|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
50-303 |
7.19e-99 |
|
Laminin N-terminal (Domain VI);
:
Pssm-ID: 459653 Cd Length: 230 Bit Score: 318.37 E-value: 7.19e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 50 LHPPYFNLAEGARITASATCGEEAPTRsvsrptedlYCKLVGGPvaggdpnqtiQGQYCDICTAANSNKAHPVSNAIDGT 129
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPER---------YCILSGLE----------GGKKCFICDSRDPHNSHPPSNLTDSN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 130 ER----WWQSPPLSrgLEYNEVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSTDFGHTYQPWQFFASskrDCLERFG 205
Cdd:pfam00055 62 NGtnetWWQSETGV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 206 -PRTLERITQDDDVICTTEYSRIVPLENGEIVVSLVNGRPGALNFSYSPLLRDFTKATNIRLRFLRTNTLLGHLmgkaLR 284
Cdd:pfam00055 136 rPSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LD 211
|
250
....*....|....*....
gi 124487155 285 DPTVTRRYYYSIKDISIGG 303
Cdd:pfam00055 212 DPSVLRKYYYAISDISVGG 230
|
|
| Laminin_I super family |
cl26988 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2194-2452 |
4.71e-65 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
The actual alignment was detected with superfamily member pfam06008:
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 222.67 E-value: 4.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2194 LQGINASSAAWARLHRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQLLDTTEST 2273
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2274 LGRAQKLLESVRAVGRALNELASRMGQGSPGDALVPSGEQLRwALAEVERLLWDMRTRDLGAQGAVAEAELAEAQRLMAR 2353
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSR-MLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2354 VQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEALQWKQELSQDNATLKATLQ 2433
Cdd:pfam06008 160 IQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 124487155 2434 AASLILGHVSELLQGIDQA 2452
Cdd:pfam06008 240 TARDSLDAANLLLQEIDDA 258
|
|
| LamB |
smart00281 |
Laminin B domain; |
1690-1819 |
1.58e-48 |
|
Laminin B domain;
:
Pssm-ID: 214597 Cd Length: 127 Bit Score: 170.13 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 1690 FSELYWQAPPSYLGDRVSSYGGTLHYELHSETQRGDifiPYESRPDVVLQGNQMSIAFLELAYPPPGQVHRGQLQLVEGN 1769
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG---THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 124487155 1770 FRHLEtHNPVSREELMMVLAGLEQLQIRALFSQTSSSVSLRRVVLEVASE 1819
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_II super family |
cl05515 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2642-2764 |
7.93e-45 |
|
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.
The actual alignment was detected with superfamily member pfam06009:
Pssm-ID: 368703 [Multi-domain] Cd Length: 138 Bit Score: 159.96 E-value: 7.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2642 LSTATHVQSQLQGMQKNVERWQSQLGGLQGQ---------DLSQVERDASSSVSTLEKTLPQLLAKLSRLENRGVHNASL 2712
Cdd:pfam06009 9 NETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNSSSL 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 2713 alSANIGRVRKLIAQARSAASKVKVSMKFNGRSGVRLRTPRDLADLAAYTAL 2764
Cdd:pfam06009 89 --SDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
smart00282 |
Laminin G domain; |
3542-3669 |
5.93e-26 |
|
Laminin G domain;
:
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 105.50 E-value: 5.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3542 SLELEMRPLAAAGLIFHLGQALATPYMQLKVLTEQVLLQANDGAGEFSTWVTYPKLCDGRWHRVAVIMGRDTLRLEVDtQ 3621
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD-G 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 3622 SNHTTGRLPESLAG--SPALLHLGSLPKSSTARPEL--PAYRGCLRKLLING 3669
Cdd:smart00282 80 GNRVSGESPGGLTIlnLDGPLYLGGLPEDLKLPPLPvtPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3337-3495 |
1.70e-24 |
|
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: 102.11 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3337 AYQFGGPlpSYLQFVGiSPSHRNRLHLSMLVRPHAASqGLLLSTAPmSGRSPSLVLFLNHGHFVAQTEGPGPRLQVQSRQ 3416
Cdd:cd00110 1 GVSFSGS--SYVRLPT-LPAPRTRLSISFSFRTTSPN-GLLLYAGS-QNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3417 HSRAGQWHRVSVRWGMQQIQLVVDGSQTwsqkaLHHRVPR--AERPQPYTLSVGGLPASSYSSKLPVSVGFSGCLKKLQL 3494
Cdd:cd00110 76 PLNDGQWHSVSVERNGRSVTLSVDGERV-----VESGSPGgsALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
.
gi 124487155 3495 D 3495
Cdd:cd00110 151 N 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3155-3273 |
4.45e-17 |
|
Laminin G domain;
:
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 80.46 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3155 FGFRGTQDNNLLYYRTSPDGP--YQVSLREGHVTLRFMN-----QEVETQRVFADGAPHYVAFYSNVTGVWLYVDDQLQL 3227
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLgsgpaRLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGGNRV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 3228 VKSHERTTPMLQLqpeePSRLLLGGLP------VSGTFHNFSGCISNVFVQR 3273
Cdd:smart00282 84 SGESPGGLTILNL----DGPLYLGGLPedlklpPLPVTPGFRGCIRNLKVNG 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1443-1491 |
6.84e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 68.15 E-value: 6.84e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 1443 CGCHEVGAVSPTCEPFGGQCPCRGHVIGRDCSRCATGYWGFPNCRPCDC 1491
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1582-1630 |
3.49e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.22 E-value: 3.49e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 1582 CDCHEAGTMASVCDPLTGQCHCKENVQGSRCDQCRVGTFSLDAANPKGC 1630
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2783-2912 |
4.42e-13 |
|
Laminin G domain;
:
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 68.91 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2783 DHFVLYMGSRQaTGDYMGVSLRNQKVHWVYRLGkAGPTTLSIDE---NIGeQFAAVSIDRTLQFGHMSVTVEKQMVheik 2859
Cdd:smart00282 12 NGLLLYAGSKG-GGDYLALELRDGRLVLRYDLG-SGPARLTSDPtplNDG-QWHRVAVERNGRSVTLSVDGGNRVS---- 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 124487155 2860 gdTVAPGSEGLLNLHPDdfvFYVGGYPSNFTPPEPLRFPGYLGCIEMETLNEE 2912
Cdd:smart00282 85 --GESPGGLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
682-724 |
6.81e-13 |
|
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: 65.45 E-value: 6.81e-13
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124487155 682 PCHCSADGSLHTTCDPTTGQCRCRPRVTGLHCDMCVPGAYNFP 724
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
593-640 |
1.06e-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: 65.07 E-value: 1.06e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 593 CGCSPAGTLPEGCD-EAGRCQCRPGFDGPHCDRCLPGYHGYPDCHACAC 640
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1533-1584 |
1.63e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.30 E-value: 1.63e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 1533 CNCSGPGVqelTDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYGYPSCRPCDC 1584
Cdd:pfam00053 1 CDCNPHGS---LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2947-3099 |
2.37e-12 |
|
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: 67.44 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2947 GSYLDGSGFARISFEKQFSNTKRFDQELRLVSYNGIIFFL--KQESQFLCLAVQEGTLVLFYDFGSGLKKadpLQPPQAL 3024
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLV---LSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487155 3025 tAASKAIQVFLLAGNRKRVLV--RVERATVFSVDQDNMLEMADAYYLGGVPPEQLPLSLrqlfPSGGSVRGCIKGIK 3099
Cdd:cd00110 78 -NDGQWHSVSVERNGRSVTLSvdGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL----PVSPGFVGCIRDLK 149
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1970-2023 |
2.43e-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: 63.91 E-value: 2.43e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 124487155 1970 PCDCSGNGDPNmifSDCDPLTGACRgCLRHTTGPHCERCAPGFYGNALLPGNCT 2023
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2025-2069 |
8.47e-12 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 8.47e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 124487155 2025 CDCSPCGT--ETCDPQSGRCLCKAGVTGQRCDRCLEGYFGfEQCQGC 2069
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. |
638-685 |
9.29e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 9.29e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 638 CACDPRGALDQQC-GVGGLCHCRPGYTGATCQECSPGFYGFPSCIPCHC 685
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2071-2117 |
1.17e-11 |
|
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: 61.99 E-value: 1.17e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 124487155 2071 PCAC-GPAAKGSECHPQSGQCHCQPGTTGPQCLECAPGYWGLPEK--GCR 2117
Cdd:cd00055 1 PCDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
546-589 |
6.22e-11 |
|
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: 60.06 E-value: 6.22e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 124487155 546 PCQCSSPGVANSLCDPESGQCMCRTGFEGDRCDHCALGYFHFPL 589
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
500-547 |
1.68e-10 |
|
Laminin-type epidermal growth factor-like domai;
:
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 1.68e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 124487155 500 CDCNAAGTQGNACrkDPRLGRCVCKPNFRGAHCELCAPGFHGPSCHPC 547
Cdd:smart00180 1 CDCDPGGSASGTC--DPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1915-1968 |
1.97e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 124487155 1915 CPCPLAVPSNnfaDGCVLRNGrtQCLCRPGYAGASCERCAPGFFGNPLVLGSSC 1968
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1864-1900 |
5.17e-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: 5.17e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 124487155 1864 PCQCHGH---SDRCLPGSGICVgCQHNTEGDQCERCRPGF 1900
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
304-352 |
4.17e-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: 49.27 E-value: 4.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 304 RCVCHGHADV---CDakdpldPFRLQCACQHNTCGGSCDRCCPGFNQQPWKP 352
Cdd:cd00055 1 PCDCNGHGSLsgqCD------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
781-832 |
7.50e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.50 E-value: 7.50e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 124487155 781 RCSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFGLDYAdYFGCR 832
Cdd:cd00055 1 PCDCNGHGSLSG--QCdPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
833-872 |
9.77e-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: 9.77e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 124487155 833 SCRCDVGGALGQGCEPKTGACRCRPNTQGPTCSEPAKDHY 872
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| RecN super family |
cl33912 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
2364-2623 |
1.22e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
The actual alignment was detected with superfamily member COG0497:
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 54.31 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2364 ENQSL---ATHIR--DQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEA--LQWK-QELsqDNATLKA----T 2431
Cdd:COG0497 133 EHQSLldpDAQREllDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELdlLRFQlEEL--EAAALQPgeeeE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2432 LQAASLILGHVSELLQGIDQAkedLEHLAASLDGAwTPLLKR-MQAFSPASskvDLVEAAEAHAQKLNQLAINLSGIIlg 2510
Cdd:COG0497 211 LEEERRRLSNAEKLREALQEA---LEALSGGEGGA-LDLLGQaLRALERLA---EYDPSLAELAERLESALIELEEAA-- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2511 inqdRFIQRAVEASNAYSSILQAVQAAEDAAGQALRQASRTWEMVVQrgLAAGARQLLANSSALEETILGHQGRLGLAQG 2590
Cdd:COG0497 282 ----SELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVEELLA--YAEELRAELAELENSDERLEELEAELAEAEA 355
|
250 260 270
....*....|....*....|....*....|....*.
gi 124487155 2591 RLQAAGIQLHNvwARKN---QLAAQIQEAQAMLAMD 2623
Cdd:COG0497 356 ELLEAAEKLSA--ARKKaakKLEKAVTAELADLGMP 389
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
433-474 |
4.05e-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: 46.19 E-value: 4.05e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124487155 433 PCDCESDFT-DGTCEDLTGRCYCRPNFTGELCAACAEGYTDFP 474
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
363-426 |
2.01e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
:
Pssm-ID: 238012 Cd Length: 50 Bit Score: 44.27 E-value: 2.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487155 363 SCNCHGHAydcyydpevdrrnasQNQDNVYQGGGVCLdCQHHTTGINCERCLPGFFRAPDQPLD 426
Cdd:cd00055 1 PCDCNGHG---------------SLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2119-2147 |
2.05e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
:
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.57 E-value: 2.05e-04
10 20 30
....*....|....*....|....*....|....
gi 124487155 2119 CQCP-----RGHCDPHTGHCTCPPGLSGERCDTC 2147
Cdd:pfam00053 1 CDCNphgslSDTCDPETGQCLCKPGVTGRHCDRC 34
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
50-303 |
7.19e-99 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 318.37 E-value: 7.19e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 50 LHPPYFNLAEGARITASATCGEEAPTRsvsrptedlYCKLVGGPvaggdpnqtiQGQYCDICTAANSNKAHPVSNAIDGT 129
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPER---------YCILSGLE----------GGKKCFICDSRDPHNSHPPSNLTDSN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 130 ER----WWQSPPLSrgLEYNEVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSTDFGHTYQPWQFFASskrDCLERFG 205
Cdd:pfam00055 62 NGtnetWWQSETGV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 206 -PRTLERITQDDDVICTTEYSRIVPLENGEIVVSLVNGRPGALNFSYSPLLRDFTKATNIRLRFLRTNTLLGHLmgkaLR 284
Cdd:pfam00055 136 rPSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LD 211
|
250
....*....|....*....
gi 124487155 285 DPTVTRRYYYSIKDISIGG 303
Cdd:pfam00055 212 DPSVLRKYYYAISDISVGG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
49-303 |
6.46e-97 |
|
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: 313.14 E-value: 6.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 49 SLHPPYFNLAEGARITASATCGEEAPTRsvsrptedlYCKLVGGpvaggdpnqTIQGQYCDICTAANSNKAHPVSNAIDG 128
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGEPGPER---------YCKLVGH---------TEQGKKCDYCDARNPRRSHPAENLTDG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 129 TE----RWWQSPPLSRGLEYneVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERStDFGHTYQPWQFFASskrDCLERF 204
Cdd:smart00136 68 NNpnnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 205 G--PRTLERITQDDDVICTTEYSRIVPLENGEIVVSLVNGRPGALNFSYSPLLRDFTKATNIRLRFLRTNTLLGHLMGKA 282
Cdd:smart00136 141 GrpPRGPITKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR 220
|
250 260
....*....|....*....|.
gi 124487155 283 lrdPTVTRRYYYSIKDISIGG 303
Cdd:smart00136 221 ---PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2194-2452 |
4.71e-65 |
|
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: 222.67 E-value: 4.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2194 LQGINASSAAWARLHRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQLLDTTEST 2273
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2274 LGRAQKLLESVRAVGRALNELASRMGQGSPGDALVPSGEQLRwALAEVERLLWDMRTRDLGAQGAVAEAELAEAQRLMAR 2353
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSR-MLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2354 VQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEALQWKQELSQDNATLKATLQ 2433
Cdd:pfam06008 160 IQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 124487155 2434 AASLILGHVSELLQGIDQA 2452
Cdd:pfam06008 240 TARDSLDAANLLLQEIDDA 258
|
|
| LamB |
smart00281 |
Laminin B domain; |
1690-1819 |
1.58e-48 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 170.13 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 1690 FSELYWQAPPSYLGDRVSSYGGTLHYELHSETQRGDifiPYESRPDVVLQGNQMSIAFLELAYPPPGQVHRGQLQLVEGN 1769
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG---THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 124487155 1770 FRHLEtHNPVSREELMMVLAGLEQLQIRALFSQTSSSVSLRRVVLEVASE 1819
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1694-1830 |
2.16e-48 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 170.14 E-value: 2.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 1694 YWQAPPSYLGDRVSSYGGTLHYELHSETQRGDIfiPYESRPDVVLQGNQMSIAFL--ELAYPPPGQVHRGQLQLVEGNFR 1771
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGG--SLNSEPDVILEGNGLRLSYSspDQPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 124487155 1772 HlETHNPVSREELMMVLAGLEQLQIRALFSQTSSSVSLRRVVLEVASEAGRGPPASNVE 1830
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2642-2764 |
7.93e-45 |
|
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: 159.96 E-value: 7.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2642 LSTATHVQSQLQGMQKNVERWQSQLGGLQGQ---------DLSQVERDASSSVSTLEKTLPQLLAKLSRLENRGVHNASL 2712
Cdd:pfam06009 9 NETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNSSSL 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 2713 alSANIGRVRKLIAQARSAASKVKVSMKFNGRSGVRLRTPRDLADLAAYTAL 2764
Cdd:pfam06009 89 --SDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
smart00282 |
Laminin G domain; |
3542-3669 |
5.93e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 105.50 E-value: 5.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3542 SLELEMRPLAAAGLIFHLGQALATPYMQLKVLTEQVLLQANDGAGEFSTWVTYPKLCDGRWHRVAVIMGRDTLRLEVDtQ 3621
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD-G 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 3622 SNHTTGRLPESLAG--SPALLHLGSLPKSSTARPEL--PAYRGCLRKLLING 3669
Cdd:smart00282 80 GNRVSGESPGGLTIlnLDGPLYLGGLPEDLKLPPLPvtPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3519-3668 |
1.56e-25 |
|
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: 105.19 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3519 GLFFPGSeGVVTLELPKAKMPYVSLELEMRPLAAAGLIFHLGQALATPYMQLKVLTEQVLLQANDGAGefSTWVTYP-KL 3597
Cdd:cd00110 1 GVSFSGS-SYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSG--SLVLSSKtPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487155 3598 CDGRWHRVAVIMGRDTLRLEVD-TQSNHTTGRLPESLAGSPALLHLGSLPKSSTARPEL--PAYRGCLRKLLIN 3668
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDgERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPvsPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3337-3495 |
1.70e-24 |
|
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: 102.11 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3337 AYQFGGPlpSYLQFVGiSPSHRNRLHLSMLVRPHAASqGLLLSTAPmSGRSPSLVLFLNHGHFVAQTEGPGPRLQVQSRQ 3416
Cdd:cd00110 1 GVSFSGS--SYVRLPT-LPAPRTRLSISFSFRTTSPN-GLLLYAGS-QNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3417 HSRAGQWHRVSVRWGMQQIQLVVDGSQTwsqkaLHHRVPR--AERPQPYTLSVGGLPASSYSSKLPVSVGFSGCLKKLQL 3494
Cdd:cd00110 76 PLNDGQWHSVSVERNGRSVTLSVDGERV-----VESGSPGgsALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
.
