|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
238-439 |
4.85e-68 |
|
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: 230.38 E-value: 4.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 238 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 317
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 318 TQSAKELDVKIKNVIRNVH--------------------------------------------------------MLNRI 341
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKeinekvatlgendfalpssdlsrmlaeaqrmlgeirsrdfgtqlqnaeaelkaaqdLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 342 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 421
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 732170495 422 ADSSLLQTNIALQLMEKS 439
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
623-751 |
5.90e-43 |
|
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: 153.41 E-value: 5.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 623 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 693
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 732170495 694 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 751
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1493-1644 |
2.79e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 132.16 E-value: 2.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1493 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 1571
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732170495 1572 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVN 1644
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1516-1645 |
1.21e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 115.13 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1516 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 1593
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 732170495 1594 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNH 1645
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1329-1469 |
2.24e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 115.21 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1329 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 1406
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732170495 1407 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 1469
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1521-1646 |
2.75e-29 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 114.05 E-value: 2.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1521 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 1600
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 732170495 1601 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHI 1646
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
1346-1471 |
2.45e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 105.88 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1346 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 1422
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 732170495 1423 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 1471
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
937-1077 |
1.30e-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: 104.42 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 937 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 1013
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170495 1014 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 1077
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
956-1077 |
6.09e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 93.17 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 956 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 1032
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 732170495 1033 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 1077
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1353-1471 |
2.88e-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: 90.94 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1353 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 1429
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 732170495 1430 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 1471
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1104-1236 |
6.41e-21 |
|
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: 90.94 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1104 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGP-IFKSPQTYMD 1180
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732170495 1181 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 1236
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
1129-1238 |
1.15e-15 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.07 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1129 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 1204
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 732170495 1205 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 1238
Cdd:smart00282 83 VSGESPGGltILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
77-123 |
5.58e-15 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 70.46 E-value: 5.58e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170495 77 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 123
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
963-1077 |
8.68e-15 |
|
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: 72.45 E-value: 8.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 963 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 1041
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 732170495 1042 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 1077
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
125-175 |
5.56e-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: 67.76 E-value: 5.56e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170495 125 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 175
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
124-176 |
4.05e-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: 65.07 E-value: 4.05e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 732170495 124 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 176
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
78-125 |
5.25e-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: 64.68 E-value: 5.25e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170495 78 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 125
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
125-175 |
1.46e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 63.48 E-value: 1.46e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170495 125 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPqkfGGSC 175
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
229-676 |
1.62e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 72.75 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQV 302
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 303 NSRKAQTLNNNVNRATQSAKELDVKIKNV---IRNVHMLNRIRTWQ-KTHQGENNGLANSIRDSLNEYE---AKLSDLRA 375
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETIIknnSEIKDLTN 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 376 RLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQ 455
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 456 ELS-------DKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaa 528
Cdd:TIGR04523 528 KLEsekkekeSKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT----------------QKSLKK--------- 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 529 nraasaSESALQTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLT 602
Cdd:TIGR04523 583 ------KQEEKQELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 603 TLRDGLHGIqrgdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DF 663
Cdd:TIGR04523 656 EIRNKWPEI--------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEF 726
|
490
....*....|...
gi 732170495 664 KKALTDADNSVNK 676
Cdd:TIGR04523 727 SKELENIIKNFNK 739
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
229-522 |
9.39e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQ 308
Cdd:COG1196 220 EELKELEAELLLLKLRE-LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 309 TLNNNVNRATQSAKELDVKIKNVIRnvhmlnRIRTWQKTHQGENNGLAnSIRDSLNEYEAKLSDLRARLQEAAAQAKQAN 388
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEE------ELAELEEELEELEEELE-ELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 389 GLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSA 468
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 732170495 469 GKtsLVEEAEKHARSLQELAKQLEEIKrnASGDELVRCAVDAATAYENILNAIK 522
Cdd:COG1196 452 AE--LEEEEEALLELLAELLEEAALLE--AALAELLEELAEAAARLLLLLEAEA 501
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
78-120 |
1.26e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 1.26e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 732170495 78 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 120
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
725-903 |
4.54e-11 |
|
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: 62.82 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 725 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 804
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 805 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 878
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 732170495 879 PPDFKLPSRLSFPPYKGCIELDDLN 903
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
770-905 |
5.15e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 61.97 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 770 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 843
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732170495 844 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 905
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
394-711 |
1.55e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 394 NERALGAIQRQvKEINSLQSDFTKylttADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKtsL 473
Cdd:TIGR02168 666 AKTNSSILERR-REIEELEEKIEE----LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR--L 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 474 VEEAEKHARSLQELAKQLEEI---------KRNASGDELVRCAVDAATAYENIlNAIKAAEDAANRAASASESALQTVIK 544
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELeaeieeleeRLEEAEEELAEAEAEIEELEAQI-EQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 545 E--DLPRKAKTLSSNSDKLLNEAKMTQKKLKQ------EVSPALNNLQQT-------LNIVTVQKEVIDTNLTTLRDglh 609
Cdd:TIGR02168 818 EaaNLRERLESLERRIAATERRLEDLEEQIEElsedieSLAAEIEELEELieeleseLEALLNERASLEEALALLRS--- 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 610 giQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQ---NEDFKKALTDADNSVNKLTNKLPDLWR 686
Cdd:TIGR02168 895 --ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlSEEYSLTLEEAEALENKIEDDEEEARR 972
|
330 340
....*....|....*....|....*
gi 732170495 687 KIESINQQLLPLGNIsdNMDRIREL 711
Cdd:TIGR02168 973 RLKRLENKIKELGPV--NLAAIEEY 995
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
247-724 |
2.13e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 247 LLEQMRHMetqakdLRNQLLNYRSAISN-HGSKIEGLERELTDLNQEFETLQEKAQVNSRKA---QTLNNNVNRATQSAK 322
Cdd:COG4717 39 LLAFIRAM------LLERLEKEADELFKpQGRKPELNLKELKELEEELKEAEEKEEEYAELQeelEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 323 ELDVKIKNVirnVHMLNRIRTWQKTHQgennglansIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQ 402
Cdd:COG4717 113 ELREELEKL---EKLLQLLPLYQELEA---------LEAELAELPERLEELEERL--------------EELRELEEELE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 403 RQVKEINSLQSDFTKYLTtadsslLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAR 482
Cdd:COG4717 167 ELEAELAELQEELEELLE------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 483 SLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAI----------------KAAEDAANRAASASESALQTVIKED 546
Cdd:COG4717 241 LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallflllarEKASLGKEAEELQALPALEELEEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 547 LPRKAKTL---SSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEvidtnlttLRDGLHGIQRGDIDAMISSA 623
Cdd:COG4717 321 LEELLAALglpPDLSPEELLELLDRIEELQELLR-EAEELEEELQLEELEQE--------IAALLAEAGVEDEEELRAAL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 624 K------SMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKLTNKLpdlwRKIESINQQLLP 697
Cdd:COG4717 392 EqaeeyqELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL----AELEAELEQLEE 467
|
490 500
....*....|....*....|....*..
gi 732170495 698 LGNISDNMDRIRELIQQARDAASKVAV 724
Cdd:COG4717 468 DGELAELLQELEELKAELRELAEEWAA 494
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
244-717 |
2.96e-09 |
|
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: 62.11 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 244 SAGLLEQMRHMETQAKDLRNQLLNYRSAISN-HGSKIEgLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAK 322
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKlQLEKVT-TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 323 ELDVKIKNV--IRNVH------MLNRIRTWQKTHQG-ENN-----GLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQAN 388
Cdd:pfam01576 170 EEEEKAKSLskLKNKHeamisdLEERLKKEEKGRQElEKAkrkleGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 389 GLNQENERALGAIQRQVKE----INSLQSDFtkylttaDSSLLQTNIALQLMEKSQKEYEKLAASLNE------ARQELS 458
Cdd:pfam01576 250 ARLEEETAQKNNALKKIREleaqISELQEDL-------ESERAARNKAEKQRRDLGEELEALKTELEDtldttaAQQELR 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 459 DK----VRELSRSAGKTSLVEEAE------KHARSLQELAKQLEEIKRNASGDELVRCAVDAATA-YENILNAIKAAEDA 527
Cdd:pfam01576 323 SKreqeVTELKKALEEETRSHEAQlqemrqKHTQALEELTEQLEQAKRNKANLEKAKQALESENAeLQAELRTLQQAKQD 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 528 ANRAASASESALQTV---------IKEDLPRKAKTLSSNSDK---LLNEAKMTQKKLKQEVSPALNNLQQT---LNIVTV 592
Cdd:pfam01576 403 SEHKRKKLEGQLQELqarlseserQRAELAEKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQDTqelLQEETR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 593 QKEVIDTNLTTLRDGLHGIQrgdidamissaksmvrkanditdEVLDGLNPIQTDVERIKDTYgRTQNEDFKKALTDADN 672
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQ-----------------------EQLEEEEEAKRNVERQLSTL-QAQLSDMKKKLEEDAG 538
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 732170495 673 SVNKLTNKLPDLWRKIESINQQLLPLGNISDNMDRIRELIQQARD 717
Cdd:pfam01576 539 TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELD 583
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1132-1236 |
1.16e-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: 55.12 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1132 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGGP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 1206
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 732170495 1207 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 1236
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
247-687 |
1.80e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 247 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNVNRATQSAK--- 322
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLEGSKRKLEEKire 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 323 ------ELDVKIKNVIRNVHMLNRIRtWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENER 396
Cdd:PRK03918 264 leerieELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 397 ALGAIQRQVKEINSLQSDFTKY------LTTADSslLQTNIALQLMEKSQKEYEKLA-----------------ASLNEA 453
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYeeakakKEELER--LKKRLTGLTPEKLEKELEELEkakeeieeeiskitariGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 454 RQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQELAKQLEEIKRNASGDELVRCAVDAATAYEN 516
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 517 ILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEV 596
Cdd:PRK03918 501 LAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 597 IDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQTDVERIKDTYGRTQNE--DFKKALTDADNSV 674
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEEldKAFEELAETEKRL 642
|
490
....*....|...
