610-662 |
1.79e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.44 E-value: 1.79e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 610 PCNCSGNVDplEAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVTAKNCR 662
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. |
216-262 |
4.25e-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: 54.28 E-value: 4.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 216 CDCRTVGSLNeDPCIE---PCLCKKNVEGKNCDRCKPGFYNLKERNPEGC 262
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
759-804 |
2.30e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.30e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 759 PCDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGLDPE-QGCQ 804
Cdd:cd00055 1 PCDCnghGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
553-608 |
4.08e-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: 51.59 E-value: 4.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389100 553 CACPLSIDSnnfSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGGTC 608
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETG---QC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
32-79 |
4.89e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 4.89e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 32 CICYGHAS---SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPGT 79
Cdd:cd00055 2 CDCNGHGSlsgQC----DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1466-1790 |
6.00e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
:
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1466 LGLIKERNFTEMQQNATLE-LKAAKDLLSRIQKRFQKPQEKLKALKE----ANSLLSNHSEKLQAAEELLKEAGSKTQES 1540
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEqLRKALFELDKLQEELEQLREELEQAREeleqLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1541 NLLLLLVKANLKEFQEKKLRVQEEqnvtseliakgrewvdaagthtaaaqdtLTQLEHHRDELLLWARKIRSHVDDLVMQ 1620
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEE----------------------------LEELQKERQDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1621 MSKRRARdlvhraeqhASELQSRAGALDRDLENVRNvSLNATSAAHVHSNIQTLTEEAEMLAADAHKTANKTDLISESLA 1700
Cdd:COG4372 145 IAEREEE---------LKELEEQLESLQEELAALEQ-ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1701 SRGKAVLQRSSRFLKESVSTRRKQQGITMKLDELKNLTSQFQESMDNIMKQANDSLA-MLRESPGGMREKGRKARELAAA 1779
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKdTEEEELEIAALELEALEEAALE 294
|
330
....*....|.
gi 1720389100 1780 ANESAVKTLED 1790
Cdd:COG4372 295 LKLLALLLNLA 305
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1214-1268 |
3.02e-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: 46.19 E-value: 3.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 1214 CTCPHHPpfSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGSC 1268
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_N super family |
cl02806 |
Laminin N-terminal (Domain VI); |
7-30 |
2.47e-04 |
|
Laminin N-terminal (Domain VI);
The actual alignment was detected with superfamily member smart00136:
Pssm-ID: 470680 Cd Length: 238 Bit Score: 45.43 E-value: 2.47e-04
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
470-494 |
6.48e-03 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 6.48e-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 ... |
1337-1592 |
3.21e-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: 3.21e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1337 VLSLN-LTGVSPAPYGILENLENTTKYFQRYLIKENAKKIRAEI---QLEGIAEQTENLQKELTRVLARHQKVNAEMERT 1412
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEIlekELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1413 SNGTQALATFIEQLHANIKEITEKVATLNQtarKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLL 1492
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1493 SRIQKRFQKPQEKLKALKEA-NSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSEL 1571
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANAlRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 1720389100 1572 IAKGREWVDAAGTHTAAAQDT 1592
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
1773-1907 |
7.25e-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: 7.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1773 ARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKT 1852
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389100 1853 LEEN---LSRNLSEIKLLISRARKQVASIKVAVSADRDCIRAYQPQTSSTNYNTLILN 1907
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
980-1122 |
4.97e-49 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 171.30 E-value: 4.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 980 YWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGTGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQDYEVRMKEEFWKYf 1059
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 1060 nsVSEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGRKAvelpAEGEAALLLE 1122
Cdd:pfam00052 80 --SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG----GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
330-469 |
6.91e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 156.66 E-value: 6.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 330 YWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETvdSDLMSHADIIIKGNGLTISTRAEG-LSLQPYEEYFNVVRLVPENFR 408
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG--GSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 409 DfDTRREIDRDQLMTVLANVTHLLIRANYNSaKMALYRLDSVSLDIASPNAIDLaVAADVE 469
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYST-GSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
327-457 |
1.34e-43 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 155.50 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 327 STYYWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETVdsdLMSHADIIIKGNGLTISTRAEGlSLQPYEEYFNVVRLVPEN 406
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGT---HVSAPDVILEGNGLRISHPAEG-PPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 407 FRDFDtRREIDRDQLMTVLANVTHLLIRANYnSAKMALYRLDSVSLDIASP 457
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATY-SQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2506-2635 |
3.06e-42 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 151.70 E-value: 3.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2506 IRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSVT 2585
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 2586 -VVGNATTLDVERKLYLGGLPSHYRARNIGTITHSIPACIGEIMVNGQQLD 2635
Cdd:pfam00054 81 sPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
976-1106 |
6.01e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 145.10 E-value: 6.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 976 AEPFYWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGtGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQdyEVRMKEEF 1055
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGNGLRISHPAEGPPLPDELTTV--EVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 1056 WKYFNsvsEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGR 1106
Cdd:smart00281 79 WQYYG---GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAV 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2655-2808 |
3.21e-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: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2655 GTFFEGSGYAALVKEGYKvRLDLNITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRaar 2733
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 2734 aLCDGKWHTLQAHKSKHRIVLTVDGNSVRAESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 2808
Cdd:cd00110 77 -LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2069-2225 |
3.48e-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: 3.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2069 SFHFDGSGYAMVEKTLRPTV-TQIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNG 2147
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTrLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389100 2148 TWYKIAFQRNRKQGLLAVfdaydtsDKEtKQGETPGAASDLNRLEKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2225
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV-------DGE-RVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2678-2810 |
2.04e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 132.46 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2678 NITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRAaraLCDGKWHTLQAHKSKHRIVLTV 2756
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKgGGDYLALELRDGRLVLRYDLGSGPARLTSDPTP---LNDGQWHRVAVERNGRSVTLSV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 2757 DG-NSVRAESPHTHsTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRLSR 2810
Cdd:smart00282 78 DGgNRVSGESPGGL-TILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2479-2630 |
6.89e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 131.77 E-value: 6.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2479 FGLSQNSHLVLPlNQSDVRKRLQVQLSIRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDG 2558
Cdd:cd00110 2 VSFSGSSYVRLP-TLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389100 2559 KWHTVKTEYIKRKAFMTVDGQESPSVTVVGNATTLDVERKLYLGGLPSHYRARnIGTITHSIPACIGEIMVN 2630
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP-GLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2501-2632 |
1.81e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 126.69 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2501 QVQLSIRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPAL-LSDGKWHTVKTEYIKRKAFMTVDGQ 2579
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 2580 ESPSVTVVGNATTLDVERKLYLGGLPSHYRARnIGTITHSIPACIGEIMVNGQ 2632
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLP-PLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2090-2227 |
7.12e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 125.14 E-value: 7.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2090 QIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLM-TDRRYNNGTWYKIAFQRNRKQGLLAVfda 2168
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTsDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2169 ydtsDKETKQ-GETPGAASDLNRleKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEISR 2227
Cdd:smart00282 78 ----DGGNRVsGESPGGLTILNL--DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2250-2414 |
6.67e-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: 6.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2250 SVSFLRGGYVEMPPKSL-SPESSLLATFATKNSSGILLVAlgkdaeeagGAQAHVPFFSIMLLEGRIEVHVNSGDGTslr 2328
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYA---------GSQNGGDFLALELEDGRLVLRYDLGSGS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2329 kALLHAPTgSYSDGQEHSISLVRNRRVITIQVDENSPVEMKLgPLTEGKTIDISNLYIGGLPEDKATPMLKMRTSFHGCI 2408
Cdd:cd00110 69 -LVLSSKT-PLNDGQWHSVSVERNGRSVTLSVDGERVVESGS-PGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 1720389100 2409 KNVVLD 2414
Cdd:cd00110 146 RDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2683-2808 |
9.41e-30 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 115.98 E-value: 9.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2683 FRTTSKNGVLLGISSAKVDAIGLEIVDGKVLFHVNNGAGRITATYQPRAaraLCDGKWHTLQAHKSKHRIVLTVDGNSVR 2762
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKN---LNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720389100 2763 AESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 2808
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2095-2227 |
1.12e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 115.88 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2095 FSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNGTWYKIAFQRNRKQGLLAVfdaydtSDK 2174
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSV------DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 2175 ETKQGETP-GAASDLNrlEKDLIYVGGLPHSKAVRK-GVSSRSYVGCIKNLEISR 2227
Cdd:pfam00054 75 ARPTGESPlGATTDLD--VDGPLYVGGLPSLGVKKRrLAISPSFDGCIRDVIVNG 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1891-2040 |
2.65e-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: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1891 AYQPQTSSTNYNTLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEfPEVSINNNRWHSIYITR 1970
Cdd:cd00110 11 RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQWHSVSVER 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1971 FGNMGSLSVKeasaaENPPVRTSKSPGPskvLDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLN 2040
Cdd:cd00110 90 NGRSVTLSVD-----GERVVESGSPGGS---ALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1903-2042 |
3.31e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 114.74 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1903 TLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVSINNNRWHSIYITRFGNMGSLSVkea 1982
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1983 saaENPPVRTSKSPGPSKVLDINnsTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLNGK 2042
Cdd:smart00282 78 ---DGGNRVSGESPGGLTILNLD--GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1908-2045 |
1.56e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 109.71 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1908 VKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVsINNNRWHSIYITRFGNMGSLSVkeasaAEN 1987
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK-LNDGKWHSVELERNGRSGTLSV-----DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389100 1988 PPVRTSKSPGPSKVLDINnsTLMFVGGLGGQI-KKSPAVKVTHFKGCMGEAFLNGKSIG 2045
Cdd:pfam00054 75 ARPTGESPLGATTDLDVD--GPLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2275-2414 |
1.78e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 109.74 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2275 TFATKNSSGILLVALGKDaeeaggaqaHVPFFSIMLLEGRIEVHVNSGDGTslrkALLHAPTGSYSDGQEHSISLVRNRR 2354
Cdd:smart00282 5 SFRTTSPNGLLLYAGSKG---------GGDYLALELRDGRLVLRYDLGSGP----ARLTSDPTPLNDGQWHRVAVERNGR 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2355 VITIQVDENSPVEMKLGPLTEGKTIDiSNLYIGGLPEDKATPMLKMRTSFHGCIKNVVLD 2414
Cdd:smart00282 72 SVTLSVDGGNRVSGESPGGLTILNLD-GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2276-2419 |
2.99e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 108.94 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2276 FATKNSSGILLValgkdaeeaGGAQAHVPFFSIMLLEGRIEVHVNSGDGtslrKALLHAPTGsYSDGQEHSISLVRNRRV 2355
Cdd:pfam00054 1 FRTTEPSGLLLY---------NGTQTERDFLALELRDGRLEVSYDLGSG----AAVVRSGDK-LNDGKWHSVELERNGRS 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389100 2356 ITIQVDENSPV--EMKLGPLTEGKTIDisNLYIGGLPEDKATPMLK-MRTSFHGCIKNVVLDAQLLD 2419
Cdd:pfam00054 67 GTLSVDGEARPtgESPLGATTDLDVDG--PLYVGGLPSLGVKKRRLaISPSFDGCIRDVIVNGKPLD 131
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1353-1884 |
3.94e-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: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1353 LENLENTTKYFQRYLIKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKE 1432
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1433 ITEKVATLN---QTARKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLlsriQKRFQKPQEKLKAL 1509
Cdd:TIGR02168 391 LELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL----QEELERLEEALEEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1510 KEANSLLsnhSEKLQAAEELLKEAGSKTqesnLLLLLVKANLKEFQEKKLRVQEEQN-------VTSELIAKGREW---V 1579
Cdd:TIGR02168 467 REELEEA---EQALDAAERELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSglsgilgVLSELISVDEGYeaaI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1580 DAA-GTHTAA-----------AQDTLTQLEHHRDELL----LWARKIRShvDDLVMQMSKRRARDLVHRAEQHASELQ-- 1641
Cdd:TIGR02168 540 EAAlGGRLQAvvvenlnaakkAIAFLKQNELGRVTFLpldsIKGTEIQG--NDREILKNIEGFLGVAKDLVKFDPKLRka 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1642 ------------SRAGALD---RDLENVRNVSLN-----------------ATSAAHVHSNIQTLTEEAEMLAADAHKTA 1689
Cdd:TIGR02168 618 lsyllggvlvvdDLDNALElakKLRPGYRIVTLDgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1690 NKTDLISESLASRGKAVLQRssrfLKESVSTRRKQQGITMKLDELKNLTSQFQESMDnimkQANDSLAMLRESPGGMREK 1769
Cdd:TIGR02168 698 KALAELRKELEELEEELEQL----RKELEELSRQISALRKDLARLEAEVEQLEERIA----QLSKELTELEAEIEELEER 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1770 GRKARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKP 1849
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
570 580 590
....*....|....*....|....*....|....*
gi 1720389100 1850 LKTLEENLSRNLSEIKLLISRARKQVASIKVAVSA 1884
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
664-710 |
4.42e-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: 71.23 E-value: 4.42e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 664 CDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGLDTGLGC 710
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
663-711 |
1.79e-14 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 69.69 E-value: 1.79e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 663 ACDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGLDT-GLGCV 711
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
664-710 |
4.80e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.49 E-value: 4.80e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 664 CDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGlDTGLGC 710
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. |
159-218 |
2.45e-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: 63.53 E-value: 2.45e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 159 CNCDPVGSLSSVCIKddrhadlangkWPGQCPCRKGYAGDKCDRCQFGYRGFPNCIPCDC 218
Cdd:pfam00053 1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1271-1308 |
6.72e-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: 62.37 E-value: 6.72e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1720389100 1271 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1308
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1271-1308 |
9.70e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.99 E-value: 9.70e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1720389100 1271 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1308
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1271-1308 |
1.31e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.56 E-value: 1.31e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1720389100 1271 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1308
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
806-854 |
1.71e-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: 61.22 E-value: 1.71e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720389100 806 CNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGYRSFPDCVPCGC 854
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1165-1211 |
1.76e-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: 61.22 E-value: 1.76e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1165 CNCNNH---SDVCDPETGKCLsCRDHTSGDHCELCASGYYGKVTGLPGDC 1211