gi 124487155 3495 D 3495
Cdd:cd00110 151 N 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3547-3669 |
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: 92.48 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3547 MRPLAAAGLIFHLGQALaTPYMQLKVLTEQVLLQANDGAGEFSTWVTYPKLCDGRWHRVAVIMGRDTLRLEVDTQSNHTT 3626
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 124487155 3627 GRLPESLA-GSPALLHLGSLPK--SSTARPELPAYRGCLRKLLING 3669
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPllLLPALPVRAGFVGCIRDVRVNG 125
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3372-3497 |
2.34e-20 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 89.40 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3372 ASQGLLLSTApmSGRSPSLVLFLNHGHFVAQTE-GPGPRLQVQSRQHSRAGQWHRVSVRWGMQQIQLVVDGSQTWSQKAL 3450
Cdd:pfam02210 5 QPNGLLLYAG--GGGSDFLALELVNGRLVLRYDlGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 124487155 3451 HHRVPraeRPQPYTLSVGGLPASSYSSKLPVSVGFSGCLKKLQLDKR 3497
Cdd:pfam02210 83 GESLL---LNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
3362-3497 |
3.60e-19 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 86.24 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3362 HLSMLVRPHAASqGLLLSTAPmSGRSPSLVLFLNHGHFVAQTEGPGPRLQVQS-RQHSRAGQWHRVSVRWGMQQIQLVVD 3440
Cdd:smart00282 1 SISFSFRTTSPN-GLLLYAGS-KGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 124487155 3441 GSQTWSQKALHHRvPRAERPQPytLSVGGLPASSYSSKLPVSVGFSGCLKKLQLDKR 3497
Cdd:smart00282 79 GGNRVSGESPGGL-TILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
3155-3273 |
4.45e-17 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 80.46 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3155 FGFRGTQDNNLLYYRTSPDGP--YQVSLREGHVTLRFMN-----QEVETQRVFADGAPHYVAFYSNVTGVWLYVDDQLQL 3227
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLgsgpaRLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGGNRV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 3228 VKSHERTTPMLQLqpeePSRLLLGGLP------VSGTFHNFSGCISNVFVQR 3273
Cdd:smart00282 84 SGESPGGLTILNL----DGPLYLGGLPedlklpPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3128-3271 |
7.31e-15 |
|
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: 74.76 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3128 TMTFHGHGFLPLALPDVAPITEVVysGFGFRGTQDNN-LLYYRTSPDGPY-QVSLREGHVTLRFMNQE----VETQRVFA 3201
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSI--SFSFRTTSPNGlLLYAGSQNGGDFlALELEDGRLVLRYDLGSgslvLSSKTPLN 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124487155 3202 DGAPHYVAFYSNVTGVWLYVDDQLQLvkshERTTPMLQLQPEEPSRLLLGGLPVSGTF------HNFSGCISNVFV 3271
Cdd:cd00110 79 DGQWHSVSVERNGRSVTLSVDGERVV----ESGSPGGSALLNLDGPLYLGGLPEDLKSpglpvsPGFVGCIRDLKV 150
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1443-1491 |
6.84e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 68.15 E-value: 6.84e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 1443 CGCHEVGAVSPTCEPFGGQCPCRGHVIGRDCSRCATGYWGFPNCRPCDC 1491
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1582-1630 |
3.49e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.22 E-value: 3.49e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 1582 CDCHEAGTMASVCDPLTGQCHCKENVQGSRCDQCRVGTFSLDAANPKGC 1630
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2783-2912 |
4.42e-13 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 68.91 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2783 DHFVLYMGSRQaTGDYMGVSLRNQKVHWVYRLGkAGPTTLSIDE---NIGeQFAAVSIDRTLQFGHMSVTVEKQMVheik 2859
Cdd:smart00282 12 NGLLLYAGSKG-GGDYLALELRDGRLVLRYDLG-SGPARLTSDPtplNDG-QWHRVAVERNGRSVTLSVDGGNRVS---- 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 124487155 2860 gdTVAPGSEGLLNLHPDdfvFYVGGYPSNFTPPEPLRFPGYLGCIEMETLNEE 2912
Cdd:smart00282 85 --GESPGGLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
682-724 |
6.81e-13 |
|
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: 65.45 E-value: 6.81e-13
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124487155 682 PCHCSADGSLHTTCDPTTGQCRCRPRVTGLHCDMCVPGAYNFP 724
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
593-640 |
1.06e-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: 65.07 E-value: 1.06e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 593 CGCSPAGTLPEGCD-EAGRCQCRPGFDGPHCDRCLPGYHGYPDCHACAC 640
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1533-1584 |
1.63e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.30 E-value: 1.63e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 1533 CNCSGPGVqelTDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYGYPSCRPCDC 1584
Cdd:pfam00053 1 CDCNPHGS---LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2947-3099 |
2.37e-12 |
|
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: 67.44 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2947 GSYLDGSGFARISFEKQFSNTKRFDQELRLVSYNGIIFFL--KQESQFLCLAVQEGTLVLFYDFGSGLKKadpLQPPQAL 3024
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLV---LSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487155 3025 tAASKAIQVFLLAGNRKRVLV--RVERATVFSVDQDNMLEMADAYYLGGVPPEQLPLSLrqlfPSGGSVRGCIKGIK 3099
Cdd:cd00110 78 -NDGQWHSVSVERNGRSVTLSvdGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL----PVSPGFVGCIRDLK 149
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1970-2023 |
2.43e-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: 63.91 E-value: 2.43e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 124487155 1970 PCDCSGNGDPNmifSDCDPLTGACRgCLRHTTGPHCERCAPGFYGNALLPGNCT 2023
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1442-1484 |
4.19e-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: 63.14 E-value: 4.19e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124487155 1442 PCGCHEVGAVSPTCEPFGGQCPCRGHVIGRDCSRCATGYWGFP 1484
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2192-2754 |
7.21e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2192 EQLQGINASSAAwaRLHRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQLLDTTE 2271
Cdd:TIGR02168 284 EELQKELYALAN--EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2272 STLGRAQKLLESVRAVGRALNELASRMgqgspgDALVPSGEQLRwalAEVERL------LWDMRTRdLGAQGAVAEAELA 2345
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKV------AQLELQIASLN---NEIERLearlerLEDRRER-LQQEIEELLKKLE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2346 EAQrlMARVQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRnQERLKEALQWKQELSQDN 2425
Cdd:TIGR02168 432 EAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-LDSLERLQENLEGFSEGV 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2426 ATLKATLQAASLILGHVSELLQ-----------------------GIDQAKEDLEHLAASLDGAWTPLLkrmqafspass 2482
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSELISvdegyeaaieaalggrlqavvveNLNAAKKAIAFLKQNELGRVTFLP----------- 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2483 kVDLVEAAEAHAQKLNQLAiNLSGiILGINQDrFIQRAVEASNAYSSILQAVQAAEDAAgQALRQASRT---WEMVVQ-- 2557
Cdd:TIGR02168 578 -LDSIKGTEIQGNDREILK-NIEG-FLGVAKD-LVKFDPKLRKALSYLLGGVLVVDDLD-NALELAKKLrpgYRIVTLdg 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2558 -----RGLAAGAR-----QLLANSSA---LEETILGHQGRLGLAQGRLQAAGIQLHNVWARKNQLAAQIQEAQAMLamdt 2624
Cdd:TIGR02168 653 dlvrpGGVITGGSaktnsSILERRREieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI---- 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2625 SETSEKIAHAKAVAAEALSTATHVQSQLQGMQKNVERWQSQLGGLQG---------QDLSQVERDASSSVSTLEKTLPQL 2695
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaeaeiEELEAQIEQLKEELKALREALDEL 808
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124487155 2696 LAKLSRLeNRGVHNASLA---LSANIGRVRKLIAQARSAASKVKVSMKFNGRSGVRLRTPRD 2754
Cdd:TIGR02168 809 RAELTLL-NEEAANLRERlesLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2025-2069 |
8.47e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 8.47e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 124487155 2025 CDCSPCGT--ETCDPQSGRCLCKAGVTGQRCDRCLEGYFGfEQCQGC 2069
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. |
638-685 |
9.29e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 9.29e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 638 CACDPRGALDQQC-GVGGLCHCRPGYTGATCQECSPGFYGFPSCIPCHC 685
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1533-1578 |
9.90e-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: 9.90e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124487155 1533 CNCSGPGVQeltDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYGYPS 1578
Cdd:cd00055 2 CDCNGHGSL---SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2024-2070 |
1.11e-11 |
|
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: 61.99 E-value: 1.11e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 124487155 2024 RCDCSPCGT--ETCDPQSGRCLCKAGVTGQRCDRCLEGYFGF-EQCQGCR 2070
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2071-2117 |
1.17e-11 |
|
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: 61.99 E-value: 1.17e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 124487155 2071 PCAC-GPAAKGSECHPQSGQCHCQPGTTGPQCLECAPGYWGLPEK--GCR 2117
Cdd:cd00055 1 PCDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
683-731 |
1.23e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.99 E-value: 1.23e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 683 CHCSADGSLHTTCDPTTGQCRCRPRVTGLHCDMCVPGAYNFPYCEAGSC 731
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1581-1631 |
1.26e-11 |
|
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: 61.99 E-value: 1.26e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124487155 1581 PCDCHEAGTMASVCDPLTGQCHCKENVQGSRCDQCRVGTFSlDAANPKGCT 1631
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1533-1577 |
2.18e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 2.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124487155 1533 CNCSGPGVQeltDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYGYP 1577
Cdd:smart00180 1 CDCDPGGSA---SGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1582-1630 |
2.23e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 2.23e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 1582 CDCHEAGTMASVCDPLTGQCHCKENVQGSRCDQCRVGTFsldAANPKGC 1630
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1443-1486 |
2.32e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 2.32e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124487155 1443 CGCHEVGAVSPTCEPFGGQCPCRGHVIGRDCSRCATGYWG--FPNC 1486
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| LamG |
smart00282 |
Laminin G domain; |
2969-3103 |
2.34e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.90 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2969 RFDQELRLVSYNGIIFFL--KQESQFLCLAVQEGTLVLFYDFGSGLKKadpLQPPQALTAASKAIQVFLLAgNRKRVLVR 3046
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPAR---LTSDPTPLNDGQWHRVAVER-NGRSVTLS 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3047 V---ERATVFSVDQDNMLEMADAYYLGGVPPEQLPLSLrqlfPSGGSVRGCIKGIKALGK 3103
Cdd:smart00282 77 VdggNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL----PVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
683-725 |
2.60e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.60e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124487155 683 CHCSADGSLHTTCDPTTGQCRCRPRVTGLHCDMCVPGAYNFPY 725
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2072-2116 |
3.49e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.49e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124487155 2072 CACGPA-AKGSECHPQSGQCHCQPGTTGPQCLECAPGYWGLPEKGC 2116
Cdd:smart00180 1 CDCDPGgSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
546-589 |
6.22e-11 |
|
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: 60.06 E-value: 6.22e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 124487155 546 PCQCSSPGVANSLCDPESGQCMCRTGFEGDRCDHCALGYFHFPL 589
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3157-3271 |
6.36e-11 |
|
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: 62.44 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3157 FRGTQDNNLLYYRTSPDGPY-QVSLREGHVTLRFM-----NQEVETQRVFADGAPHYVAF---YSNVTgvwLYVDDQlql 3227
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFlALELVNGRLVLRYDlgsgpESLLSSGKNLNDGQWHSVRVernGNTLT---LSVDGQ--- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 124487155 3228 vKSHERTTPMLQLQPEEPSRLLLGGLP------VSGTFHNFSGCISNVFV 3271
Cdd:pfam02210 75 -TVVSSLPPGESLLLNLNGPLYLGGLPpllllpALPVRAGFVGCIRDVRV 123
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2025-2069 |
6.69e-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: 59.67 E-value: 6.69e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 124487155 2025 CDCSPCGT--ETCDPQSGRCLCKAGVTGQRCDRCLEGYFGFEQCQGC 2069
Cdd:pfam00053 1 CDCNPHGSlsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2974-3099 |
1.34e-10 |
|
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: 61.67 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2974 LRLVSYNGIIFFLKQE-SQFLCLAVQEGTLVLFYDFGSGlkkadplqpPQALTAASKAiqvfLLAGNRKRVLVRVERATV 3052
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDLGSG---------PESLLSSGKN----LNDGQWHSVRVERNGNTL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 124487155 3053 -FSVDQDNMLEMA-----------DAYYLGGVPpeqlPLSLRQLFPSGGSVRGCIKGIK 3099
Cdd:pfam02210 68 tLSVDGQTVVSSLppgeslllnlnGPLYLGGLP----PLLLLPALPVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
500-547 |
1.68e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 1.68e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 124487155 500 CDCNAAGTQGNACrkDPRLGRCVCKPNFRGAHCELCAPGFHGPSCHPC 547
Cdd:smart00180 1 CDCDPGGSASGTC--DPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
593-634 |
1.75e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 1.75e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124487155 593 CGCSPAGTLPEGCD-EAGRCQCRPGFDGPHCDRCLPGYHGYPD 634
Cdd:cd00055 2 CDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2072-2119 |
2.43e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 2.43e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 2072 CACGP-AAKGSECHPQSGQCHCQPGTTGPQCLECAPGYWGLPEKGCRRC 2119
Cdd:pfam00053 1 CDCNPhGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2204-2738 |
3.00e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2204 WARLHRLNAS-IADLQSKLRSppgpRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQLldtteSTLGRAQKLLE 2282
Cdd:COG4717 62 QGRKPELNLKeLKELEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2283 SVRAVGRALNELASRMgqgspgdalvpsgEQLRWALAEVERLlwdmrtrdlgaqgavaeaelaeaQRLMARVQEQLTsfw 2362
Cdd:COG4717 133 ELEALEAELAELPERL-------------EELEERLEELREL-----------------------EEELEELEAELA--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2363 EENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEA------LQWKQELSQDNATLKATLQ--- 2433
Cdd:COG4717 174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELeeeleqLENELEAAALEERLKEARLlll 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2434 AASLILGHVSELLQGIDQAKEDLEHLAASLDGAWTPLLKRMQAFSPASSKVDLVEAAEAHaQKLNQLAINLSGIILGINQ 2513
Cdd:COG4717 254 IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL-EELEEEELEELLAALGLPP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2514 DRFIQRAVEASNAYSSILQAVQAAEDAAGQALRQAsrtwemvvqrgLAAGARQLLANSSALEETILghqgrlglaqgrlq 2593
Cdd:COG4717 333 DLSPEELLELLDRIEELQELLREAEELEEELQLEE-----------LEQEIAALLAEAGVEDEEEL-------------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2594 aagIQLHNVWARKNQLAAQIQEAQAMLAmdtSETSEKIAHAKAVAAEALSTA-THVQSQLQGMQKNVERWQSQLGGLQGQ 2672
Cdd:COG4717 388 ---RAALEQAEEYQELKEELEELEEQLE---ELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAE 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124487155 2673 dLSQVERDAssSVSTLEKTLPQLLAKLSRLENRgvhNASLALsanigrVRKLIAQARSAASKVKVS 2738
Cdd:COG4717 462 -LEQLEEDG--ELAELLQELEELKAELRELAEE---WAALKL------ALELLEEAREEYREERLP 515
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1971-2021 |
3.02e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 3.02e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124487155 1971 CDCSGNGDPNmifSDCDPLTGACRgCLRHTTGPHCERCAPGFYGNALLPGN 2021
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
500-549 |
3.80e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 3.80e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 124487155 500 CDCNAAGTQGNACrkDPRLGRCVCKPNFRGAHCELCAPGFHGPSCHPCQC 549
Cdd:cd00055 2 CDCNGHGSLSGQC--DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
593-633 |
5.95e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 124487155 593 CGCSPAGTLPEGCD-EAGRCQCRPGFDGPHCDRCLPGYHGYP 633
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2738-2905 |
7.43e-10 |
|
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: 60.12 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2738 SMKFNGRSGVRLRTPRDLADlaaYTALKFHIQSPVPapepgkntgDHFVLYMGSrQATGDYMGVSLRNQKVHWVYRLGKa 2817
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT---RLSISFSFRTTSP---------NGLLLYAGS-QNGGDFLALELEDGRLVLRYDLGS- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2818 GPTTLSIDENIGE-QFAAVSIDRTLQFGHMSVTVEKQMvheikgDTVAPGSEGLLNLHPDdfvFYVGGYPSNFTPPEPLR 2896
Cdd:cd00110 67 GSLVLSSKTPLNDgQWHSVSVERNGRSVTLSVDGERVV------ESGSPGGSALLNLDGP---LYLGGLPEDLKSPGLPV 137
|
....*....