gi 732170495 675 NKLTNKLPDLWRK 687
Cdd:PRK03918 643 EELRKELEELEKK 655
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
220-493 |
4.76e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 220 LLNDLATMGEQLRLVKSQLQGLSASAGLLEQmRHMETQ-AKDLRNQLLNYRSAISnhGSKIEGLERELTDLNQEFETLQE 298
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEeAKAKKEELERLKKRLT--GLTPEKLEKELEELEKAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 299 K-AQVNSRKAQtLNNNVNRATQSAKELdvkiKNVIRNVHMLNRIRTwqKTHQGEnnglansirdSLNEYEAKLSDLRARL 377
Cdd:PRK03918 406 EiSKITARIGE-LKKEIKELKKAIEEL----KKAKGKCPVCGRELT--EEHRKE----------LLEEYTAELKRIEKEL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 378 QEAAaqakqanglnqENERALGAIQRQVKEINSLQSDFTKYLTTAD------SSLLQTNiaLQLMEKSQKEYEKLAASLN 451
Cdd:PRK03918 469 KEIE-----------EKERKLRKELRELEKVLKKESELIKLKELAEqlkeleEKLKKYN--LEELEKKAEEYEKLKEKLI 535
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 732170495 452 EARQELSDKVRELSRSAG----KTSLVEEAEKHARSLQELAKQLEE 493
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEElkkkLAELEKKLDELEEELAELLKELEE 581
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
72-193 |
2.53e-06 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 49.22 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 72 TGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtnsfatgcvvNGGDVRCSC 148
Cdd:cd13416 51 TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP-----------PGQGVVQSC 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 732170495 149 KAGyTGTQCERCAPGYFGNPQKFGGSCQPCS-CNSNG-QLGSCHPLT 193
Cdd:cd13416 110 GPN-QDTVCEACPEGTYSDEDSSTDPCLPCTvCEDGEvELRECTPVS 155
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
772-898 |
7.45e-05 |
|
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: 43.95 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 772 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 847
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 732170495 848 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 898
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
427-591 |
1.53e-04 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 43.85 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 427 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 504
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 505 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 579
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 732170495 580 LNNLQQTLNIVT 591
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
426-522 |
3.11e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 426 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 499
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 732170495 500 GDELvrcavdaATAYENILNAIK 522
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
238-439 |
4.85e-68 |
|
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: 230.38 E-value: 4.85e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 238 LQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRA 317
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 318 TQSAKELDVKIKNVIRNVH--------------------------------------------------------MLNRI 341
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKeinekvatlgendfalpssdlsrmlaeaqrmlgeirsrdfgtqlqnaeaelkaaqdLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 342 RTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTT 421
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 732170495 422 ADSSLLQTNIALQLMEKS 439
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
623-751 |
5.90e-43 |
|
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: 153.41 E-value: 5.90e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 623 AKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNE---------DFKKALTDADNSVNKLTNKLPDLWRKIESINQ 693
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 732170495 694 QLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSL 751
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1493-1644 |
2.79e-35 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 132.16 E-value: 2.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1493 GIYFSEeGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSL 1571
Cdd:cd00110 1 GVSFSG-SSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNGGdFLALELEDGRLVLRYDLGSG--SLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732170495 1572 CDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVN 1644
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
1516-1645 |
1.21e-29 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 115.13 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1516 KLVFSIRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGGTSTSVTPKQsLCDGQWHSVAVTIKQHILHLELD- 1593
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGGGdYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDg 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 732170495 1594 TDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNH 1645
Cdd:smart00282 80 GNRVSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1329-1469 |
2.24e-29 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 115.21 E-value: 2.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1329 TSHLLFKLPQeLLKPRSQFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTV 1406
Cdd:cd00110 7 SSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSQNggDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWHSV 85
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732170495 1407 VFGHDGEKGRLVVDGLR-AREGSLPGNSTISIRAPVYLG-SPPSGKPKSLP-TNSFVGCLKNFQLD 1469
Cdd:cd00110 86 SVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGgLPEDLKSPGLPvSPGFVGCIRDLKVN 151
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1521-1646 |
2.75e-29 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 114.05 E-value: 2.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1521 IRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKqSLCDGQWHSVAVTIKQHILHLELDTDSSYTA 1600
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGK-NLNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 732170495 1601 GQIPFPPA-STQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHI 1646
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
1346-1471 |
2.45e-26 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 105.88 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1346 QFAVDMQTTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSK-EKCNDGKWHTVVFGHDGEKGRLVVDGL 1422
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSKGggDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 732170495 1423 RAREGSLPGNSTI-SIRAPVYLGSPPSG--KPKSLPTNSFVGCLKNFQLDSK 1471
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEDlkLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
937-1077 |
1.30e-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: 104.42 E-value: 1.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 937 YFEGTGYARVPT-QPHAPIPTFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERgVGDAINNGR 1013
Cdd:cd00110 3 SFSGSSYVRLPTlPAPRTRLSISFSFRTTSPNGLLLYAgsQNGGDFLALELEDGRLVLRYDLGSGSLVLS-SKTPLNDGQ 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170495 1014 DHSIQIKIGKLQKRMWINVDVQNTIIDGE----VFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLK 1077
Cdd:cd00110 82 WHSVSVERNGRSVTLSVDGERVVESGSPGgsalLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| LamG |
smart00282 |
Laminin G domain; |
956-1077 |
6.09e-22 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 93.17 E-value: 6.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 956 TFGQTIQTTVDRGLLFFA--ENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINV- 1032
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 732170495 1033 DVQNTIIDGEVFDFST---YYLGGIPIAIRERFNISTPAFRGCMKNLK 1077
Cdd:smart00282 81 NRVSGESPGGLTILNLdgpLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1353-1471 |
2.88e-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: 90.94 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1353 TTSSRGLVFHTG-TKNSFMALYLSKGRLVFA--LGTDGKKLRIkSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSL 1429
Cdd:pfam02210 3 TRQPNGLLLYAGgGGSDFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 732170495 1430 PGNS-TISIRAPVYLG--SPPSGKPKSLPTNSFVGCLKNFQLDSK 1471
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
1104-1236 |
6.41e-21 |
|
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: 90.94 E-value: 6.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1104 SASFSRGGQLSFTDLGLPPTdHLQASFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGP-IFKSPQTYMD 1180
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPRT-RLSISFSFRTTSPNGLLLYAGSQNGGdfLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732170495 1181 GLLHYVSVISDNSGLRLLIDD-QLLRNSKRLKH-ISSSRQSLRLGG-------------SNFEGCISNVFV 1236
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGeRVVESGSPGGSaLLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1353-1473 |
1.70e-18 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 83.14 E-value: 1.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1353 TTSSRGLVFHTGTKN--SFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGS-- 1428
Cdd:pfam00054 3 TTEPSGLLLYNGTQTerDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGEsp 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 732170495 1429 LPGNSTISIRAPVYLGSPPSGKPKSLPTN---SFVGCLKNFQLDSKPL 1473
Cdd:pfam00054 83 LGATTDLDVDGPLYVGGLPSLGVKKRRLAispSFDGCIRDVIVNGKPL 130
|
|
| LamG |
smart00282 |
Laminin G domain; |
1129-1238 |
1.15e-15 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.07 E-value: 1.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1129 SFGFQTFQPSGILLDHQTWTRN--LQVTLEDGYIELSTSDSGGPIFKSPQ--TYMDGLLHYVSVISDNSGLRLLIDDQLL 1204
Cdd:smart00282 3 SFSFRTTSPNGLLLYAGSKGGGdyLALELRDGRLVLRYDLGSGPARLTSDptPLNDGQWHRVAVERNGRSVTLSVDGGNR 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 732170495 1205 RNSKRLKH--ISSSRQSLRLGG-------------SNFEGCISNVFVQR 1238
Cdd:smart00282 83 VSGESPGGltILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNG 131
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
77-123 |
5.58e-15 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 70.46 E-value: 5.58e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170495 77 PCNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG-SCR 123
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
963-1077 |
8.68e-15 |
|
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: 72.45 E-value: 8.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 963 TTVDRGLLFFAENGDR-FISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDG 1041
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 732170495 1042 EVFDF----STYYLGGIPIAIRERFNISTPAFRGCMKNLK 1077
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
1521-1648 |
1.59e-14 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 71.96 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1521 IRPRSLTGILIHIGSQPGK-HLCVYLEAGKVTASMDSGAGgtSTSVTPKQSLCDGQWHSVAVTIKQHILHLELD------ 1593
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTERdFLALELRDGRLEVSYDLGSG--AAVVRSGDKLNDGKWHSVELERNGRSGTLSVDgearpt 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 732170495 1594 -TDSSYTAGQIPFPpastqEPLHLGGAPANLTTLRI-PVWKSFFGCLRNIHVNHIPV 1648
Cdd:pfam00054 79 gESPLGATTDLDVD-----GPLYVGGLPSLGVKKRRlAISPSFDGCIRDVIVNGKPL 130
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
125-175 |
5.56e-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: 67.76 E-value: 5.56e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170495 125 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKFGGSC 175
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
124-176 |
4.05e-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: 65.07 E-value: 4.05e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 732170495 124 ACPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPQKfGGSCQ 176
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
78-125 |
5.25e-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: 64.68 E-value: 5.25e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170495 78 CNCNGH---SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAvHGSCRAC 125
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLP-SDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
125-175 |
1.46e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 63.48 E-value: 1.46e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 732170495 125 CPCPHTNSFATGCVVNGGdvRCSCKAGYTGTQCERCAPGYFGNPqkfGGSC 175
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG---PPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
229-676 |
1.62e-12 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 72.75 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKSQLQGLS--ASAGLL----EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQV 302
Cdd:TIGR04523 288 KQLNQLKSEISDLNnqKEQDWNkelkSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 303 NSRKAQTLNNNVNRATQSAKELDVKIKNV---IRNVHMLNRIRTWQ-KTHQGENNGLANSIRDSLNEYE---AKLSDLRA 375
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETIIknnSEIKDLTN 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 376 RLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQ 455
Cdd:TIGR04523 448 QDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 456 ELS-------DKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNasgdelvrcavdaataYENILNaikaaedaa 528
Cdd:TIGR04523 528 KLEsekkekeSKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQT----------------QKSLKK--------- 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 529 nraasaSESALQTVIKE------DLPRKAKTLSSNSDKLLNEAKMTQKKlKQEVSPALNNLQQTLNIVTVQKEVIDTNLT 602
Cdd:TIGR04523 583 ------KQEEKQELIDQkekekkDLIKEIEEKEKKISSLEKELEKAKKE-NEKLSSIIKNIKSKKNKLKQEVKQIKETIK 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 603 TLRDGLHGIqrgdidamISSAKSMVRKANDITDEVLDGLN--------------PIQtDVERIKDTYGRTQNE-----DF 663
Cdd:TIGR04523 656 EIRNKWPEI--------IKKIKESKTKIDDIIELMKDWLKelslhykkyitrmiRIK-DLPKLEEKYKEIEKElkkldEF 726
|
490
....*....|...