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
503-551 |
2.16e-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: 58.13 E-value: 2.16e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 503 PCECHGHAS---ECD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRgtPGDCQ 551
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. |
852-909 |
2.61e-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: 57.75 E-value: 2.61e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389100 852 CGCDLRGTLPDTCDLEqglcscsedGGTCSCKENAVGPQCSKCQAGTFALRGDNPQGC 909
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1353-1879 |
4.17e-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: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1353 LENLENTTKYFQRYLIKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNG-------TQALATFIEQ 1425
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiarleerRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1426 LHANIKEITEKVATLNQTARkdfqppvsALQSMHQNISSLLGLIKErnftEMQQNATLELKAAKDLLSRIQKRFQKPQEK 1505
Cdd:COG1196 321 LEEELAELEEELEELEEELE--------ELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1506 LKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREwvdaAGTH 1585
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1586 TAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQHASELQ--SRAGALDRDLENVRNVSLnATS 1663
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEAAL-EAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1664 AAHVHSNIQTLTEEAEMLAADAHKTANK---TDLISESLASRGKAVLQRSSRFLKESV----STRRKQQGITMKLDELKN 1736
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAVdlvaSDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1737 LTSQFQESMDNIMKQAND--------SLAMLRESPGGMREKGRKARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRV 1808
Cdd:COG1196 624 GRTLVAARLEAALRRAVTlagrlrevTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 1809 NATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIkLLISRARKQVASIK 1879
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELERELERLE 773
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
713-757 |
5.21e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1720389100 713 CNCSVEGSVSDNC-TEEGQCHCGPGVSGKQCDRCSHGFYAFQDGGC 757
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1164-1212 |
5.31e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 5.31e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720389100 1164 PCNCNNHSDV---CDPETGKCLsCRDHTSGDHCELCASGYYGkVTGLPGDCT 1212
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
158-211 |
9.37e-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: 56.21 E-value: 9.37e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1720389100 158 PCNCDPVGSLSSVCIKDDrhadlangkwpGQCPCRKGYAGDKCDRCQFGYRGFP 211
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. |
713-760 |
9.51e-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: 56.21 E-value: 9.51e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720389100 713 CNCSVEGSVSDNCTEE-GQCHCGPGVSGKQCDRCSHGFYAFQDGGCTPC 760
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
610-662 |
1.79e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.44 E-value: 1.79e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 610 PCNCSGNVDplEAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVTAKNCR 662
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. |
611-657 |
3.11e-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: 3.11e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 611 CNCSGNVDPleAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVT 657
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. |
216-262 |
4.25e-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: 54.28 E-value: 4.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 216 CDCRTVGSLNeDPCIE---PCLCKKNVEGKNCDRCKPGFYNLKERNPEGC 262
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
805-848 |
6.63e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 6.63e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1720389100 805 ACNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGYRSFPD 848
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
504-550 |
1.06e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 1.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 504 CECHGHAS---ECDIH-GICsVCTHNTTGDHCEQCLPGFYGTPSrGTPGDC 550
Cdd:pfam00053 1 CDCNPHGSlsdTCDPEtGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
712-758 |
1.33e-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: 53.13 E-value: 1.33e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 712 PCNCSVEGSVSDNCTEE-GQCHCGPGVSGKQCDRCSHGFY--AFQDGGCT 758
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYglPSQGGGCQ 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1368-1893 |
1.46e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1368 IKENAKKIRAEIQ-LEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITE--KVATLNQTA 1444
Cdd:PRK03918 219 LREELEKLEKEVKeLEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1445 RKDFQPPVSALQSMHQNISSLLGLIK--ERNFTEmqqnatLELKAAKdlLSRIQKRFQKPQEKLKALKEANSLLSNHSEK 1522
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINgiEERIKE------LEEKEER--LEELKKKLKELEKRLEELEERHELYEEAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1523 LQAAEELLKEAGSKTQESnlllllVKANLKEFQEKKLRVQEEqnvTSELIAKGREWVDAAGTHTAA------AQDT---- 1592
Cdd:PRK03918 371 KEELERLKKRLTGLTPEK------LEKELEELEKAKEEIEEE---ISKITARIGELKKEIKELKKAieelkkAKGKcpvc 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1593 ---LTqlEHHRDELLlwarkirshvddlvmqmskRRARDLVHRAEQHASELQSRAGALDRDLENVRNVslnatsaahvhs 1669
Cdd:PRK03918 442 greLT--EEHRKELL-------------------EEYTAELKRIEKELKEIEEKERKLRKELRELEKV------------ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1670 niqtLTEEAEMLAadAHKTANKTDLISESLASRGKAVLQRSS---RFLKESVSTRRKQQGITM----KLDELKNLTSQFQ 1742
Cdd:PRK03918 489 ----LKKESELIK--LKELAEQLKELEEKLKKYNLEELEKKAeeyEKLKEKLIKLKGEIKSLKkeleKLEELKKKLAELE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1743 ESMDNIMKQANDSLAMLRE-SPGGMREKGRKARELAAAANE-----SAVKTLEDVL----ALSLRVFNTSEDLSRVNATV 1812
Cdd:PRK03918 563 KKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEylelkDAEKELEREEkelkKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1813 QET----NDLLHN-STMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIKL---LISRARKQVASIKVA--- 1881
Cdd:PRK03918 643 EELrkelEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEeleEREKAKKELEKLEKAler 722
|
570
....*....|..
gi 1720389100 1882 VSADRDCIRAYQ 1893
Cdd:PRK03918 723 VEELREKVKKYK 734
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
806-849 |
1.84e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 1.84e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1720389100 806 CNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGY--RSFPDC 849
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1165-1211 |
1.97e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 1.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1165 CNCN---NHSDVCDPETGKCLsCRDHTSGDHCELCASGYYGKVtglPGDC 1211
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
159-213 |
2.04e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.04e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389100 159 CNCDPVGSLSSVCIKDDrhadlangkwpGQCPCRKGYAGDKCDRCQFGYRG--FPNC 213
Cdd:smart00180 1 CDCDPGGSASGTCDPDT-----------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
759-804 |
2.30e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.30e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 759 PCDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGLDPE-QGCQ 804
Cdd:cd00055 1 PCDCnghGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
553-608 |
4.08e-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: 51.59 E-value: 4.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389100 553 CACPLSIDSnnfSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGGTC 608
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETG---QC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
852-909 |
4.52e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 4.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389100 852 CGCDLRGTLPDTCDLeqglcscseDGGTCSCKENAVGPQCSKCQAGTFalrGDNPQGC 909
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. |
760-803 |
4.77e-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: 51.59 E-value: 4.77e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720389100 760 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGL--DPEQGC 803
Cdd:pfam00053 1 CDCnphGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
32-79 |
4.89e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 4.89e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 32 CICYGHAS---SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPGT 79
Cdd:cd00055 2 CDCNGHGSlsgQC----DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
760-803 |
9.61e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 9.61e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 760 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGlDPEQGC 803
Cdd:smart00180 1 CDCdpgGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
215-262 |
1.54e-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: 50.05 E-value: 1.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 215 PCDCRTVGSLNEDpCIEP---CLCKKNVEGKNCDRCKPGFYNLKERnPEGC 262
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGtgqCECKPNTTGRRCDRCAPGYYGLPSQ-GGGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1466-1790 |
6.00e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1466 LGLIKERNFTEMQQNATLE-LKAAKDLLSRIQKRFQKPQEKLKALKE----ANSLLSNHSEKLQAAEELLKEAGSKTQES 1540
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEqLRKALFELDKLQEELEQLREELEQAREeleqLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1541 NLLLLLVKANLKEFQEKKLRVQEEqnvtseliakgrewvdaagthtaaaqdtLTQLEHHRDELLLWARKIRSHVDDLVMQ 1620
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEE----------------------------LEELQKERQDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1621 MSKRRARdlvhraeqhASELQSRAGALDRDLENVRNvSLNATSAAHVHSNIQTLTEEAEMLAADAHKTANKTDLISESLA 1700
Cdd:COG4372 145 IAEREEE---------LKELEEQLESLQEELAALEQ-ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1701 SRGKAVLQRSSRFLKESVSTRRKQQGITMKLDELKNLTSQFQESMDNIMKQANDSLA-MLRESPGGMREKGRKARELAAA 1779
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKdTEEEELEIAALELEALEEAALE 294
|
330
....*....|.
gi 1720389100 1780 ANESAVKTLED 1790
Cdd:COG4372 295 LKLLALLLNLA 305
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
851-909 |
8.07e-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: 48.12 E-value: 8.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389100 851 PCGCDLRGTLPDTCDLEqglcscsedGGTCSCKENAVGPQCSKCQAGTFALRgDNPQGC 909
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
504-545 |
1.10e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.10e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1720389100 504 CECH--GHASE-CD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRG 545
Cdd:smart00180 1 CDCDpgGSASGtCDpDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
216-262 |
1.49e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 1.49e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 216 CDCRTVGSLNeDPCIEP---CLCKKNVEGKNCDRCKPGFYNlkeRNPEGC 262
Cdd:smart00180 1 CDCDPGGSAS-GTCDPDtgqCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1356-1888 |
1.82e-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: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1356 LENTTKYFQ-RYLIKENAKKiraeiQLEGIAEQT-ENLQKELTRVLARHQKVNAEMERTSNGTQALatfIEQLHANIKEI 1433
Cdd:TIGR00606 267 LDNEIKALKsRKKQMEKDNS-----ELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1434 T-EKVATLNQTARKDFQPPVSALQSMHQNISSL-LGLIKERNFTEMQQNATLELKAAKDLLSRIQKRfqkpqeklKAlKE 1511
Cdd:TIGR00606 339 NqEKTELLVEQGRLQLQADRHQEHIRARDSLIQsLATRLELDGFERGPFSERQIKNFHTLVIERQED--------EA-KT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1512 ANSLLSNhsekLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKlrVQEEQNVTSELiakgrewvdaagthtaaaqd 1591
Cdd:TIGR00606 410 AAQLCAD----LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK--QEELKFVIKEL-------------------- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1592 tlTQLEHHRDELLLWARKIRSHVDDLvmqmSKRRARDLVHRAEQHASELQSRAGALDRDL--ENVRNVSLNAtsaaHVHS 1669
Cdd:TIGR00606 464 --QQLEGSSDRILELDQELRKAEREL----SKAEKNSLTETLKKEVKSLQNEKADLDRKLrkLDQEMEQLNH----HTTT 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1670 NIQTLTEEAEMLAADAHKTANK----------------TDLISESLASRGKAVLQRSSRFLKESVSTRRKQQGITMKLDE 1733
Cdd:TIGR00606 534 RTQMEMLTKDKMDKDEQIRKIKsrhsdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1734 LKNLTSQFQESMDNIMK----QANDS-LAMLRESpggmREKGRKARE-LAAAAN--ESAVKTLED----VLALSLRVFNT 1801
Cdd:TIGR00606 614 LESKEEQLSSYEDKLFDvcgsQDEESdLERLKEE----IEKSSKQRAmLAGATAvySQFITQLTDenqsCCPVCQRVFQT 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1802 SEDLSRVNATVQETNDLL---HNSTMTTLLAGRKMKD-----MEMQANLLLDRLKPLKTLEE---NLSRNLSEIKLLISR 1870
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLApdkLKSTESELKKKEKRRDemlglAPGRQSIIDLKEKEIPELRNklqKVNRDIQRLKNDIEE 769
|
570
....*....|....*...
gi 1720389100 1871 ARKQVASIKVAVSADRDC 1888
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVC 787
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
610-654 |
2.61e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.54 E-value: 2.61e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1720389100 610 PCNCSGNVDPleagHCDSVTGECLkCLWNTDGAHCERCADGFYGD 654
Cdd:smart00180 2 DCDPGGSASG----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1214-1268 |
3.02e-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: 46.19 E-value: 3.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 1214 CTCPHHPpfSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGSC 1268
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1593-1847 |
5.67e-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: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1593 LTQLEHHRDELLLWARKIRSHVDDlvMQMSKRRARDLvhraEQHASELQSRAGALDRDLENVRNVSlNATSaahvhSNIQ 1672
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQ--IEILEKELSSL----AQETEELQKKATQTLAKAQQVNAES-ERTL-----GHAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1673 TLTEEAEMLAADAHKTANKTDLISE--SLASRGK--AVLQRSSRFLKE--SVSTRRKQQGITMKLDELKNLTSQFQESMD 1746
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLGEndFALPSSDlsRMLAEAQRMLGEirSRDFGTQLQNAEAELKAAQDLLSRIQTWFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1747 NIMKQANDSLAMLRESPGGMREKGRKARELaaaANESAVKTlEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNstmtT 1826
Cdd:pfam06008 166 SPQEENKALANALRDSLAEYEAKLSDLREL---LREAAAKT-RDANRLNLANQANLREFQRKKEEVSEQKNQLEE----T 237
|
250 260
....*....|....*....|.
gi 1720389100 1827 LLAGRkmkDMEMQANLLLDRL 1847
Cdd:pfam06008 238 LKTAR---DSLDAANLLLQEI 255
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
552-606 |
7.93e-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: 45.04 E-value: 7.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 552 PCACPLSIDSNnfsPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGG 606
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTG---QC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1213-1269 |
2.22e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.88 E-value: 2.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389100 1213 PCTCPHHPpfSFSPTCVVEgdsDFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGsCQ 1269
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
471-665 |
4.90e-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: 46.14 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 471 CECPQGY---TGTSCEACLPGyyrvdgilfggicqpcechghasecdiHGICSVCTHNTTGdhCEQCLPGFYGTPSRGTP 547
Cdd:cd13416 1 EACPSGQytsSGECCEQCPPG---------------------------EGVARPCGDNQTV--CEPCLDGVTFSDVVSHT 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 548 GDCQPCA-CPLSIdsnnfSPTCHLTDGEEVVCdqcapgysgswceRCADGYYgnPTVPGGTCVPCNCsgnvdpleaghCD 626
Cdd:cd13416 52 EPCQPCTrCPGLM-----SMRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCEPCTV-----------CP 100
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720389100 627 SVTGECLKCLWNTDgAHCERCADGFYGDAVTAKN----CRACD 665
Cdd:cd13416 101 PGQGVVQSCGPNQD-TVCEACPEGTYSDEDSSTDpclpCTVCE 142
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
553-601 |
5.22e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.68 E-value: 5.22e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720389100 553 CACPLSidsNNFSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNP 601
Cdd:smart00180 1 CDCDPG---GSASGTCDPDTG---QC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
32-75 |
1.42e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 1.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 32 CICY--GHAS-SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPW 75
Cdd:smart00180 1 CDCDpgGSASgTC----DPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
7-30 |
2.47e-04 |
|
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: 45.43 E-value: 2.47e-04
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1214-1261 |
1.66e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.45 E-value: 1.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1720389100 1214 CTCphHPPFSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNP 1261
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. |
32-78 |
2.64e-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: 2.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 32 CICYGHASSCPwDEEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPG 78
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
470-494 |
6.48e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 6.48e-03
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
12-30 |
7.31e-03 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 40.64 E-value: 7.31e-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 ... |
1337-1592 |
3.21e-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: 3.21e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1337 VLSLN-LTGVSPAPYGILENLENTTKYFQRYLIKENAKKIRAEI---QLEGIAEQTENLQKELTRVLARHQKVNAEMERT 1412
Cdd:pfam06008 1 LLSLNsLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEIlekELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1413 SNGTQALATFIEQLHANIKEITEKVATLNQtarKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLL 1492
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGE---NDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1493 SRIQKRFQKPQEKLKALKEA-NSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSEL 1571
Cdd:pfam06008 158 SRIQTWFQSPQEENKALANAlRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEET 237
|
250 260
....*....|....*....|.