gi 124487155 2897 FPGYLGCIE 2905
Cdd:cd00110 138 SPGFVGCIR 146
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
547-588 |
7.90e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 7.90e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 124487155 547 CQCSSPGVANSLCDPESGQCMCRTGFEGDRCDHCALGYFHFP 588
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
547-595 |
1.32e-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: 56.21 E-value: 1.32e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 547 CQCSSPGVANSLCDPESGQCMCRTGFEGDRCDHCALGYFHFPLCQLCGC 595
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
500-549 |
1.43e-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: 56.21 E-value: 1.43e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124487155 500 CDCNAAGTQGNACrkDPRLGRCVCKPNFRGAHCELCAPGFHG-PSCHPCQC 549
Cdd:pfam00053 1 CDCNPHGSLSDTC--DPETGQCLCKPGVTGRHCDRCKPGYYGlPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
637-679 |
2.08e-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: 2.08e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 124487155 637 ACACDPRGALDQQC-GVGGLCHCRPGYTGATCQECSPGFYGFPS 679
Cdd:cd00055 1 PCDCNGHGSLSGQCdPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
638-680 |
9.67e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 9.67e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124487155 638 CACDPRGALDQQC-GVGGLCHCRPGYTGATCQECSPGFYG--FPSC 680
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2787-2905 |
1.24e-08 |
|
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: 55.89 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2787 LYMGSRQatGDYMGVSLRNQKVHWVYRLGKAGPTTLSIDENI--GeQFAAVSIDRTLQfgHMSVTVEKQMVHEikgdTVA 2864
Cdd:pfam02210 11 LYAGGGG--SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLndG-QWHSVRVERNGN--TLTLSVDGQTVVS----SLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 124487155 2865 PGSEGLLNLHPDdfvFYVGGYPSNFTPPEPLRFPGYLGCIE 2905
Cdd:pfam02210 82 PGESLLLNLNGP---LYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1915-1968 |
1.97e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 124487155 1915 CPCPLAVPSNnfaDGCVLRNGrtQCLCRPGYAGASCERCAPGFFGNPLVLGSSC 1968
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2177-2585 |
2.00e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2177 LDDLERAGALLPAIREQLQGINASSAAWARLHRLNASIADLQSKLRSPPG---PRYQAAQQLQTLEQQSISLQQDTERLG 2253
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2254 SQAT-GVQGQAGQLLDTTESTLGRAQKLLESVRAVGRALNELASRMGQGSPGDALVPSGEQLRWA----LAEVERLLWDM 2328
Cdd:COG4717 184 EQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2329 RTRDLGAQGAVAEAELAEAQRLMA-------RVQEQLTSFWEENQSLATH-------IRDQLAQYESGLMDLREALNQAV 2394
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLAllflllaREKASLGKEAEELQALPALeeleeeeLEELLAALGLPPDLSPEELLELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2395 NTTREAEELNSRnQERLKEALQWkQELSQDNATLKATLQAASL-ILGHVSELLQGIDQAKEDLEHLAASLDGAWTPLLKR 2473
Cdd:COG4717 344 DRIEELQELLRE-AEELEEELQL-EELEQEIAALLAEAGVEDEeELRAALEQAEEYQELKEELEELEEQLEELLGELEEL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2474 MQAFSPASSKV---DLVEAAEAHAQKLNQLAINLSGIILGINQdrfiqraVEASNAYSSILQAVQAAEDAAGQALRQASR 2550
Cdd:COG4717 422 LEALDEEELEEeleELEEELEELEEELEELREELAELEAELEQ-------LEEDGELAELLQELEELKAELRELAEEWAA 494
|
410 420 430
....*....|....*....|....*....|....*
gi 124487155 2551 twemvvqrglAAGARQLLANssALEETILGHQGRL 2585
Cdd:COG4717 495 ----------LKLALELLEE--AREEYREERLPPV 517
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1864-1900 |
5.17e-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: 5.17e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 124487155 1864 PCQCHGH---SDRCLPGSGICVgCQHNTEGDQCERCRPGF 1900
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1971-2015 |
1.07e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 1.07e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124487155 1971 CDCSGNGdpnMIFSDCDPLTGACRgCLRHTTGPHCERCAPGFYGN 2015
Cdd:smart00180 1 CDCDPGG---SASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1915-1961 |
1.15e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.15e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 124487155 1915 CPCPlavPSNNFADGCVLRNGrtQCLCRPGYAGASCERCAPGFFGNP 1961
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1865-1912 |
1.86e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.04 E-value: 1.86e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124487155 1865 CQCHGH---SDRCLPGSGICVgCQHNTEGDQCERCRPGFVsSDPSNPASPC 1912
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYY-GLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
304-352 |
4.17e-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: 49.27 E-value: 4.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 304 RCVCHGHADV---CDakdpldPFRLQCACQHNTCGGSCDRCCPGFNQQPWKP 352
Cdd:cd00055 1 PCDCNGHGSLsgqCD------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
781-832 |
7.50e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.50 E-value: 7.50e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 124487155 781 RCSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFGLDYAdYFGCR 832
Cdd:cd00055 1 PCDCNGHGSLSG--QCdPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1914-1969 |
8.36e-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: 8.36e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 124487155 1914 SCPCPLAVPSNNfadGCVLRNGrtQCLCRPGYAGASCERCAPGFFGNPLVlGSSCQ 1969
Cdd:cd00055 1 PCDCNGHGSLSG---QCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
833-872 |
9.77e-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: 9.77e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 124487155 833 SCRCDVGGALGQGCEPKTGACRCRPNTQGPTCSEPAKDHY 872
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
2364-2623 |
1.22e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 54.31 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2364 ENQSL---ATHIR--DQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEA--LQWK-QELsqDNATLKA----T 2431
Cdd:COG0497 133 EHQSLldpDAQREllDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELdlLRFQlEEL--EAAALQPgeeeE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2432 LQAASLILGHVSELLQGIDQAkedLEHLAASLDGAwTPLLKR-MQAFSPASskvDLVEAAEAHAQKLNQLAINLSGIIlg 2510
Cdd:COG0497 211 LEEERRRLSNAEKLREALQEA---LEALSGGEGGA-LDLLGQaLRALERLA---EYDPSLAELAERLESALIELEEAA-- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2511 inqdRFIQRAVEASNAYSSILQAVQAAEDAAGQALRQASRTWEMVVQrgLAAGARQLLANSSALEETILGHQGRLGLAQG 2590
Cdd:COG0497 282 ----SELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVEELLA--YAEELRAELAELENSDERLEELEAELAEAEA 355
|
250 260 270
....*....|....*....|....*....|....*.
gi 124487155 2591 RLQAAGIQLHNvwARKN---QLAAQIQEAQAMLAMD 2623
Cdd:COG0497 356 ELLEAAEKLSA--ARKKaakKLEKAVTAELADLGMP 389
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2173-2463 |
2.20e-06 |
|
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: 53.91 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2173 VVLLLDDLERAGALLPAIREQLQGINASSAAWA-RLHRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTER 2251
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2252 LGSQatgvqgqagqlLDTTESTLGRAQKLLESVRavgRALNELASRMgqgspgdalvpsgEQLRWALAEVERLLWDM--R 2329
Cdd:TIGR02168 794 LKEE-----------LKALREALDELRAELTLLN---EEAANLRERL-------------ESLERRIAATERRLEDLeeQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2330 TRDLGAQGAVAEAELAEAQRLMARVQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSR-NQ 2408
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKlAQ 926
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124487155 2409 ERLKealqwKQELSQDNATLKATLQA-ASLILGHVSELLQGIDQAKEDLEHLAASL 2463
Cdd:TIGR02168 927 LELR-----LEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
782-831 |
4.03e-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: 4.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124487155 782 CSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFGLDYADYFGC 831
Cdd:pfam00053 1 CDCNPHGSLSD--TCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
433-474 |
4.05e-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: 46.19 E-value: 4.05e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124487155 433 PCDCESDFT-DGTCEDLTGRCYCRPNFTGELCAACAEGYTDFP 474
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
834-872 |
4.42e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 4.42e-06
10 20 30
....*....|....*....|....*....|....*....
gi 124487155 834 CRCDVGGALGQGCEPKTGACRCRPNTQGPTCSEPAKDHY 872
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
782-825 |
5.33e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 5.33e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124487155 782 CSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFGLDY 825
Cdd:smart00180 1 CDCDPGGSASG--TCdPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2313-2681 |
8.48e-06 |
|
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: 51.98 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2313 QLRWALAEVERLLWDMRTRDLGAQgavaeaelaeaqrlMARVQEQLtsfwEENQSLATHIRDQLAQYESGLMDLREALNQ 2392
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREE--------------LEELQEEL----KEAEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2393 AvntTREAEELnsrnQERLKEALQWKQELSQDNATLKATLQAASLILGHVSELLQGIDQAKEDLEHLAASLDGAWTPLLK 2472
Cdd:TIGR02168 279 L---EEEIEEL----QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2473 RMQAFSPA-SSKVDLVEAAEAHAQKLNQLAINLSGIILGINQDrfiqravEASNAySSILQAVQAAEDAAGQALRQASRT 2551
Cdd:TIGR02168 352 ELESLEAElEELEAELEELESRLEELEEQLETLRSKVAQLELQ-------IASLN-NEIERLEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2552 wEMVVQRGLAAGARQLLANSSALEETILGHQGRLGLAQGRLQAAGIQLHNVWARKNQLAAQIQEAQAMLAMDTSetseki 2631
Cdd:TIGR02168 424 -EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER------ 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 124487155 2632 ahakavaaealstathVQSQLQGMQ---KNVERWQSQLGGLQGQDLSQVERDA 2681
Cdd:TIGR02168 497 ----------------LQENLEGFSegvKALLKNQSGLSGILGVLSELISVDE 533
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2176-2722 |
1.10e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2176 LLDDL----------ERAG-------ALLPAIREQLQGINASSAA------WARLHRLNASIADLQSKLRSPPGPRYQAA 2232
Cdd:PRK02224 154 MIDDLlqlgkleeyrERASdarlgveRVLSDQRGSLDQLKAQIEEkeekdlHERLNGLESELAELDEEIERYEEQREQAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2233 QQLQTLE---------QQSI-SLQQDTERLGSQATGVQgqagqllDTTESTLGRAQKLLESVRAVGRALNELASRMGQGS 2302
Cdd:PRK02224 234 ETRDEADevleeheerREELeTLEAEIEDLRETIAETE-------REREELAEEVRDLRERLEELEEERDDLLAEAGLDD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2303 PGD-ALVPSGEQLRWALAEVERLLWDMRTrDLGAQGAVAEAELAEAQRLMARVQE------QLTSFWEENQSLATHIRDQ 2375
Cdd:PRK02224 307 ADAeAVEARREELEDRDEELRDRLEECRV-AAQAHNEEAESLREDADDLEERAEElreeaaELESELEEAREAVEDRREE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2376 LAQYESGLMDLREALNqavNTTREAEELNSRNQERLKEalqwKQELSQDNATLKATLQAASLILGHVSELLQ-------- 2447
Cdd:PRK02224 386 IEELEEEIEELRERFG---DAPVDLGNAEDFLEELREE----RDELREREAELEATLRTARERVEEAEALLEagkcpecg 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2448 ----------GIDQAKEDLEHLAASLDGAWTPLLKRMQAFSPASskvDLVEaAEAHAQKLNQLAINLSGII----LGINQ 2513
Cdd:PRK02224 459 qpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAE---DLVE-AEDRIERLEERREDLEELIaerrETIEE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2514 DRfiqRAVEASNAYSSILQA-VQAAEDAAGQALRQASRTWEMVV----QRGLAAGARQLLANSSALEETILGHQGRLG-L 2587
Cdd:PRK02224 535 KR---ERAEELRERAAELEAeAEEKREAAAEAEEEAEEAREEVAelnsKLAELKERIESLERIRTLLAAIADAEDEIErL 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2588 AQGRLQAAGI------QLHNVWARKNQLAAQIQEAQAMLAMDTSETSEKIAHakavaaealstatHVQSQLQGMQKNVER 2661
Cdd:PRK02224 612 REKREALAELnderreRLAEKRERKRELEAEFDEARIEEAREDKERAEEYLE-------------QVEEKLDELREERDD 678
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124487155 2662 WQSQLGGLQGQdLSQVErdasssvsTLEKTLPQLLAKLSRLENrgVHNASLALSANIGRVR 2722
Cdd:PRK02224 679 LQAEIGAVENE-LEELE--------ELRERREALENRVEALEA--LYDEAEELESMYGDLR 728
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1865-1900 |
1.26e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.61 E-value: 1.26e-05
10 20 30
....*....|....*....|....*....|....*....
gi 124487155 1865 CQCHG---HSDRCLPGSGICVgCQHNTEGDQCERCRPGF 1900
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
434-476 |
1.76e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 1.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124487155 434 CDCESDFT-DGTCEDLTGRCYCRPNFTGELCAACAEGY--TDFPHC 476
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
363-426 |
2.01e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 44.27 E-value: 2.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487155 363 SCNCHGHAydcyydpevdrrnasQNQDNVYQGGGVCLdCQHHTTGINCERCLPGFFRAPDQPLD 426
Cdd:cd00055 1 PCDCNGHG---------------SLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
834-872 |
5.03e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.11 E-value: 5.03e-05
10 20 30
....*....|....*....|....*....|....*....
gi 124487155 834 CRCDVGGALGQGCEPKTGACRCRPNTQGPTCSEPAKDHY 872
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
434-478 |
9.62e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 42.34 E-value: 9.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124487155 434 CDC-ESDFTDGTCEDLTGRCYCRPNFTGELCAACAEGYTDFPHCYP 478
Cdd:pfam00053 1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2119-2147 |
2.05e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.57 E-value: 2.05e-04
10 20 30
....*....|....*....|....*....|....
gi 124487155 2119 CQCP-----RGHCDPHTGHCTCPPGLSGERCDTC 2147
Cdd:pfam00053 1 CDCNphgslSDTCDPETGQCLCKPGVTGRHCDRC 34
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2119-2169 |
2.08e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 2.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 124487155 2119 CQC-PRGH----CDPHTGHCTCPPGLSGERCDTCsqqhqvpvpgKPGGHGIHCEVC 2169
Cdd:smart00180 1 CDCdPGGSasgtCDPDTGQCECKPNVTGRRCDRC----------APGYYGDGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
364-431 |
4.42e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 40.41 E-value: 4.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124487155 364 CNCHGHAydcyydpevdrrnasQNQDNVYQGGGVCLdCQHHTTGINCERCLPGFFRapdQPLDSPHVC 431
Cdd:pfam00053 1 CDCNPHG---------------SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYG---LPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2118-2147 |
5.19e-04 |
|
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: 40.42 E-value: 5.19e-04
10 20 30
....*....|....*....|....*....|....*
gi 124487155 2118 RCQCP-----RGHCDPHTGHCTCPPGLSGERCDTC 2147
Cdd:cd00055 1 PCDCNghgslSGQCDPGTGQCECKPNTTGRRCDRC 35
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2177-2569 |
5.37e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2177 LDDLERAGALL----PAIREQLQGINASSAAWARLHRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTERL 2252
Cdd:PRK04863 316 LAELNEAESDLeqdyQAASDHLNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDEL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2253 GSQATGVQ-------------GQAGQLLDTTES-------TLGRAQKLLESVRA----VGRALNELASRM---------- 2298
Cdd:PRK04863 396 KSQLADYQqaldvqqtraiqyQQAVQALERAKQlcglpdlTADNAEDWLEEFQAkeqeATEELLSLEQKLsvaqaahsqf 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2299 -----------GQGSPGDA----------------LVPSGEQLRWALAEVERLLWDMRTrdlgaqgavaeaelaeAQRLM 2351
Cdd:PRK04863 476 eqayqlvrkiaGEVSRSEAwdvarellrrlreqrhLAEQLQQLRMRLSELEQRLRQQQR----------------AERLL 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2352 ARVQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEALQWKQ------ELS-QD 2424
Cdd:PRK04863 540 AEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAaqdalaRLReQS 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2425 NATLKATLQAASLILGHVsELLQGIDQAKEDLEHLAASLDGAWTPLLKRMQAFSPasskvdlveaaeahaqKLNQLAINL 2504
Cdd:PRK04863 620 GEEFEDSQDVTEYMQQLL-ERERELTVERDELAARKQALDEEIERLSQPGGSEDP----------------RLNALAERF 682
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124487155 2505 SGIILG-INQDRFIQRAVEASNAYssilqavqaaedaaGQAlRQAsrtwemVVQRGLAAGARQLLA 2569
Cdd:PRK04863 683 GGVLLSeIYDDVSLEDAPYFSALY--------------GPA-RHA------IVVPDLSDAAEQLAG 727
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
392-421 |
6.76e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.99 E-value: 6.76e-04
10 20 30
....*....|....*....|....*....|
gi 124487155 392 YQGGGVCLdCQHHTTGINCERCLPGFFRAP 421
Cdd:smart00180 14 DPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
305-350 |
8.23e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 8.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 305 CVCH--GHAD-VCDakdpldPFRLQCACQHNTCGGSCDRCCPGFNQQPW 350
Cdd:smart00180 1 CDCDpgGSASgTCD------PDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
305-361 |
2.11e-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: 38.49 E-value: 2.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 124487155 305 CVCHGHADVcdaKDPLDPFRLQCACQHNTCGGSCDRCCPGFNQQPwkpatTDSANEC 361
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-----SDPPQGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2572-2737 |
6.76e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2572 SALEETILGHQGRLGLAQGRLQAAGIQLHNVWARKNQLAAQIQEAQAMLamdtSETSEKIAHAKAVAAEALSTATHVQSQ 2651
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSEL----EQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2652 LQGMQKNVERWQSQLGGLQGQ--DLSQVERDASSSVSTLEKTLPQLLAKLSRLENR-----------GVHNASLALSANI 2718
Cdd:COG4372 103 LESLQEEAEELQEELEELQKErqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQleslqeelaalEQELQALSEAEAE 182
|
170
....*....|....*....
gi 124487155 2719 GRVRKLIAQARSAASKVKV 2737
Cdd:COG4372 183 QALDELLKEANRNAEKEEE 201
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
1874-1981 |
8.60e-03 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 39.69 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 1874 CLPGSGICVGCQHNTEgDQCERCRPGFVSSDPS-NPASPCVSCpcplavpsNNFADGCVLRN----GRTQCLCRPGY--- 1945
Cdd:cd13406 18 CPPGEGMESRCTGTQD-TVCSPCEPGFYNEAVNyEPCKPCTQC--------NQRSGSEEKQKctktSDTVCRCRPGTqpl 88
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 124487155 1946 ----AGASCERCAPGFFGNPlvLGSSCQP-CDCSGNGDPNM 1981
Cdd:cd13406 89 dsykPGVDCVPCPPGHFSRG--DNQACKPwTNCSLAGKRTL 127
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
50-303 |
7.19e-99 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 318.37 E-value: 7.19e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 50 LHPPYFNLAEGARITASATCGEEAPTRsvsrptedlYCKLVGGPvaggdpnqtiQGQYCDICTAANSNKAHPVSNAIDGT 129
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLNGPER---------YCILSGLE----------GGKKCFICDSRDPHNSHPPSNLTDSN 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 130 ER----WWQSPPLSrgLEYNEVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERSTDFGHTYQPWQFFASskrDCLERFG 205
Cdd:pfam00055 62 NGtnetWWQSETGV--IQYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFG 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 206 -PRTLERITQDDDVICTTEYSRIVPLENGEIVVSLVNGRPGALNFSYSPLLRDFTKATNIRLRFLRTNTLLGHLmgkaLR 284
Cdd:pfam00055 136 rPSGPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LD 211
|
250
....*....|....*....
gi 124487155 285 DPTVTRRYYYSIKDISIGG 303
Cdd:pfam00055 212 DPSVLRKYYYAISDISVGG 230
|
|
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
49-303 |
6.46e-97 |
|
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: 313.14 E-value: 6.46e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 49 SLHPPYFNLAEGARITASATCGEEAPTRsvsrptedlYCKLVGGpvaggdpnqTIQGQYCDICTAANSNKAHPVSNAIDG 128
Cdd:smart00136 6 SCYPPFVNLAFGREVTATSTCGEPGPER---------YCKLVGH---------TEQGKKCDYCDARNPRRSHPAENLTDG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 129 TE----RWWQSPPLSRGLEYneVNVTLDLGQVFHVAYVLIKFAnSPRPDLWVLERStDFGHTYQPWQFFASskrDCLERF 204
Cdd:smart00136 68 NNpnnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 205 G--PRTLERITQDDDVICTTEYSRIVPLENGEIVVSLVNGRPGALNFSYSPLLRDFTKATNIRLRFLRTNTLLGHLMGKA 282
Cdd:smart00136 141 GrpPRGPITKGNEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR 220
|
250 260
....*....|....*....|.