gi 732170495 664 KKALTDADNSVNK 676
Cdd:TIGR04523 727 SKELENIIKNFNK 739
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
229-522 |
9.39e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 70.35 E-value: 9.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQ 308
Cdd:COG1196 220 EELKELEAELLLLKLRE-LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 309 TLNNNVNRATQSAKELDVKIKNVIRnvhmlnRIRTWQKTHQGENNGLAnSIRDSLNEYEAKLSDLRARLQEAAAQAKQAN 388
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEE------ELAELEEELEELEEELE-ELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 389 GLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSA 468
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 732170495 469 GKtsLVEEAEKHARSLQELAKQLEEIKrnASGDELVRCAVDAATAYENILNAIK 522
Cdd:COG1196 452 AE--LEEEEEALLELLAELLEEAALLE--AALAELLEELAEAAARLLLLLEAEA 501
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
78-120 |
1.26e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 60.79 E-value: 1.26e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 732170495 78 CNCN--GH-SNQCQDGSGICVnCQHNTAGEHCERCQEGYYGNAVHG 120
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
725-903 |
4.54e-11 |
|
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: 62.82 E-value: 4.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 725 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPNSrENGgtenmFVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREA 804
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTTS-PNG-----LLLYAGSQNGG-DFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 805 ELQvdqiltkseTKEAVMD----RVKFQRIYQFARL--NYTKGATSSKPETpgvydmdgrnsNTLLNLDPEnvvFYVGGY 878
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSPGG-----------SALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 732170495 879 PPDFKLPSRLSFPPYKGCIELDDLN 903
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
770-905 |
5.15e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 61.97 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 770 FVMYLGNKDASrDYIGMAVVDGQLTCVYNLGDREAELQVDQiltksetkEAVMD----RVKFQRIYQFARL--NYTKGAT 843
Cdd:smart00282 14 LLLYAGSKGGG-DYLALELRDGRLVLRYDLGSGPARLTSDP--------TPLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732170495 844 SSKPEtpgvydmdgrnSNTLLNLDPEnvvFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNEN 905
Cdd:smart00282 85 GESPG-----------GLTILNLDGP---LYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
220-489 |
5.98e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 220 LLNDLA------TMGEQLRlVKSQLQGLSASAGLLE-QMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQE 292
Cdd:TIGR02169 273 LLEELNkkikdlGEEEQLR-VKEKIGELEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 293 FETLQEkaQVNSRKaQTLNNNVNRATQSAKELD---VKIKNVIRNVHMLNRIRTWQKTHQGENNGLANSIRDSLNEYEAK 369
Cdd:TIGR02169 352 RDKLTE--EYAELK-EELEDLRAELEEVDKEFAetrDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 370 LSDLRARLqeaaaqakqaNGLNQENERALGAIQRQVKEINSLQSDftkylttadssllqtnialqlMEKSQKEYEKLAAS 449
Cdd:TIGR02169 429 IAGIEAKI----------NELEEEKEDKALEIKKQEWKLEQLAAD---------------------LSKYEQELYDLKEE 477
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 732170495 450 LNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAK 489
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLK 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
222-494 |
1.07e-10 |
|
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: 67.00 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 222 NDLATMGEQLRLVKSQLQGLSASAGLLEQMRH--------METQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEF 293
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEqlrkeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEI 763
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 294 ETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHMLNRIRTwqkthqgENNGLANSIRDSLNEYEAKLSDL 373
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT-------LLNEEAANLRERLESLERRIAAT 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 374 RARLQEaaaqakqangLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEA 453
Cdd:TIGR02168 837 ERRLED----------LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELREL 906
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 732170495 454 RQELSDKVRELSRSagKTSLVEEAEKHARSLQELAKQLEEI 494
Cdd:TIGR02168 907 ESKRSELRRELEEL--REKLAQLELRLEGLEVRIDNLQERL 945
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
249-722 |
1.12e-10 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 66.58 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 249 EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLqekaqvNSRKAQTLNNNVNRATQSAK----EL 324
Cdd:TIGR04523 253 TQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDL------NNQKEQDWNKELKSELKNQEkkleEI 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 325 DVKIKNVIRNVHMLNR----IRTWQKTHQGENnglaNSIRDSLNEYEAKLSDlrarlqeaaaqakqangLNQENERALGA 400
Cdd:TIGR04523 327 QNQISQNNKIISQLNEqisqLKKELTNSESEN----SEKQRELEEKQNEIEK-----------------LKKENQSYKQE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 401 IQRQVKEINSLQSDFTKYltTADSSLLQTNIALQLMEKS--QKEYEKLAASLNEARQELSDKVRElsrsagKTSLVEEAE 478
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQ--EKLNQQKDEQIKKLQQEKEllEKEIERLKETIIKNNSEIKDLTNQ------DSVKELIIK 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 479 KHARSLQELAKQLEEIKRNasgdelvrcavdaatayeniLNAIKAAEDAANRAASASESALQTVIKE--DLPRKAKTLSS 556
Cdd:TIGR04523 458 NLDNTRESLETQLKVLSRS--------------------INKIKQNLEQKQKELKSKEKELKKLNEEkkELEEKVKDLTK 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 557 NSDKLLNeakmTQKKLKQEVSpalnnlQQTLNIVTVQKEVI--DTNLTtlRDGLHGIQRGdIDAMISSAK---SMVRKAN 631
Cdd:TIGR04523 518 KISSLKE----KIEKLESEKK------EKESKISDLEDELNkdDFELK--KENLEKEIDE-KNKEIEELKqtqKSLKKKQ 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 632 DITDEVLDGLNPIQTDVERIKDTYGRTQNEdFKKALTDADNSVNKLTNKLPDLWRKIESINQQllpLGNISDNMDRIR-- 709
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISS-LEKELEKAKKENEKLSSIIKNIKSKKNKLKQE---VKQIKETIKEIRnk 660
|
490
....*....|....*
gi 732170495 710 --ELIQQARDAASKV 722
Cdd:TIGR04523 661 wpEIIKKIKESKTKI 675
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
229-602 |
4.91e-10 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 63.38 E-value: 4.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEkaqvnsrKAQ 308
Cdd:COG4372 11 ARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEE-------ELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 309 TLNNNVNRATQSAKELDVKIKNVirnvhmlnrirtwqkthQGEnnglANSIRDSLNEYEAKLSDLRARlqeaaaqakqAN 388
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESL-----------------QEE----AEELQEELEELQKERQDLEQQ----------RK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 389 GLNQENERALGAIQRQVKEINSLQSDFTKylttadsslLQTNIalqlmEKSQKEYEKLaaSLNEARQELSDKVRELSRSA 468
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLES---------LQEEL-----AALEQELQAL--SEAEAEQALDELLKEANRNA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 469 GKTSLVEEAEKHARSLQELAKQLEEIKRNAsgDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLP 548
Cdd:COG4372 197 EKEEELAEAEKLIESLPRELAEELLEAKDS--LEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTE 274
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 732170495 549 RKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLT 602
Cdd:COG4372 275 EEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
394-711 |
1.55e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 63.15 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 394 NERALGAIQRQvKEINSLQSDFTKylttADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKtsL 473
Cdd:TIGR02168 666 AKTNSSILERR-REIEELEEKIEE----LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR--L 738
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 474 VEEAEKHARSLQELAKQLEEI---------KRNASGDELVRCAVDAATAYENIlNAIKAAEDAANRAASASESALQTVIK 544
Cdd:TIGR02168 739 EAEVEQLEERIAQLSKELTELeaeieeleeRLEEAEEELAEAEAEIEELEAQI-EQLKEELKALREALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 545 E--DLPRKAKTLSSNSDKLLNEAKMTQKKLKQ------EVSPALNNLQQT-------LNIVTVQKEVIDTNLTTLRDglh 609
Cdd:TIGR02168 818 EaaNLRERLESLERRIAATERRLEDLEEQIEElsedieSLAAEIEELEELieeleseLEALLNERASLEEALALLRS--- 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 610 giQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQ---NEDFKKALTDADNSVNKLTNKLPDLWR 686
Cdd:TIGR02168 895 --ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlSEEYSLTLEEAEALENKIEDDEEEARR 972
|
330 340
....*....|....*....|....*
gi 732170495 687 KIESINQQLLPLGNIsdNMDRIREL 711
Cdd:TIGR02168 973 RLKRLENKIKELGPV--NLAAIEEY 995
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
247-724 |
2.13e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 2.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 247 LLEQMRHMetqakdLRNQLLNYRSAISN-HGSKIEGLERELTDLNQEFETLQEKAQVNSRKA---QTLNNNVNRATQSAK 322
Cdd:COG4717 39 LLAFIRAM------LLERLEKEADELFKpQGRKPELNLKELKELEEELKEAEEKEEEYAELQeelEELEEELEELEAELE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 323 ELDVKIKNVirnVHMLNRIRTWQKTHQgennglansIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQ 402
Cdd:COG4717 113 ELREELEKL---EKLLQLLPLYQELEA---------LEAELAELPERLEELEERL--------------EELRELEEELE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 403 RQVKEINSLQSDFTKYLTtadsslLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHAR 482
Cdd:COG4717 167 ELEAELAELQEELEELLE------QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 483 SLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAI----------------KAAEDAANRAASASESALQTVIKED 546
Cdd:COG4717 241 LEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLflvlgllallflllarEKASLGKEAEELQALPALEELEEEE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 547 LPRKAKTL---SSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEvidtnlttLRDGLHGIQRGDIDAMISSA 623
Cdd:COG4717 321 LEELLAALglpPDLSPEELLELLDRIEELQELLR-EAEELEEELQLEELEQE--------IAALLAEAGVEDEEELRAAL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 624 K------SMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKLTNKLpdlwRKIESINQQLLP 697
Cdd:COG4717 392 EqaeeyqELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL----AELEAELEQLEE 467
|
490 500
....*....|....*....|....*..
gi 732170495 698 LGNISDNMDRIRELIQQARDAASKVAV 724
Cdd:COG4717 468 DGELAELLQELEELKAELRELAEEWAA 494
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
244-717 |
2.96e-09 |
|
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: 62.11 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 244 SAGLLEQMRHMETQAKDLRNQLLNYRSAISN-HGSKIEgLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAK 322
Cdd:pfam01576 91 SQQLQNEKKKMQQHIQDLEEQLDEEEAARQKlQLEKVT-TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 323 ELDVKIKNV--IRNVH------MLNRIRTWQKTHQG-ENN-----GLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQAN 388
Cdd:pfam01576 170 EEEEKAKSLskLKNKHeamisdLEERLKKEEKGRQElEKAkrkleGESTDLQEQIAELQAQIAELRAQLAKKEEELQAAL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 389 GLNQENERALGAIQRQVKE----INSLQSDFtkylttaDSSLLQTNIALQLMEKSQKEYEKLAASLNE------ARQELS 458
Cdd:pfam01576 250 ARLEEETAQKNNALKKIREleaqISELQEDL-------ESERAARNKAEKQRRDLGEELEALKTELEDtldttaAQQELR 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 459 DK----VRELSRSAGKTSLVEEAE------KHARSLQELAKQLEEIKRNASGDELVRCAVDAATA-YENILNAIKAAEDA 527
Cdd:pfam01576 323 SKreqeVTELKKALEEETRSHEAQlqemrqKHTQALEELTEQLEQAKRNKANLEKAKQALESENAeLQAELRTLQQAKQD 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 528 ANRAASASESALQTV---------IKEDLPRKAKTLSSNSDK---LLNEAKMTQKKLKQEVSPALNNLQQT---LNIVTV 592
Cdd:pfam01576 403 SEHKRKKLEGQLQELqarlseserQRAELAEKLSKLQSELESvssLLNEAEGKNIKLSKDVSSLESQLQDTqelLQEETR 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 593 QKEVIDTNLTTLRDGLHGIQrgdidamissaksmvrkanditdEVLDGLNPIQTDVERIKDTYgRTQNEDFKKALTDADN 672
Cdd:pfam01576 483 QKLNLSTRLRQLEDERNSLQ-----------------------EQLEEEEEAKRNVERQLSTL-QAQLSDMKKKLEEDAG 538
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 732170495 673 SVNKLTNKLPDLWRKIESINQQLLPLGNISDNMDRIRELIQQARD 717
Cdd:pfam01576 539 TLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELD 583
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
226-621 |
3.85e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.67 E-value: 3.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 226 TMGEQLRLVksQLQGLSASAGLLEQMRHMETQAKDLRNQLlnyRSAISNHGSKIEGLERELTDLNQEF-ETLQEKAQVnS 304
Cdd:pfam15921 296 SIQSQLEII--QEQARNQNSMYMRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELtEARTERDQF-S 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 305 RKAQTLNNNVNRAT----QSAKEL-----------DVKIKNVIRNVHM----------LNRIRTWQKTH----------- 348
Cdd:pfam15921 370 QESGNLDDQLQKLLadlhKREKELslekeqnkrlwDRDTGNSITIDHLrrelddrnmeVQRLEALLKAMksecqgqmerq 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 349 ----QGENNGLAN---------SIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINS---LQ 412
Cdd:pfam15921 450 maaiQGKNESLEKvssltaqleSTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSrvdLK 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 413 SDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAG-----KTSLVEEAEKHARSLQEL 487
Cdd:pfam15921 530 LQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGamqveKAQLEKEINDRRLELQEF 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 488 --------AK-----------QLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASEsalqtVIKEDLP 548
Cdd:pfam15921 610 kilkdkkdAKirelearvsdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYE-----VLKRNFR 684
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732170495 549 RKAKtlssnsdkllnEAKMTQKKLKQEVSPALNNLQQTLNIVTvQKEVIDTNLTTLRDGLHG---IQRGDIDAMIS 621
Cdd:pfam15921 685 NKSE-----------EMETTTNKLKMQLKSAQSELEQTRNTLK-SMEGSDGHAMKVAMGMQKqitAKRGQIDALQS 748
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
278-496 |
4.23e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.62 E-value: 4.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 278 KIEGLERELTDLNQEFET-------LQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHMLNRIRTWQKTHQG 350
Cdd:TIGR02169 682 RLEGLKRELSSLQSELRRienrldeLSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 351 ENNGLANSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnqeNERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTN 430
Cdd:TIGR02169 762 ELEARIEELEEDLHKLEEALNDLEARL----------------SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732170495 431 IALQLMEKSQKEYEKLAASLNEARQELSDKVRELsrSAGKTSLVEEAEKHARSLQELAKQLEEIKR 496
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENL--NGKKEELEEELEELEAALRDLESRLGDLKK 889
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
1132-1236 |
1.16e-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: 55.12 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1132 FQTFQPSGILLDHQTWTRN-LQVTLEDGYIELSTSDSGGP--IFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQ--LLRN 1206
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDfLALELVNGRLVLRYDLGSGPesLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQtvVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 732170495 1207 SKRLKHISSSRQSLRLGG-------------SNFEGCISNVFV 1236
Cdd:pfam02210 81 PPGESLLLNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
249-503 |
2.38e-08 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 57.61 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 249 EQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNnnvnratqsaKELDVKI 328
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELR----------EKRDELN 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 329 KNVirnvhmlnrirtwqkthqgennglaNSIRDSLNEYEAKLSDLRARLQEAAAQAKQANglnqENERALGAIQrqvKEI 408
Cdd:COG1340 71 EKV-------------------------KELKEERDELNEKLNELREELDELRKELAELN----KAGGSIDKLR---KEI 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 409 NSLQSDF-TKYLTTAD-------SSLLQTNI-ALQLMEKSQKEYEKLAASLNEARQELSDKVRELsrsagkTSLVEEAEK 479
Cdd:COG1340 119 ERLEWRQqTEVLSPEEekelvekIKELEKELeKAKKALEKNEKLKELRAELKELRKEAEEIHKKI------KELAEEAQE 192
|
250 260
....*....|....*....|....