gi 1720389100 1572 IAKGREWVDAAGTHTAAAQDT 1592
Cdd:pfam06008 238 LKTARDSLDAANLLLQEIDDA 258
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
1773-1907 |
7.25e-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: 7.25e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1773 ARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKT 1852
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389100 1853 LEEN---LSRNLSEIKLLISRARKQVASIKVAVSADRDCIRAYQPQTSSTNYNTLILN 1907
Cdd:pfam06009 81 LEVNsssLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
980-1122 |
4.97e-49 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 171.30 E-value: 4.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 980 YWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGTGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQDYEVRMKEEFWKYf 1059
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGGSLNSEPDVILEGNGLRLSYSSPDQPPPDPGQEQTYSVRLHEENWRD- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 1060 nsVSEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGRKAvelpAEGEAALLLE 1122
Cdd:pfam00052 80 --SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPG----GSGPPASWVE 136
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
330-469 |
6.91e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 156.66 E-value: 6.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 330 YWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETvdSDLMSHADIIIKGNGLTISTRAEG-LSLQPYEEYFNVVRLVPENFR 408
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG--GSLNSEPDVILEGNGLRLSYSSPDqPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 409 DfDTRREIDRDQLMTVLANVTHLLIRANYNSaKMALYRLDSVSLDIASPNAIDLaVAADVE 469
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYST-GSGQVSLSNVSLDSAVPGGSGP-PASWVE 136
|
|
| LamB |
smart00281 |
Laminin B domain; |
327-457 |
1.34e-43 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 155.50 E-value: 1.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 327 STYYWAAPEAYLGNKLTAFGGFLKYTVSYDIPVETVdsdLMSHADIIIKGNGLTISTRAEGlSLQPYEEYFNVVRLVPEN 406
Cdd:smart00281 3 EPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGGT---HVSAPDVILEGNGLRISHPAEG-PPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 407 FRDFDtRREIDRDQLMTVLANVTHLLIRANYnSAKMALYRLDSVSLDIASP 457
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATY-SQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2506-2635 |
3.06e-42 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 151.70 E-value: 3.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2506 IRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSVT 2585
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 2586 -VVGNATTLDVERKLYLGGLPSHYRARNIGTITHSIPACIGEIMVNGQQLD 2635
Cdd:pfam00054 81 sPLGATTDLDVDGPLYVGGLPSLGVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamB |
smart00281 |
Laminin B domain; |
976-1106 |
6.01e-40 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 145.10 E-value: 6.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 976 AEPFYWRLPKQFQGDQLLAYGGKLQYSVAFYSTLGtGTSNYEPQVLIKGGRARKHVIYMDAPAPENGVRQdyEVRMKEEF 1055
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRG-GTHVSAPDVILEGNGLRISHPAEGPPLPDELTTV--EVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 1056 WKYFNsvsEKHVTHSDFMSVLSNIDYILIKASYGQGLQQSRIANISMEVGR 1106
Cdd:smart00281 79 WQYYG---GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAV 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2655-2808 |
3.21e-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: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2655 GTFFEGSGYAALVKEGYKvRLDLNITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRaar 2733
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAP-RTRLSISFSFRTTSPNGLLLYAGSQnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTP--- 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 2734 aLCDGKWHTLQAHKSKHRIVLTVDGNSVRAESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 2808
Cdd:cd00110 77 -LNDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2069-2225 |
3.48e-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: 3.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2069 SFHFDGSGYAMVEKTLRPTV-TQIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNG 2147
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTrLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389100 2148 TWYKIAFQRNRKQGLLAVfdaydtsDKEtKQGETPGAASDLNRLEKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2225
Cdd:cd00110 81 QWHSVSVERNGRSVTLSV-------DGE-RVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2678-2810 |
2.04e-35 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 132.46 E-value: 2.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2678 NITLEFRTTSKNGVLLGISSA-KVDAIGLEIVDGKVLFHVNNGAGRITATYQPRAaraLCDGKWHTLQAHKSKHRIVLTV 2756
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKgGGDYLALELRDGRLVLRYDLGSGPARLTSDPTP---LNDGQWHRVAVERNGRSVTLSV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 2757 DG-NSVRAESPHTHsTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRLSR 2810
Cdd:smart00282 78 DGgNRVSGESPGGL-TILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2479-2630 |
6.89e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 131.77 E-value: 6.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2479 FGLSQNSHLVLPlNQSDVRKRLQVQLSIRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPALLSDG 2558
Cdd:cd00110 2 VSFSGSSYVRLP-TLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720389100 2559 KWHTVKTEYIKRKAFMTVDGQESPSVTVVGNATTLDVERKLYLGGLPSHYRARnIGTITHSIPACIGEIMVN 2630
Cdd:cd00110 81 QWHSVSVERNGRSVTLSVDGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSP-GLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
2501-2632 |
1.81e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 126.69 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2501 QVQLSIRTFASSGLIYYVAHQNQMDYATLQLQEGRLHFMFDLGKGRTKVSHPAL-LSDGKWHTVKTEYIKRKAFMTVDGQ 2579
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTpLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 2580 ESPSVTVVGNATTLDVERKLYLGGLPSHYRARnIGTITHSIPACIGEIMVNGQ 2632
Cdd:smart00282 81 NRVSGESPGGLTILNLDGPLYLGGLPEDLKLP-PLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
2090-2227 |
7.12e-33 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 125.14 E-value: 7.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2090 QIVILFSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLM-TDRRYNNGTWYKIAFQRNRKQGLLAVfda 2168
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTsDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2169 ydtsDKETKQ-GETPGAASDLNRleKDLIYVGGLPHSKAVRKGVSSRSYVGCIKNLEISR 2227
Cdd:smart00282 78 ----DGGNRVsGESPGGLTILNL--DGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2250-2414 |
6.67e-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: 6.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2250 SVSFLRGGYVEMPPKSL-SPESSLLATFATKNSSGILLVAlgkdaeeagGAQAHVPFFSIMLLEGRIEVHVNSGDGTslr 2328
Cdd:cd00110 1 GVSFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYA---------GSQNGGDFLALELEDGRLVLRYDLGSGS--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2329 kALLHAPTgSYSDGQEHSISLVRNRRVITIQVDENSPVEMKLgPLTEGKTIDISNLYIGGLPEDKATPMLKMRTSFHGCI 2408
Cdd:cd00110 69 -LVLSSKT-PLNDGQWHSVSVERNGRSVTLSVDGERVVESGS-PGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCI 145
|
....*.
gi 1720389100 2409 KNVVLD 2414
Cdd:cd00110 146 RDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2683-2808 |
9.41e-30 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 115.98 E-value: 9.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2683 FRTTSKNGVLLGISSAKVDAIGLEIVDGKVLFHVNNGAGRITATYQPRAaraLCDGKWHTLQAHKSKHRIVLTVDGNSVR 2762
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKN---LNDGQWHSVRVERNGNTLTLSVDGQTVV 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1720389100 2763 AESPHTHSTSADTNDPIYVGGYPAHIKQNCLSSRASFRGCVRNLRL 2808
Cdd:pfam02210 78 SSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRV 123
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2095-2227 |
1.12e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 115.88 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2095 FSTFSPNGLLFYLASNGTKDFLSIELVRGRVKVMVDLGSGPLTLMTDRRYNNGTWYKIAFQRNRKQGLLAVfdaydtSDK 2174
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSV------DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 2175 ETKQGETP-GAASDLNrlEKDLIYVGGLPHSKAVRK-GVSSRSYVGCIKNLEISR 2227
Cdd:pfam00054 75 ARPTGESPlGATTDLD--VDGPLYVGGLPSLGVKKRrLAISPSFDGCIRDVIVNG 127
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1891-2040 |
2.65e-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: 2.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1891 AYQPQTSSTNYNTLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEfPEVSINNNRWHSIYITR 1970
Cdd:cd00110 11 RLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQWHSVSVER 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1971 FGNMGSLSVKeasaaENPPVRTSKSPGPskvLDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLN 2040
Cdd:cd00110 90 NGRSVTLSVD-----GERVVESGSPGGS---ALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1903-2042 |
3.31e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 114.74 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1903 TLILNVKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVSINNNRWHSIYITRFGNMGSLSVkea 1982
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSV--- 77
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1983 saaENPPVRTSKSPGPSKVLDINnsTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLNGK 2042
Cdd:smart00282 78 ---DGGNRVSGESPGGLTILNLD--GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2683-2813 |
9.03e-29 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 113.18 E-value: 9.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2683 FRTTSKNGVLL-GISSAKVDAIGLEIVDGKVLFHVNNGAGRITATYQPRaaraLCDGKWHTLQAHKSKHRIVLTVDGN-S 2760
Cdd:pfam00054 1 FRTTEPSGLLLyNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK----LNDGKWHSVELERNGRSGTLSVDGEaR 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1720389100 2761 VRAESPHTHSTSADTNDPIYVGGYPAHIKQN-CLSSRASFRGCVRNLRLSRGSQ 2813
Cdd:pfam00054 77 PTGESPLGATTDLDVDGPLYVGGLPSLGVKKrRLAISPSFDGCIRDVIVNGKPL 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1908-2045 |
1.56e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 109.71 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1908 VKTQEPDNLLFYLGSSSSSDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVsINNNRWHSIYITRFGNMGSLSVkeasaAEN 1987
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVVRSGDK-LNDGKWHSVELERNGRSGTLSV-----DGE 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389100 1988 PPVRTSKSPGPSKVLDINnsTLMFVGGLGGQI-KKSPAVKVTHFKGCMGEAFLNGKSIG 2045
Cdd:pfam00054 75 ARPTGESPLGATTDLDVD--GPLYVGGLPSLGvKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
smart00282 |
Laminin G domain; |
2275-2414 |
1.78e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 109.74 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2275 TFATKNSSGILLVALGKDaeeaggaqaHVPFFSIMLLEGRIEVHVNSGDGTslrkALLHAPTGSYSDGQEHSISLVRNRR 2354
Cdd:smart00282 5 SFRTTSPNGLLLYAGSKG---------GGDYLALELRDGRLVLRYDLGSGP----ARLTSDPTPLNDGQWHRVAVERNGR 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2355 VITIQVDENSPVEMKLGPLTEGKTIDiSNLYIGGLPEDKATPMLKMRTSFHGCIKNVVLD 2414
Cdd:smart00282 72 SVTLSVDGGNRVSGESPGGLTILNLD-GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVN 130
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2276-2419 |
2.99e-27 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 108.94 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2276 FATKNSSGILLValgkdaeeaGGAQAHVPFFSIMLLEGRIEVHVNSGDGtslrKALLHAPTGsYSDGQEHSISLVRNRRV 2355
Cdd:pfam00054 1 FRTTEPSGLLLY---------NGTQTERDFLALELRDGRLEVSYDLGSG----AAVVRSGDK-LNDGKWHSVELERNGRS 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389100 2356 ITIQVDENSPV--EMKLGPLTEGKTIDisNLYIGGLPEDKATPMLK-MRTSFHGCIKNVVLDAQLLD 2419
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 ... |
2095-2225 |
1.43e-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: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2095 FSTFSPNGLLFYlASNGTKDFLSIELVRGRVKVMVDLGSGPLTLM-TDRRYNNGTWYKIAFQRNRKQGLLAVfdaydtsD 2173
Cdd:pfam02210 1 FRTRQPNGLLLY-AGGGGSDFLALELVNGRLVLRYDLGSGPESLLsSGKNLNDGQWHSVRVERNGNTLTLSV-------D 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1720389100 2174 KETKQGETPGAASDLNRLEKDLiYVGGLPHSKAVRKGVSSRSYVGCIKNLEI 2225
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 ... |
2276-2416 |
8.83e-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: 8.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2276 FATKNSSGILLVALGKDAEeaggaqahvpFFSIMLLEGRIEVHVNSGDGTslrkALLHAPTGSYSDGQEHSISLVRNRRV 2355
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSD----------FLALELVNGRLVLRYDLGSGP----ESLLSSGKNLNDGQWHSVRVERNGNT 66
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 2356 ITIQVDENSPVEMKLGPLTEGKTIDiSNLYIGGLPEDKATPMLKMRTSFHGCIKNVVLDAQ 2416
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 ... |
1908-2042 |
1.60e-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: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1908 VKTQEPDNLLFYLGSSSSsDFLAVEMRRGKVAFLWDLGSGSTRLEFPEVSINNNRWHSIYITRFGNMGSLSVKEasaaen 1987
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDG------ 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 1988 ppVRTSKSPGPSKVLDINNSTLMFVGGLGGQIKKSPAVKVTHFKGCMGEAFLNGK 2042
Cdd:pfam02210 74 --QTVVSSLPPGESLLLNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2506-2632 |
2.11e-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: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 2506 IRTFASSGLIYYVAHQNQmDYATLQLQEGRLHFMFDLGKGRTKV-SHPALLSDGKWHTVKTEYIKRKAFMTVDGQESPSV 2584
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGS-DFLALELVNGRLVLRYDLGSGPESLlSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1720389100 2585 TVVGNATTLDVERKLYLGGLPSHYRARNIGTiTHSIPACIGEIMVNGQ 2632
Cdd:pfam02210 80 LPPGESLLLNLNGPLYLGGLPPLLLLPALPV-RAGFVGCIRDVRVNGE 126
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1353-1884 |
3.94e-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: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1353 LENLENTTKYFQRYLIKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKE 1432
Cdd:TIGR02168 311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1433 ITEKVATLN---QTARKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLlsriQKRFQKPQEKLKAL 1509
Cdd:TIGR02168 391 LELQIASLNneiERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEEL----QEELERLEEALEEL 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1510 KEANSLLsnhSEKLQAAEELLKEAGSKTqesnLLLLLVKANLKEFQEKKLRVQEEQN-------VTSELIAKGREW---V 1579
Cdd:TIGR02168 467 REELEEA---EQALDAAERELAQLQARL----DSLERLQENLEGFSEGVKALLKNQSglsgilgVLSELISVDEGYeaaI 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1580 DAA-GTHTAA-----------AQDTLTQLEHHRDELL----LWARKIRShvDDLVMQMSKRRARDLVHRAEQHASELQ-- 1641
Cdd:TIGR02168 540 EAAlGGRLQAvvvenlnaakkAIAFLKQNELGRVTFLpldsIKGTEIQG--NDREILKNIEGFLGVAKDLVKFDPKLRka 617
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1642 ------------SRAGALD---RDLENVRNVSLN-----------------ATSAAHVHSNIQTLTEEAEMLAADAHKTA 1689
Cdd:TIGR02168 618 lsyllggvlvvdDLDNALElakKLRPGYRIVTLDgdlvrpggvitggsaktNSSILERRREIEELEEKIEELEEKIAELE 697
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1690 NKTDLISESLASRGKAVLQRssrfLKESVSTRRKQQGITMKLDELKNLTSQFQESMDnimkQANDSLAMLRESPGGMREK 1769
Cdd:TIGR02168 698 KALAELRKELEELEEELEQL----RKELEELSRQISALRKDLARLEAEVEQLEERIA----QLSKELTELEAEIEELEER 769
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1770 GRKARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKP 1849
Cdd:TIGR02168 770 LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEE 849
|
570 580 590
....*....|....*....|....*....|....*
gi 1720389100 1850 LKTLEENLSRNLSEIKLLISRARKQVASIKVAVSA 1884
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESELEALLNERAS 884
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
664-710 |
4.42e-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: 71.23 E-value: 4.42e-15
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 664 CDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGLDTGLGC 710
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
663-711 |
1.79e-14 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 69.69 E-value: 1.79e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 663 ACDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGLDT-GLGCV 711
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSqGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
664-710 |
4.80e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 68.49 E-value: 4.80e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 664 CDCHENGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGlDTGLGC 710
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 ... |
1367-1916 |
4.83e-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: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1367 LIKENAKKIRAEIQLEGIAEQTENLQKE---LTRVLARHQKVNAEME----RTSNGTQALATFIEQLHANIKEITEKVAT 1439
Cdd:pfam01576 14 LQKVKERQQKAESELKELEKKHQQLCEEknaLQEQLQAETELCAEAEemraRLAARKQELEEILHELESRLEEEEERSQQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1440 LnQTARKDFQPPV-----------SALQSMHQNISSLLGLIK---ERNFTEMQQNATL--ELKAAKDLLSRIQKRFQKPQ 1503
Cdd:pfam01576 94 L-QNEKKKMQQHIqdleeqldeeeAARQKLQLEKVTTEAKIKkleEDILLLEDQNSKLskERKLLEERISEFTSNLAEEE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1504 EKLKALkeaNSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEK--KLRVQEEQnVTSELIAKGREwvda 1581
Cdd:pfam01576 173 EKAKSL---SKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQiaELQAQIAE-LRAQLAKKEEE---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1582 agthTAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQM-SKRRARDlvhRAEQHASELQSRAGALDRDLENvrnvSLN 1660
Cdd:pfam01576 245 ----LQAALARLEEETAQKNNALKKIRELEAQISELQEDLeSERAARN---KAEKQRRDLGEELEALKTELED----TLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1661 ATSA---------AHVHSNIQTLTEEAEM----LAADAHKTANKTDLISESL--ASRGKAVLQRSSRFLKE-----SVST 1720
Cdd:pfam01576 314 TTAAqqelrskreQEVTELKKALEEETRSheaqLQEMRQKHTQALEELTEQLeqAKRNKANLEKAKQALESenaelQAEL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1721 RRKQQGITMKLDELKNLTSQFQEsmdnIMKQANDSlamlrespggMREKGRKARELAAAANE--SAVKTLEDVLALSLRV 1798
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKLEGQLQE----LQARLSES----------ERQRAELAEKLSKLQSEleSVSSLLNEAEGKNIKL 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1799 fntSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIKLLISRARKQVASI 1878
Cdd:pfam01576 460 ---SKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEED 536
|
570 580 590
....*....|....*....|....*....|....*...