gi 124487155 283 lrdPTVTRRYYYSIKDISIGG 303
Cdd:smart00136 221 ---PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
2194-2452 |
4.71e-65 |
|
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: 222.67 E-value: 4.71e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2194 LQGINASSAAWARLHRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQLLDTTEST 2273
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2274 LGRAQKLLESVRAVGRALNELASRMGQGSPGDALVPSGEQLRwALAEVERLLWDMRTRDLGAQGAVAEAELAEAQRLMAR 2353
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSR-MLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2354 VQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEALQWKQELSQDNATLKATLQ 2433
Cdd:pfam06008 160 IQTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLK 239
|
250
....*....|....*....
gi 124487155 2434 AASLILGHVSELLQGIDQA 2452
Cdd:pfam06008 240 TARDSLDAANLLLQEIDDA 258
|
|
| LamB |
smart00281 |
Laminin B domain; |
1690-1819 |
1.58e-48 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 170.13 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 1690 FSELYWQAPPSYLGDRVSSYGGTLHYELHSETQRGDifiPYESRPDVVLQGNQMSIAFLELAYPPPGQVHRGQLQLVEGN 1769
Cdd:smart00281 2 NEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG---THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 124487155 1770 FRHLEtHNPVSREELMMVLAGLEQLQIRALFSQTSSSVSLRRVVLEVASE 1819
Cdd:smart00281 79 WQYYG-GRPVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1694-1830 |
2.16e-48 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 170.14 E-value: 2.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 1694 YWQAPPSYLGDRVSSYGGTLHYELHSETQRGDIfiPYESRPDVVLQGNQMSIAFL--ELAYPPPGQVHRGQLQLVEGNFR 1771
Cdd:pfam00052 1 YWSAPEQFLGNKLTSYGGYLTYTVRYEPLPGGG--SLNSEPDVILEGNGLRLSYSspDQPPPDPGQEQTYSVRLHEENWR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 124487155 1772 HlETHNPVSREELMMVLAGLEQLQIRALFSQTSSSVSLRRVVLEVASEAGRGPPASNVE 1830
Cdd:pfam00052 79 D-SDGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2642-2764 |
7.93e-45 |
|
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: 159.96 E-value: 7.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2642 LSTATHVQSQLQGMQKNVERWQSQLGGLQGQ---------DLSQVERDASSSVSTLEKTLPQLLAKLSRLENRGVHNASL 2712
Cdd:pfam06009 9 NETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQLEVNSSSL 88
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 2713 alSANIGRVRKLIAQARSAASKVKVSMKFNGRSGVRLRTPRDLADLAAYTAL 2764
Cdd:pfam06009 89 --SDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
smart00282 |
Laminin G domain; |
3542-3669 |
5.93e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 105.50 E-value: 5.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3542 SLELEMRPLAAAGLIFHLGQALATPYMQLKVLTEQVLLQANDGAGEFSTWVTYPKLCDGRWHRVAVIMGRDTLRLEVDtQ 3621
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVD-G 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 3622 SNHTTGRLPESLAG--SPALLHLGSLPKSSTARPEL--PAYRGCLRKLLING 3669
Cdd:smart00282 80 GNRVSGESPGGLTIlnLDGPLYLGGLPEDLKLPPLPvtPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3519-3668 |
1.56e-25 |
|
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: 105.19 E-value: 1.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3519 GLFFPGSeGVVTLELPKAKMPYVSLELEMRPLAAAGLIFHLGQALATPYMQLKVLTEQVLLQANDGAGefSTWVTYP-KL 3597
Cdd:cd00110 1 GVSFSGS-SYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGDFLALELEDGRLVLRYDLGSG--SLVLSSKtPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487155 3598 CDGRWHRVAVIMGRDTLRLEVD-TQSNHTTGRLPESLAGSPALLHLGSLPKSSTARPEL--PAYRGCLRKLLIN 3668
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDgERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPvsPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3337-3495 |
1.70e-24 |
|
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: 102.11 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3337 AYQFGGPlpSYLQFVGiSPSHRNRLHLSMLVRPHAASqGLLLSTAPmSGRSPSLVLFLNHGHFVAQTEGPGPRLQVQSRQ 3416
Cdd:cd00110 1 GVSFSGS--SYVRLPT-LPAPRTRLSISFSFRTTSPN-GLLLYAGS-QNGGDFLALELEDGRLVLRYDLGSGSLVLSSKT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3417 HSRAGQWHRVSVRWGMQQIQLVVDGSQTwsqkaLHHRVPR--AERPQPYTLSVGGLPASSYSSKLPVSVGFSGCLKKLQL 3494
Cdd:cd00110 76 PLNDGQWHSVSVERNGRSVTLSVDGERV-----VESGSPGgsALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKV 150
|
.
gi 124487155 3495 D 3495
Cdd:cd00110 151 N 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3547-3669 |
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: 92.48 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3547 MRPLAAAGLIFHLGQALaTPYMQLKVLTEQVLLQANDGAGEFSTWVTYPKLCDGRWHRVAVIMGRDTLRLEVDTQSNHTT 3626
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGG-SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 124487155 3627 GRLPESLA-GSPALLHLGSLPK--SSTARPELPAYRGCLRKLLING 3669
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPllLLPALPVRAGFVGCIRDVRVNG 125
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3372-3497 |
2.34e-20 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 89.40 E-value: 2.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3372 ASQGLLLSTApmSGRSPSLVLFLNHGHFVAQTE-GPGPRLQVQSRQHSRAGQWHRVSVRWGMQQIQLVVDGSQTWSQKAL 3450
Cdd:pfam02210 5 QPNGLLLYAG--GGGSDFLALELVNGRLVLRYDlGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 124487155 3451 HHRVPraeRPQPYTLSVGGLPASSYSSKLPVSVGFSGCLKKLQLDKR 3497
Cdd:pfam02210 83 GESLL---LNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
3362-3497 |
3.60e-19 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 86.24 E-value: 3.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3362 HLSMLVRPHAASqGLLLSTAPmSGRSPSLVLFLNHGHFVAQTEGPGPRLQVQS-RQHSRAGQWHRVSVRWGMQQIQLVVD 3440
Cdd:smart00282 1 SISFSFRTTSPN-GLLLYAGS-KGGGDYLALELRDGRLVLRYDLGSGPARLTSdPTPLNDGQWHRVAVERNGRSVTLSVD 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 124487155 3441 GSQTWSQKALHHRvPRAERPQPytLSVGGLPASSYSSKLPVSVGFSGCLKKLQLDKR 3497
Cdd:smart00282 79 GGNRVSGESPGGL-TILNLDGP--LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
smart00282 |
Laminin G domain; |
3155-3273 |
4.45e-17 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 80.46 E-value: 4.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3155 FGFRGTQDNNLLYYRTSPDGP--YQVSLREGHVTLRFMN-----QEVETQRVFADGAPHYVAFYSNVTGVWLYVDDQLQL 3227
Cdd:smart00282 4 FSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLgsgpaRLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGGNRV 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 3228 VKSHERTTPMLQLqpeePSRLLLGGLP------VSGTFHNFSGCISNVFVQR 3273
Cdd:smart00282 84 SGESPGGLTILNL----DGPLYLGGLPedlklpPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3128-3271 |
7.31e-15 |
|
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: 74.76 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3128 TMTFHGHGFLPLALPDVAPITEVVysGFGFRGTQDNN-LLYYRTSPDGPY-QVSLREGHVTLRFMNQE----VETQRVFA 3201
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSI--SFSFRTTSPNGlLLYAGSQNGGDFlALELEDGRLVLRYDLGSgslvLSSKTPLN 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124487155 3202 DGAPHYVAFYSNVTGVWLYVDDQLQLvkshERTTPMLQLQPEEPSRLLLGGLPVSGTF------HNFSGCISNVFV 3271
Cdd:cd00110 79 DGQWHSVSVERNGRSVTLSVDGERVV----ESGSPGGSALLNLDGPLYLGGLPEDLKSpglpvsPGFVGCIRDLKV 150
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1443-1491 |
6.84e-14 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 68.15 E-value: 6.84e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 1443 CGCHEVGAVSPTCEPFGGQCPCRGHVIGRDCSRCATGYWGFPNCRPCDC 1491
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1582-1630 |
3.49e-13 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 66.22 E-value: 3.49e-13
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 1582 CDCHEAGTMASVCDPLTGQCHCKENVQGSRCDQCRVGTFSLDAANPKGC 1630
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2783-2912 |
4.42e-13 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 68.91 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2783 DHFVLYMGSRQaTGDYMGVSLRNQKVHWVYRLGkAGPTTLSIDE---NIGeQFAAVSIDRTLQFGHMSVTVEKQMVheik 2859
Cdd:smart00282 12 NGLLLYAGSKG-GGDYLALELRDGRLVLRYDLG-SGPARLTSDPtplNDG-QWHRVAVERNGRSVTLSVDGGNRVS---- 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 124487155 2860 gdTVAPGSEGLLNLHPDdfvFYVGGYPSNFTPPEPLRFPGYLGCIEMETLNEE 2912
Cdd:smart00282 85 --GESPGGLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
682-724 |
6.81e-13 |
|
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: 65.45 E-value: 6.81e-13
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124487155 682 PCHCSADGSLHTTCDPTTGQCRCRPRVTGLHCDMCVPGAYNFP 724
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
593-640 |
1.06e-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: 65.07 E-value: 1.06e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 593 CGCSPAGTLPEGCD-EAGRCQCRPGFDGPHCDRCLPGYHGYPDCHACAC 640
Cdd:pfam00053 1 CDCNPHGSLSDTCDpETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1533-1584 |
1.63e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 64.30 E-value: 1.63e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 1533 CNCSGPGVqelTDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYGYPSCRPCDC 1584
Cdd:pfam00053 1 CDCNPHGS---LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2947-3099 |
2.37e-12 |
|
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: 67.44 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2947 GSYLDGSGFARISFEKQFSNTKRFDQELRLVSYNGIIFFL--KQESQFLCLAVQEGTLVLFYDFGSGLKKadpLQPPQAL 3024
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLV---LSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487155 3025 tAASKAIQVFLLAGNRKRVLV--RVERATVFSVDQDNMLEMADAYYLGGVPPEQLPLSLrqlfPSGGSVRGCIKGIK 3099
Cdd:cd00110 78 -NDGQWHSVSVERNGRSVTLSvdGERVVESGSPGGSALLNLDGPLYLGGLPEDLKSPGL----PVSPGFVGCIRDLK 149
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1970-2023 |
2.43e-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: 63.91 E-value: 2.43e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 124487155 1970 PCDCSGNGDPNmifSDCDPLTGACRgCLRHTTGPHCERCAPGFYGNALLPGNCT 2023
Cdd:cd00055 1 PCDCNGHGSLS---GQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1442-1484 |
4.19e-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: 63.14 E-value: 4.19e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124487155 1442 PCGCHEVGAVSPTCEPFGGQCPCRGHVIGRDCSRCATGYWGFP 1484
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2192-2754 |
7.21e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 72.01 E-value: 7.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2192 EQLQGINASSAAwaRLHRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQLLDTTE 2271
Cdd:TIGR02168 284 EELQKELYALAN--EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2272 STLGRAQKLLESVRAVGRALNELASRMgqgspgDALVPSGEQLRwalAEVERL------LWDMRTRdLGAQGAVAEAELA 2345
Cdd:TIGR02168 362 ELEAELEELESRLEELEEQLETLRSKV------AQLELQIASLN---NEIERLearlerLEDRRER-LQQEIEELLKKLE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2346 EAQrlMARVQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRnQERLKEALQWKQELSQDN 2425
Cdd:TIGR02168 432 EAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR-LDSLERLQENLEGFSEGV 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2426 ATLKATLQAASLILGHVSELLQ-----------------------GIDQAKEDLEHLAASLDGAWTPLLkrmqafspass 2482
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSELISvdegyeaaieaalggrlqavvveNLNAAKKAIAFLKQNELGRVTFLP----------- 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2483 kVDLVEAAEAHAQKLNQLAiNLSGiILGINQDrFIQRAVEASNAYSSILQAVQAAEDAAgQALRQASRT---WEMVVQ-- 2557
Cdd:TIGR02168 578 -LDSIKGTEIQGNDREILK-NIEG-FLGVAKD-LVKFDPKLRKALSYLLGGVLVVDDLD-NALELAKKLrpgYRIVTLdg 652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2558 -----RGLAAGAR-----QLLANSSA---LEETILGHQGRLGLAQGRLQAAGIQLHNVWARKNQLAAQIQEAQAMLamdt 2624
Cdd:TIGR02168 653 dlvrpGGVITGGSaktnsSILERRREieeLEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQI---- 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2625 SETSEKIAHAKAVAAEALSTATHVQSQLQGMQKNVERWQSQLGGLQG---------QDLSQVERDASSSVSTLEKTLPQL 2695
Cdd:TIGR02168 729 SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaeaeaeiEELEAQIEQLKEELKALREALDEL 808
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 124487155 2696 LAKLSRLeNRGVHNASLA---LSANIGRVRKLIAQARSAASKVKVSMKFNGRSGVRLRTPRD 2754
Cdd:TIGR02168 809 RAELTLL-NEEAANLRERlesLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE 869
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2025-2069 |
8.47e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 62.33 E-value: 8.47e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 124487155 2025 CDCSPCGT--ETCDPQSGRCLCKAGVTGQRCDRCLEGYFGfEQCQGC 2069
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. |
638-685 |
9.29e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.37 E-value: 9.29e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 638 CACDPRGALDQQC-GVGGLCHCRPGYTGATCQECSPGFYGFPSCIPCHC 685
Cdd:pfam00053 1 CDCNPHGSLSDTCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1533-1578 |
9.90e-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: 9.90e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124487155 1533 CNCSGPGVQeltDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYGYPS 1578
Cdd:cd00055 2 CDCNGHGSL---SGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2024-2070 |
1.11e-11 |
|
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: 61.99 E-value: 1.11e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 124487155 2024 RCDCSPCGT--ETCDPQSGRCLCKAGVTGQRCDRCLEGYFGF-EQCQGCR 2070
Cdd:cd00055 1 PCDCNGHGSlsGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLpSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2071-2117 |
1.17e-11 |
|
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: 61.99 E-value: 1.17e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 124487155 2071 PCAC-GPAAKGSECHPQSGQCHCQPGTTGPQCLECAPGYWGLPEK--GCR 2117
Cdd:cd00055 1 PCDCnGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQggGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
683-731 |
1.23e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.99 E-value: 1.23e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 683 CHCSADGSLHTTCDPTTGQCRCRPRVTGLHCDMCVPGAYNFPYCEAGSC 731
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1581-1631 |
1.26e-11 |
|
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: 61.99 E-value: 1.26e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124487155 1581 PCDCHEAGTMASVCDPLTGQCHCKENVQGSRCDQCRVGTFSlDAANPKGCT 1631
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYG-LPSQGGGCQ 50
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1533-1577 |
2.18e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 2.18e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124487155 1533 CNCSGPGVQeltDPTCDMDSGQCRCRPNVAGRRCDTCAPGFYGYP 1577
Cdd:smart00180 1 CDCDPGGSA---SGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1582-1630 |
2.23e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 2.23e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 1582 CDCHEAGTMASVCDPLTGQCHCKENVQGSRCDQCRVGTFsldAANPKGC 1630
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1443-1486 |
2.32e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.17 E-value: 2.32e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124487155 1443 CGCHEVGAVSPTCEPFGGQCPCRGHVIGRDCSRCATGYWG--FPNC 1486
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| LamG |
smart00282 |
Laminin G domain; |
2969-3103 |
2.34e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 63.90 E-value: 2.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2969 RFDQELRLVSYNGIIFFL--KQESQFLCLAVQEGTLVLFYDFGSGLKKadpLQPPQALTAASKAIQVFLLAgNRKRVLVR 3046
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPAR---LTSDPTPLNDGQWHRVAVER-NGRSVTLS 76
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3047 V---ERATVFSVDQDNMLEMADAYYLGGVPPEQLPLSLrqlfPSGGSVRGCIKGIKALGK 3103
Cdd:smart00282 77 VdggNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPL----PVTPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
683-725 |
2.60e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 2.60e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124487155 683 CHCSADGSLHTTCDPTTGQCRCRPRVTGLHCDMCVPGAYNFPY 725
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2072-2116 |
3.49e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.40 E-value: 3.49e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124487155 2072 CACGPA-AKGSECHPQSGQCHCQPGTTGPQCLECAPGYWGLPEKGC 2116
Cdd:smart00180 1 CDCDPGgSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3554-3673 |
4.83e-11 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 63.10 E-value: 4.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3554 GLIFHLGQALATPYMQLKVLTEQVLLQANDGAGEFSTwVTYPKLCDGRWHRVAVIMGRDTLRLEVDTQSNHTTgrlpESL 3633
Cdd:pfam00054 8 GLLLYNGTQTERDFLALELRDGRLEVSYDLGSGAAVV-RSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTG----ESP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 124487155 3634 AGS------PALLHLGSLPKSSTARPEL---PAYRGCLRKLLINGAPVN 3673
Cdd:pfam00054 83 LGAttdldvDGPLYVGGLPSLGVKKRRLaisPSFDGCIRDVIVNGKPLD 131
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
546-589 |
6.22e-11 |
|
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: 60.06 E-value: 6.22e-11
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 124487155 546 PCQCSSPGVANSLCDPESGQCMCRTGFEGDRCDHCALGYFHFPL 589
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3157-3271 |
6.36e-11 |
|
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: 62.44 E-value: 6.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3157 FRGTQDNNLLYYRTSPDGPY-QVSLREGHVTLRFM-----NQEVETQRVFADGAPHYVAF---YSNVTgvwLYVDDQlql 3227
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFlALELVNGRLVLRYDlgsgpESLLSSGKNLNDGQWHSVRVernGNTLT---LSVDGQ--- 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 124487155 3228 vKSHERTTPMLQLQPEEPSRLLLGGLP------VSGTFHNFSGCISNVFV 3271
Cdd:pfam02210 75 -TVVSSLPPGESLLLNLNGPLYLGGLPpllllpALPVRAGFVGCIRDVRV 123
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2025-2069 |
6.69e-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: 59.67 E-value: 6.69e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 124487155 2025 CDCSPCGT--ETCDPQSGRCLCKAGVTGQRCDRCLEGYFGFEQCQGC 2069
Cdd:pfam00053 1 CDCNPHGSlsDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2974-3099 |
1.34e-10 |
|
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: 61.67 E-value: 1.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2974 LRLVSYNGIIFFLKQE-SQFLCLAVQEGTLVLFYDFGSGlkkadplqpPQALTAASKAiqvfLLAGNRKRVLVRVERATV 3052
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGgSDFLALELVNGRLVLRYDLGSG---------PESLLSSGKN----LNDGQWHSVRVERNGNTL 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 124487155 3053 -FSVDQDNMLEMA-----------DAYYLGGVPpeqlPLSLRQLFPSGGSVRGCIKGIK 3099
Cdd:pfam02210 68 tLSVDGQTVVSSLppgeslllnlnGPLYLGGLP----PLLLLPALPVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
500-547 |
1.68e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 58.48 E-value: 1.68e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 124487155 500 CDCNAAGTQGNACrkDPRLGRCVCKPNFRGAHCELCAPGFHGPSCHPC 547
Cdd:smart00180 1 CDCDPGGSASGTC--DPDTGQCECKPNVTGRRCDRCAPGYYGDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
593-634 |
1.75e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 1.75e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124487155 593 CGCSPAGTLPEGCD-EAGRCQCRPGFDGPHCDRCLPGYHGYPD 634
Cdd:cd00055 2 CDCNGHGSLSGQCDpGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2072-2119 |
2.43e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 2.43e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 2072 CACGP-AAKGSECHPQSGQCHCQPGTTGPQCLECAPGYWGLPEKGCRRC 2119
Cdd:pfam00053 1 CDCNPhGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2204-2738 |
3.00e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2204 WARLHRLNAS-IADLQSKLRSppgpRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQLldtteSTLGRAQKLLE 2282
Cdd:COG4717 62 QGRKPELNLKeLKELEEELKE----AEEKEEEYAELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2283 SVRAVGRALNELASRMgqgspgdalvpsgEQLRWALAEVERLlwdmrtrdlgaqgavaeaelaeaQRLMARVQEQLTsfw 2362
Cdd:COG4717 133 ELEALEAELAELPERL-------------EELEERLEELREL-----------------------EEELEELEAELA--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2363 EENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEA------LQWKQELSQDNATLKATLQ--- 2433
Cdd:COG4717 174 ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELeeeleqLENELEAAALEERLKEARLlll 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2434 AASLILGHVSELLQGIDQAKEDLEHLAASLDGAWTPLLKRMQAFSPASSKVDLVEAAEAHaQKLNQLAINLSGIILGINQ 2513
Cdd:COG4717 254 IAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL-EELEEEELEELLAALGLPP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2514 DRFIQRAVEASNAYSSILQAVQAAEDAAGQALRQAsrtwemvvqrgLAAGARQLLANSSALEETILghqgrlglaqgrlq 2593
Cdd:COG4717 333 DLSPEELLELLDRIEELQELLREAEELEEELQLEE-----------LEQEIAALLAEAGVEDEEEL-------------- 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2594 aagIQLHNVWARKNQLAAQIQEAQAMLAmdtSETSEKIAHAKAVAAEALSTA-THVQSQLQGMQKNVERWQSQLGGLQGQ 2672
Cdd:COG4717 388 ---RAALEQAEEYQELKEELEELEEQLE---ELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEAE 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124487155 2673 dLSQVERDAssSVSTLEKTLPQLLAKLSRLENRgvhNASLALsanigrVRKLIAQARSAASKVKVS 2738
Cdd:COG4717 462 -LEQLEEDG--ELAELLQELEELKAELRELAEE---WAALKL------ALELLEEAREEYREERLP 515
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1971-2021 |
3.02e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 3.02e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124487155 1971 CDCSGNGDPNmifSDCDPLTGACRgCLRHTTGPHCERCAPGFYGNALLPGN 2021
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPSDPPQ 47
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
500-549 |
3.80e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 57.75 E-value: 3.80e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 124487155 500 CDCNAAGTQGNACrkDPRLGRCVCKPNFRGAHCELCAPGFHGPSCHPCQC 549
Cdd:cd00055 2 CDCNGHGSLSGQC--DPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGGGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
593-633 |
5.95e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.94 E-value: 5.95e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 124487155 593 CGCSPAGTLPEGCD-EAGRCQCRPGFDGPHCDRCLPGYHGYP 633
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2738-2905 |
7.43e-10 |
|
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: 60.12 E-value: 7.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2738 SMKFNGRSGVRLRTPRDLADlaaYTALKFHIQSPVPapepgkntgDHFVLYMGSrQATGDYMGVSLRNQKVHWVYRLGKa 2817
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT---RLSISFSFRTTSP---------NGLLLYAGS-QNGGDFLALELEDGRLVLRYDLGS- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2818 GPTTLSIDENIGE-QFAAVSIDRTLQFGHMSVTVEKQMvheikgDTVAPGSEGLLNLHPDdfvFYVGGYPSNFTPPEPLR 2896
Cdd:cd00110 67 GSLVLSSKTPLNDgQWHSVSVERNGRSVTLSVDGERVV------ESGSPGGSALLNLDGP---LYLGGLPEDLKSPGLPV 137
|
....*....