gi 732170495 480 HARSLQELAKQLEEIKRNAsgDEL 503
Cdd:COG1340 193 LHEEMIELYKEADELRKEA--DEL 214
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
961-1077 |
2.64e-08 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 54.25 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 961 IQTTVDRGLLFFAE--NGDRFISLNIEDGKLMVRYKLNSELPKERGvGDAINNGRDHSI---------QIKIGKLQKRMW 1029
Cdd:pfam00054 1 FRTTEPSGLLLYNGtqTERDFLALELRDGRLEVSYDLGSGAAVVRS-GDKLNDGKWHSVelerngrsgTLSVDGEARPTG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 732170495 1030 INVDVQNTIIDGEvfdfSTYYLGGIPIAI--RERFNISTPaFRGCMKNLK 1077
Cdd:pfam00054 80 ESPLGATTDLDVD----GPLYVGGLPSLGvkKRRLAISPS-FDGCIRDVI 124
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
227-695 |
2.96e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 58.49 E-value: 2.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 227 MGEQLRLVKSQLqglsasaglleqmRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNqefetlqEKAQVNSRK 306
Cdd:TIGR04523 38 LEKKLKTIKNEL-------------KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLN-------DKLKKNKDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 307 AQTLNNNVNRatqSAKELDVKIKNVIRNVHMLNRIRTwQKTHQGEN-NGLANSIR---DSLNEYEAKLSDLRARLqeaaa 382
Cdd:TIGR04523 98 INKLNSDLSK---INSEIKNDKEQKNKLEVELNKLEK-QKKENKKNiDKFLTEIKkkeKELEKLNNKYNDLKKQK----- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 383 qakqangLNQENERALgaiqrQVKEINSLQSDftkyLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEAR-------- 454
Cdd:TIGR04523 169 -------EELENELNL-----LEKEKLNIQKN----IDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKkqnnqlkd 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 455 ------QELSDKVRELSRSAGK-TSLVEEAEKHARSLQElaKQLEEIKRNASGDELvrcavdaatayENILNAIKaaeDA 527
Cdd:TIGR04523 233 niekkqQEINEKTTEISNTQTQlNQLKDEQNKIKKQLSE--KQKELEQNNKKIKEL-----------EKQLNQLK---SE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 528 ANRAASASESALQTVIKEDLPRKAKTLS------SNSDKLLNEAKMTQKKLKQEVSPALNN---LQQTLN-----IVTVQ 593
Cdd:TIGR04523 297 ISDLNNQKEQDWNKELKSELKNQEKKLEeiqnqiSQNNKIISQLNEQISQLKKELTNSESEnseKQRELEekqneIEKLK 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 594 KEvIDTNLTTLRDgLHgIQRGDIDAMISSAKsmvrKANDITDEVLDGL----NPIQTDVERIKDTygRTQNEDFKKALTD 669
Cdd:TIGR04523 377 KE-NQSYKQEIKN-LE-SQINDLESKIQNQE----KLNQQKDEQIKKLqqekELLEKEIERLKET--IIKNNSEIKDLTN 447
|
490 500
....*....|....*....|....*.
gi 732170495 670 ADNSVNKLTNKLPdlwRKIESINQQL 695
Cdd:TIGR04523 448 QDSVKELIIKNLD---NTRESLETQL 470
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
216-473 |
3.02e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 216 CVMTLLNDLATMGEQLRLVKSQLQGLSAS-AGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFE 294
Cdd:COG4942 7 LALLLALAAAAQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 295 TLQEK-----AQVNSRK---AQTLNNNVNRATQSAKELDVKIKNV---IRNVHMLNRIRTWQKThqgenngLANSIRDSL 363
Cdd:COG4942 87 ELEKEiaelrAELEAQKeelAELLRALYRLGRQPPLALLLSPEDFldaVRRLQYLKYLAPARRE-------QAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 364 NEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEY 443
Cdd:COG4942 160 AELAALRAELEAER--------------AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
250 260 270
....*....|....*....|....*....|
gi 732170495 444 EKLAASLNEARQELSDKVRELSRSAGKTSL 473
Cdd:COG4942 226 EALIARLEAEAAAAAERTPAAGFAALKGKL 255
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
247-687 |
1.80e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 247 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVNSRKAQTLNNNVNRATQSAK--- 322
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEElKEEIEELEKELESLEGSKRKLEEKire 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 323 ------ELDVKIKNVIRNVHMLNRIRtWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENER 396
Cdd:PRK03918 264 leerieELKKEIEELEEKVKELKELK-EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 397 ALGAIQRQVKEINSLQSDFTKY------LTTADSslLQTNIALQLMEKSQKEYEKLA-----------------ASLNEA 453
Cdd:PRK03918 343 LKKKLKELEKRLEELEERHELYeeakakKEELER--LKKRLTGLTPEKLEKELEELEkakeeieeeiskitariGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 454 RQELSDKVRELSRSAGKT-----SLVEEAEKH------------ARSLQELAKQLEEIKRNASGDELVRCAVDAATAYEN 516
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCpvcgrELTEEHRKElleeytaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIKLKE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 517 ILNAIKaaedaanraasASESALQTVIKEDLPRKAKTLsSNSDKLLNEAKMTQKKLKQEVSpALNNLQQTLNIVTVQKEV 596
Cdd:PRK03918 501 LAEQLK-----------ELEEKLKKYNLEELEKKAEEY-EKLKEKLIKLKGEIKSLKKELE-KLEELKKKLAELEKKLDE 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 597 IDTNLTTLRDGLHGIQRGDIDAMissaKSMVRKANDITDEVLDgLNPIQTDVERIKDTYGRTQNE--DFKKALTDADNSV 674
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEEL----EERLKELEPFYNEYLE-LKDAEKELEREEKELKKLEEEldKAFEELAETEKRL 642
|
490
....*....|...
gi 732170495 675 NKLTNKLPDLWRK 687
Cdd:PRK03918 643 EELRKELEELEKK 655
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
220-493 |
4.76e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 220 LLNDLATMGEQLRLVKSQLQGLSASAGLLEQmRHMETQ-AKDLRNQLLNYRSAISnhGSKIEGLERELTDLNQEFETLQE 298
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEE-RHELYEeAKAKKEELERLKKRLT--GLTPEKLEKELEELEKAKEEIEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 299 K-AQVNSRKAQtLNNNVNRATQSAKELdvkiKNVIRNVHMLNRIRTwqKTHQGEnnglansirdSLNEYEAKLSDLRARL 377
Cdd:PRK03918 406 EiSKITARIGE-LKKEIKELKKAIEEL----KKAKGKCPVCGRELT--EEHRKE----------LLEEYTAELKRIEKEL 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 378 QEAAaqakqanglnqENERALGAIQRQVKEINSLQSDFTKYLTTAD------SSLLQTNiaLQLMEKSQKEYEKLAASLN 451
Cdd:PRK03918 469 KEIE-----------EKERKLRKELRELEKVLKKESELIKLKELAEqlkeleEKLKKYN--LEELEKKAEEYEKLKEKLI 535
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 732170495 452 EARQELSDKVRELSRSAG----KTSLVEEAEKHARSLQELAKQLEE 493
Cdd:PRK03918 536 KLKGEIKSLKKELEKLEElkkkLAELEKKLDELEEELAELLKELEE 581
|
|
| TNFRSF4 |
cd13406 |
Tumor necrosis factor receptor superfamily member 4 (TNFRSF4), also known as CD134 or OXO40; ... |
79-179 |
5.26e-07 |
|
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: 50.86 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 79 NCNGHS--------NQCQDGSGICVNCQHNTAGEhCERCQEGYYGNAVH--------------GSCRACPCPHTNsfatg 136
Cdd:cd13406 2 HCVGDTypsgekccHECPPGEGMESRCTGTQDTV-CSPCEPGFYNEAVNyepckpctqcnqrsGSEEKQKCTKTS----- 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 732170495 137 cvvnggDVRCSCKAGYT-------GTQCERCAPGYFGNPQkfGGSCQP---CS 179
Cdd:cd13406 76 ------DTVCRCRPGTQpldsykpGVDCVPCPPGHFSRGD--NQACKPwtnCS 120
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
1335-1473 |
5.75e-07 |
|
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin A-like lectin/glucanases superfamily.