gi 1720389100 1879 KVAVSADRDCIRAYQPQTSSTnynTLILNVKTQEPDNL 1916
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. |
159-218 |
2.45e-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: 63.53 E-value: 2.45e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 159 CNCDPVGSLSSVCIKddrhadlangkWPGQCPCRKGYAGDKCDRCQFGYRGFPNCIPCDC 218
Cdd:pfam00053 1 CDCNPHGSLSDTCDP-----------ETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1271-1308 |
6.72e-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: 62.37 E-value: 6.72e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1720389100 1271 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1308
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1271-1308 |
9.70e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.99 E-value: 9.70e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1720389100 1271 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1308
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1271-1308 |
1.31e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.56 E-value: 1.31e-11
10 20 30
....*....|....*....|....*....|....*...
gi 1720389100 1271 CDCNPQGSVHSDCDRASGQCVCKPGATGLHCEKCLPRH 1308
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGY 38
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
806-854 |
1.71e-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: 61.22 E-value: 1.71e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720389100 806 CNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGYRSFPDCVPCGC 854
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1165-1211 |
1.76e-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: 61.22 E-value: 1.76e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1165 CNCNNH---SDVCDPETGKCLsCRDHTSGDHCELCASGYYGKVTGLPGDC 1211
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
503-551 |
2.16e-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: 58.13 E-value: 2.16e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 503 PCECHGHAS---ECD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRgtPGDCQ 551
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. |
852-909 |
2.61e-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: 57.75 E-value: 2.61e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389100 852 CGCDLRGTLPDTCDLEqglcscsedGGTCSCKENAVGPQCSKCQAGTFALRGDNPQGC 909
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE---------TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1353-1879 |
4.17e-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: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1353 LENLENTTKYFQRYLIKENAKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNG-------TQALATFIEQ 1425
Cdd:COG1196 241 LEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiarleerRRELEERLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1426 LHANIKEITEKVATLNQTARkdfqppvsALQSMHQNISSLLGLIKErnftEMQQNATLELKAAKDLLSRIQKRFQKPQEK 1505
Cdd:COG1196 321 LEEELAELEEELEELEEELE--------ELEEELEEAEEELEEAEA----ELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1506 LKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREwvdaAGTH 1585
Cdd:COG1196 389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA----LLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1586 TAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQHASELQ--SRAGALDRDLENVRNVSLnATS 1663
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglAGAVAVLIGVEAAYEAAL-EAA 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1664 AAHVHSNIQTLTEEAEMLAADAHKTANK---TDLISESLASRGKAVLQRSSRFLKESV----STRRKQQGITMKLDELKN 1736
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAgraTFLPLDKIRARAALAAALARGAIGAAVdlvaSDLREADARYYVLGDTLL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1737 LTSQFQESMDNIMKQAND--------SLAMLRESPGGMREKGRKARELAAAANESAVKTLEDVLALSLRVFNTSEDLSRV 1808
Cdd:COG1196 624 GRTLVAARLEAALRRAVTlagrlrevTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEE 703
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 1809 NATVQETNDLLHNSTMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIkLLISRARKQVASIK 1879
Cdd:COG1196 704 EEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP-PDLEELERELERLE 773
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
713-757 |
5.21e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.21e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1720389100 713 CNCSVEGSVSDNC-TEEGQCHCGPGVSGKQCDRCSHGFYAFQDGGC 757
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1164-1212 |
5.31e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 56.98 E-value: 5.31e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1720389100 1164 PCNCNNHSDV---CDPETGKCLsCRDHTSGDHCELCASGYYGkVTGLPGDCT 1212
Cdd:cd00055 1 PCDCNGHGSLsgqCDPGTGQCE-CKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
158-211 |
9.37e-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: 56.21 E-value: 9.37e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1720389100 158 PCNCDPVGSLSSVCIKDDrhadlangkwpGQCPCRKGYAGDKCDRCQFGYRGFP 211
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. |
713-760 |
9.51e-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: 56.21 E-value: 9.51e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720389100 713 CNCSVEGSVSDNCTEE-GQCHCGPGVSGKQCDRCSHGFYAFQDGGCTPC 760
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
610-662 |
1.79e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 55.44 E-value: 1.79e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 610 PCNCSGNVDplEAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVTAKNCR 662
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. |
611-657 |
3.11e-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: 3.11e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 611 CNCSGNVDPleAGHCDSVTGECLkCLWNTDGAHCERCADGFYGDAVT 657
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. |
216-262 |
4.25e-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: 54.28 E-value: 4.25e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 216 CDCRTVGSLNeDPCIE---PCLCKKNVEGKNCDRCKPGFYNLKERNPEGC 262
Cdd:pfam00053 1 CDCNPHGSLS-DTCDPetgQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1377-1582 |
5.27e-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: 5.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1377 AEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLNQ---TARKDFQPPVS 1453
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1454 ALQSMHQNISSLLGLIKERNFTEMQQNATL---ELKAAKDLLSRIQKRfqkpQEKLKALK-EANSLLSNHSEKLQAAEEL 1529
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESFSDFLDRLSAlskIADADADLLEELKAD----KAELEAKKaELEAKLAELEALKAELEAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 1530 LKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVDAA 1582
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAA 222
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
805-848 |
6.63e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 53.90 E-value: 6.63e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1720389100 805 ACNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGYRSFPD 848
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1410-1776 |
7.18e-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: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1410 ERTSNGTQALATFIEQLHANIKEITEKVATLNQTarkdfqppVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAK 1489
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKA--------LAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1490 dLLSRIQKRFQKPQEKLKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTS 1569
Cdd:TIGR02168 738 -LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLN 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1570 ELIAKGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKRRAR-----DLVHRAEQHASELQSRA 1644
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESEleallNERASLEEALALLRSEL 896
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1645 GALDRDLENVRNvslnatsaaHVHSNIQTLTEEAEMLAA---DAHKTANKTDLISESLASRGK----AVLQRSSRFLKES 1717
Cdd:TIGR02168 897 EELSEELRELES---------KRSELRRELEELREKLAQlelRLEGLEVRIDNLQERLSEEYSltleEAEALENKIEDDE 967
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389100 1718 VSTRRKQQGITMKLDELK--NLTS-----QFQESMDNIMKQAND---SLAMLRESpggMREKGRKAREL 1776
Cdd:TIGR02168 968 EEARRRLKRLENKIKELGpvNLAAieeyeELKERYDFLTAQKEDlteAKETLEEA---IEEIDREARER 1033
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1353-1885 |
8.26e-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: 61.78 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1353 LENLENTTKYFQryliKENAKKIRAEI-QLEGIAEQTENLQKELTRVLARHQKVNAEME-RTSNGTQALATFIEQLHANI 1430
Cdd:pfam12128 324 LEALEDQHGAFL----DADIETAAADQeQLPSWQSELENLEERLKALTGKHQDVTAKYNrRRSKIKEQNNRDIAGIKDKL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1431 KEITEKVATLNQTARKDFQPPVSALQSMHQ----NISSLLGLIKER----NFTEMQQNATLELK---AAKDLL-----SR 1494
Cdd:pfam12128 400 AKIREARDRQLAVAEDDLQALESELREQLEagklEFNEEEYRLKSRlgelKLRLNQATATPELLlqlENFDERierarEE 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1495 IQKRFQKPQEKLKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFqekkLRVQeeqnvtseliAK 1574
Cdd:pfam12128 480 QEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF----LRKE----------AP 545
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1575 GreWVDAAGTHTAAAQDTLTQL------EHHRDELLLWARKIR----SHVDDLVMQMSKRRARDLVHRAEQHASELQSRA 1644
Cdd:pfam12128 546 D--WEQSIGKVISPELLHRTDLdpevwdGSVGGELNLYGVKLDlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAA 623
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1645 ----GALDRDLENV-RNVSLNATSAAHVHSNIQTLTEEAEMLAadahktanktDLISESLASRGKAVLQRSSRFLKESVS 1719
Cdd:pfam12128 624 eeqlVQANGELEKAsREETFARTALKNARLDLRRLFDEKQSEK----------DKKNKALAERKDSANERLNSLEAQLKQ 693
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1720 TRRKQQGITMKLDE-LKNLTSQFQESMDNIMKQANDSLAMLRESPGGmREKGRKA----------RELAA--------AA 1780
Cdd:pfam12128 694 LDKKHQAWLEEQKEqKREARTEKQAYWQVVEGALDAQLALLKAAIAA-RRSGAKAelkaletwykRDLASlgvdpdviAK 772
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1781 NESAVKTLEDVL---------ALSLRVF----------NTSEDLSRVNATVQETNDLLhnstmttllaGRKMKDMEMQAN 1841
Cdd:pfam12128 773 LKREIRTLERKIeriavrrqeVLRYFDWyqetwlqrrpRLATQLSNIERAISELQQQL----------ARLIADTKLRRA 842
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1720389100 1842 LLLDRLKPLKTLEENLSRNLSEIKLLISRarkqVASIKVAVSAD 1885
Cdd:pfam12128 843 KLEMERKASEKQQVRLSENLRGLRCEMSK----LATLKEDANSE 882
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1375-1712 |
8.51e-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: 8.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1375 IRAEI--QLEGIAEQTEnlqkeltrVLARHQKVNAEMERTSNgtQALATFIEQLHANIKEITEKVATLNQTARkdfqppv 1452
Cdd:COG1196 194 ILGELerQLEPLERQAE--------KAERYRELKEELKELEA--ELLLLKLRELEAELEELEAELEELEAELE------- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1453 sALQSMHQNISSLLGLIKERnftemQQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEansllsnhseKLQAAEELLKE 1532
Cdd:COG1196 257 -ELEAELAELEAELEELRLE-----LEELELELEEAQAEEYELLAELARLEQDIARLEE----------RRRELEERLEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1533 AGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRS 1612
Cdd:COG1196 321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1613 HVDDLvmqmsKRRARDLVHRAEQHASELQSRAGALDRDLENVRNVSLNATSAAHVHSNIQTLTEEAE-MLAADAHKTANK 1691
Cdd:COG1196 401 QLEEL-----EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLeLLAELLEEAALL 475
|
330 340
....*....|....*....|.
gi 1720389100 1692 TDLISESLASRGKAVLQRSSR 1712
Cdd:COG1196 476 EAALAELLEELAEAAARLLLL 496
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1352-1761 |
9.68e-09 |
|
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: 9.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1352 ILENLENTTKYF---QRYLIKENAKKIRAEIQLEGIAEQTENL----QKELTRVLARHQKVNAEMERTSNGTQALATFIE 1424
Cdd:TIGR00606 696 FISDLQSKLRLApdkLKSTESELKKKEKRRDEMLGLAPGRQSIidlkEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG 775
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1425 QLHAniKEITEKVATLNQTARKDFQPPVSALQ-SMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLLSRI---QKRFQ 1500
Cdd:TIGR00606 776 TIMP--EEESAKVCLTDVTIMERFQMELKDVErKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIelnRKLIQ 853
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1501 KPQEKLKALKEANSLLSnhSEKLQAAEElLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVD 1580
Cdd:TIGR00606 854 DQQEQIQHLKSKTNELK--SEKLQIGTN-LQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELIS 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1581 AAGTHTAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQhASELQSRAGALDRDLENVRnvsln 1660
Cdd:TIGR00606 931 SKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQ-LEECEKHQEKINEDMRLMR----- 1004
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1661 atsaahvhSNIQTlTEEAEMLAADAHKTANKTDLISEslasrgkavlqrssrfLKESVSTRRKQQGiTMKLDELKNLTSQ 1740
Cdd:TIGR00606 1005 --------QDIDT-QKIQERWLQDNLTLRKRENELKE----------------VEEELKQHLKEMG-QMQVLQMKQEHQK 1058
|
410 420
....*....|....*....|.