gi 124487155 2897 FPGYLGCIE 2905
Cdd:cd00110 138 SPGFVGCIR 146
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
547-588 |
7.90e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 56.55 E-value: 7.90e-10
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 124487155 547 CQCSSPGVANSLCDPESGQCMCRTGFEGDRCDHCALGYFHFP 588
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
547-595 |
1.32e-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: 56.21 E-value: 1.32e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 547 CQCSSPGVANSLCDPESGQCMCRTGFEGDRCDHCALGYFHFPLCQLCGC 595
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
500-549 |
1.43e-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: 56.21 E-value: 1.43e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124487155 500 CDCNAAGTQGNACrkDPRLGRCVCKPNFRGAHCELCAPGFHG-PSCHPCQC 549
Cdd:pfam00053 1 CDCNPHGSLSDTC--DPETGQCLCKPGVTGRHCDRCKPGYYGlPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
637-679 |
2.08e-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: 2.08e-09
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 124487155 637 ACACDPRGALDQQC-GVGGLCHCRPGYTGATCQECSPGFYGFPS 679
Cdd:cd00055 1 PCDCNGHGSLSGQCdPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2189-2735 |
4.58e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 4.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2189 AIREQLQ--GINASSAAW----ARLHRLNASIADLQSKLRsppgpryQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQ 2262
Cdd:COG1196 217 ELKEELKelEAELLLLKLreleAELEELEAELEELEAELE-------ELEAELAELEAELEELRLELEELELELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2263 AGQLLDTTESTLGRAQKLLESVRAVGRALNELASRMgqgspgdalvpsgEQLRWALAEVERllwdmRTRDLGAQgavaea 2342
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEEL-------------AELEEELEELEE-----ELEELEEE------ 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2343 eLAEAQRLMARVQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEALQWKQELS 2422
Cdd:COG1196 346 -LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2423 QDNATLKATLQAASLILGHVSELLQGIDQAKEDLEHLAASL--DGAWTPLL-----KRMQAFSPASSKVDLVEAAEAHAQ 2495
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLaeLLEEAALLeaalaELLEELAEAAARLLLLLEAEADYE 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2496 ------KLNQLAINLSGIILGINQDRFIQRAVEAsnayssilqavqAAEDAAGQALRQASRTWEMVVQRGLAAGARQLLA 2569
Cdd:COG1196 505 gflegvKAALLLAGLRGLAGAVAVLIGVEAAYEA------------ALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2570 NSSALE-ETILGHQGRLGLAQGRLQAAGIQLHNVWARknQLAAQIQEAQAMLAMDTSETsekiahakavaaEALSTATHV 2648
Cdd:COG1196 573 RATFLPlDKIRARAALAAALARGAIGAAVDLVASDLR--EADARYYVLGDTLLGRTLVA------------ARLEAALRR 638
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2649 QSQLQGMQKNVERwqSQLGGLQGQDLSQVERDASSSVSTLEKTLPQLLAKLSRLENRGVHNASLALSANIGRVRKLIAQA 2728
Cdd:COG1196 639 AVTLAGRLREVTL--EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER 716
|
....*..
gi 124487155 2729 RSAASKV 2735
Cdd:COG1196 717 LEEELEE 723
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
638-680 |
9.67e-09 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 9.67e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124487155 638 CACDPRGALDQQC-GVGGLCHCRPGYTGATCQECSPGFYG--FPSC 680
Cdd:smart00180 1 CDCDPGGSASGTCdPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2787-2905 |
1.24e-08 |
|
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: 55.89 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2787 LYMGSRQatGDYMGVSLRNQKVHWVYRLGKAGPTTLSIDENI--GeQFAAVSIDRTLQfgHMSVTVEKQMVHEikgdTVA 2864
Cdd:pfam02210 11 LYAGGGG--SDFLALELVNGRLVLRYDLGSGPESLLSSGKNLndG-QWHSVRVERNGN--TLTLSVDGQTVVS----SLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 124487155 2865 PGSEGLLNLHPDdfvFYVGGYPSNFTPPEPLRFPGYLGCIE 2905
Cdd:pfam02210 82 PGESLLLNLNGP---LYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1915-1968 |
1.97e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 52.74 E-value: 1.97e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 124487155 1915 CPCPLAVPSNnfaDGCVLRNGrtQCLCRPGYAGASCERCAPGFFGNPLVLGSSC 1968
Cdd:pfam00053 1 CDCNPHGSLS---DTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2177-2585 |
2.00e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2177 LDDLERAGALLPAIREQLQGINASSAAWARLHRLNASIADLQSKLRSPPG---PRYQAAQQLQTLEQQSISLQQDTERLG 2253
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2254 SQAT-GVQGQAGQLLDTTESTLGRAQKLLESVRAVGRALNELASRMGQGSPGDALVPSGEQLRWA----LAEVERLLWDM 2328
Cdd:COG4717 184 EQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEArlllLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2329 RTRDLGAQGAVAEAELAEAQRLMA-------RVQEQLTSFWEENQSLATH-------IRDQLAQYESGLMDLREALNQAV 2394
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLAllflllaREKASLGKEAEELQALPALeeleeeeLEELLAALGLPPDLSPEELLELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2395 NTTREAEELNSRnQERLKEALQWkQELSQDNATLKATLQAASL-ILGHVSELLQGIDQAKEDLEHLAASLDGAWTPLLKR 2473
Cdd:COG4717 344 DRIEELQELLRE-AEELEEELQL-EELEQEIAALLAEAGVEDEeELRAALEQAEEYQELKEELEELEEQLEELLGELEEL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2474 MQAFSPASSKV---DLVEAAEAHAQKLNQLAINLSGIILGINQdrfiqraVEASNAYSSILQAVQAAEDAAGQALRQASR 2550
Cdd:COG4717 422 LEALDEEELEEeleELEEELEELEEELEELREELAELEAELEQ-------LEEDGELAELLQELEELKAELRELAEEWAA 494
|
410 420 430
....*....|....*....|....*....|....*
gi 124487155 2551 twemvvqrglAAGARQLLANssALEETILGHQGRL 2585
Cdd:COG4717 495 ----------LKLALELLEE--AREEYREERLPPV 517
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1864-1900 |
5.17e-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: 5.17e-08
10 20 30 40
....*....|....*....|....*....|....*....|
gi 124487155 1864 PCQCHGH---SDRCLPGSGICVgCQHNTEGDQCERCRPGF 1900
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1971-2015 |
1.07e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.77 E-value: 1.07e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124487155 1971 CDCSGNGdpnMIFSDCDPLTGACRgCLRHTTGPHCERCAPGFYGN 2015
Cdd:smart00180 1 CDCDPGG---SASGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGD 41
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1915-1961 |
1.15e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.15e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 124487155 1915 CPCPlavPSNNFADGCVLRNGrtQCLCRPGYAGASCERCAPGFFGNP 1961
Cdd:smart00180 1 CDCD---PGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2268-2627 |
1.48e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.83 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2268 DTTESTLGRAQKLLESVRAVGRALNELASrmgqgspgdalvpsgEQLRWALAEVERLLWDMRtrDLGAQgavaeaeLAEA 2347
Cdd:COG4372 2 DRLGEKVGKARLSLFGLRPKTGILIAALS---------------EQLRKALFELDKLQEELE--QLREE-------LEQA 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2348 QRLMARVQEQLTSfweenqslathIRDQLAQYESGLMDLREALNQAVNTTREA-EELNSRNQE--RLKEALqwkQELSQD 2424
Cdd:COG4372 58 REELEQLEEELEQ-----------ARSELEQLEEELEELNEQLQAAQAELAQAqEELESLQEEaeELQEEL---EELQKE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2425 NATLKATLQAaslILGHVSELLQGIDQAKEDLEHLAASLDGAWTPLLKRMQAFS-----PASSKVD-LVEAAEAHAQKLN 2498
Cdd:COG4372 124 RQDLEQQRKQ---LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQalseaEAEQALDeLLKEANRNAEKEE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2499 QLA----INLSGIILGINQDRFIQRAVEASNAYSSILQAVQAAEDAAGQALRQASRTWEMVVQRGLAAGARQLLANSSAL 2574
Cdd:COG4372 201 ELAeaekLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEI 280
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 124487155 2575 EETILGHQGRLGLAQGRLQAAGIQLHNVWARKNQLAAQIQEAQAMLAMDTSET 2627
Cdd:COG4372 281 AALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1865-1912 |
1.86e-07 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 50.04 E-value: 1.86e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124487155 1865 CQCHGH---SDRCLPGSGICVgCQHNTEGDQCERCRPGFVsSDPSNPASPC 1912
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYY-GLPSDPPQGC 49
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3371-3499 |
2.47e-07 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 52.32 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 3371 AASQGLLLSTAPMSGRsPSLVLFLNHGHfvaqtegpgprLQVQSRQHSRA-----------GQWHRVSVRWGMQQIQLVV 3439
Cdd:pfam00054 4 TEPSGLLLYNGTQTER-DFLALELRDGR-----------LEVSYDLGSGAavvrsgdklndGKWHSVELERNGRSGTLSV 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 124487155 3440 DGSQtwsqkalhhrVPRAERPQPYT--------LSVGGLPASSYS-SKLPVSVGFSGCLKKLQLDKRPL 3499
Cdd:pfam00054 72 DGEA----------RPTGESPLGATtdldvdgpLYVGGLPSLGVKkRRLAISPSFDGCIRDVIVNGKPL 130
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2175-2423 |
2.56e-07 |
|
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: 54.61 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2175 LLLDDLERAGALLPAIREQlqginassaawarlhrlNASIADLQSKLRSPPGPRYQAAQQLQTLEQQ----------SIS 2244
Cdd:pfam12795 17 KLLQDLQQALSLLDKIDAS-----------------KQRAAAYQKALDDAPAELRELRQELAALQAKaeaapkeilaSLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2245 LQQDTERLG---SQATGVQGQAGQL---LDTTESTLGRAQKLLESVRavgRALNELASRMGQGSPGDAlvPSGEQLRWAL 2318
Cdd:pfam12795 80 LEELEQRLLqtsAQLQELQNQLAQLnsqLIELQTRPERAQQQLSEAR---QRLQQIRNRLNGPAPPGE--PLSEAQRWAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2319 aEVERllwdmrtrdlgaqgavaeaelaeaQRLMARVQEQltsfweeNQSLATH-IRDQLAQYESGLMDLR--------EA 2389
Cdd:pfam12795 155 -QAEL------------------------AALKAQIDML-------EQELLSNnNRQDLLKARRDLLTLRiqrleqqlQA 202
|
250 260 270
....*....|....*....|....*....|....*
gi 124487155 2390 LNQAVNTTREAE-ELNSRNQERLKEALQWKQELSQ 2423
Cdd:pfam12795 203 LQELLNEKRLQEaEQAVAQTEQLAEEAAGDHPLVQ 237
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2205-2486 |
4.03e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2205 ARLHRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQagqlLDTTESTLGRAQKLLESV 2284
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2285 RAVGRALNELASRMGQGSPGDALVPSGEQLRwalaeverllwdmrtrdlgaqgavaeaelaeaqrlMARVQEQLTSFWEE 2364
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLD-----------------------------------AVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2365 NQSLATHIRDQLAQyesgLMDLREALNQAVNTTREAEELNSRNQERLKEALQWKQELSQDNATLKATLQAAslilghvse 2444
Cdd:COG4942 148 RREQAEELRADLAE----LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAE--------- 214
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 124487155 2445 lLQGIDQAKEDLEHLAASLDGAWTPLLKRMQAFSPASSKVDL 2486
Cdd:COG4942 215 -LAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
304-352 |
4.17e-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: 49.27 E-value: 4.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 124487155 304 RCVCHGHADV---CDakdpldPFRLQCACQHNTCGGSCDRCCPGFNQQPWKP 352
Cdd:cd00055 1 PCDCNGHGSLsgqCD------PGTGQCECKPNTTGRRCDRCAPGYYGLPSQG 46
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2176-2468 |
4.45e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 55.29 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2176 LLDDLERAGALLPAIREQLQGINAS-SAAWARLHRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTERLGS 2254
Cdd:COG4372 43 LQEELEQLREELEQAREELEQLEEElEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2255 QATGVQGQAGQL---LDTTESTLGRAQKLLESVRAVGRALNELASRMGQGSPGDALVPSGEQLRWALAEVERLLWDMRTR 2331
Cdd:COG4372 123 ERQDLEQQRKQLeaqIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2332 DLGAQgavaeaELAEAQRLMARVQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERL 2411
Cdd:COG4372 203 AEAEK------LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEE 276
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 124487155 2412 KEALQWKQELSQDNATLKATLQAASLILGHVSELLQGIDQAKEDLEHLAASLDGAWT 2468
Cdd:COG4372 277 ELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| HemX |
COG2959 |
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis ... |
2229-2325 |
5.02e-07 |
|
Proteobacterial HemX domain, involved in 2-ketogluconate production (unrelated to B. subtilis HemX, COG0755, no evidence of involvement in heme biosynthesis) [General function prediction only];
Pssm-ID: 442199 [Multi-domain] Cd Length: 361 Bit Score: 54.97 E-value: 5.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2229 YQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQL---LDTTESTLGRAQKLLESVRAVGRALNELASRMGQGSPGD 2305
Cdd:COG2959 49 YLGWQQLQQQQAELAQLAQQLAALQQQAQELRALAQQLqelLQQLAARLAQLEQRLAELQQQLAALQQLLQSLSGSSRDD 128
|
90 100
....*....|....*....|
gi 124487155 2306 alvpsgeqlrWALAEVERLL 2325
Cdd:COG2959 129 ----------WLLAEAEYLL 138
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
781-832 |
7.50e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.50 E-value: 7.50e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 124487155 781 RCSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFGLDYAdYFGCR 832
Cdd:cd00055 1 PCDCNGHGSLSG--QCdPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1914-1969 |
8.36e-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: 8.36e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 124487155 1914 SCPCPLAVPSNNfadGCVLRNGrtQCLCRPGYAGASCERCAPGFFGNPLVlGSSCQ 1969
Cdd:cd00055 1 PCDCNGHGSLSG---QCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
833-872 |
9.77e-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: 9.77e-07
10 20 30 40
....*....|....*....|....*....|....*....|
gi 124487155 833 SCRCDVGGALGQGCEPKTGACRCRPNTQGPTCSEPAKDHY 872
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYY 40
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
2364-2623 |
1.22e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 54.31 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2364 ENQSL---ATHIR--DQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEA--LQWK-QELsqDNATLKA----T 2431
Cdd:COG0497 133 EHQSLldpDAQREllDAFAGLEELLEEYREAYRAWRALKKELEELRADEAERARELdlLRFQlEEL--EAAALQPgeeeE 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2432 LQAASLILGHVSELLQGIDQAkedLEHLAASLDGAwTPLLKR-MQAFSPASskvDLVEAAEAHAQKLNQLAINLSGIIlg 2510
Cdd:COG0497 211 LEEERRRLSNAEKLREALQEA---LEALSGGEGGA-LDLLGQaLRALERLA---EYDPSLAELAERLESALIELEEAA-- 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2511 inqdRFIQRAVEASNAYSSILQAVQAAEDAAGQALRQASRTWEMVVQrgLAAGARQLLANSSALEETILGHQGRLGLAQG 2590
Cdd:COG0497 282 ----SELRRYLDSLEFDPERLEEVEERLALLRRLARKYGVTVEELLA--YAEELRAELAELENSDERLEELEAELAEAEA 355
|
250 260 270
....*....|....*....|....*....|....*.