Pssm-ID: 463865 [Multi-domain] Cd Length: 151 Bit Score: 50.85 E-value: 5.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1335 KLPQELLkPRSQFAVDM-----QTTSSRGLVFHTGTKNSFMALYLSKGRLVFALGTDGKKLR-IKSKEKCNDGKWHTVVF 1408
Cdd:pfam13385 8 TLPDALL-PTSDFTVSAwvkpdSLPGWARAIISSSGGGGYSLGLDGDGRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAV 86
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732170495 1409 GHDGEKGRLVVDGLRAREGSLPGNSTISIRAPVYLGSPPSGKPkslptnSFVGCLKNFQLDSKPL 1473
Cdd:pfam13385 87 TYDGGTLRLYVNGVLVGSSTLTGGPPPGTGGPLYIGRSPGGDD------YFNGLIDEVRIYDRAL 145
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
219-687 |
8.64e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 54.14 E-value: 8.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 219 TLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRH-------METQAKDLRNQLL-------NYRSAISNHGS---KIEG 281
Cdd:PRK01156 302 KYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKdyndyikKKSRYDDLNNQILelegyemDYNSYLKSIESlkkKIEE 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 282 LERELTDLNQEFETLQEKAQVN-----------SRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHMLN--RIRTWQKTH 348
Cdd:PRK01156 382 YSKNIERMSAFISEILKIQEIDpdaikkelneiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNgqSVCPVCGTT 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 349 QGEnnglaNSIRDSLNEYEAKLSdlrarlqeaaaqakqanGLNQEneraLGAIQRQVKEINSLQSDFTKylttadsslLQ 428
Cdd:PRK01156 462 LGE-----EKSNHIINHYNEKKS-----------------RLEEK----IREIEIEVKDIDEKIVDLKK---------RK 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 429 TNIALQLMEKSQKEYEKlaasLNEARQELSDKVRELSRSAGKTSLVEEAEKHARS--LQEL-AKQLEEIKRNAsgdelVR 505
Cdd:PRK01156 507 EYLESEEINKSINEYNK----IESARADLEDIKIKINELKDKHDKYEEIKNRYKSlkLEDLdSKRTSWLNALA-----VI 577
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 506 CAVDaatayeniLNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSS------------NSDKLLNEAKMTQKKLK 573
Cdd:PRK01156 578 SLID--------IETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSireieneannlnNKYNEIQENKILIEKLR 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 574 QEV------SPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHgiqrgDIDAMISSAKSMVRKANDITDEVLDGLNPIQTD 647
Cdd:PRK01156 650 GKIdnykkqIAEIDSIIPDLKEITSRINDIEDNLKKSRKALD-----DAKANRARLESTIEILRTRINELSDRINDINET 724
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 732170495 648 VERIKdtygrtqneDFKKALTDADNSVNKLT-NKLPDLWRK 687
Cdd:PRK01156 725 LESMK---------KIKKAIGDLKRLREAFDkSGVPAMIRK 756
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
217-723 |
1.02e-06 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 53.49 E-value: 1.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 217 VMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETL 296
Cdd:COG0840 4 LLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVVLLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 297 QEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHMLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRAR 376
Cdd:COG0840 84 LLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAAAAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 377 LQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQT-------NIALQLMEKSQKEYEKLAAS 449
Cdd:COG0840 164 AALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVleriaegDLTVRIDVDSKDEIGQLADA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 450 LNEARQELSDKVRELSRSAgkTSLVEEAEKHARSLQELAKQLEEIKRNASgdelvrcavDAATAYENILNAIKaaedaan 529
Cdd:COG0840 244 FNRMIENLRELVGQVRESA--EQVASASEELAASAEELAAGAEEQAASLE---------ETAAAMEELSATVQ------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 530 raaSASESALQTvikEDLPRKAKTLSSNSDKLLNEAKMTQKKLK---QEVSPALNNL----QQTLNIVTVQKEVID-TNL 601
Cdd:COG0840 306 ---EVAENAQQA---AELAEEASELAEEGGEVVEEAVEGIEEIResvEETAETIEELgessQEIGEIVDVIDDIAEqTNL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 602 TTL-------RDGLHGiqRG--------------------DIDAMISSAKSMVRKANDITDEVLDGlnpIQTDVERIKDT 654
Cdd:COG0840 380 LALnaaieaaRAGEAG--RGfavvadevrklaersaeatkEIEELIEEIQSETEEAVEAMEEGSEE---VEEGVELVEEA 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 655 ygrtqnedfKKALTDADNSVNKLTNKLpdlwRKI-ESINQQLLPLGNISDNMDRIRELIQQARDAASKVA 723
Cdd:COG0840 455 ---------GEALEEIVEAVEEVSDLI----QEIaAASEEQSAGTEEVNQAIEQIAAAAQENAASVEEVA 511
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
394-710 |
1.14e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 53.42 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 394 NERALGAIQRQVKEINSLQSDFTKYlTTADSSLLQTNIAL-QLMEKSQK-------EYEKLAASLNEARQELSDKVRELS 465
Cdd:COG5185 217 SESTLLEKAKEIINIEEALKGFQDP-ESELEDLAQTSDKLeKLVEQNTDlrleklgENAESSKRLNENANNLIKQFENTK 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 466 RSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATayENILNAIKAAEDAANRAASASESALQTVIKE 545
Cdd:COG5185 296 EKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLT--AEIEQGQESLTENLEAIKEEIENIVGEVELS 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 546 DLPRKAKTLSSNSDKL---LNEAKMTQKKLKQEvspALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGdIDAMISS 622
Cdd:COG5185 374 KSSEELDSFKDTIESTkesLDEIPQNQRGYAQE---ILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKL-LNELISE 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 623 AKSMVRKANDITDEVLDGLNpiqtdveRIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLW----RKIESINQQLLPL 698
Cdd:COG5185 450 LNKVMREADEESQSRLEEAY-------DEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRakleRQLEGVRSKLDQV 522
|
330
....*....|..
gi 732170495 699 GNISDNMDRIRE 710
Cdd:COG5185 523 AESLKDFMRARG 534
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
219-681 |
1.25e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.51 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 219 TLLNDLATMGEQLRLVKSQLQGLsasagllEQMR-HMETQAKDLRNQLLNYRSAI------SNHGSKIEGLERELTDLNQ 291
Cdd:TIGR00606 581 SKSKEINQTRDRLAKLNKELASL-------EQNKnHINNELESKEEQLSSYEDKLfdvcgsQDEESDLERLKEEIEKSSK 653
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 292 EFETLQEKAQVNSRKAQTLNNN-------VNRATQSAKELDVKIKNVirnVHMLNRIRTWQKTHQGENN----------G 354
Cdd:TIGR00606 654 QRAMLAGATAVYSQFITQLTDEnqsccpvCQRVFQTEAELQEFISDL---QSKLRLAPDKLKSTESELKkkekrrdemlG 730
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 355 LANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTkylttadsslLQTNIALQ 434
Cdd:TIGR00606 731 LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVT----------IMERFQME 800
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 435 LmEKSQKEYEKLAASLN---------EARQELSDKVRELSrsagktSLVEEAEKHARSLQELAKQLEEIKR--NASGDEL 503
Cdd:TIGR00606 801 L-KDVERKIAQQAAKLQgsdldrtvqQVNQEKQEKQHELD------TVVSKIELNRKLIQDQQEQIQHLKSktNELKSEK 873
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 504 VRCAVDAATA---YENILNAIKAAEDAANRAASASE--SALQTVIKEDLPRKAKTLSSNSD---KLLNEAKMTQKKLKQE 575
Cdd:TIGR00606 874 LQIGTNLQRRqqfEEQLVELSTEVQSLIREIKDAKEqdSPLETFLEKDQQEKEELISSKETsnkKAQDKVNDIKEKVKNI 953
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 576 V---SPALNNLQQTLNIVTVQKEvidTNLTTLRDGLHGIQR------GDIDAMISSAKSMVRKANDITDEV-LDGLNPIQ 645
Cdd:TIGR00606 954 HgymKDIENKIQDGKDDYLKQKE---TELNTVNAQLEECEKhqekinEDMRLMRQDIDTQKIQERWLQDNLtLRKRENEL 1030
|
490 500 510
....*....|....*....|....*....|....*.
gi 732170495 646 TDVERIKDTYGRTQNEDfkkALTDADNSVNKLTNKL 681
Cdd:TIGR00606 1031 KEVEEELKQHLKEMGQM---QVLQMKQEHQKLEENI 1063
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
221-492 |
1.44e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 221 LNDLATMGEQLRLVKSQLQGLSAsaglleQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEfetlqeka 300
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKL------QMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKE-------- 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 301 qVNSRKAQTLNNNVNRATQSAK--ELDVKIKNV-IRNVHMLN----RIRTWQKTHQgENNGLANSIRDSLNE-------Y 366
Cdd:pfam15921 599 -INDRRLELQEFKILKDKKDAKirELEARVSDLeLEKVKLVNagseRLRAVKDIKQ-ERDQLLNEVKTSRNElnslsedY 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 367 EAKLSDLRARlqeAAAQAKQANGLNQENERALGAIQRQVKEINSLQ-SD---------FTKYLTTADSSL--LQTNIAL- 433
Cdd:pfam15921 677 EVLKRNFRNK---SEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgSDghamkvamgMQKQITAKRGQIdaLQSKIQFl 753
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 434 -QLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEkhaRSLQELAKQLE 492
Cdd:pfam15921 754 eEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQE---RRLKEKVANME 810
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
262-721 |
1.55e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 53.52 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 262 RNQLLNYRSAISNHGSKIEGLERELTDLNqefetlqekaqvnsrkAQTLNNNVNRATQSAKELDVKIKNVIRNvhMLNRI 341
Cdd:TIGR01612 695 KAKLDDLKSKIDKEYDKIQNMETATVELH----------------LSNIENKKNELLDIIVEIKKHIHGEINK--DLNKI 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 342 RTWQKTHQGEnngLANSI------RDSLNEYEAKLSDLRARLQEAAAQAkqaNGLNQENERALGAIQRQVKEINSLQSDF 415
Cdd:TIGR01612 757 LEDFKNKEKE---LSNKIndyakeKDELNKYKSKISEIKNHYNDQINID---NIKDEDAKQNYDKSKEYIKTISIKEDEI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 416 TKYLTTA----DSSLLQTNIALQL----MEKSQKEYEKLAASLNEARQELSDKvrELSRSAGK----TSLVEEA----EK 479
Cdd:TIGR01612 831 FKIINEMkfmkDDFLNKVDKFINFenncKEKIDSEHEQFAELTNKIKAEISDD--KLNDYEKKfndsKSLINEInksiEE 908
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 480 HARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNA-IKAAEDAANRAASASESALQTVI--KEDLPRKAKTLS- 555
Cdd:TIGR01612 909 EYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILNKnIDTIKESNLIEKSYKDKFDNTLIdkINELDKAFKDASl 988
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 556 ----SNSDKLL---NEAKMTQKKLKQ--------EVSPALNNLQQtlNIVTVQKEVIDTNLTtLRDGLHGIQRgDIDAMI 620
Cdd:TIGR01612 989 ndyeAKNNELIkyfNDLKANLGKNKEnmlyhqfdEKEKATNDIEQ--KIEDANKNIPNIEIA-IHTSIYNIID-EIEKEI 1064
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 621 SSAKSMVRKanditdEVLDGLNPIQTDVERIKDTYGRTQNEDF-KKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLG 699
Cdd:TIGR01612 1065 GKNIELLNK------EILEEAEINITNFNEIKEKLKHYNFDDFgKEENIKYADEINKIKDDIKNLDQKIDHHIKALEEIK 1138
|
490 500
....*....|....*....|...
gi 732170495 700 NISDN-MDRIRELIQQARDAASK 721
Cdd:TIGR01612 1139 KKSENyIDEIKAQINDLEDVADK 1161
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
250-472 |
1.56e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 250 QMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKE------ 323
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 324 --------LDV-----KIKNVIRNVHMLNRIRTwqktHQGENNGLANSIRDSLNEYEAKLSDLRARLQEaaaqakqangL 390
Cdd:COG3883 97 rsggsvsyLDVllgseSFSDFLDRLSALSKIAD----ADADLLEELKADKAELEAKKAELEAKLAELEA----------L 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 391 NQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGK 470
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
..
gi 732170495 471 TS 472
Cdd:COG3883 243 AA 244
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
199-478 |
1.86e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 199 QEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGLsasagllEQMRHMETQAKDLRNQLLNYRSAISNHGSK 278
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA-------EDLVEAEDRIERLEERREDLEELIAERRET 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 279 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHMLNRIRTwqkthqgennglans 358
Cdd:PRK02224 532 IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRT--------------- 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 359 IRDSLNEYEAKLSDLRARLqeaaaqaKQANGLNQENERALGAIQRQVKE---------INSLQSD---FTKYLTTADSSL 426
Cdd:PRK02224 597 LLAAIADAEDEIERLREKR-------EALAELNDERRERLAEKRERKREleaefdearIEEAREDkerAEEYLEQVEEKL 669
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732170495 427 ---------LQTNIAlqLMEKSQKEYEklaaSLNEARQELSDKVRELSrsagktSLVEEAE 478
Cdd:PRK02224 670 delreerddLQAEIG--AVENELEELE----ELRERREALENRVEALE------ALYDEAE 718
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
72-193 |
2.53e-06 |
|
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 neurotrophin receptor (p75NTR) or CD271; TNFRSF16 (also known as nerve growth factor receptor (NGFR) or p75 neurotrophin receptor (p75NTR or p75(NTR)), CD271, Gp80-LNGFR) is a common receptor for both neurotrophins and proneurotrophins, and plays a diverse role in many tissues, including the nervous system. It has been shown to be expressed in various types of stem cells and has been used to prospectively isolate stem cells with different degrees of potency. p75NTR owes its signaling to the recruitment of intracellular binding proteins, leading to the activation of different signaling pathways. It binds nerve growth factor (NGF) and the complex can initiate a signaling cascade which has been associated with both neuronal apoptosis and neuronal survival of discrete populations of neurons, depending on the presence or absence of intracellular signaling molecules downstream of p75NTR (e.g. NF-kB, JNK, or p75NTR intracellular death domain). p75NTR can also bind NGF in concert with the neurotrophic tyrosine kinase receptor type 1 (TrkA) protein where it is thought to modulate the formation of the high-affinity neurotrophin binding complex. On melanoma cell, p75NTR is an immunosuppressive factor, induced by interferon (IFN)-gamma, and mediates down-regulation of melanoma antigens. It can interact with the aggregated form of amyloid beta (Abeta) peptides, and plays an important role in etiopathogenesis of Alzheimer's disease by influencing protein tau hyper-phosphorylation. p75(NTR) is involved in the formation and progression of retina diseases; its expression is induced in retinal pigment epithelium (RPE) cells and its knockdown rescues RPE cell proliferation activity and inhibits RPE apoptosis induced by hypoxia. It can therefore be a potential therapeutic target for RPE hypoxia or oxidative stress diseases.