gi 1720389100 1741 FQESMDNIMKQANDSLAMLRE 1761
Cdd:TIGR00606 1059 LEENIDLIKRNHVLALGRQKG 1079
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
504-550 |
1.06e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.13 E-value: 1.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 504 CECHGHAS---ECDIH-GICsVCTHNTTGDHCEQCLPGFYGTPSrGTPGDC 550
Cdd:pfam00053 1 CDCNPHGSlsdTCDPEtGQC-LCKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
712-758 |
1.33e-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: 53.13 E-value: 1.33e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 712 PCNCSVEGSVSDNCTEE-GQCHCGPGVSGKQCDRCSHGFY--AFQDGGCT 758
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYglPSQGGGCQ 50
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1368-1893 |
1.46e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.46 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1368 IKENAKKIRAEIQ-LEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITE--KVATLNQTA 1444
Cdd:PRK03918 219 LREELEKLEKEVKeLEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKElkEKAEEYIKL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1445 RKDFQPPVSALQSMHQNISSLLGLIK--ERNFTEmqqnatLELKAAKdlLSRIQKRFQKPQEKLKALKEANSLLSNHSEK 1522
Cdd:PRK03918 299 SEFYEEYLDELREIEKRLSRLEEEINgiEERIKE------LEEKEER--LEELKKKLKELEKRLEELEERHELYEEAKAK 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1523 LQAAEELLKEAGSKTQESnlllllVKANLKEFQEKKLRVQEEqnvTSELIAKGREWVDAAGTHTAA------AQDT---- 1592
Cdd:PRK03918 371 KEELERLKKRLTGLTPEK------LEKELEELEKAKEEIEEE---ISKITARIGELKKEIKELKKAieelkkAKGKcpvc 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1593 ---LTqlEHHRDELLlwarkirshvddlvmqmskRRARDLVHRAEQHASELQSRAGALDRDLENVRNVslnatsaahvhs 1669
Cdd:PRK03918 442 greLT--EEHRKELL-------------------EEYTAELKRIEKELKEIEEKERKLRKELRELEKV------------ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1670 niqtLTEEAEMLAadAHKTANKTDLISESLASRGKAVLQRSS---RFLKESVSTRRKQQGITM----KLDELKNLTSQFQ 1742
Cdd:PRK03918 489 ----LKKESELIK--LKELAEQLKELEEKLKKYNLEELEKKAeeyEKLKEKLIKLKGEIKSLKkeleKLEELKKKLAELE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1743 ESMDNIMKQANDSLAMLRE-SPGGMREKGRKARELAAAANE-----SAVKTLEDVL----ALSLRVFNTSEDLSRVNATV 1812
Cdd:PRK03918 563 KKLDELEEELAELLKELEElGFESVEELEERLKELEPFYNEylelkDAEKELEREEkelkKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1813 QET----NDLLHN-STMTTLLAGRKMKDMEMQANLLLDRLKPLKTLEENLSRNLSEIKL---LISRARKQVASIKVA--- 1881
Cdd:PRK03918 643 EELrkelEELEKKySEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEeleEREKAKKELEKLEKAler 722
|
570
....*....|..
gi 1720389100 1882 VSADRDCIRAYQ 1893
Cdd:PRK03918 723 VEELREKVKKYK 734
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
806-849 |
1.84e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 1.84e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1720389100 806 CNCSAVGSTSAQCDVLSGHCPCKKGFGGQSCHQCSLGY--RSFPDC 849
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1165-1211 |
1.97e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 1.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1165 CNCN---NHSDVCDPETGKCLsCRDHTSGDHCELCASGYYGKVtglPGDC 1211
Cdd:smart00180 1 CDCDpggSASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
159-213 |
2.04e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 52.31 E-value: 2.04e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389100 159 CNCDPVGSLSSVCIKDDrhadlangkwpGQCPCRKGYAGDKCDRCQFGYRG--FPNC 213
Cdd:smart00180 1 CDCDPGGSASGTCDPDT-----------GQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
759-804 |
2.30e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 52.36 E-value: 2.30e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 759 PCDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGLDPE-QGCQ 804
Cdd:cd00055 1 PCDCnghGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQgGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
553-608 |
4.08e-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: 51.59 E-value: 4.08e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389100 553 CACPLSIDSnnfSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGGTC 608
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETG---QC-LCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
852-909 |
4.52e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 51.54 E-value: 4.52e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389100 852 CGCDLRGTLPDTCDLeqglcscseDGGTCSCKENAVGPQCSKCQAGTFalrGDNPQGC 909
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. |
760-803 |
4.77e-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: 51.59 E-value: 4.77e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720389100 760 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGL--DPEQGC 803
Cdd:pfam00053 1 CDCnphGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLpsDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
32-79 |
4.89e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.59 E-value: 4.89e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 32 CICYGHAS---SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPGT 79
Cdd:cd00055 2 CDCNGHGSlsgQC----DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1370-1886 |
6.79e-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: 6.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1370 ENAKKIRAEIQLEGIAEQTEN--LQKELtRVLARhQKVNAEMERTSNGTQalatfIEQLHANIKEiTEKvatlnqtARKD 1447
Cdd:pfam01576 366 EQAKRNKANLEKAKQALESENaeLQAEL-RTLQQ-AKQDSEHKRKKLEGQ-----LQELQARLSE-SER-------QRAE 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1448 FQPPVSALQSMHQNISSLLGLIKERNftemqqnatleLKAAKDLlSRIQKRFQKPQE--------------KLKALK-EA 1512
Cdd:pfam01576 431 LAEKLSKLQSELESVSSLLNEAEGKN-----------IKLSKDV-SSLESQLQDTQEllqeetrqklnlstRLRQLEdER 498
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1513 NSLLsnhsEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEF-------QEKKLRVQEE-QNVTSELIAKGREWVDAAGT 1584
Cdd:pfam01576 499 NSLQ----EQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDagtlealEEGKKRLQRElEALTQQLEEKAAAYDKLEKT 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1585 HTAAAQ---DTLTQLEHHRdELLLWARKIRSHVDDLVMQ---MSKRRA--RDlvhRAEQHASELQSRAGALDRDLENVR- 1655
Cdd:pfam01576 575 KNRLQQeldDLLVDLDHQR-QLVSNLEKKQKKFDQMLAEekaISARYAeeRD---RAEAEAREKETRALSLARALEEALe 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1656 --------NVSLNA------TSAAHVHSNI-----------QTLTE--------EAEMLAAD-----------AHKTANK 1691
Cdd:pfam01576 651 akeelertNKQLRAemedlvSSKDDVGKNVhelerskraleQQVEEmktqleelEDELQATEdaklrlevnmqALKAQFE 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1692 TDLIS-ESLASRGKAVLQRSSRFLKESVSTRRKQQGITM----KLD-ELKNLTSQfqesMDNIMKQANDSLAMLRESPGG 1765
Cdd:pfam01576 731 RDLQArDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVaakkKLElDLKELEAQ----IDAANKGREEAVKQLKKLQAQ 806
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1766 MREKGRKARELAAA---------ANESAVKTLE-DVLALslrvfntSEDLS---RVNATVQETNDLLHNStmttLLAGRK 1832
Cdd:pfam01576 807 MKDLQRELEEARASrdeilaqskESEKKLKNLEaELLQL-------QEDLAaseRARRQAQQERDELADE----IASGAS 875
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 1833 MKdmemqaNLLLDRLKPLKT----LEENLSRNLSEIKLLISRARK---QVASIKVAVSADR 1886
Cdd:pfam01576 876 GK------SALQDEKRRLEAriaqLEEELEEEQSNTELLNDRLRKstlQVEQLTTELAAER 930
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1423-1754 |
8.35e-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: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1423 IEQLHANIKEITEKVATLNQTARK--DFQPPVSALQSMHqnISSLLGLIKERNftEMQQNATLELKAAKDLLSRIQKRFQ 1500
Cdd:TIGR02168 188 LDRLEDILNELERQLKSLERQAEKaeRYKELKAELRELE--LALLVLRLEELR--EELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1501 KPQEKL------------------KALKEANSLLSN-------HSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQ 1555
Cdd:TIGR02168 264 ELEEKLeelrlevseleeeieelqKELYALANEISRleqqkqiLRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1556 EKKLRVQEEQNVTSELIAKGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRSHVddlvmqmskRRARDLVHRAEQ 1635
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI---------ERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1636 HASELQSRAGALDRDLENVRnvslnatsAAHVHSNIQTLTEEAEMLAADAHKTANKTDLISESLASRGKAVLQRSSRFlk 1715
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAE--------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL-- 484
|
330 340 350
....*....|....*....|....*....|....*....
gi 1720389100 1716 esvstRRKQQGITMkLDELKNLTSQFQESMDNIMKQAND 1754
Cdd:TIGR02168 485 -----AQLQARLDS-LERLQENLEGFSEGVKALLKNQSG 517
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1364-1589 |
9.03e-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: 9.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1364 QRYLIKENAKKIRA-EIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLNQ 1442
Cdd:COG4942 18 QADAAAEAEAELEQlQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1443 ---TARKDFQPPVSALQSMHQNiSSLLGLIKERNFTEMQQNATLelkaAKDLLSRIQKRFQKPQEKLKALKEANSLLSNH 1519
Cdd:COG4942 98 eleAQKEELAELLRALYRLGRQ-PPLALLLSPEDFLDAVRRLQY----LKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720389100 1520 SEKLQAA----EELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVDAAGTHTAAA 1589
Cdd:COG4942 173 RAELEALlaelEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
760-803 |
9.61e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 9.61e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 760 CDC---AHTQNNCDPASGECLCPPHTQGLKCEECEEAYWGlDPEQGC 803
Cdd:smart00180 1 CDCdpgGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG-DGPPGC 46
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1367-1686 |
1.45e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.45 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1367 LIKENAKKIRAEI-QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLN---- 1441
Cdd:COG4372 25 LIAALSEQLRKALfELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeele 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1442 --QTARKDFQPPVSALQSMHQNissllgLIKERNFTEMQQNATLELKAAKD-LLSRIQKRFQKPQEKLKALKEANSLLSN 1518
Cdd:COG4372 105 slQEEAEELQEELEELQKERQD------LEQQRKQLEAQIAELQSEIAEREeELKELEEQLESLQEELAALEQELQALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1519 HsEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSEliakGREWVDAAGTHTAAAQDTLTQLEH 1598
Cdd:COG4372 179 A-EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEA----KLGLALSALLDALELEEDKEELLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1599 HRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQHASELQSRAGALDRDLENVRNVSLNATSAAHVHSNIQTLTEEA 1678
Cdd:COG4372 254 EVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
....*...