gi 124487155 2591 RLQAAGIQLHNvwARKN---QLAAQIQEAQAMLAMD 2623
Cdd:COG0497 356 ELLEAAEKLSA--ARKKaakKLEKAVTAELADLGMP 389
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2173-2463 |
2.20e-06 |
|
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: 53.91 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2173 VVLLLDDLERAGALLPAIREQLQGINASSAAWA-RLHRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTER 2251
Cdd:TIGR02168 714 LEQLRKELEELSRQISALRKDLARLEAEVEQLEeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2252 LGSQatgvqgqagqlLDTTESTLGRAQKLLESVRavgRALNELASRMgqgspgdalvpsgEQLRWALAEVERLLWDM--R 2329
Cdd:TIGR02168 794 LKEE-----------LKALREALDELRAELTLLN---EEAANLRERL-------------ESLERRIAATERRLEDLeeQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2330 TRDLGAQGAVAEAELAEAQRLMARVQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSR-NQ 2408
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKlAQ 926
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 124487155 2409 ERLKealqwKQELSQDNATLKATLQA-ASLILGHVSELLQGIDQAKEDLEHLAASL 2463
Cdd:TIGR02168 927 LELR-----LEGLEVRIDNLQERLSEeYSLTLEEAEALENKIEDDEEEARRRLKRL 977
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2190-2426 |
2.69e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.48 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2190 IREQLQGINAssaawaRLHRLNASIADLQSK--LRSPPGPRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQLL 2267
Cdd:COG3206 180 LEEQLPELRK------ELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGP 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2268 DTTESTLG--RAQKLLESVRAVGRALNELASRMGQGSPgdALVpsgeQLRWALAEVERLLwdmrtrdlgaqgavaeaela 2345
Cdd:COG3206 254 DALPELLQspVIQQLRAQLAELEAELAELSARYTPNHP--DVI----ALRAQIAALRAQL-------------------- 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2346 eaQRLMARVQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEelnsRNQERLKEALQWKQELSQDN 2425
Cdd:COG3206 308 --QQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE----VARELYESLLQRLEEARLAE 381
|
.
gi 124487155 2426 A 2426
Cdd:COG3206 382 A 382
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
782-831 |
4.03e-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: 4.03e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 124487155 782 CSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFGLDYADYFGC 831
Cdd:pfam00053 1 CDCNPHGSLSD--TCdPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
433-474 |
4.05e-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: 46.19 E-value: 4.05e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 124487155 433 PCDCESDFT-DGTCEDLTGRCYCRPNFTGELCAACAEGYTDFP 474
Cdd:cd00055 1 PCDCNGHGSlSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
834-872 |
4.42e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 46.15 E-value: 4.42e-06
10 20 30
....*....|....*....|....*....|....*....
gi 124487155 834 CRCDVGGALGQGCEPKTGACRCRPNTQGPTCSEPAKDHY 872
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
782-825 |
5.33e-06 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 45.77 E-value: 5.33e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 124487155 782 CSCDPRGTLGGvtEC-QGNGQCFCKAHVCGKTCAACKDGFFGLDY 825
Cdd:smart00180 1 CDCDPGGSASG--TCdPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2178-2708 |
5.49e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.61 E-value: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2178 DDLERAGALLPAIREQ---LQGINASSAAWARLHRLNASIADLQSKLRSppgprYQAAQQLQTLEQQSISLQQDTERLGS 2254
Cdd:COG4913 235 DDLERAHEALEDAREQielLEPIRELAERYAAARERLAELEYLRAALRL-----WFAQRRLELLEAELEELRAELARLEA 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2255 QATgvqgQAGQLLDTTESTLGRAQKLLESvrAVGRALNELASRMgqgspgdalvpsgEQLRWALAEVERLL--WDMRTRD 2332
Cdd:COG4913 310 ELE----RLEARLDALREELDELEAQIRG--NGGDRLEQLEREI-------------ERLERELEERERRRarLEALLAA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2333 LGAQGAVAEAELAEAQRLMARVQEQLTSFWEENQSLATHIRDQLAQ---------------------YESGLMDLREALN 2391
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDlrrelreleaeiaslerrksnIPARLLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2392 QAVNTT-------------REAEE---------LNSR------NQERLKEALQWkqelsqdnatLKATLQAASLILGHVS 2443
Cdd:COG4913 451 EALGLDeaelpfvgelievRPEEErwrgaiervLGGFaltllvPPEHYAAALRW----------VNRLHLRGRLVYERVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2444 ELLQGIDQAKEDLEHLAASLDGAWTP----LLKRMQAFSPAsSKVDLVEAAEAHAQklnqlAINLSGII-----LGINQD 2514
Cdd:COG4913 521 TGLPDPERPRLDPDSLAGKLDFKPHPfrawLEAELGRRFDY-VCVDSPEELRRHPR-----AITRAGQVkgngtRHEKDD 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2515 RF----------------------IQRAVEASNAYSSILQAVQAAEDAAGQALRQASR----TWEMV----VQRGLAAGA 2564
Cdd:COG4913 595 RRrirsryvlgfdnraklaaleaeLAELEEELAEAEERLEALEAELDALQERREALQRlaeySWDEIdvasAEREIAELE 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2565 RQ---LLANSSALEEtiLghQGRLGLAQGRLQAAGIQLHNVWARKNQLAAQIQEAQAML--AMDTSETSEKIAHAKAVAA 2639
Cdd:COG4913 675 AElerLDASSDDLAA--L--EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELdeLQDRLEAAEDLARLELRAL 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2640 -----EALSTATHVQSQLQGMQKNVERWQSQLGGLQGQDLSQVER------DASSSVSTLEKTLPQLLAKLSRLENRGVH 2708
Cdd:COG4913 751 leerfAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfnrewpAETADLDADLESLPEYLALLDRLEEDGLP 830
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2208-2691 |
5.75e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 52.48 E-value: 5.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2208 HRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQLLDTTESTLGR-----AQK--L 2280
Cdd:pfam01576 183 NKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARleeetAQKnnA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2281 LESVRAVGRALNELASRMgqgspgdalvpsgEQLRWALAEVERllwdmRTRDLGAQGAVAEAELAEAQRLMARVQEQLTS 2360
Cdd:pfam01576 263 LKKIRELEAQISELQEDL-------------ESERAARNKAEK-----QRRDLGEELEALKTELEDTLDTTAAQQELRSK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2361 FWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEAlqwKQELSQDNATLKATLQaaslilg 2440
Cdd:pfam01576 325 REQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKA---KQALESENAELQAELR------- 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2441 hvseLLQgidQAKEDLEHLAASLDGAwtplLKRMQAFSPASSKVDlVEAAEahaqKLNQLAINLSGI--ILGINQDRFIQ 2518
Cdd:pfam01576 395 ----TLQ---QAKQDSEHKRKKLEGQ----LQELQARLSESERQR-AELAE----KLSKLQSELESVssLLNEAEGKNIK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2519 RAVEASNAySSILQAVQA-AEDAAGQALRQASRTwemvvqrglaagaRQLLANSSALEEtilghqgrlglaqgrlqaagi 2597
Cdd:pfam01576 459 LSKDVSSL-ESQLQDTQElLQEETRQKLNLSTRL-------------RQLEDERNSLQE--------------------- 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2598 QLHNVWARKNQLAAQIQEAQAMLamdtSETSEKIAhakavaaealstatHVQSQLQGMQKNVERWQSQLgglqgQDLSQV 2677
Cdd:pfam01576 504 QLEEEEEAKRNVERQLSTLQAQL----SDMKKKLE--------------EDAGTLEALEEGKKRLQREL-----EALTQQ 560
|
490
....*....|....
gi 124487155 2678 ERDASSSVSTLEKT 2691
Cdd:pfam01576 561 LEEKAAAYDKLEKT 574
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2348-2733 |
7.87e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.83 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2348 QRLMARVQEQLTS---FweenqsLATHIRDQLAQYESGLMDLREALNQAVNTTREaeelNSRNQERLKE----ALQWKQE 2420
Cdd:COG5278 53 EELLSALLDAETGqrgY------LLTGDESFLEPYEEARAEIDELLAELRSLTAD----NPEQQARLDElealIDQWLAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2421 LSQ-----DNATLKATLQAASLILGhvSELLQGIDQAKEDLEHLAASLdgawtpLLKRMQAFSPASSKVDLVEAAEAHAQ 2495
Cdd:COG5278 123 LEQvialrRAGGLEAALALVRSGEG--KALMDEIRARLLLLALALAAL------LLAAAALLLLLLALAALLALAELLLL 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2496 KLNQLAINLSGIILGINQDRFIQRAVEASNAYSSILQAVQAAEDAAGQALRQASRTWEMVVQRGLAAGARQLLANSSALE 2575
Cdd:COG5278 195 ALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2576 ETILGHQGRLGLAQGRLQAAGIQLHNVWARKNQLAAQIQEAQAMLAMDTSETSEKIAHAKAVAAEALSTATHVQSQLQGM 2655
Cdd:COG5278 275 LALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEA 354
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124487155 2656 QKNVERWQSQLGGLQGQDLSQVERDASSSVSTLEKTLPQLLAKLSRLENRGVHNASLALSANIGRVRKLIAQARSAAS 2733
Cdd:COG5278 355 AAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2313-2681 |
8.48e-06 |
|
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: 51.98 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2313 QLRWALAEVERLLWDMRTRDLGAQgavaeaelaeaqrlMARVQEQLtsfwEENQSLATHIRDQLAQYESGLMDLREALNQ 2392
Cdd:TIGR02168 217 ELKAELRELELALLVLRLEELREE--------------LEELQEEL----KEAEEELEELTAELQELEEKLEELRLEVSE 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2393 AvntTREAEELnsrnQERLKEALQWKQELSQDNATLKATLQAASLILGHVSELLQGIDQAKEDLEHLAASLDGAWTPLLK 2472
Cdd:TIGR02168 279 L---EEEIEEL----QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2473 RMQAFSPA-SSKVDLVEAAEAHAQKLNQLAINLSGIILGINQDrfiqravEASNAySSILQAVQAAEDAAGQALRQASRT 2551
Cdd:TIGR02168 352 ELESLEAElEELEAELEELESRLEELEEQLETLRSKVAQLELQ-------IASLN-NEIERLEARLERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2552 wEMVVQRGLAAGARQLLANSSALEETILGHQGRLGLAQGRLQAAGIQLHNVWARKNQLAAQIQEAQAMLAMDTSetseki 2631
Cdd:TIGR02168 424 -EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER------ 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 124487155 2632 ahakavaaealstathVQSQLQGMQ---KNVERWQSQLGGLQGQDLSQVERDA 2681
Cdd:TIGR02168 497 ----------------LQENLEGFSegvKALLKNQSGLSGILGVLSELISVDE 533
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2176-2722 |
1.10e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.58 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2176 LLDDL----------ERAG-------ALLPAIREQLQGINASSAA------WARLHRLNASIADLQSKLRSPPGPRYQAA 2232
Cdd:PRK02224 154 MIDDLlqlgkleeyrERASdarlgveRVLSDQRGSLDQLKAQIEEkeekdlHERLNGLESELAELDEEIERYEEQREQAR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2233 QQLQTLE---------QQSI-SLQQDTERLGSQATGVQgqagqllDTTESTLGRAQKLLESVRAVGRALNELASRMGQGS 2302
Cdd:PRK02224 234 ETRDEADevleeheerREELeTLEAEIEDLRETIAETE-------REREELAEEVRDLRERLEELEEERDDLLAEAGLDD 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2303 PGD-ALVPSGEQLRWALAEVERLLWDMRTrDLGAQGAVAEAELAEAQRLMARVQE------QLTSFWEENQSLATHIRDQ 2375
Cdd:PRK02224 307 ADAeAVEARREELEDRDEELRDRLEECRV-AAQAHNEEAESLREDADDLEERAEElreeaaELESELEEAREAVEDRREE 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2376 LAQYESGLMDLREALNqavNTTREAEELNSRNQERLKEalqwKQELSQDNATLKATLQAASLILGHVSELLQ-------- 2447
Cdd:PRK02224 386 IEELEEEIEELRERFG---DAPVDLGNAEDFLEELREE----RDELREREAELEATLRTARERVEEAEALLEagkcpecg 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2448 ----------GIDQAKEDLEHLAASLDGAWTPLLKRMQAFSPASskvDLVEaAEAHAQKLNQLAINLSGII----LGINQ 2513
Cdd:PRK02224 459 qpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAE---DLVE-AEDRIERLEERREDLEELIaerrETIEE 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2514 DRfiqRAVEASNAYSSILQA-VQAAEDAAGQALRQASRTWEMVV----QRGLAAGARQLLANSSALEETILGHQGRLG-L 2587
Cdd:PRK02224 535 KR---ERAEELRERAAELEAeAEEKREAAAEAEEEAEEAREEVAelnsKLAELKERIESLERIRTLLAAIADAEDEIErL 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2588 AQGRLQAAGI------QLHNVWARKNQLAAQIQEAQAMLAMDTSETSEKIAHakavaaealstatHVQSQLQGMQKNVER 2661
Cdd:PRK02224 612 REKREALAELnderreRLAEKRERKRELEAEFDEARIEEAREDKERAEEYLE-------------QVEEKLDELREERDD 678
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124487155 2662 WQSQLGGLQGQdLSQVErdasssvsTLEKTLPQLLAKLSRLENrgVHNASLALSANIGRVR 2722
Cdd:PRK02224 679 LQAEIGAVENE-LEELE--------ELRERREALENRVEALEA--LYDEAEELESMYGDLR 728
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1865-1900 |
1.26e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.61 E-value: 1.26e-05
10 20 30
....*....|....*....|....*....|....*....
gi 124487155 1865 CQCHG---HSDRCLPGSGICVgCQHNTEGDQCERCRPGF 1900
Cdd:smart00180 1 CDCDPggsASGTCDPDTGQCE-CKPNVTGRRCDRCAPGY 38
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
434-476 |
1.76e-05 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 44.22 E-value: 1.76e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124487155 434 CDCESDFT-DGTCEDLTGRCYCRPNFTGELCAACAEGY--TDFPHC 476
Cdd:smart00180 1 CDCDPGGSaSGTCDPDTGQCECKPNVTGRRCDRCAPGYygDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
363-426 |
2.01e-05 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 44.27 E-value: 2.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 124487155 363 SCNCHGHAydcyydpevdrrnasQNQDNVYQGGGVCLdCQHHTTGINCERCLPGFFRAPDQPLD 426
Cdd:cd00055 1 PCDCNGHG---------------SLSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
834-872 |
5.03e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.11 E-value: 5.03e-05
10 20 30
....*....|....*....|....*....|....*....