Pssm-ID: 276921 [Multi-domain] Cd Length: 159 Bit Score: 49.22 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 72 TGRCVPCNcnghsnQCQDGSGICVNCQ--HNTageHCErCQEGYYGNAVHGSCRACP-CPhtnsfatgcvvNGGDVRCSC 148
Cdd:cd13416 51 TEPCQPCT------RCPGLMSMRAPCTatHDT---VCE-CAYGYYLDEDSGTCEPCTvCP-----------PGQGVVQSC 109
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 732170495 149 KAGyTGTQCERCAPGYFGNPQKFGGSCQPCS-CNSNG-QLGSCHPLT 193
Cdd:cd13416 110 GPN-QDTVCEACPEGTYSDEDSSTDPCLPCTvCEDGEvELRECTPVS 155
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
277-578 |
6.87e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 50.80 E-value: 6.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 277 SKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKI---KNVIRNVHMLN------RIR----- 342
Cdd:pfam05701 138 AELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELiatKESLESAHAAHleaeehRIGaalar 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 343 -----TWQKT-HQGE------NNGL--ANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENER--------ALGA 400
Cdd:pfam05701 218 eqdklNWEKElKQAEeelqrlNQQLlsAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKktstsiqaALAS 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 401 IQRQVKEIN-SLQ--SDFTKYLTTADSSLlqtnialqlmeKSQKEYEKlaASLNEARQE-------LSDKVRELSRSAGK 470
Cdd:pfam05701 298 AKKELEEVKaNIEkaKDEVNCLRVAAASL-----------RSELEKEK--AELASLRQRegmasiaVSSLEAELNRTKSE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 471 TSLVEEAEKHARS-LQELAKQLEEIKRNAsgDElvrcAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPR 549
Cdd:pfam05701 365 IALVQAKEKEAREkMVELPKQLQQAAQEA--EE----AKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAA 438
|
330 340 350
....*....|....*....|....*....|
gi 732170495 550 KA-KTLSSNSDKLLNEAKMTQKKLKQEVSP 578
Cdd:pfam05701 439 KAsEKLALAAIKALQESESSAESTNQEDSP 468
|
|
| TNFRSF |
cd00185 |
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) ... |
106-179 |
8.34e-06 |
|
Tumor necrosis factor receptor superfamily (TNFRSF); Members of TNFR superfamily (TNFRSF) interactions with TNF superfamily (TNFSF) ligands (TNFL) control key cellular processes such as differentiation, proliferation, apoptosis, and cell growth. Dysregulation of these pathways has been shown to result in a wide range of pathological conditions, including autoimmune diseases, inflammation, cancer, and viral infection. There are 29 very diverse family members of TNFRSF reported in humans: 22 are type I transmembrane receptors (single pass with the N terminus on extracellular side of the cell membrane) and have a clear signal peptide; the remaining 7 members are either type III transmembrane receptors (single pass with the N terminus on extracellular side of the membrane but no signal sequence; TNFR13B, TNFR13C, TNFR17, and XEDAR), or attached to the membrane via a glycosylphosphatidylinositol (GPI) linker (TNFR10C), or secreted as soluble receptors (TNFR11B and TNFR6B). All TNFRs contain relatively short cysteine-rich domains (CRDs) in the ectodomain, and are involved in interaction with the TNF homology domain (THD) of their ligands. TNFRs often have multiple CRDs (between one and six), with the most frequent configurations of three or four copies; most CRDs possess three disulfide bridges, but could have between one and four. Localized or genome-wide duplication and evolution of the TNFRSF members appear to have paralleled the emergence of the adaptive immune system; teleosts (i.e. ray-finned, bony fish), which possess an immune system with B and T cells, possess primary and secondary lymphoid organs, and are capable of adaptive responses to pathogens also display several characteristics that are different from the mammalian immune system, making teleost TNFSF orthologs and paralogs of interest to better understand immune system evolution and the immunological pathways elicited to pathogens.
Pssm-ID: 276900 [Multi-domain] Cd Length: 87 Bit Score: 45.66 E-value: 8.34e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732170495 106 CERCQEGYYgNAVHGSCRAC-PCPHtnsfatgCVVNGGDVRCSCKAgyTGTQCERCAPGYFGNPQKFGGSCQPCS 179
Cdd:cd00185 23 CSPCPPGTY-SESWNSLSKClPCTT-------CGGGNQVEKTPCTA--TDNRCCTCKPGFYCDEGTNVEECKPCT 87
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
220-498 |
8.40e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 8.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 220 LLNDLATMGEQLRLVKSQLQGL--SASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQ 297
Cdd:COG4717 161 LEEELEELEAELAELQEELEELleQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 298 EKAQVNSRK---------------AQTLNNNVNR-----------------ATQSAKELDVKIKNVIRNVHMLNRIRTWQ 345
Cdd:COG4717 241 LEERLKEARlllliaaallallglGGSLLSLILTiagvlflvlgllallflLLAREKASLGKEAEELQALPALEELEEEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 346 KTHQGENNGLANSIRDS-----------LNEYEAKLSDLRARLQEAAAQAKQANGLNQ---ENERALGAIQRQVKEINSL 411
Cdd:COG4717 321 LEELLAALGLPPDLSPEellelldrieeLQELLREAEELEEELQLEELEQEIAALLAEagvEDEEELRAALEQAEEYQEL 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 412 QSDFTKY---LTTADSSLLQTNIALQLmEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELA 488
Cdd:COG4717 401 KEELEELeeqLEELLGELEELLEALDE-EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELE 479
|
330
....*....|
gi 732170495 489 KQLEEIKRNA 498
Cdd:COG4717 480 ELKAELRELA 489
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
232-515 |
9.87e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 50.42 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 232 RLVKSQLQGLSASAgLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKA----------- 300
Cdd:PRK02224 298 LLAEAGLDDADAEA-VEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAaeleseleear 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 301 -QVNSRKAQ------------------------------TLNNNVNRATQSAKELDVKIKNVIRNVHMLNRIRTWQKTHQ 349
Cdd:PRK02224 377 eAVEDRREEieeleeeieelrerfgdapvdlgnaedfleELREERDELREREAELEATLRTARERVEEAEALLEAGKCPE 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 350 GENNGLANSIRDSLNEYEAKLSDLRARLqeaAAQAKQANGLNQENERA--LGAIQRQVKEINSLQSDFTKYLTTADSSll 427
Cdd:PRK02224 457 CGQPVEGSPHVETIEEDRERVEELEAEL---EDLEEEVEEVEERLERAedLVEAEDRIERLEERREDLEELIAERRET-- 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 428 qtnialqLMEKSQKeyeklAASLNEARQELSDKVRELSRSAgkTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVRCA 507
Cdd:PRK02224 532 -------IEEKRER-----AEELRERAAELEAEAEEKREAA--AEAEEEAEEAREEVAELNSKLAELKERIESLERIRTL 597
|
....*...
gi 732170495 508 VDAATAYE 515
Cdd:PRK02224 598 LAAIADAE 605
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
225-451 |
1.34e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 225 ATMGEQLRLVKsqLQGL-SASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVN 303
Cdd:COG1579 1 AMPEDLRALLD--LQELdSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 304 SRKAQTLNNNvnratqsaKELDvkikNVIRNVHMLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLqeaaaq 383
Cdd:COG1579 79 EEQLGNVRNN--------KEYE----ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEL------ 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170495 384 akqaNGLNQENERALGAIQrqvKEINSLQSDFTKYLTTADSSLLqtnialqlmeksqKEYEKLAASLN 451
Cdd:COG1579 141 ----EEKKAELDEELAELE---AELEELEAEREELAAKIPPELL-------------ALYERIRKRKN 188
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
229-689 |
1.43e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.05 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKSQLQGLSASA-----------------GLLEQMRHMET---QAKDLRNQLLNYRSAISNHGSKIEGLERELTD 288
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSdrileldqelrkaerelSKAEKNSLTETlkkEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTT 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 289 LNQEFETLQEKA-------QVNSRKAQTL--------NNNVNRATQSAKELDVKI---------KNVIRNVHMLNRIRTW 344
Cdd:TIGR00606 534 RTQMEMLTKDKMdkdeqirKIKSRHSDELtsllgyfpNKKQLEDWLHSKSKEINQtrdrlaklnKELASLEQNKNHINNE 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 345 QKTHQGENNGLANSIRD--SLNEYEAKLSDLRARLQEAAAQAKQANG-----------LNQENERALGAIQRQVK---EI 408
Cdd:TIGR00606 614 LESKEEQLSSYEDKLFDvcGSQDEESDLERLKEEIEKSSKQRAMLAGatavysqfitqLTDENQSCCPVCQRVFQteaEL 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 409 NSLQSDFTKYLTTADSSLLQTNialQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKT-SLVEEAEKHARSLQEL 487
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTE---SELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLqKVNRDIQRLKNDIEEQ 770
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 488 AKQLEEIkrNASGDELVRCAVDaATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLNEAKM 567
Cdd:TIGR00606 771 ETLLGTI--MPEEESAKVCLTD-VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL 847
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 568 TQkKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTtlrdglhgiQRGDID----AMISSAKSMVRKANDITDEVLDGLNP 643
Cdd:TIGR00606 848 NR-KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQ---------RRQQFEeqlvELSTEVQSLIREIKDAKEQDSPLETF 917
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 732170495 644 IQTDVERiKDTYGRTQNEDFKKALTDADNSVNKLTNK---LPDLWRKIE 689
Cdd:TIGR00606 918 LEKDQQE-KEELISSKETSNKKAQDKVNDIKEKVKNIhgyMKDIENKIQ 965
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
220-500 |
1.65e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 220 LLNDLATMGEQLRLVKSQLQGLSasagllEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTD-----LNQEFE 294
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLE------QEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHsripeIQAELS 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 295 TLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHML-NRIRTWQKThQGENNGLANSIRDSLNEYEAKLSDL 373
Cdd:TIGR02169 802 KLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLkEQIKSIEKE-IENLNGKKEELEEELEELEAALRDL 880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 374 RARLQeaaaqakqanGLNQENERA---LGAIQRQVKEINSlqsdftkYLTTADSSLLQTNIALQLMEKSQKEYEKLAASL 450
Cdd:TIGR02169 881 ESRLG----------DLKKERDELeaqLRELERKIEELEA-------QIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732170495 451 NEARQELSD---------KVRELSRSAGKTSL--VEEAEKHARSLQELAKQLEEIKRNASG 500
Cdd:TIGR02169 944 EEIPEEELSledvqaelqRVEEEIRALEPVNMlaIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
260-744 |
2.00e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.51 E-value: 2.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 260 DLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLN---NNVNRATQSAKELDVKIKNVIRNVH 336
Cdd:PRK01156 187 YLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKsalNELSSLEDMKNRYESEIKTAESDLS 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 337 MLNRIRTWQKTHQGENNGLANSI----RDSLNEYEAKLSDLrarlqeaAAQAKQANGLNQEneraLGAIQRQVKEINSLQ 412
Cdd:PRK01156 267 MELEKNNYYKELEERHMKIINDPvyknRNYINDYFKYKNDI-------ENKKQILSNIDAE----INKYHAIIKKLSVLQ 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 413 SDFTKYlttadssllqtnialqlmEKSQKEYEKLAASLNEARQELSDKVrelsrsagktSLVEEAEKHARSLQElakqlE 492
Cdd:PRK01156 336 KDYNDY------------------IKKKSRYDDLNNQILELEGYEMDYN----------SYLKSIESLKKKIEE-----Y 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 493 EIKRNASGDELVRcAVDAATAYENILNAIKAAEDAANRAASASESALQTVI------KEDLPRKAKTLSSNS-----DKL 561
Cdd:PRK01156 383 SKNIERMSAFISE-ILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIralrenLDELSRNMEMLNGQSvcpvcGTT 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 562 LNEAKMtqKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDeVLDGL 641
Cdd:PRK01156 462 LGEEKS--NHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARADLED-IKIKI 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 642 NPI---QTDVERIKDTYG-----------------------------RTQNEDFKKALTDADNSVNKLTNKLPDLWRKIE 689
Cdd:PRK01156 539 NELkdkHDKYEEIKNRYKslkledldskrtswlnalavislidietnRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYID 618
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 732170495 690 S----INQQLLPLGN----ISDN---MDRIRELIQQARDAASKvaVPMRFNGKSGVEVRLpNDLED 744
Cdd:PRK01156 619 KsireIENEANNLNNkyneIQENkilIEKLRGKIDNYKKQIAE--IDSIIPDLKEITSRI-NDIED 681
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
249-713 |
2.31e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 49.25 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 249 EQMRHMETQAKDLRNQLLnyrsaISNhgSKIEGLERELTDLN--------------QEFETLQEKAQVNSRKAQTLNNNV 314
Cdd:TIGR04523 75 NKIKILEQQIKDLNDKLK-----KNK--DKINKLNSDLSKINseikndkeqknkleVELNKLEKQKKENKKNIDKFLTEI 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 315 NRATQSAKELDVKIKNVIRNVHML--------NRIRTWQKTHQGENNGLAN-----SIRDSLNE----YEAKLSDLRARl 377
Cdd:TIGR04523 148 KKKEKELEKLNNKYNDLKKQKEELenelnlleKEKLNIQKNIDKIKNKLLKlelllSNLKKKIQknksLESQISELKKQ- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 378 qeaaaQAKQANGLNQENERalgaIQRQVKEINSLQsdfTKYLTTADSsllQTNIALQLMEKsQKEYEK-------LAASL 450
Cdd:TIGR04523 227 -----NNQLKDNIEKKQQE----INEKTTEISNTQ---TQLNQLKDE---QNKIKKQLSEK-QKELEQnnkkikeLEKQL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 451 NEARQELSD----KVRELSRsagktSLVEEAEKHARSLQELAKQLEEIKRNASgdELvrcavdaatayENILNAIKaaed 526
Cdd:TIGR04523 291 NQLKSEISDlnnqKEQDWNK-----ELKSELKNQEKKLEEIQNQISQNNKIIS--QL-----------NEQISQLK---- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 527 aANRAASASE-SALQTVIKEDLpRKAKTLSSNSDKLLNEAkmtqKKLKQEVspalNNLQQTLNIVTVQKEVIDTNLTTLR 605
Cdd:TIGR04523 349 -KELTNSESEnSEKQRELEEKQ-NEIEKLKKENQSYKQEI----KNLESQI----NDLESKIQNQEKLNQQKDEQIKKLQ 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 606 dglhgIQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTygrtqNEDFKKALTDADNSVNKLTNKLPDLW 685
Cdd:TIGR04523 419 -----QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT-----RESLETQLKVLSRSINKIKQNLEQKQ 488
|
490 500 510
....*....|....*....|....*....|....*.