gi 1720389100 1679 EMLAADAH 1686
Cdd:COG4372 334 ILLAELAD 341
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
215-262 |
1.54e-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: 50.05 E-value: 1.54e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 215 PCDCRTVGSLNEDpCIEP---CLCKKNVEGKNCDRCKPGFYNLKERnPEGC 262
Cdd:cd00055 1 PCDCNGHGSLSGQ-CDPGtgqCECKPNTTGRRCDRCAPGYYGLPSQ-GGGC 49
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1372-1648 |
1.74e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1372 AKKIRAEIQLEGIAEQTENLQKEL----TRVLARHQKVNA-EMERTSNGTQALA-----TFIEQLHANIKEITEKVATLN 1441
Cdd:PRK04863 383 ARAEAAEEEVDELKSQLADYQQALdvqqTRAIQYQQAVQAlERAKQLCGLPDLTadnaeDWLEEFQAKEQEATEELLSLE 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1442 Q------TARKDFQ----------PPVSALQSMHQNISSLLGLIKERNftEMQQNATLELKaakdlLSRIQKRFQKPQEK 1505
Cdd:PRK04863 463 QklsvaqAAHSQFEqayqlvrkiaGEVSRSEAWDVARELLRRLREQRH--LAEQLQQLRMR-----LSELEQRLRQQQRA 535
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1506 LKALKEANSLLSNHSEKLQAAEELLKEAGSKTQESNllllLVKANLKEfQEKKLRVQEEQ--NVTSELIAKGREWVdaag 1583
Cdd:PRK04863 536 ERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLS----ESVSEARE-RRMALRQQLEQlqARIQRLAARAPAWL---- 606
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1584 thtaAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQM-SKRRARDLVHRA----EQHASELQSRAGALD 1648
Cdd:PRK04863 607 ----AAQDALARLREQSGEEFEDSQDVTEYMQQLLERErELTVERDELAARkqalDEEIERLSQPGGSED 672
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1484-1874 |
2.18e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1484 ELKAAKDLLSRIQKRfqKPQEKLKALKEANSLLS-------------NHSEKLQAAEELLKEAGSKTQESNLLLLLVKAN 1550
Cdd:COG4717 50 RLEKEADELFKPQGR--KPELNLKELKELEEELKeaeekeeeyaelqEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1551 ---LKEFQEKKLRVQEEQNVTSELIAKGREWVDAAgTHTAAAQDTLTQLEHHRDELL-LWARKIRSHVDDLVMQMSKRRA 1626
Cdd:COG4717 128 lplYQELEALEAELAELPERLEELEERLEELRELE-EELEELEAELAELQEELEELLeQLSLATEEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1627 RdlVHRAEQHASELQSRAGALDRDLENVRNVSLNATSAAHVHSNIQTLTEEAEM--LAADAHKTANKTDLISESLASRGK 1704
Cdd:COG4717 207 R--LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALlaLLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1705 AVLQRSSRFLKESVSTRRKQQGITmKLDELKNLTSQ-FQESMDNIMKQANDSLAMLRESPGGMREKGRKARELAAAANES 1783
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQ-ALPALEELEEEeLEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEEL 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1784 AVKTLEDVLALSLRVFNTS---------EDLSRVNATVQETNDL-----LHNSTMTTLLAGRKMKDMEMQANLLLDRLKP 1849
Cdd:COG4717 364 QLEELEQEIAALLAEAGVEdeeelraalEQAEEYQELKEELEELeeqleELLGELEELLEALDEEELEEELEELEEELEE 443
|
410 420
....*....|....*....|....*
gi 1720389100 1850 LKTLEENLSRNLSEIKLLISRARKQ 1874
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEED 468
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1372-1788 |
2.63e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 56.59 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1372 AKKIRAEIQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVatlnQTARKDFQPP 1451
Cdd:PRK02224 265 ETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRL----EECRVAAQAH 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1452 VSALQSMHQNISSLlgliKERNFTEMQQNATLE--LKAAKDLLSRIQKRFQKPQEKLKALKEAnslLSNHSEKLQAAEEL 1529
Cdd:PRK02224 341 NEEAESLREDADDL----EERAEELREEAAELEseLEEAREAVEDRREEIEELEEEIEELRER---FGDAPVDLGNAEDF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1530 LKEAGSKTQESNLLLLLVKANLKEFQEkklRVQEEQnvtsELIAKGR-----EWVDAAGtHTAAAQDTLTQLEHHRDELL 1604
Cdd:PRK02224 414 LEELREERDELREREAELEATLRTARE---RVEEAE----ALLEAGKcpecgQPVEGSP-HVETIEEDRERVEELEAELE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1605 lwarKIRSHVDDLvmqmSKR--RARDLVhRAEQHASELQSRAGALDRDLENVRNvSLNATSAAhvhsnIQTLTEEAEMLA 1682
Cdd:PRK02224 486 ----DLEEEVEEV----EERleRAEDLV-EAEDRIERLEERREDLEELIAERRE-TIEEKRER-----AEELRERAAELE 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1683 ADA---HKTANKTDLISESLASRGKAVLQRssrfLKESVSTRRKQQGITMKLDELKNLTSQFQ------ESMDNIMKQAN 1753
Cdd:PRK02224 551 AEAeekREAAAEAEEEAEEAREEVAELNSK----LAELKERIESLERIRTLLAAIADAEDEIErlrekrEALAELNDERR 626
|
410 420 430
....*....|....*....|....*....|....*
gi 1720389100 1754 DSLAMLREspggmrekgRKaRELAAAANESAVKTL 1788
Cdd:PRK02224 627 ERLAEKRE---------RK-RELEAEFDEARIEEA 651
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1456-1876 |
4.15e-07 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 55.82 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1456 QSMhqnISSLLGLIKERNFTEMQQNATLelkAAKDLLSRIQKRFQKPQEKLKAlKEANSLlsnHsEKLQAAEELLKEags 1535
Cdd:PRK02224 152 QDM---IDDLLQLGKLEEYRERASDARL---GVERVLSDQRGSLDQLKAQIEE-KEEKDL---H-ERLNGLESELAE--- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1536 ktqesnlllllVKANLKEFQEKKLRVQEEQNVTSELIA---KGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRS 1612
Cdd:PRK02224 218 -----------LDEEIERYEEQREQARETRDEADEVLEeheERREELETLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1613 HVDDLVMQMSKRRARDLVHRA-----EQHASELQSRAGALDRDLENVRnvslnaTSAAHVHSNIQTLTEEAEMLAADAHK 1687
Cdd:PRK02224 287 RLEELEEERDDLLAEAGLDDAdaeavEARREELEDRDEELRDRLEECR------VAAQAHNEEAESLREDADDLEERAEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1688 TANKTDLISESLASRGKAVLQRSSRF--LKESVSTRRKQ-QGITMKLDELKNLTSQFQESMDNIMKQANDSLAMLREspg 1764
Cdd:PRK02224 361 LREEAAELESELEEAREAVEDRREEIeeLEEEIEELRERfGDAPVDLGNAEDFLEELREERDELREREAELEATLRT--- 437
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1765 gMREKGRKARELAAAAN----------ESAVKTLED----VLALSLRVFNTSEDLSRVNATVQETNDLlhnstmttllag 1830
Cdd:PRK02224 438 -ARERVEEAEALLEAGKcpecgqpvegSPHVETIEEdrerVEELEAELEDLEEEVEEVEERLERAEDL------------ 504
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1720389100 1831 rkmKDMEMQANLLLDRLKPLKTLEENLSRNLSEIKLLISRARKQVA 1876
Cdd:PRK02224 505 ---VEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1354-1632 |
4.50e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.91 E-value: 4.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1354 ENLENTTKYFQRylIKENAKKIRAEI-----QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHA 1428
Cdd:COG4372 80 EELEELNEQLQA--AQAELAQAQEELeslqeEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1429 NIKEITEKVATLNQTARKdfqppvsalQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLLSRIQKRFQKPQEKLKA 1508
Cdd:COG4372 158 QLESLQEELAALEQELQA---------LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1509 LKEANSLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEEQNVTSELIAkgrEWVDAAGTHTAA 1588
Cdd:COG4372 229 AKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL---ELKLLALLLNLA 305
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1720389100 1589 AQDTLTQLEHHRDELLLW-ARKIRSHVDDLVMQMSKRRARDLVHR 1632
Cdd:COG4372 306 ALSLIGALEDALLAALLElAKKLELALAILLAELADLLQLLLVGL 350
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1466-1790 |
6.00e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 54.52 E-value: 6.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1466 LGLIKERNFTEMQQNATLE-LKAAKDLLSRIQKRFQKPQEKLKALKE----ANSLLSNHSEKLQAAEELLKEAGSKTQES 1540
Cdd:COG4372 13 LSLFGLRPKTGILIAALSEqLRKALFELDKLQEELEQLREELEQAREeleqLEEELEQARSELEQLEEELEELNEQLQAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1541 NLLLLLVKANLKEFQEKKLRVQEEqnvtseliakgrewvdaagthtaaaqdtLTQLEHHRDELLLWARKIRSHVDDLVMQ 1620
Cdd:COG4372 93 QAELAQAQEELESLQEEAEELQEE----------------------------LEELQKERQDLEQQRKQLEAQIAELQSE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1621 MSKRRARdlvhraeqhASELQSRAGALDRDLENVRNvSLNATSAAHVHSNIQTLTEEAEMLAADAHKTANKTDLISESLA 1700
Cdd:COG4372 145 IAEREEE---------LKELEEQLESLQEELAALEQ-ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1701 SRGKAVLQRSSRFLKESVSTRRKQQGITMKLDELKNLTSQFQESMDNIMKQANDSLA-MLRESPGGMREKGRKARELAAA 1779
Cdd:COG4372 215 ELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKdTEEEELEIAALELEALEEAALE 294
|
330
....*....|.
gi 1720389100 1780 ANESAVKTLED 1790
Cdd:COG4372 295 LKLLALLLNLA 305
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
851-909 |
8.07e-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: 48.12 E-value: 8.07e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389100 851 PCGCDLRGTLPDTCDLEqglcscsedGGTCSCKENAVGPQCSKCQAGTFALRgDNPQGC 909
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG---------TGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
504-545 |
1.10e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 47.31 E-value: 1.10e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1720389100 504 CECH--GHASE-CD-IHGICsVCTHNTTGDHCEQCLPGFYGTPSRG 545
Cdd:smart00180 1 CDCDpgGSASGtCDpDTGQC-ECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1372-1653 |
1.23e-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: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1372 AKKIRAEIQLEGIAEQTENLQKEL----TRVLARHQKVNAeMERTSNGTQA-------LATFIEQLHANIKEITEKVATL 1440
Cdd:COG3096 382 ARLEAAEEEVDSLKSQLADYQQALdvqqTRAIQYQQAVQA-LEKARALCGLpdltpenAEDYLAAFRAKEQQATEEVLEL 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1441 NQ------TARKDFQPPVSALQSM---------HQNISSLLglikeRNFTEmQQNATLELKAAKDLLSRIQKRFQKpQEK 1505
Cdd:COG3096 461 EQklsvadAARRQFEKAYELVCKIageversqaWQTARELL-----RRYRS-QQALAQRLQQLRAQLAELEQRLRQ-QQN 533
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1506 LKALkeANSLLSNHSEKLQAAEEL--LKEAGSKTQESnlllllVKANLKEFQEKK--LRVQEEQNVT--SELIAKGREWV 1579
Cdd:COG3096 534 AERL--LEEFCQRIGQQLDAAEELeeLLAELEAQLEE------LEEQAAEAVEQRseLRQQLEQLRAriKELAARAPAWL 605
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720389100 1580 daagthtaAAQDTLTQLEHHRDELLLWARKIRSHvddlvMQMSKRRARDlvhrAEQHASELQSRAGALDRDLEN 1653
Cdd:COG3096 606 --------AAQDALERLREQSGEALADSQEVTAA-----MQQLLERERE----ATVERDELAARKQALESQIER 662
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
216-262 |
1.49e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.92 E-value: 1.49e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1720389100 216 CDCRTVGSLNeDPCIEP---CLCKKNVEGKNCDRCKPGFYNlkeRNPEGC 262
Cdd:smart00180 1 CDCDPGGSAS-GTCDPDtgqCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1356-1888 |
1.82e-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: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1356 LENTTKYFQ-RYLIKENAKKiraeiQLEGIAEQT-ENLQKELTRVLARHQKVNAEMERTSNGTQALatfIEQLHANIKEI 1433
Cdd:TIGR00606 267 LDNEIKALKsRKKQMEKDNS-----ELELKMEKVfQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLL 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1434 T-EKVATLNQTARKDFQPPVSALQSMHQNISSL-LGLIKERNFTEMQQNATLELKAAKDLLSRIQKRfqkpqeklKAlKE 1511
Cdd:TIGR00606 339 NqEKTELLVEQGRLQLQADRHQEHIRARDSLIQsLATRLELDGFERGPFSERQIKNFHTLVIERQED--------EA-KT 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1512 ANSLLSNhsekLQAAEELLKEAGSKTQESNLLLLLVKANLKEFQEKKlrVQEEQNVTSELiakgrewvdaagthtaaaqd 1591
Cdd:TIGR00606 410 AAQLCAD----LQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKK--QEELKFVIKEL-------------------- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1592 tlTQLEHHRDELLLWARKIRSHVDDLvmqmSKRRARDLVHRAEQHASELQSRAGALDRDL--ENVRNVSLNAtsaaHVHS 1669
Cdd:TIGR00606 464 --QQLEGSSDRILELDQELRKAEREL----SKAEKNSLTETLKKEVKSLQNEKADLDRKLrkLDQEMEQLNH----HTTT 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1670 NIQTLTEEAEMLAADAHKTANK----------------TDLISESLASRGKAVLQRSSRFLKESVSTRRKQQGITMKLDE 1733
Cdd:TIGR00606 534 RTQMEMLTKDKMDKDEQIRKIKsrhsdeltsllgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNE 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1734 LKNLTSQFQESMDNIMK----QANDS-LAMLRESpggmREKGRKARE-LAAAAN--ESAVKTLED----VLALSLRVFNT 1801
Cdd:TIGR00606 614 LESKEEQLSSYEDKLFDvcgsQDEESdLERLKEE----IEKSSKQRAmLAGATAvySQFITQLTDenqsCCPVCQRVFQT 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1802 SEDLSRVNATVQETNDLL---HNSTMTTLLAGRKMKD-----MEMQANLLLDRLKPLKTLEE---NLSRNLSEIKLLISR 1870
Cdd:TIGR00606 690 EAELQEFISDLQSKLRLApdkLKSTESELKKKEKRRDemlglAPGRQSIIDLKEKEIPELRNklqKVNRDIQRLKNDIEE 769
|
570
....*....|....*...
gi 1720389100 1871 ARKQVASIKVAVSADRDC 1888
Cdd:TIGR00606 770 QETLLGTIMPEEESAKVC 787
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
610-654 |
2.61e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.54 E-value: 2.61e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1720389100 610 PCNCSGNVDPleagHCDSVTGECLkCLWNTDGAHCERCADGFYGD 654
Cdd:smart00180 2 DCDPGGSASG----TCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1214-1268 |
3.02e-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: 46.19 E-value: 3.02e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 1214 CTCPHHPpfSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGSC 1268
Cdd:pfam00053 1 CDCNPHG--SLSDTCDPET---GQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1369-1814 |
3.23e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1369 KENAKKIRAEIQ-LEGIAEQTENLQKELTRVLARHQKVN---------AEMERTSNGTQALATFIEQLHANIKEITEKVA 1438
Cdd:COG4717 84 EEKEEEYAELQEeLEELEEELEELEAELEELREELEKLEkllqllplyQELEALEAELAELPERLEELEERLEELRELEE 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1439 TLNQTARKdfqppvsaLQSMHQNISSLLGLIKERNFTEMQQNATlELKAAKDLLSRIQKRFQKPQEKLKALKEANSLLSN 1518
Cdd:COG4717 164 ELEELEAE--------LAELQEELEELLEQLSLATEEELQDLAE-ELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1519 HSEKLQAAEELLKEAGSKTQESnlLLLLVKANLKEFQEKKLRVQEEQNVTSELIAKGREWVDAAGTHTAAAQDTLTQLEH 1598
Cdd:COG4717 235 ELEAAALEERLKEARLLLLIAA--ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1599 HRDellLWARKIRSHVDDLVM--QMSKRRARDLVHRAEQhASELQSRAGALDRDL-----ENVRNVSLNATSAahvhSNI 1671
Cdd:COG4717 313 LEE---LEEEELEELLAALGLppDLSPEELLELLDRIEE-LQELLREAEELEEELqleelEQEIAALLAEAGV----EDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1672 QTLTEEAEmLAADAHKTANKTDLISESLASRGKAVLQRSSRFLKESVSTRRKQqgITMKLDELKNLTSQFQESM---DNI 1748
Cdd:COG4717 385 EELRAALE-QAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEE--LEEELEELEEELEELREELaelEAE 461
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389100 1749 MKQA--NDSLAMLREspggmrEKGRKARELAAAANE-SAVKTLEDVLALSLRVFnTSEDLSRVNATVQE 1814
Cdd:COG4717 462 LEQLeeDGELAELLQ------ELEELKAELRELAEEwAALKLALELLEEAREEY-REERLPPVLERASE 523
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1593-1847 |
5.67e-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: 5.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1593 LTQLEHHRDELLLWARKIRSHVDDlvMQMSKRRARDLvhraEQHASELQSRAGALDRDLENVRNVSlNATSaahvhSNIQ 1672
Cdd:pfam06008 18 NYNLENLTKQLQEYLSPENAHKIQ--IEILEKELSSL----AQETEELQKKATQTLAKAQQVNAES-ERTL-----GHAK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1673 TLTEEAEMLAADAHKTANKTDLISE--SLASRGK--AVLQRSSRFLKE--SVSTRRKQQGITMKLDELKNLTSQFQESMD 1746
Cdd:pfam06008 86 ELAEAIKNLIDNIKEINEKVATLGEndFALPSSDlsRMLAEAQRMLGEirSRDFGTQLQNAEAELKAAQDLLSRIQTWFQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1747 NIMKQANDSLAMLRESPGGMREKGRKARELaaaANESAVKTlEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNstmtT 1826
Cdd:pfam06008 166 SPQEENKALANALRDSLAEYEAKLSDLREL---LREAAAKT-RDANRLNLANQANLREFQRKKEEVSEQKNQLEE----T 237
|
250 260
....*....|....*....|.