gi 124487155 834 CRCDVGGALGQGCEPKTGACRCRPNTQGPTCSEPAKDHY 872
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2176-2463 |
5.97e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.14 E-value: 5.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2176 LLDDLERAGALLPAIREQLQGINASSAAWARLHRLNASIADLQSKLRsppgpRYQAAQQ-----------LQTLEQQSIS 2244
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAER-----EIAELEAelerldassddLAALEEQLEE 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2245 LQQDTERLGSQATGVQGQAGQLldttESTLGRAQKLLESVRAVGRALNELASrmgqgspgdalvpsgEQLRWALAE-VER 2323
Cdd:COG4913 697 LEAELEELEEELDELKGEIGRL----EKELEQAEEELDELQDRLEAAEDLAR---------------LELRALLEErFAA 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2324 LLWDMRTRDLGAQgavaeaelaeaqrLMARVQEQLTSFWEENQSLATHIRDQLAQYESGLMDLR---EALN--QAVNTTR 2398
Cdd:COG4913 758 ALGDAVERELREN-------------LEERIDALRARLNRAEEELERAMRAFNREWPAETADLDadlESLPeyLALLDRL 824
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 124487155 2399 EAEELnSRNQERLKEALqwkQELSQDNatlKATLQaaslilghvSELLQGIDQAKEDLEHLAASL 2463
Cdd:COG4913 825 EEDGL-PEYEERFKELL---NENSIEF---VADLL---------SKLRRAIREIKERIDPLNDSL 873
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2405-2737 |
6.08e-05 |
|
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: 49.28 E-value: 6.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2405 SRNQERLKEALQwKQELSQDNatlkatLQAASLILGHVSELLQGID-QA---------KEDLEHLAASLDGA-WTPLLKR 2473
Cdd:TIGR02168 168 SKYKERRKETER-KLERTREN------LDRLEDILNELERQLKSLErQAekaerykelKAELRELELALLVLrLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2474 MQAFSpaSSKVDLVEAAEAHAQKLNQLAINLSGIILGINQ-DRFIQRAVEASNAYSSILQAVQAAEDAAGQALRQASRTW 2552
Cdd:TIGR02168 241 LEELQ--EELKEAEEELEELTAELQELEEKLEELRLEVSElEEEIEELQKELYALANEISRLEQQKQILRERLANLERQL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2553 EMVVQRGLAAGARQ--LLANSSALEETILGHQGRLGLAQGRLQAAGIQLHNVWARKNQLAAQIQEAQAMLAmdtsETSEK 2630
Cdd:TIGR02168 319 EELEAQLEELESKLdeLAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA----QLELQ 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2631 IAhakavaaealSTATHVQ---SQLQGMQKNVERWQSQLGGLQGQDLSQVERDASSSVSTLEKTLPQLLAKLSRLENRgV 2707
Cdd:TIGR02168 395 IA----------SLNNEIErleARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEA-L 463
|
330 340 350
....*....|....*....|....*....|
gi 124487155 2708 HNASLALSANIGRVRKLIAQARSAASKVKV 2737
Cdd:TIGR02168 464 EELREELEEAEQALDAAERELAQLQARLDS 493
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
2244-2458 |
6.65e-05 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 46.49 E-value: 6.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2244 SLQQDTERLGSQATGVQGQAGQLLDTTESTLGRAQKLLesVRAVGRALNELASRmgqgspgdaLVPSGEQLRWAL-AEVE 2322
Cdd:pfam01442 1 LLEDSLDELSTYAEELQEQLGPVAQELVDRLEKETEAL--RERLQKDLEEVRAK---------LEPYLEELQAKLgQNVE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2323 RLlwdmRTRdLGAQGavaeaelaeaQRLMARVQEQLtsfwEEnqslathIRDQLAQYesgLMDLREALNQAVNTTRE--- 2399
Cdd:pfam01442 70 EL----RQR-LEPYT----------EELRKRLNADA----EE-------LQEKLAPY---GEELRERLEQNVDALRArla 120
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 124487155 2400 --AEELNSRNQERLKEalqWKQELSQDNATLKATLQaaslilGHVSELLQGIDQAKEDLEH 2458
Cdd:pfam01442 121 pyAEELRQKLAERLEE---LKESLAPYAEEVQAQLS------QRLQELREKLEPQAEDLRE 172
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
434-478 |
9.62e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 42.34 E-value: 9.62e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 124487155 434 CDC-ESDFTDGTCEDLTGRCYCRPNFTGELCAACAEGYTDFPHCYP 478
Cdd:pfam00053 1 CDCnPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPP 46
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2176-2702 |
1.01e-04 |
|
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: 48.43 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2176 LLDDLERAGALLPAIREQLQGINaSSAAWARLHRLNASI-----------ADLQSKLRSPPGPRYQ---AAQQLQTLEQQ 2241
Cdd:TIGR00618 265 LRARIEELRAQEAVLEETQERIN-RARKAAPLAAHIKAVtqieqqaqrihTELQSKMRSRAKLLMKraaHVKQQSSIEEQ 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2242 SISLQQ--DTERLGSQATGVQGQAGQLLDTTESTLGRAQKLLESVRAVGRALNELASRMgqgspgdalvpsgEQLRWALA 2319
Cdd:TIGR00618 344 RRLLQTlhSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEL-------------DILQREQA 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2320 EVERLlwDMRTRDLgaQGavaeaelaeaQRLMARVQEQLTSFWEENQSLATHIRDQLA-QYESGLMDLREALNQAVNTTR 2398
Cdd:TIGR00618 411 TIDTR--TSAFRDL--QG----------QLAHAKKQQELQQRYAELCAAAITCTAQCEkLEKIHLQESAQSLKEREQQLQ 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2399 EAEELNSRNQERLKEALQWKQELSQDNATLKATL------QAASLILGHVSELLQGIDQAKEDLEHLAASLDGAWTPLLK 2472
Cdd:TIGR00618 477 TKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCihpnpaRQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERK 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2473 RMQAFSpasskvdlvEAAEAHAQKLNQLAINlsgiilginqdrfIQRAVEASNAYSSILQAVQ---AAEDAAGQALRQAS 2549
Cdd:TIGR00618 557 QRASLK---------EQMQEIQQSFSILTQC-------------DNRSKEDIPNLQNITVRLQdltEKLSEAEDMLACEQ 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2550 RTWEMVVQRGLA----AGARQLLANSSALEETILgHQGRLGLAQGRLQAAgiqlhnvWARKNQLaaQIQEAQAMLAMDTS 2625
Cdd:TIGR00618 615 HALLRKLQPEQDlqdvRLHLQQCSQELALKLTAL-HALQLTLTQERVREH-------ALSIRVL--PKELLASRQLALQK 684
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 124487155 2626 ETSEKiahakAVAAEALSTATHVQSQLQGMQKNVERWQSQLgglqgQDLSQVERDASSSVSTLEKTLPQLLAKLSRL 2702
Cdd:TIGR00618 685 MQSEK-----EQLTYWKEMLAQCQTLLRELETHIEEYDREF-----NEIENASSSLGSDLAAREDALNQSLKELMHQ 751
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
2119-2147 |
2.05e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 41.57 E-value: 2.05e-04
10 20 30
....*....|....*....|....*....|....
gi 124487155 2119 CQCP-----RGHCDPHTGHCTCPPGLSGERCDTC 2147
Cdd:pfam00053 1 CDCNphgslSDTCDPETGQCLCKPGVTGRHCDRC 34
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
2119-2169 |
2.08e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 41.53 E-value: 2.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 124487155 2119 CQC-PRGH----CDPHTGHCTCPPGLSGERCDTCsqqhqvpvpgKPGGHGIHCEVC 2169
Cdd:smart00180 1 CDCdPGGSasgtCDPDTGQCECKPNVTGRRCDRC----------APGYYGDGPPGC 46
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2786-2910 |
3.06e-04 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 43.46 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2786 VLYMGSrQATGDYMGVSLRNQKVHWVYRLGKaGPTTLSIDENIGE-QFAAVSIDRTLQfgHMSVTVEKQMVHEIkgdTVA 2864
Cdd:pfam00054 10 LLYNGT-QTERDFLALELRDGRLEVSYDLGS-GAAVVRSGDKLNDgKWHSVELERNGR--SGTLSVDGEARPTG---ESP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 124487155 2865 PGSEGLLNLhpdDFVFYVGGYPSNFTPPEPLRF-PGYLGCIEMETLN 2910
Cdd:pfam00054 83 LGATTDLDV---DGPLYVGGLPSLGVKKRRLAIsPSFDGCIRDVIVN 126
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2227-2543 |
3.85e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 3.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2227 PRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQLldTTESTLGRA-------QKLLESVRAVGRALNELASRMG 2299
Cdd:COG3206 51 PVYEASATLLVEPQSSDVLLSGLSSLSASDSPLETQIEIL--KSRPVLERVvdklnldEDPLGEEASREAAIERLRKNLT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2300 QGSPGDALV-------PSGEQLR---WALAE--VERLLwDMRTRDLGAQGAVAEAELAEAQRLMARVQEQLTSFWEENQS 2367
Cdd:COG3206 129 VEPVKGSNVieisytsPDPELAAavaNALAEayLEQNL-ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2368 L-----ATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEALQWK--QELSQDNATLKATLQAASLILG 2440
Cdd:COG3206 208 VdlseeAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAELSARYT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2441 HVSELLQGIDQAKEDLEhlaasldgawtPLLKRMQAFSPASSKVDlVEAAEAHAQKLNQLAINLSGIILGINQD----RF 2516
Cdd:COG3206 288 PNHPDVIALRAQIAALR-----------AQLQQEAQRILASLEAE-LEALQAREASLQAQLAQLEARLAELPELeaelRR 355
|
330 340
....*....|....*....|....*...
gi 124487155 2517 IQRAVEASNA-YSSILQAVQAAEDAAGQ 2543
Cdd:COG3206 356 LEREVEVARElYESLLQRLEEARLAEAL 383
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2980-3106 |
4.24e-04 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 43.07 E-value: 4.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2980 NGIIFFLKQ--ESQFLCLAVQEGTLVLFYDFGSGLKkadpLQPPQALTAASKAIQVFLLAgNRKRVLVRV---ERATVFS 3054
Cdd:pfam00054 7 SGLLLYNGTqtERDFLALELRDGRLEVSYDLGSGAA----VVRSGDKLNDGKWHSVELER-NGRSGTLSVdgeARPTGES 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 124487155 3055 V-DQDNMLEMADAYYLGGVPPEqlpLSLRQLFPSGGSVRGCIKGIKALGKYVD 3106
Cdd:pfam00054 82 PlGATTDLDVDGPLYVGGLPSL---GVKKRRLAISPSFDGCIRDVIVNGKPLD 131
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
364-431 |
4.42e-04 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 40.41 E-value: 4.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 124487155 364 CNCHGHAydcyydpevdrrnasQNQDNVYQGGGVCLdCQHHTTGINCERCLPGFFRapdQPLDSPHVC 431
Cdd:pfam00053 1 CDCNPHG---------------SLSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYG---LPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
2118-2147 |
5.19e-04 |
|
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: 40.42 E-value: 5.19e-04
10 20 30
....*....|....*....|....*....|....*
gi 124487155 2118 RCQCP-----RGHCDPHTGHCTCPPGLSGERCDTC 2147
Cdd:cd00055 1 PCDCNghgslSGQCDPGTGQCECKPNTTGRRCDRC 35
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2177-2569 |
5.37e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2177 LDDLERAGALL----PAIREQLQGINASSAAWARLHRLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTERL 2252
Cdd:PRK04863 316 LAELNEAESDLeqdyQAASDHLNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDEL 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2253 GSQATGVQ-------------GQAGQLLDTTES-------TLGRAQKLLESVRA----VGRALNELASRM---------- 2298
Cdd:PRK04863 396 KSQLADYQqaldvqqtraiqyQQAVQALERAKQlcglpdlTADNAEDWLEEFQAkeqeATEELLSLEQKLsvaqaahsqf 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2299 -----------GQGSPGDA----------------LVPSGEQLRWALAEVERLLWDMRTrdlgaqgavaeaelaeAQRLM 2351
Cdd:PRK04863 476 eqayqlvrkiaGEVSRSEAwdvarellrrlreqrhLAEQLQQLRMRLSELEQRLRQQQR----------------AERLL 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2352 ARVQEQLTSFWEENQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEALQWKQ------ELS-QD 2424
Cdd:PRK04863 540 AEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAaqdalaRLReQS 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2425 NATLKATLQAASLILGHVsELLQGIDQAKEDLEHLAASLDGAWTPLLKRMQAFSPasskvdlveaaeahaqKLNQLAINL 2504
Cdd:PRK04863 620 GEEFEDSQDVTEYMQQLL-ERERELTVERDELAARKQALDEEIERLSQPGGSEDP----------------RLNALAERF 682
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 124487155 2505 SGIILG-INQDRFIQRAVEASNAYssilqavqaaedaaGQAlRQAsrtwemVVQRGLAAGARQLLA 2569
Cdd:PRK04863 683 GGVLLSeIYDDVSLEDAPYFSALY--------------GPA-RHA------IVVPDLSDAAEQLAG 727
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
392-421 |
6.76e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.99 E-value: 6.76e-04
10 20 30
....*....|....*....|....*....|
gi 124487155 392 YQGGGVCLdCQHHTTGINCERCLPGFFRAP 421
Cdd:smart00180 14 DPDTGQCE-CKPNVTGRRCDRCAPGYYGDG 42
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2231-2539 |
7.54e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 7.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2231 AAQQLQTLEQQSISLQQDterlgsqatgvqgqagqlLDTTESTLGRAQKLLESVRAVGRALNELasrmgqgspgdalvps 2310
Cdd:COG4913 608 NRAKLAALEAELAELEEE------------------LAEAEERLEALEAELDALQERREALQRL---------------- 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2311 gEQLRWALAEVERLlwdmrtrdlgaqgavaeaelaeaQRLMARVQEQLTSFWEENQSLAThIRDQLAQyesglmdLREAL 2390
Cdd:COG4913 654 -AEYSWDEIDVASA-----------------------EREIAELEAELERLDASSDDLAA-LEEQLEE-------LEAEL 701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2391 NQAVNTTREAEELNSRNQERLKEALQWKQELSQ--DNATLKATLQAASLILGHVSELLQG------IDQAKEDLEHLAAS 2462
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDrlEAAEDLARLELRALLEERFAAALGDaverelRENLEERIDALRAR 781
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2463 LDGAWTPLLKRMQAFSPA--SSKVDL---VEAAEAHAQKLNQLAinlsGIILGINQDRFIQRAVEASNA-----YSSILQ 2532
Cdd:COG4913 782 LNRAEEELERAMRAFNREwpAETADLdadLESLPEYLALLDRLE----EDGLPEYEERFKELLNENSIEfvadlLSKLRR 857
|
....*..
gi 124487155 2533 AVQAAED 2539
Cdd:COG4913 858 AIREIKE 864
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2205-2536 |
7.93e-04 |
|
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: 45.43 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2205 ARLHRLNASIADLQSKLRsppgpryQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQLLDTTESTLGRAQKLLESV 2284
Cdd:TIGR02168 677 REIEELEEKIEELEEKIA-------ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERI 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2285 RAVGRALNELASRMgqgspgDALVPSGEQLRWALAEVERllwdmrtrdlgaqgavaeaELAEAQRLMARVQEQLTSFWEE 2364
Cdd:TIGR02168 750 AQLSKELTELEAEI------EELEERLEEAEEELAEAEA-------------------EIEELEAQIEQLKEELKALREA 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2365 NQSLathiRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEALQWKQELSQDNATLKATLQAASLILGHVSE 2444
Cdd:TIGR02168 805 LDEL----RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2445 LLQGIDQAKEDLEHLAASLDGAWTPLLKRMQafspasskvDLVEAAEAHAQKLNQLAINLSGIILGInqDRFIQRaveAS 2524
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRS---------ELRRELEELREKLAQLELRLEGLEVRI--DNLQER---LS 946
|
330
....*....|..
gi 124487155 2525 NAYSSILQAVQA 2536
Cdd:TIGR02168 947 EEYSLTLEEAEA 958
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
305-350 |
8.23e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 8.23e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 124487155 305 CVCH--GHAD-VCDakdpldPFRLQCACQHNTCGGSCDRCCPGFNQQPW 350
Cdd:smart00180 1 CDCDpgGSASgTCD------PDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2179-2539 |
1.11e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 45.18 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2179 DLERAGALLPAIREQLQGINASSAAWARLHRLNASIADLQS-KLRSPPG-----------PRYQAAQQLQTLEQQS--IS 2244
Cdd:PRK10246 455 EQTQRNAALNEMRQRYKEKTQQLADVKTICEQEARIKDLEAqRAQLQAGqpcplcgstshPAVEAYQALEPGVNQSrlDA 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2245 LQQDTERLGSQATGVQGQAGQLLDTTESTLGRAQKLLESVRAVGRALNELASRMG-QGSPGDALVPsgeqlrW--ALAEV 2321
Cdd:PRK10246 535 LEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNiTLQPQDDIQP------WldAQEEH 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2322 ERLLWDMRTR-DLGAQGAVAEAELAEAQRLMARVQEQLTS---------------------------FWEENQSLATHIR 2373
Cdd:PRK10246 609 ERQLRLLSQRhELQGQIAAHNQQIIQYQQQIEQRQQQLLTalagyaltlpqedeeaswlatrqqeaqSWQQRQNELTALQ 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2374 DQLAQyesgLMDLREALNQAVNTTREAE---------------ELNSRNQERLKEALQWKQELSQDNATLKATLQA---- 2434
Cdd:PRK10246 689 NRIQQ----LTPLLETLPQSDDLPHSEEtvaldnwrqvheqclSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQAsvfd 764
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2435 ------ASLIlghVSELLQGIDQAKEDLE---HLAASLDGAWTPLLKRMQAFSPASskVDLVEAAEAHAQKLNQLAINLS 2505
Cdd:PRK10246 765 dqqaflAALL---DEETLTQLEQLKQNLEnqrQQAQTLVTQTAQALAQHQQHRPDG--LDLTVTVEQIQQELAQLAQQLR 839
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 124487155 2506 G-------IILGINQD---RFIQRAVEAsnaysSILQAVQAAED 2539
Cdd:PRK10246 840 EnttrqgeIRQQLKQDadnRQQQQALMQ-----QIAQATQQVED 878
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2209-2461 |
1.63e-03 |
|
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: 44.56 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2209 RLNASIADLQSKLRSPPGPRYQAAQQLQTLEQQSISLQQDTERLGSQATGVQgqagQLLDTTEStlgRAQKLLESVRAVG 2288
Cdd:COG3096 351 RYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQ----QALDVQQT---RAIQYQQAVQALE 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2289 RA-----LNELASrmgqgspgDALVPSGEQLRWALAEVERLLWDMRTR-DLGAQGAVAEAELAEAQRLMA---------- 2352
Cdd:COG3096 424 KAralcgLPDLTP--------ENAEDYLAAFRAKEQQATEEVLELEQKlSVADAARRQFEKAYELVCKIAgeversqawq 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2353 RVQEQLTSfWEENQSLAthirDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEALQWKQELSQDNATLKATL 2432
Cdd:COG3096 496 TARELLRR-YRSQQALA----QRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELE 570
|
250 260
....*....|....*....|....*....
gi 124487155 2433 QAASLILGHVSELLQGIDQAKEDLEHLAA 2461
Cdd:COG3096 571 EQAAEAVEQRSELRQQLEQLRARIKELAA 599
|
|
| Mod_r |
pfam07200 |
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region ... |
2355-2465 |
1.91e-03 |
|
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region approximately 150 residues long within a number of eukaryotic proteins that show homology with Drosophila melanogaster Modifier of rudimentary (Mod(r)) proteins. The N-terminal half of Mod(r) proteins is acidic, whereas the C-terminal half is basic, and both of these regions are represented in this family. Members of this family include the Vps37 subunit of the endosomal sorting complex ESCRT-I, a complex involved in recruiting transport machinery for protein sorting at the multivesicular body (MVB). The yeast ESCRT-I complex consists of three proteins (Vps23, Vps28 and Vps37). The mammalian homolog of Vps37 interacts with Tsg101 (Pfam: PF05743) through its mod(r) domain and its function is essential for lysosomal sorting of EGF receptors.