gi 732170495 686 RKIESINQQLLPL--------GNISDNMDRIRELIQ 713
Cdd:TIGR04523 489 KELKSKEKELKKLneekkeleEKVKDLTKKISSLKE 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
220-718 |
2.66e-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: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 220 LLNDLATMGEQLRLVKSQLQGLSASAGLLEQmrhmetQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEK 299
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEE------KLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 300 -AQVNSRKAQtLNNNVNRATQSAKELDVKIKNVIRNVHMLNRIRTWQKthqgennglANSIRDSLNEYEAKLSDLRARLQ 378
Cdd:TIGR02168 388 vAQLELQIAS-LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE---------LKELQAELEELEEELEELQEELE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 379 EAAAQAKQANGLNQENERALGAIQRQVKE----INSLQSDFTKYLTtadsslLQTNIALQLMEKSQ-------------- 440
Cdd:TIGR02168 458 RLEEALEELREELEEAEQALDAAERELAQlqarLDSLERLQENLEG------FSEGVKALLKNQSGlsgilgvlselisv 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 441 -KEYEK-LAASLNEARQEL-----------------SDKVR----ELSRSAGKTSLVEEAE--KHARSLQELAKQLEEIK 495
Cdd:TIGR02168 532 dEGYEAaIEAALGGRLQAVvvenlnaakkaiaflkqNELGRvtflPLDSIKGTEIQGNDREilKNIEGFLGVAKDLVKFD 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 496 ---RNASGDELVRCAV----DAATAYENILNA-----------IKAAEDAANRAASASESALQTVIK-EDLPRKAKTLSS 556
Cdd:TIGR02168 612 pklRKALSYLLGGVLVvddlDNALELAKKLRPgyrivtldgdlVRPGGVITGGSAKTNSSILERRREiEELEEKIEELEE 691
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 557 NSDKL---LNEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDT------NLTTLRDGLHgIQRGDIDAMISSAKSMV 627
Cdd:TIGR02168 692 KIAELekaLAELRKELEELEEELEQLRKELEELSRQISALRKDLARleaeveQLEERIAQLS-KELTELEAEIEELEERL 770
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 628 RKANDITDEVLDGLNPIQTDVERIKD--TYGRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQllpLGNISDNM 705
Cdd:TIGR02168 771 EEAEEELAEAEAEIEELEAQIEQLKEelKALREALDELRAELTLLNEEAANLRERLESLERRIAATERR---LEDLEEQI 847
|
570
....*....|...
gi 732170495 706 DRIRELIQQARDA 718
Cdd:TIGR02168 848 EELSEDIESLAAE 860
|
|
| TNFRSF6B |
cd10575 |
Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor ... |
71-177 |
2.75e-05 |
|
Tumor necrosis factor receptor superfamily member 6B (TNFRSF6B), also known as decoy receptor 3 (DcR3); The subfamily TNFRSF6B is also known as decoy receptor 3 (DcR3), M68, or TR6. This protein is a soluble receptor without death domain and cytoplasmic domain, and secreted by cells. It acts as a decoy receptor that competes with death receptors for ligand binding. It is a pleiotropic immunomodulator and biomarker for inflammatory diseases, autoimmune diseases, and cancer. Over-expression of this gene has been noted in several cancers, including pancreatic carcinoma, and gastrointestinal tract tumors. It can neutralize the biological effects of three tumor necrosis factor superfamily (TNFSF) members: TNFSF6 (Fas ligand/FasL/CD95L) and TNFSF14 (LIGHT) which are both involved in apoptosis and inflammation, and TNFSF15 (TNF-like molecule 1A/TL1A), which is a T cell co-stimulator and involved in gut inflammation. DcR3 is a novel inflammatory marker; higher DcR3 levels strongly correlate with inflammation and independently predict cardiovascular and all-cause mortality in chronic kidney disease (CKD) patients on hemodialysis. Increased synovial inflammatory cells infiltration in rheumatoid arthritis and ankylosing spondylitis is also associated with the elevated DcR3 expression. In cartilaginous fish, mRNA expression of DcR3 in the thymus and leydig, which are the representative lymphoid tissues of elasmobranchs, suggests that DcR3 may act as a modulator in the immune system. Interestingly, in banded dogfish (Triakis scyllia), DcR3 mRNA is strongly expressed in the gill, compared with human expression in the normal lung; both are respiratory organs, suggesting potential relevance of DcR3 to respiratory function.
Pssm-ID: 276901 [Multi-domain] Cd Length: 163 Bit Score: 46.25 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 71 YTGRCVPCN--CNGH---SNQCqdgsgicvNCQHNTAgehCErCQEGYYGNavHGSC---RACPcPhtnsfATGCVVNGg 142
Cdd:cd10575 51 YLEKCRYCNvfCTERqveKRQC--------NATHNRV---CE-CKPGYYME--HGFClrhSSCP-P-----GEGVIKLG- 109
|
90 100 110
....*....|....*....|....*....|....*
gi 732170495 143 dvrcsckAGYTGTQCERCAPGYFGNPQKFGGSCQP 177
Cdd:cd10575 110 -------TPYSDTQCEPCPPGFFSASSSSTEPCQP 137
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
267-642 |
2.93e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 2.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 267 NYRSAISnhgsKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKEldvkiknvirnvhmlnrirtwqk 346
Cdd:COG4372 32 QLRKALF----ELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE----------------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 347 thqgennglansIRDSLNEYEAKLSDLRARLqeaaaqakqaNGLNQENERALGAIQRQVKEINSLQSdftkylttadssl 426
Cdd:COG4372 85 ------------LNEQLQAAQAELAQAQEEL----------ESLQEEAEELQEELEELQKERQDLEQ------------- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 427 lqtniALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVRC 506
Cdd:COG4372 130 -----QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 507 AVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQQT 586
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 732170495 587 LNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEVLDGLN 642
Cdd:COG4372 285 LEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELA 340
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
280-637 |
3.22e-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: 48.90 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 280 EGLEReLTDLNQEFETlqekaQVNSRKAQTlnnnvnRATQSAKELdvkiKNVIRNVHmlnrIRTWQKTHQGENNGLANsI 359
Cdd:TIGR02168 186 ENLDR-LEDILNELER-----QLKSLERQA------EKAERYKEL----KAELRELE----LALLVLRLEELREELEE-L 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 360 RDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL--LQTNIA----- 432
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLanLERQLEeleaq 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 433 LQLMEKSQKEYEKLAASLNEARQELSDKVrelsrsagkTSLVEEAEKHARSLQELAKQLEEIKRNAsgdELVRCAVDAAT 512
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEEL---------ESLEAELEELEAELEELESRLEELEEQL---ETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 513 AYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLNIVTV 592
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELRE 468
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 732170495 593 QKEVIDTNLTTLRDGLHGIQrgdidAMISSAKSMVRKANDITDEV 637
Cdd:TIGR02168 469 ELEEAEQALDAAERELAQLQ-----ARLDSLERLQENLEGFSEGV 508
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
226-608 |
3.40e-05 |
|
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: 49.02 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 226 TMGEQLRLVKSQLQglsasaglleQMRHMETQA-KDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE-KAQVN 303
Cdd:pfam01576 335 ALEEETRSHEAQLQ----------EMRQKHTQAlEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQaKQDSE 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 304 SRKA------QTLNNNVN---RATQSAKELDVKIKNVIRNV-HMLNRIRTWQKTHQGENNGLANSIRDSLN----EYEAK 369
Cdd:pfam01576 405 HKRKklegqlQELQARLSeseRQRAELAEKLSKLQSELESVsSLLNEAEGKNIKLSKDVSSLESQLQDTQEllqeETRQK 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 370 LSdLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSL---------LQTNI--ALQLMEK 438
Cdd:pfam01576 485 LN-LSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLealeegkkrLQRELeaLTQQLEE 563
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 439 SQKEYEKLAASLNEARQELSDKVRELSRsagKTSLVEEAEKHARSL-QELAKQLEEIKRNAsgDELVRCavdAATAYENI 517
Cdd:pfam01576 564 KAAAYDKLEKTKNRLQQELDDLLVDLDH---QRQLVSNLEKKQKKFdQMLAEEKAISARYA--EERDRA---EAEAREKE 635
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 518 LNAIkaaedaanRAASASESALQTviKEDLPRKAKTLSSNSDKLLNEakmtqkklKQEVSPALNNLQQTLNIVTVQKEVI 597
Cdd:pfam01576 636 TRAL--------SLARALEEALEA--KEELERTNKQLRAEMEDLVSS--------KDDVGKNVHELERSKRALEQQVEEM 697
|
410
....*....|.