gi 1720389100 1827 LLAGRkmkDMEMQANLLLDRL 1847
Cdd:pfam06008 238 LKTAR---DSLDAANLLLQEI 255
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
552-606 |
7.93e-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: 45.04 E-value: 7.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 552 PCACPLSIDSNnfsPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNPTVPGG 606
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTG---QC-ECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1352-1865 |
8.55e-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: 8.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1352 ILENLENTTKYFQRYLIKEN-AKKIRAEIQleGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFI------- 1423
Cdd:TIGR04523 133 KKENKKNIDKFLTEIKKKEKeLEKLNNKYN--DLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlkkki 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1424 ---EQLHANIKEITEKVATLNQTARK---DFQPPVSALQSMHQNISSLLGLiKERNFTEMQQNaTLELKAAKDLLSRIQK 1497
Cdd:TIGR04523 211 qknKSLESQISELKKQNNQLKDNIEKkqqEINEKTTEISNTQTQLNQLKDE-QNKIKKQLSEK-QKELEQNNKKIKELEK 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1498 RFQKPQEKLKAL---KEANsLLSNHSEKLQAAEELLKEAGSKTQESNLLLLLvkanLKEfQEKKLRvQEEQNVTSELIAK 1574
Cdd:TIGR04523 289 QLNQLKSEISDLnnqKEQD-WNKELKSELKNQEKKLEEIQNQISQNNKIISQ----LNE-QISQLK-KELTNSESENSEK 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1575 GREwvdaagthTAAAQDTLTQLEHHRDELLLWARKIRSHVDDLVMQMSKrrARDLVHRAEQHASELQSRAGALDRDLENV 1654
Cdd:TIGR04523 362 QRE--------LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN--QEKLNQQKDEQIKKLQQEKELLEKEIERL 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1655 R--NVSLNATsaahvhsnIQTLTEEaemlaaDAHKtanktDLISESLASRGKAVLQRSSRFLKESVSTRR----KQQGIT 1728
Cdd:TIGR04523 432 KetIIKNNSE--------IKDLTNQ------DSVK-----ELIIKNLDNTRESLETQLKVLSRSINKIKQnleqKQKELK 492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1729 MKLDELKNLTSQFQESMDNImKQANDSLAMLREspggmrekgrKARELAAAAN--ESAVKTLEDVLaLSLRVFNTSEDLS 1806
Cdd:TIGR04523 493 SKEKELKKLNEEKKELEEKV-KDLTKKISSLKE----------KIEKLESEKKekESKISDLEDEL-NKDDFELKKENLE 560
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 1807 RVNATVQETNDLLHNsTMTTLLAGRKMKDmEMQANLLLDRLKPLKTLEE------NLSRNLSEIK 1865
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 ... |
1353-1876 |
1.21e-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: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1353 LENLENTTKYFQRYLIKENAKKiraeiQLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNG------TQALATFIEQL 1426
Cdd:TIGR00618 235 LQQTQQSHAYLTQKREAQEEQL-----KKQQLLKQLRARIEELRAQEAVLEETQERINRARKAaplaahIKAVTQIEQQA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1427 HANIKEITEKVATLNQtARKDFQPPVSALQSMHQNISSLLGLIKERNFTEMQQNATLELKAAKDLLSRIQKRFQKPQEKL 1506
Cdd:TIGR00618 310 QRIHTELQSKMRSRAK-LLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQK 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1507 KALKEANSLLSNHSEKLQaaEELLKEAGSKTQESNLLLLLVKANLKEFQEKKLRVQEE---QNVTSELIAKGREWVDAAG 1583
Cdd:TIGR00618 389 TTLTQKLQSLCKELDILQ--REQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAaaiTCTAQCEKLEKIHLQESAQ 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1584 THTAAAQ-----DTLTQ-------------LEHHRDELLLWARKIRSH---VDDLVMQMSKRRARDLVHRAEQHASELQS 1642
Cdd:TIGR00618 467 SLKEREQqlqtkEQIHLqetrkkavvlarlLELQEEPCPLCGSCIHPNparQDIDNPGPLTRRMQRGEQTYAQLETSEED 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1643 RAGALDRDLENVRNVSLNATSAAHvhsNIQTLTEEAEMLAADAHKTANKTDLI-----SESLASRGKAVLQRSS-RFLKE 1716
Cdd:TIGR00618 547 VYHQLTSERKQRASLKEQMQEIQQ---SFSILTQCDNRSKEDIPNLQNITVRLqdlteKLSEAEDMLACEQHALlRKLQP 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1717 SVSTRRKQQGITMKLDEL-KNLTSQFQESMDNIMKQANDSLAMLRESPggMREKGRKARELAAAANE------------- 1782
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELaLKLTALHALQLTLTQERVREHALSIRVLP--KELLASRQLALQKMQSEkeqltywkemlaq 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1783 --SAVKTLEDVLALSLRVFNTSEDLSRVNATVQETNDLLHNSTMTTLLAGRKMKdmeMQANLLLD-RLKPLKTLEENLSR 1859
Cdd:TIGR00618 702 cqTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTV---LKARTEAHfNNNEEVTAALQTGA 778
|
570
....*....|....*..
gi 1720389100 1860 NLSEIKLLISRARKQVA 1876
Cdd:TIGR00618 779 ELSHLAAEIQFFNRLRE 795
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1364-1654 |
1.41e-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: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1364 QRYLIKENAKKIRA-EIQLEGIAEQTENLQKELTRVLARHQKVNAEMERtsngtqalatfIEQLhanIKEITEKVATLNQ 1442
Cdd:TIGR02169 221 REYEGYELLKEKEAlERQKEAIERQLASLEEELEKLTEEISELEKRLEE-----------IEQL---LEELNKKIKDLGE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1443 TARKDFQppvSALQSMHQNISSLLGLIKERNftEMQQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEANSLLSNHSEK 1522
Cdd:TIGR02169 287 EEQLRVK---EKIGELEAEIASLERSIAEKE--RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1523 LQAAEELLKeagSKTQESNLLLLLVKANLKEFQEKKLRVQEEQN----VTSELIAKGREWVDAAGTHTAA---AQDTLTQ 1595
Cdd:TIGR02169 362 LKEELEDLR---AELEEVDKEFAETRDELKDYREKLEKLKREINelkrELDRLQEELQRLSEELADLNAAiagIEAKINE 438
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389100 1596 LEHHRDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQhaSELQSRAGALDRDLENV 1654
Cdd:TIGR02169 439 LEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY--DRVEKELSKLQRELAEA 495
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1368-1712 |
2.05e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1368 IKENAKKIRAEIQ-----LEGIAEQTENLQKELTRVLARHQkvNAEMERtsngtQALATFIEQLHANIKEITEKVATLN- 1441
Cdd:PRK02224 361 LREEAAELESELEeareaVEDRREEIEELEEEIEELRERFG--DAPVDL-----GNAEDFLEELREERDELREREAELEa 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1442 --QTARKDFQ---------------------PPVSALQSMHQNISSLlglikernftemqqnaTLELKAAKDLLSRIQKR 1498
Cdd:PRK02224 434 tlRTARERVEeaealleagkcpecgqpvegsPHVETIEEDRERVEEL----------------EAELEDLEEEVEEVEER 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1499 FqkpqEKLKALKEANSLLSNHSEKLQAAEELLKEAGSKTQEsnlllllvkanlkefqeKKLRVQEEQNVTSELIAKGREW 1578
Cdd:PRK02224 498 L----ERAEDLVEAEDRIERLEERREDLEELIAERRETIEE-----------------KRERAEELRERAAELEAEAEEK 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1579 VDAAGTHTAAAQDT----------LTQLEHHRDELllwaRKIR---SHVDDLVMQMSKRRAR--DLVHRAEQHASELQSR 1643
Cdd:PRK02224 557 REAAAEAEEEAEEAreevaelnskLAELKERIESL----ERIRtllAAIADAEDEIERLREKreALAELNDERRERLAEK 632
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720389100 1644 -------AGALDRD-LENVRNVSLNATSA-AHVHSNIQTLTEEAEMLAADAHKTANKTDLIsESLASRGKAVLQRSSR 1712
Cdd:PRK02224 633 rerkrelEAEFDEArIEEAREDKERAEEYlEQVEEKLDELREERDDLQAEIGAVENELEEL-EELRERREALENRVEA 709
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1213-1269 |
2.22e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 43.88 E-value: 2.22e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389100 1213 PCTCPHHPpfSFSPTCVVEgdsDFRCNaCLPGYEGQYCERCSAGYHGNPRAAGGsCQ 1269
Cdd:cd00055 1 PCDCNGHG--SLSGQCDPG---TGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG-CQ 50
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
471-665 |
4.90e-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: 46.14 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 471 CECPQGY---TGTSCEACLPGyyrvdgilfggicqpcechghasecdiHGICSVCTHNTTGdhCEQCLPGFYGTPSRGTP 547
Cdd:cd13416 1 EACPSGQytsSGECCEQCPPG---------------------------EGVARPCGDNQTV--CEPCLDGVTFSDVVSHT 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 548 GDCQPCA-CPLSIdsnnfSPTCHLTDGEEVVCdqcapgysgswceRCADGYYgnPTVPGGTCVPCNCsgnvdpleaghCD 626
Cdd:cd13416 52 EPCQPCTrCPGLM-----SMRAPCTATHDTVC-------------ECAYGYY--LDEDSGTCEPCTV-----------CP 100
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1720389100 627 SVTGECLKCLWNTDgAHCERCADGFYGDAVTAKN----CRACD 665
Cdd:cd13416 101 PGQGVVQSCGPNQD-TVCEACPEGTYSDEDSSTDpclpCTVCE 142
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
553-601 |
5.22e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 42.68 E-value: 5.22e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1720389100 553 CACPLSidsNNFSPTCHLTDGeevVCdQCAPGYSGSWCERCADGYYGNP 601
Cdd:smart00180 1 CDCDPG---GSASGTCDPDTG---QC-ECKPNVTGRRCDRCAPGYYGDG 42
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1378-1841 |
5.38e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 48.87 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1378 EIQLEGIAEQTENLQKELtrVLARHQKVNA--EMERTSNgtqalatFIEQLHANIkeitEKVATLNQTARKDFQPPVSAL 1455
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQS--EAAEAAKAQVleELESTKR-------LIEELKLNL----ERAQTEEAQAKQDSELAKLRV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1456 QSMHQNISS--------LLGLIKERnftemQQNATLELKAAKDLLSRIQKrfqkpqeklkalkEANSLLSnhsEKlQAAE 1527
Cdd:pfam05701 108 EEMEQGIADeasvaakaQLEVAKAR-----HAAAVAELKSVKEELESLRK-------------EYASLVS---ER-DIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1528 ELLKEAGSKTQESnlllllvkanlkefqEKklRVQEeqnVTSELIAKgREWVDAAgtHTA----------AA----QDTL 1593
Cdd:pfam05701 166 KRAEEAVSASKEI---------------EK--TVEE---LTIELIAT-KESLESA--HAAhleaeehrigAAlareQDKL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1594 T---QLEHHRDEL------LLWARKIRSHVDDLVMQMSKRRArDLVHRAEQHASELQSRAGALDRDlenvrNVSLNATSA 1664
Cdd:pfam05701 223 NwekELKQAEEELqrlnqqLLSAKDLKSKLETASALLLDLKA-ELAAYMESKLKEEADGEGNEKKT-----STSIQAALA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1665 A------HVHSNIQTLTEEAEML--AADAHKT---ANKTDLIS----ESLASRGKAVLQ---RSSRFLKESVSTRRKQQG 1726
Cdd:pfam05701 297 SakkeleEVKANIEKAKDEVNCLrvAAASLRSeleKEKAELASlrqrEGMASIAVSSLEaelNRTKSEIALVQAKEKEAR 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1727 itmklDELKNLTSQFQESMdnimKQAND--SLAMLrespggMREKGRKARELAAAANeSAVKTLEDVLALSLR---VFNT 1801
Cdd:pfam05701 377 -----EKMVELPKQLQQAA----QEAEEakSLAQA------AREELRKAKEEAEQAK-AAASTVESRLEAVLKeieAAKA 440
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 1802 SEDLSRVNAT-VQETNDLLHNST------MTTLLA------GRKMKDMEMQAN 1841
Cdd:pfam05701 441 SEKLALAAIKaLQESESSAESTNqedsprGVTLSLeeyyelSKRAHEAEELAN 493
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
578-852 |
6.32e-05 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 48.04 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 578 CDQCAPGYSGSwCERCADGYYGNPTvpgGTCVP-CNCSGNVDPLEAGHCDSVTGECL--KCLWNTDGAHCERCADGFY-- 652
Cdd:pfam03302 28 CKACSNDKREV-CEECNSNNYLTPT---SQCIDdCAKIGNYYYTTNANNKKICKECTvaNCKTCEDQGQCQACNDGFYks 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 653 GDAVTA--KNCRAC------DCHE--NGSLSGICHLETGLCDCKPHVTGQQCDQCLSGYYGLDTGLGCVPCNCSVEGSVS 722
Cdd:pfam03302 104 GDACSPchESCKTCsggtasDCTEclTGKALRYGNDGTKGTCGEGCTTGTGAGACKTCGLTIDGTSYCSECATETEYPQN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 723 DNCTEEGQ-----CHCGPGVSGKqCDRCSHGFYAfQDGGCTPCDCAHTQNNCDPASGECLCPPHTQGLKCEE-----CEE 792
Cdd:pfam03302 184 GVCTSTAAratatCKASSVANGM-CSSCANGYFR-MNGGCYETTKFPGKSVCEEANSGGTCQKEAPGYKLNNgdlvtCSP 261
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 793 AYWGLDPEQGCQACNCSAVGSTSAqCDVLSGHCPCKKGfGGQSCHQCSLG-YRSFPDCVPC 852
Cdd:pfam03302 262 GCKTCTSNTVCTTCMDGYVKTSDS-CTKCDSSCETCTG-ATTTCKTCATGyYKSGTGCVSC 320
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
482-823 |
1.33e-04 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 47.27 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 482 CEACLPGYyrvdGILFGGICQPCechghASECDIHGiCSVCThNTTGDHCEQCLPGFYGTPSRGTPGDCQPCAcplsids 561
Cdd:pfam03302 1 CDECKPGY----ELSADKTKCTS-----SAPCKTEN-CKACS-NDKREVCEECNSNNYLTPTSQCIDDCAKIG------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 562 NNFSPTChltDGEEVVCDQCAPGY-----SGSWCERCADGYYGNptvpGGTCVPC--NCSGNVDPLEAGHCDSVTGECLK 634