Pssm-ID: 462117 [Multi-domain] Cd Length: 146 Bit Score: 41.45 E-value: 1.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2355 QEQLTSFWEENQSLAthiRDQLAQyESGLMDLREALNQAVNTTREAEELNSRNQERLKEALqwkQELSQDnaTLKATLQA 2434
Cdd:pfam07200 32 QAEKEELLAENESLA---EENLSL-EPELEELRSQLQELLEELKALKSEYEEKEQELDELL---SKFSPD--ALLARLQA 102
|
90 100 110
....*....|....*....|....*....|..
gi 124487155 2435 AslilghvsellqgIDQAKEDLEHLAAS-LDG 2465
Cdd:pfam07200 103 A-------------AAEAEEESEALAESfLEG 121
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
305-361 |
2.11e-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: 38.49 E-value: 2.11e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 124487155 305 CVCHGHADVcdaKDPLDPFRLQCACQHNTCGGSCDRCCPGFNQQPwkpatTDSANEC 361
Cdd:pfam00053 1 CDCNPHGSL---SDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLP-----SDPPQGC 49
|
|
| VSP |
pfam03302 |
Giardia variant-specific surface protein; |
1843-2148 |
2.33e-03 |
|
Giardia variant-specific surface protein;
Pssm-ID: 146106 [Multi-domain] Cd Length: 397 Bit Score: 43.42 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 1843 CQECAPGYYRDTKGLFLGRCVPCQchghsdrcLPGSGICVgcqhNTEGDQCERCRPGFVSSDPSNPASPCVSCPCPLAVP 1922
Cdd:pfam03302 1 CDECKPGYELSADKTKCTSSAPCK--------TENCKACS----NDKREVCEECNSNNYLTPTSQCIDDCAKIGNYYYTT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 1923 SNNFADGCVlrnGRTQCLCRPGYAGASCERCAPGFFGNplvlGSSCQPCDCSGNGDPNMIFSDC-------------DPL 1989
Cdd:pfam03302 69 NANNKKICK---ECTVANCKTCEDQGQCQACNDGFYKS----GDACSPCHESCKTCSGGTASDCtecltgkalrygnDGT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 1990 TGAC-RGCLRHTTGPHCERCAPGFYGNALlpgnctrcdCSPCGTETCDPQSGRC---------LCKAG-VTGQRCDRCLE 2058
Cdd:pfam03302 142 KGTCgEGCTTGTGAGACKTCGLTIDGTSY---------CSECATETEYPQNGVCtstaarataTCKASsVANGMCSSCAN 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2059 GYfgFEQCQGCRPCA-------CGPAAKGSECHPQSGQCH------------CQPGTTGPQCLECAPGYwgLPEKG-CRR 2118
Cdd:pfam03302 213 GY--FRMNGGCYETTkfpgksvCEEANSGGTCQKEAPGYKlnngdlvtcspgCKTCTSNTVCTTCMDGY--VKTSDsCTK 288
|
330 340 350
....*....|....*....|....*....|...
gi 124487155 2119 CQCPRGHCDPHTGHC-TCPPGL--SGERCDTCS 2148
Cdd:pfam03302 289 CDSSCETCTGATTTCkTCATGYykSGTGCVSCT 321
|
|
| HBM |
pfam16591 |
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in ... |
2349-2511 |
3.03e-03 |
|
Helical bimodular sensor domain; The HBM sensor domain has been identified primarily in bacterial chemoreceptors but is also present on histidine kinases. characteriztic features of this domain are its size of approximately 250 amino acids and its location in the bacterial periplasm. The McpS chemoreceptor of Pseudomonas putida KT2440 was found to possess an HBM sensor domain and its 3D structure in complex with physiologically relevant ligands has been reported. This domain is composed of 2 long and 4 short helices that form two modules each composed of a 4-helix bundle. The McpS chemoreceptor mediates chemotaxis towards a number of organic acids. Both modules of the McpS HBM domain contain a ligand binding site. Chemo-attractants binds to each of these sites and their binding was shown to trigger a chemotactic response. This domain is primarily found in different proteobacteria but also in archaea. Interestingly, amino acids in both ligand binding sites showed a high degree of conservation suggesting that members of this family sense similar ligands. This domain recognizes Multiple TCA cycle intermediates, citrate and alpha-ketoglutarate (Matilla et.al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).
Pssm-ID: 435446 [Multi-domain] Cd Length: 246 Bit Score: 42.38 E-value: 3.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2349 RLMARVQEQLTSFWE-ENQSLATHIRDQLAQYESGLMDLREALNQAvNTTREAEElnsRNQERLKEAL-----QWKQELS 2422
Cdd:pfam16591 47 ELKQQLQQLKTTFTSpENVRLLQEQLQLIQAYRKSFNELRAAYESR-NASRQVMD---SAAERALEAIdqleaEVLQTPE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2423 QDNATLkATLQAASLILGHVSE-------------------LLQGIDQAKEDLEHLAASLDGAWTPLLKRMQafSPASSK 2483
Cdd:pfam16591 123 ADSRRA-AQYQAISELKRQVQMaryqvrgytftpnedseqaAYQQLDAALASLDQLRQALAGDPGAALQQLT--SALQGY 199
|
170 180
....*....|....*....|....*...
gi 124487155 2484 VDLVEAAEAHAQKLNQLAINLSGIILGI 2511
Cdd:pfam16591 200 RDALDTFKAAVAAIEQARQEMTSQGDEI 227
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2218-2740 |
3.47e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2218 QSKLRSPPGPRYQAAQ------QLQTLEQqSISLQQDTERLGSQATGVQGQAGQLLDTTESTLGRAQKLLESVRAVGRAL 2291
Cdd:PRK04863 499 RELLRRLREQRHLAEQlqqlrmRLSELEQ-RLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEA 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2292 NELASRMGQgspgdalvpSGEQLRwalAEVERLL-----W----DMRTRdLGAQgavAEAELAEAQRLMARVQEQLtsfw 2362
Cdd:PRK04863 578 RERRMALRQ---------QLEQLQ---ARIQRLAarapaWlaaqDALAR-LREQ---SGEEFEDSQDVTEYMQQLL---- 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2363 eENQSLATHIRDQLAQYESGLMDLREALNQAvnTTREAEELNsRNQERLKEALqwkqeLS--------QDNATLKATL-Q 2433
Cdd:PRK04863 638 -ERERELTVERDELAARKQALDEEIERLSQP--GGSEDPRLN-ALAERFGGVL-----LSeiyddvslEDAPYFSALYgP 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2434 AASLI----LGHVSELLQGIDQAKEDLEHLAASLDgawtpllkrmqAFSPASSKVDLVEAA------------------- 2490
Cdd:PRK04863 709 ARHAIvvpdLSDAAEQLAGLEDCPEDLYLIEGDPD-----------SFDDSVFSVEELEKAvvvkiadrqwrysrfpevp 777
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2491 ----EAHAQKLNQLAINLSGIILGINQDRF----IQRAVEASNAYSSILQAVQAAEDAAgQALRQASRtwemvvQRglaa 2562
Cdd:PRK04863 778 lfgrAAREKRIEQLRAEREELAERYATLSFdvqkLQRLHQAFSRFIGSHLAVAFEADPE-AELRQLNR------RR---- 846
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2563 gaRQLLANSSALEETIlgHQGRLGLAQGRLQAAGIQLH----NVWARkNQLAAQIQEAQAMLamDTSETSEKiahakava 2638
Cdd:PRK04863 847 --VELERALADHESQE--QQQRSQLEQAKEGLSALNRLlprlNLLAD-ETLADRVEEIREQL--DEAEEAKR-------- 911
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2639 aealstatHVQSQlqgmQKNVERWQSQLGGLQG--QDLSQVERDASSSVSTLEKTLPQLLAkLSRLENRGVH----NASL 2712
Cdd:PRK04863 912 --------FVQQH----GNALAQLEPIVSVLQSdpEQFEQLKQDYQQAQQTQRDAKQQAFA-LTEVVQRRAHfsyeDAAE 978
|
570 580 590
....*....|....*....|....*....|.
gi 124487155 2713 ALSANIGRVRKL---IAQARSAASKVKVSMK 2740
Cdd:PRK04863 979 MLAKNSDLNEKLrqrLEQAEQERTRAREQLR 1009
|
|
| HAMP |
COG2770 |
HAMP domain [Signal transduction mechanisms]; |
2349-2703 |
3.84e-03 |
|
HAMP domain [Signal transduction mechanisms];
Pssm-ID: 442051 [Multi-domain] Cd Length: 631 Bit Score: 43.18 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2349 RLMArvqeqltsfweenQSLATHIRDQLAQYESGLMDLREALNQAVNTTREAEELNSRNQERLKEALQWKQELSQDNATL 2428
Cdd:COG2770 275 NRMA-------------DSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAALLLELLLLLLLALL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2429 KATLQAASLILGHVSELLQGIDQAKEDLEHLAASLDGAWTPLLKRMQAFSPASSKVDLVEAAEAHAQKLNQLAINLSGII 2508
Cdd:COG2770 342 LLLLLAADLLLALALAALLLLLALELLLEAELLVLLALEALALEAELAAVLALLAALAAALLLLELALEELVLALLALAL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2509 LGINQDRFIQRAVEASNAYSSILQAVQAAEDAAGQALRQASRTWEMVVQRGLAAGARQLLANSSALEETILGHQGRLGLA 2588
Cdd:COG2770 422 LALAAAAAAAEAAAAALELAAAAIAAAAAAEAEGGLAELEAEELVAAAEALLLLAALLLLAALGALELLLLEEEEEAGAA 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2589 QGRLQAAGIQLHNVWARKNQLAAQIQEAQAMLAMDTSETSEKIAHAKAVAAEALSTATHVQSQLQGMQKNVERWQSQLGG 2668
Cdd:COG2770 502 AEELAEELLLLEGLLLLLLLEAEALEVAEELLELEEAALLLAAAAELAALLALLLALAAVEAAALLLAALLLAAVAALLE 581
|
330 340 350
....*....|....*....|....*....|....*
gi 124487155 2669 LQGQDLSQVERDASSSVSTLEKTLPQLLAKLSRLE 2703
Cdd:COG2770 582 LAALLLLLLAAAEALAALELELAAAAEAALAEAEL 616
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
2349-2508 |
5.03e-03 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 42.41 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2349 RLMARVQEQLTSFWEENQSLATHIRDQLAQYESGLMDLR--------EALNQAVNTTREAEELNSRNQERLKEALQWKQE 2420
Cdd:PRK13428 28 RLMAARQDTVRQQLAESATAADRLAEADQAHTKAVEDAKaeaarvveEAREDAERIAEQLRAQADAEAERIKVQGARQVQ 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2421 LSQDNAT--------LKATLQAASLILGHVSELLQ---GIDQAKEDLEHLAASLDGAWTPLLKRMQAFSpASSKVDLVE- 2488
Cdd:PRK13428 108 LLRAQLTrqlrlelgHESVRQAGELVRNHVADPAQqsaTVDRFLDELDAMAPSTADVDYPLLAKMRSAS-RRALASLVDr 186
|
170 180
....*....|....*....|....
gi 124487155 2489 ----AAEAHAQKLNQLAINLSGII 2508
Cdd:PRK13428 187 fdsvAADLDNQALTTLADELVSVA 210
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2168-2424 |
6.58e-03 |
|
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: 42.63 E-value: 6.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2168 VCDHCVVLLLDDLEragALLPAIREQLQGINAssaawaRLHRLNASIADLQSKLRsppgpryQAAQQLQTLEqqsislqq 2247
Cdd:COG3096 822 VGGHLAVAFAPDPE---AELAALRQRRSELER------ELAQHRAQEQQLRQQLD-------QLKEQLQLLN-------- 877
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2248 dterlgsqatGVQGQAGQLLDTT--------ESTLGRAQKLLESVRAVGRALNELASRMG--QGSPgdalvPSGEQLRwa 2317
Cdd:COG3096 878 ----------KLLPQANLLADETladrleelREELDAAQEAQAFIQQHGKALAQLEPLVAvlQSDP-----EQFEQLQ-- 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2318 lAEVERLlwDMRTRDLGAQGAVaeaelaeaqrlMARVQEQLTSF-WE-------ENQSLATHIRDQLAQYESGLMDLREA 2389
Cdd:COG3096 941 -ADYLQA--KEQQRRLKQQIFA-----------LSEVVQRRPHFsYEdavgllgENSDLNEKLRARLEQAEEARREAREQ 1006
|
250 260 270
....*....|....*....|....*....|....*..
gi 124487155 2390 LNQAvnttreAEELNSRNQER--LKEALQWKQELSQD 2424
Cdd:COG3096 1007 LRQA------QAQYSQYNQVLasLKSSRDAKQQTLQE 1037
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2572-2737 |
6.76e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 6.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2572 SALEETILGHQGRLGLAQGRLQAAGIQLHNVWARKNQLAAQIQEAQAMLamdtSETSEKIAHAKAVAAEALSTATHVQSQ 2651
Cdd:COG4372 27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSEL----EQLEEELEELNEQLQAAQAELAQAQEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2652 LQGMQKNVERWQSQLGGLQGQ--DLSQVERDASSSVSTLEKTLPQLLAKLSRLENR-----------GVHNASLALSANI 2718
Cdd:COG4372 103 LESLQEEAEELQEELEELQKErqDLEQQRKQLEAQIAELQSEIAEREEELKELEEQleslqeelaalEQELQALSEAEAE 182
|
170
....*....|....*....
gi 124487155 2719 GRVRKLIAQARSAASKVKV 2737
Cdd:COG4372 183 QALDELLKEANRNAEKEEE 201
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2355-2459 |
8.34e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 40.58 E-value: 8.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2355 QEQLTsfwEENQSLATHIRDQlAQYEsglMDLREALNQAVNTTREAEELNSRNQERL-KEALQWKQELSQDNATLKATLQ 2433
Cdd:COG1842 36 EEDLV---EARQALAQVIANQ-KRLE---RQLEELEAEAEKWEEKARLALEKGREDLaREALERKAELEAQAEALEAQLA 108
|
90 100
....*....|....*....|....*.
gi 124487155 2434 AASlilGHVSELLQGIDQAKEDLEHL 2459
Cdd:COG1842 109 QLE---EQVEKLKEALRQLESKLEEL 131
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
1874-1981 |
8.60e-03 |
|
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; TNFRSF4 (also known as OX40, ACT35, CD134, IMD16, TXGP1L) activates NF-kappaB through its interaction with adaptor proteins TRAF2 and TRAF5. It also promotes the expression of apoptosis inhibitors BCL2 and BCL2lL1/BCL2-XL, and thus suppresses apoptosis. It is primarily expressed on activated CD4+ and CD8+ T cells, where it is transiently expressed and upregulated on the most recently antigen-activated T cells within inflammatory lesions. This makes it an attractive target to modulate immune responses, i.e. TNFRSF4 (OX40) blocking agents to inhibit adverse inflammation or agonists to enhance immune responses. An artificially created biologic fusion protein, OX40-immunoglobulin (OX40-Ig), prevents OX40 from reaching the T-cell receptors, thus reducing the T-cell response. Some single nucleotide polymorphisms (SNPs) of its natural ligand OX40 ligand (OX40L, CD252), which is also found on activated T cells, have been associated with systemic lupus erythematosus.
Pssm-ID: 276911 [Multi-domain] Cd Length: 142 Bit Score: 39.69 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 1874 CLPGSGICVGCQHNTEgDQCERCRPGFVSSDPS-NPASPCVSCpcplavpsNNFADGCVLRN----GRTQCLCRPGY--- 1945
Cdd:cd13406 18 CPPGEGMESRCTGTQD-TVCSPCEPGFYNEAVNyEPCKPCTQC--------NQRSGSEEKQKctktSDTVCRCRPGTqpl 88
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 124487155 1946 ----AGASCERCAPGFFGNPlvLGSSCQP-CDCSGNGDPNM 1981
Cdd:cd13406 89 dsykPGVDCVPCPPGHFSRG--DNQACKPwTNCSLAGKRTL 127
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2199-2590 |
9.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2199 ASSAAWA--RLHRLNASIADLQSKLRsppgpryQAAQQLQTLEQQSISLQQDTERLGSQATGVQGQAGQL---LDTTEST 2273
Cdd:COG3883 8 APTPAFAdpQIQAKQKELSELQAELE-------AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLqaeIAEAEAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2274 LGRAQKLL-ESVRAV---GRALNELASRMGQGSPGDALvpsgeqlrwalaeverllwdmrtrdlgaqgavaeaelaeaQR 2349
Cdd:COG3883 81 IEERREELgERARALyrsGGSVSYLDVLLGSESFSDFL----------------------------------------DR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2350 LMARvqeqltsfweenqslathirDQLAQYEsglmdlREALNQAVNTTREAEELNSRNQERLKEALQWKQELSQDNATLK 2429
Cdd:COG3883 121 LSAL--------------------SKIADAD------ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2430 ATLQAASLILghvSELLQGIDQAKEDLEHLAASLDGAWTPLLKRMQAF---SPASSKVDLVEAAEAHAQKLNQLAINLSG 2506
Cdd:COG3883 175 AQQAEQEALL---AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAaaaAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 124487155 2507 IILGINQDRFIQRAVEASNAYSSILQAVQAAEDAAGQALRQASRTWEMVVQRGLAAGARQLLANSSALEETILGHQGRLG 2586
Cdd:COG3883 252 AGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAGGVGSGGGAGAVVGGASAGGG 331
|
....
gi 124487155 2587 LAQG 2590
Cdd:COG3883 332 GGSG 335
|
|
| |