Cdd:pfam03302 63 NYYYTTN---ANNKKICKECTVANcktceDQGQCQACNDGFYKS----GDACSPCheSCKTCSGGTASDCTECLTGKALR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 635 -------------CLWNTDGAHCERCADGFYGdavtAKNCRACDCHENGSLSGICH----LETGLCDCKPHVTGqQCDQC 697
Cdd:pfam03302 136 ygndgtkgtcgegCTTGTGAGACKTCGLTIDG----TSYCSECATETEYPQNGVCTstaaRATATCKASSVANG-MCSSC 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 698 LSGYYGLDTGL----------------GCVPCNCSVEGSVSDNCT-EEGQCHCGPGVSGKQCDRCSHGfYAFQDGGCTPC 760
Cdd:pfam03302 211 ANGYFRMNGGCyettkfpgksvceeanSGGTCQKEAPGYKLNNGDlVTCSPGCKTCTSNTVCTTCMDG-YVKTSDSCTKC 289
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389100 761 DCA-HTQNNCDPASGECLCPPHTQGLKCEECE--EAYWGLDPEQGCQACNCSAVGSTSAQCDVLSG 823
Cdd:pfam03302 290 DSScETCTGATTTCKTCATGYYKSGTGCVSCTssESDNGITGVKGCLNCAPPSNNKGSVLCYLIKD 355
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
32-75 |
1.42e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 1.42e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 32 CICY--GHAS-SCpwdeEAKQLQCQCEHNTCGESCDRCCPGYHQQPW 75
Cdd:smart00180 1 CDCDpgGSASgTC----DPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1354-1574 |
2.20e-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: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1354 ENLENttkyfQRYLIKENAKKIRAEI-----QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHA 1428
Cdd:TIGR02169 836 QELQE-----QRIDLKEQIKSIEKEIenlngKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1429 NIKEITEKVATLNQTarkdfqppvsaLQSMHQNISSLlglikERNFTEMQQNATLELKAAKdllsrIQKRFQKPQEKLKA 1508
Cdd:TIGR02169 911 QIEKKRKRLSELKAK-----------LEALEEELSEI-----EDPKGEDEEIPEEELSLED-----VQAELQRVEEEIRA 969
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720389100 1509 LKEANSLlsnhseklqaAEELLKEagsktqesnlllllVKANLKEFQEKKLRVQEEQNVTSELIAK 1574
Cdd:TIGR02169 970 LEPVNML----------AIQEYEE--------------VLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
7-30 |
2.47e-04 |
|
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: 45.43 E-value: 2.47e-04
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1352-1566 |
4.11e-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: 4.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1352 ILENLENTTKYFQRYLikenaKKIRAEIQlegIAEQT-ENLQKELTRVLARHQKVNAEmertsngtqalatfIEQLHANI 1430
Cdd:TIGR04523 455 IIKNLDNTRESLETQL-----KVLSRSIN---KIKQNlEQKQKELKSKEKELKKLNEE--------------KKELEEKV 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1431 KEITEKVATLNQTARKdfqppvsaLQS----MHQNISSLlglikERNFTEMQQNATLELkaakdllsrIQKRFQKPQEKL 1506
Cdd:TIGR04523 513 KDLTKKISSLKEKIEK--------LESekkeKESKISDL-----EDELNKDDFELKKEN---------LEKEIDEKNKEI 570
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720389100 1507 KALKEAN-SLLSNHSEKlqaaEELLKEagsKTQESNLLLLLV--KANLKEFQEKKLRVQEEQN 1566
Cdd:TIGR04523 571 EELKQTQkSLKKKQEEK----QELIDQ---KEKEKKDLIKEIeeKEKKISSLEKELEKAKKEN 626
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1353-1625 |
5.17e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 5.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1353 LENLENTTKYFQRYL--IKENAKKIRAE-------IQLEGIAEQTENLQKELTRV-LARHQKVNAEMERTSNGTQALATF 1422
Cdd:PRK03918 461 LKRIEKELKEIEEKErkLRKELRELEKVlkkeselIKLKELAEQLKELEEKLKKYnLEELEKKAEEYEKLKEKLIKLKGE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1423 IEQLHANIKEITE---KVATLNqtarkdfqppvSALQSMHQNISSLLGLIKERNFTEMQQ------------NATLELKA 1487
Cdd:PRK03918 541 IKSLKKELEKLEElkkKLAELE-----------KKLDELEEELAELLKELEELGFESVEEleerlkelepfyNEYLELKD 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1488 AKDLLSRIQKRFQKPQEKL-KALKEANsllsnhsEKLQAAEELLKEagsktqesnlllllvkanLKEFqEKKLRVQEEQN 1566
Cdd:PRK03918 610 AEKELEREEKELKKLEEELdKAFEELA-------ETEKRLEELRKE------------------LEEL-EKKYSEEEYEE 663
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389100 1567 VTSELIAKGREWvdaagthtAAAQDTLTQLEHHRDElllwarkIRSHVDDLVMQMSKRR 1625
Cdd:PRK03918 664 LREEYLELSREL--------AGLRAELEELEKRREE-------IKKTLEKLKEELEERE 707
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1671-1792 |
7.65e-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: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1671 IQTLTEEAEMLAADAHKTANKTDLIS---ESLASRGKAVLQRSSRFLKESVSTRRKQ----QGITMKLDELKNLTSQFQE 1743
Cdd:pfam10168 577 LQSLEEERKSLSERAEKLAEKYEEIKdkqEKLMRRCKKVLQRLNSQLPVLSDAEREMkkelETINEQLKHLANAIKQAKK 656
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1720389100 1744 SMDnimKQAndslamlRESPGGMREKGRKARELaaaaNESAVKTLEDVL 1792
Cdd:pfam10168 657 KMN---YQR-------YQIAKSQSIRKKSSLSL----SEKQRKTIKEIL 691
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
1352-1692 |
1.01e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.82 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1352 ILENLENTTKYFQRYLIKENAKKIRAEI-QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQ------ALATFIE 1424
Cdd:PTZ00440 1155 TLNEVNEIEIEYERILIDHIVEQINNEAkKSKTIMEEIESYKKDIDQVKKNMSKERNDHLTTFEYNAyydkatASYENIE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1425 QL--HAN--------------IKEITEKVATLNQTARKDFQPPVSALQSMHqNISSLLGLIKERNFTE-----MQQNATL 1483
Cdd:PTZ00440 1235 ELttEAKglkgeanrstnvdeLKEIKLQVFSYLQQVIKENNKMENALHEIK-NMYEFLISIDSEKILKeilnsTKKAEEF 1313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1484 ELKAAKDL--LSRIQKRFQKPQEKLKALKEANSLLSNHS---EKLQAAEELLKEAGSKTQESNLLLLLVKANlKEFQEKK 1558
Cdd:PTZ00440 1314 SNDAKKELekTDNLIKQVEAKIEQAKEHKNKIYGSLEDKqidDEIKKIEQIKEEISNKRKEINKYLSNIKSN-KEKCDLH 1392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1559 LRV---------------QEEQNVTSEL-IAKGREWVDAAGTHTAAAQDTLTQLEHHRDELLLWARKIRSHVDD-LVMQM 1621
Cdd:PTZ00440 1393 VRNasrgkdkidflnkheAIEPSNSKEVnIIKITDNINKCKQYSNEAMETENKADENNDSIIKYEKEITNILNNsSILGK 1472
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720389100 1622 S------KRRARDLVHRAEQHASELQSRAGALDRDLENVRNvslnatsaahvHSNIqtlTEEAEMLAADAHKTANKT 1692
Cdd:PTZ00440 1473 KtklekkKKEATNIMDDINGEHSIIKTKLTKSSEKLNQLNE-----------QPNI---KREGDVLNNDKSTIAYET 1535
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1214-1261 |
1.66e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 38.45 E-value: 1.66e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1720389100 1214 CTCphHPPFSFSPTCVVEGdsdFRCNaCLPGYEGQYCERCSAGYHGNP 1261
Cdd:smart00180 1 CDC--DPGGSASGTCDPDT---GQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1384-1655 |
2.37e-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: 2.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1384 IAEQTENLQKELTRVLARHQkvnaEMERTSNGTQALATfIEQLHANIKEITEKVATLNQTArkdfqppvSALQsmHQNIS 1463
Cdd:COG4913 223 TFEAADALVEHFDDLERAHE----ALEDAREQIELLEP-IRELAERYAAARERLAELEYLR--------AALR--LWFAQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1464 SLLGLIKERnftemQQNATLELKAAKDLLSRIQKRFQKPQEKLKALKEAnsLLSNHSEKLQAAEELLKEAGSKTQEsnll 1543
Cdd:COG4913 288 RRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELEAQ--IRGNGGDRLEQLEREIERLERELEE---- 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1544 lllVKANLKEFQEKkLRVQEEQNVTSEliakgREWVDAAgthtAAAQDTLTQLEHHRDELllwarkiRSHVDDLvmqmsK 1623
Cdd:COG4913 357 ---RERRRARLEAL-LAALGLPLPASA-----EEFAALR----AEAAALLEALEEELEAL-------EEALAEA-----E 411
|
250 260 270
....*....|....*....|....*....|....*
gi 1720389100 1624 RRARDLVHRAEQHASE---LQSRAGALDRDLENVR 1655
Cdd:COG4913 412 AALRDLRRELRELEAEiasLERRKSNIPARLLALR 446
|
|
| F-BAR_Rgd1 |
cd07652 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Saccharomyces cerevisiae Rho ... |
1369-1541 |
2.38e-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: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1369 KENAK--KIRAEIQLEGIaeqtENLQKeltrvLARHQKvnaEMERTSNGTQAlaTFIEQLHANIkEITEKVATLNQTArk 1446
Cdd:cd07652 22 KEFATflKKRAAIEEEHA----RGLKK-----LARTTL---DTYKRPDHKQG--SFSNAYHSSL-EFHEKLADNGLRF-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1447 dfqppVSALQSMHQNISSLL-------------GLIKERNFTEMQQ---NATLELKAAKDLLSRIqkRFQKPQEKLKALK 1510
Cdd:cd07652 85 -----AKALNEMSDELSSLAktveksrksiketGKRAEKKVQDAEAaaeKAKARYDSLADDLERV--KTGDPGKKLKFGL 157
|
170 180 190
....*....|....*....|....*....|....*
gi 1720389100 1511 EANSLLSNHSE----KLQAAEELLKeagSKTQESN 1541
Cdd:cd07652 158 KGNKSAAQHEDellrKVQAADQDYA---SKVNAAQ 189
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
32-78 |
2.64e-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: 2.64e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1720389100 32 CICYGHASSCPwDEEAKQLQCQCEHNTCGESCDRCCPGYHQQPWRPG 78
Cdd:pfam00053 1 CDCNPHGSLSD-TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1521-1736 |
2.87e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 2.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1521 EKLQA-AEELLKEAGSKTqesnlllllvKANLKEFQEKKLRVQEEQNVTSELiakgrewvdaagthtAAAQDTLTQLEHH 1599
Cdd:COG4717 49 ERLEKeADELFKPQGRKP----------ELNLKELKELEEELKEAEEKEEEY---------------AELQEELEELEEE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1600 RDELLLWARKIRSHVDDLVMQMSKRRARDLVHRAEQHASELQSRAGALDRDLENVRNvslnatsaahVHSNIQTLTEEAE 1679
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRE----------LEEELEELEAELA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720389100 1680 MLAADAHKTANKTDLISE----SLASRGKAVLQRSSRFLKESVSTRRKQQGITMKLDELKN 1736
Cdd:COG4717 174 ELQEELEELLEQLSLATEeelqDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1364-1563 |
4.85e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 4.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1364 QRYLIKENAKKIRAEIqlEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLNQT 1443
Cdd:COG1340 30 KRDELNEELKELAEKR--DELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1444 arkdfQPPVSALQSMhqnISSLLglikernftEMQQNATLELKAAKDLLSRIQKRfqkpQEKLKALKEANSLLSNHSEKL 1523
Cdd:COG1340 108 -----GGSIDKLRKE---IERLE---------WRQQTEVLSPEEEKELVEKIKEL----EKELEKAKKALEKNEKLKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1720389100 1524 QAAEELLKEAGSKTQEsnlllllVKANLKEFQEKKLRVQE 1563
Cdd:COG1340 167 AELKELRKEAEEIHKK-------IKELAEEAQELHEEMIE 199
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1380-1533 |
6.11e-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: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1380 QLEGIAEQTENLQKELTRVLARHQKVNAEMERTSNGTQALATFIEQLHANIKEITEKVATLNQ---TAR--KDFQppvsA 1454
Cdd:COG1579 18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgNVRnnKEYE----A 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720389100 1455 LQsmHQnISSLLGLIKERNFTEMQQNATLElkAAKDLLSRIQKRFQKPQEKLKALKEAnslLSNHSEKLQAAEELLKEA 1533
Cdd:COG1579 94 LQ--KE-IESLKRRISDLEDEILELMERIE--ELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAE 164
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
470-494 |
6.48e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 36.91 E-value: 6.48e-03
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
12-30 |
7.31e-03 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 40.64 E-value: 7.31e-03
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1380-1595 |
8.85e-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: 8.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1380 QLEGIAEQTEN------LQKELTRVLARHQKVNAEMERtsngTQALATFIEQLHANIKEITEKVATLNQTARKDFQP--- 1450
Cdd:pfam12795 1 KLDELEKAKLDeaakkkLLQDLQQALSLLDKIDASKQR----AAAYQKALDDAPAELRELRQELAALQAKAEAAPKEila 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720389100 1451 --PVSALQSMHQNISSLLGLIKERNFTEMQQNATLE--LKAAKDLLSRIQKRFQKPQEKLKALKEANSLLSNHSEKLQAA 1526
Cdd:pfam12795 77 slSLEELEQRLLQTSAQLQELQNQLAQLNSQLIELQtrPERAQQQLSEARQRLQQIRNRLNGPAPPGEPLSEAQRWALQA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720389100 1527 EELLKEAGSKTQE-----SNLLLLLVKANLKEFQEKKLRVQEEQNVTSELI-AKGREWVDAAgthtAAAQDTLTQ 1595
Cdd:pfam12795 157 ELAALKAQIDMLEqellsNNNRQDLLKARRDLLTLRIQRLEQQLQALQELLnEKRLQEAEQA----VAQTEQLAE 227
|
|
| |