gi 732170495 598 DTNLTTLRDGL 608
Cdd:pfam01576 698 KTQLEELEDEL 708
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
199-329 |
3.65e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.60 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 199 QEPKDSSPAEEcddcdscvMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSK 278
Cdd:COG1340 125 QQTEVLSPEEE--------KELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 732170495 279 IEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIK 329
Cdd:COG1340 197 MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELK 247
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
277-538 |
5.35e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 277 SKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKnvirnvhmlnrirtwqkthqgenngla 356
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 357 nSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnqenERALGAIQRQVKEINSLQ-----SDFTKYLTTAD--SSLL-Q 428
Cdd:COG3883 69 -KLQAEIAEAEAEIEERREEL-----------------GERARALYRSGGSVSYLDvllgsESFSDFLDRLSalSKIAdA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 429 TNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagktSLVEEAEKHARSLQELAKQLEEIKRNASgDELVRCAV 508
Cdd:COG3883 131 DADLLEELKADKAELEAKKAELEAKLAELEALKAELE------AAKAELEAQQAEQEALLAQLSAEEAAAE-AQLAELEA 203
|
250 260 270
....*....|....*....|....*....|
gi 732170495 509 DAATAYENILNAIKAAEDAANRAASASESA 538
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
237-501 |
6.21e-05 |
|
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: 46.53 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 237 QLQGLSASAGLLEQmrhmETQAKDLRNQLLNYRSAISNHGSKIEGLE-------RELTDLNQEFETLQEKAQVNSRKAqt 309
Cdd:pfam12795 1 KLDELEKAKLDEAA----KKKLLQDLQQALSLLDKIDASKQRAAAYQkalddapAELRELRQELAALQAKAEAAPKEI-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 310 lnnnvnRATQSAKELDVKIKNVirnvhmLNRIRTWQKTHQGENNgLANSIRDSLNEYEAKLSDLRARLqeaaaqakqang 389
Cdd:pfam12795 75 ------LASLSLEELEQRLLQT------SAQLQELQNQLAQLNS-QLIELQTRPERAQQQLSEARQRL------------ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 390 lnQENERALgaiqrqvkeiNSLQSDFTKyLTTADSSLLQTNIALQlmeKSQ-KEYEKLAASLNeARQELSDKVRELsrsa 468
Cdd:pfam12795 130 --QQIRNRL----------NGPAPPGEP-LSEAQRWALQAELAAL---KAQiDMLEQELLSNN-NRQDLLKARRDL---- 188
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 732170495 469 gKTSLVEEAEKHARSLQEL------------AKQLEEIKRNASGD 501
Cdd:pfam12795 189 -LTLRIQRLEQQLQALQELlnekrlqeaeqaVAQTEQLAEEAAGD 232
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
307-522 |
6.32e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 6.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 307 AQTLNNNVNRATQSAKELDVKIKNVIRNVHML-NRIRTWQKTHQGEN-NGLANSIRDSLNEYEAKLSDLRARLQEAAAQA 384
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAeAALEEFRQKNGLVDlSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 385 KQANGLNQENERALGA------IQRQVKEINSLQSDFTKYLT--TADSSL---LQTNIAlQLMEKSQKEYEKLAASLNEA 453
Cdd:COG3206 243 AALRAQLGSGPDALPEllqspvIQQLRAQLAELEAELAELSAryTPNHPDviaLRAQIA-ALRAQLQQEAQRILASLEAE 321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 454 RQELSDKVRELSRSagktslVEEAEKHARSLQELAKQLEEIKRNasgdelvrcaVDAATA-YENILNAIK 522
Cdd:COG3206 322 LEALQAREASLQAQ------LAQLEARLAELPELEAELRRLERE----------VEVARElYESLLQRLE 375
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
220-456 |
7.05e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 7.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 220 LLNDLAT--MGEQLRLVKSQLQglSASAGLLEQMRHMETQAKDLRNQLLNYRSA--ISNHGSKIEGLERELTDLNQEFET 295
Cdd:COG3206 153 VANALAEayLEQNLELRREEAR--KALEFLEEQLPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 296 LQEKAQVNSRKAQTLNNNVNRATQSAKEL--DVKIKNVIRNVHMLNR-----IRTWQKTH----------QGENNGLANS 358
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELlqSPVIQQLRAQLAELEAelaelSARYTPNHpdvialraqiAALRAQLQQE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 359 IRDSLNEYEAKLSDLRARLQEaaaqakqangLNQEneraLGAIQRQVKEINSLQSDFTKylttadsslLQTNIalqlmEK 438
Cdd:COG3206 311 AQRILASLEAELEALQAREAS----------LQAQ----LAQLEARLAELPELEAELRR---------LEREV-----EV 362
|
250
....*....|....*...
gi 732170495 439 SQKEYEKLAASLNEARQE 456
Cdd:COG3206 363 ARELYESLLQRLEEARLA 380
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
772-898 |
7.45e-05 |
|
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: 43.95 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 772 MYLGNKdaSRDYIGMAVVDGQLTCVYNLGDREAELQVdqiltkseTKEAVMD----RVKFQRIYQFARLNYTKGATSSKP 847
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESLLS--------SGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 732170495 848 ETPGVYDMDgrnsntllnldpENVVFYVGGYPPDFKLPSRLSFPPYKGCIE 898
Cdd:pfam02210 81 PPGESLLLN------------LNGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
223-491 |
1.15e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 223 DLATMGEQLRLVKSQLQGLSASAGLLEQMRHM----ETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE 298
Cdd:COG4913 662 DVASAEREIAELEAELERLDASSDDLAALEEQleelEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 299 KAQVNSR-------KAQTLNNNVNRATQS-AKELDVKIKNVIRNVHMLNRI-RTWQKTHQGENNGLANSIrDSLNEYEAK 369
Cdd:COG4913 742 LARLELRalleerfAAALGDAVERELRENlEERIDALRARLNRAEEELERAmRAFNREWPAETADLDADL-ESLPEYLAL 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 370 LSDL--------RARLQEAAAQAKQAN--GLNQENERALGAIQRQVKEIN-SL-QSDFtkyltTADSSllqtniaLQLme 437
Cdd:COG4913 821 LDRLeedglpeyEERFKELLNENSIEFvaDLLSKLRRAIREIKERIDPLNdSLkRIPF-----GPGRY-------LRL-- 886
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 732170495 438 ksqkEYEKlaaSLNEARQELSDKVRELSRSAGKTSLvEEAEKHARSLQELAKQL 491
Cdd:COG4913 887 ----EARP---RPDPEVREFRQELRAVTSGASLFDE-ELSEARFAALKRLIERL 932
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
247-513 |
1.23e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 247 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKaqvNSRKAQTLNNNVNRATQSAKELDV 326
Cdd:pfam10174 406 LQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQ---REREDRERLEELESLKKENKDLKE 482
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 327 KIknvirnvhmlnrirtwqkthqgennglaNSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENEralGAIQRQVK 406
Cdd:pfam10174 483 KV----------------------------SALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLE---IAVEQKKE 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 407 EINSLQSDFTKYLTTADSSLLQTNIA--LQLME-----------KSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSL 473
Cdd:pfam10174 532 ECSKLENQLKKAHNAEEAVRTNPEINdrIRLLEqevarykeesgKAQAEVERLLGILREVENEKNDKDKKIAELESLTLR 611
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 732170495 474 -VEEAEKHARSLQelAKQLEEIKRNASGDELVRCAVDAATA 513
Cdd:pfam10174 612 qMKEQNKKVANIK--HGQQEMKKKGAQLLEEARRREDNLAD 650
|
|
| TNFRSF6 |
cd10579 |
Tumor necrosis factor receptor superfamily member 6 (TNFRSF6), also known as fas cell surface ... |
56-191 |
1.30e-04 |
|
Tumor necrosis factor receptor superfamily member 6 (TNFRSF6), also known as fas cell surface death receptor (Fas); TNFRSF6 (also known as fas cell surface death receptor (FasR) or Fas, APT1, CD95, FAS1, APO-1, FASTM, ALPS1A) contains a death domain and plays a central role in the physiological regulation of programmed cell death. It has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The receptor interactions with the Fas ligand (FasL), allowing the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10; autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, leading to apoptosis. This receptor has also been shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is involved in transducing the proliferating signals in normal diploid fibroblast and T cells. Of the several alternatively spliced transcript variants, some are candidates for nonsense-mediated mRNA decay (NMD). Isoforms lacking the transmembrane domain may negatively regulate the apoptosis mediated by the full length isoform.
Pssm-ID: 276905 [Multi-domain] Cd Length: 129 Bit Score: 43.52 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 56 SQGCSPGYYRDHKGLytgrCVPCncnghsnqcQDGSGICVNCQHNTAGEHCERCQEGY-YGNAVHGS-----CRACPCPH 129
Cdd:cd10579 7 EINCSEGLYRGGQFC----CQPC---------PPGTRKAIDCTTNGGKPDCVPCTEGKeYTDKKHYSdkcrrCKICDEEH 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732170495 130 tnsfatgcvvnGGDVRCSCkagyTGTQ---CeRCAPGYFGNPQKFgGSCQPCSCNSNGQLGSCHP 191
Cdd:cd10579 74 -----------GLEVEKNC----TRTQntkC-RCKSNFFCNSSPC-EHCDPCTTCEHGIIEECTP 121
|
|
| ApoLp-III_like |
cd13769 |
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles ... |
427-591 |
1.53e-04 |
|
Apolipophorin-III and similar insect proteins; Exchangeable apolipoproteins play vital roles in the transport of lipids and lipoprotein metabolism. Apolipophorin III (apoLp-III) assists in the loading of diacylglycerol, generated from triacylglycerol stores in the fat body through the action of adipokinetic hormone, into lipophorin, the hemolymph lipoprotein. ApoLp-III increases the lipid carrying capacity of lipophorin by covering the expanding hydrophobic surface resulting from diacylglycerol uptake. It plays a critical role in the transport of lipids during insect flight, and may also play a role in defense mechanisms and innate immunity.
Pssm-ID: 259842 [Multi-domain] Cd Length: 158 Bit Score: 43.85 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 427 LQTNIALQLMEKSQKEYEKLaasLNEARQELSDKVRELSrsagkTSLVEEAEKHArslQELAKQLEEIKRNAS--GDELV 504
Cdd:cd13769 17 LAQQVQKQLGLQNPEEVVNT---LKEQSDNFANNLQEVS-----SSLKEEAKKKQ---GEVEEAWNEFKTKLSetVPELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 505 RCAVDAATAYEnILNAIKaaedaanraasaseSALQTVIKE--DLprkAKTLSSNSDKLLNEakmTQKKLKQ---EVSPA 579
Cdd:cd13769 86 KSLPVEEKAQE-LQAKLQ--------------SGLQTLVTEsqKL---AKAISENSQKAQEE---LQKATKQaydIAVEA 144
|
170
....*....|..
gi 732170495 580 LNNLQQTLNIVT 591
Cdd:cd13769 145 AQNLQNQLQTAT 156
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
282-598 |
1.94e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 282 LEReLTDLNQEFE----TLQEKAQVnSRKAQTLNnnvnratQSAKELDVKIknvirnvhMLNRIRTWQKTHQGENNGLA- 356
Cdd:COG1196 188 LER-LEDILGELErqlePLERQAEK-AERYRELK-------EELKELEAEL--------LLLKLRELEAELEELEAELEe 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 357 -----NSIRDSLNEYEAKLSDLRARLQEAAAQAKQANG----LNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLL 427
Cdd:COG1196 251 leaelEELEAELAELEAELEELRLELEELELELEEAQAeeyeLLAELARLEQDIARLEERRRELEERLEELEEELAELEE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 428 QTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR-SAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVrc 506
Cdd:COG1196 331 ELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEaEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA-- 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 507 AVDAATAYENILNAIKAAEDAANRAASASESALQTVIKED-LPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQQ 585
Cdd:COG1196 409 EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAeEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE 488
|
330
....*....|...
gi 732170495 586 TLNIVTVQKEVID 598
Cdd:COG1196 489 AAARLLLLLEAEA 501
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
249-833 |
2.20e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.20 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 249 EQMRHMETQAKDLRNQLLNyrsaISNHGSKIEGLEREltdlnqefetLQEKAQVNSRKaqtlNNNVNRAtqsakeldVKI 328
Cdd:TIGR01612 572 EDSIHLEKEIKDLFDKYLE----IDDEIIYINKLKLE----------LKEKIKNISDK----NEYIKKA--------IDL 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 329 KNVIRN----VHMLNRIRTWQKT-HQGENNGLANSIRDSLNE-YEAKLSDLRARLQEAAAQAKQAnglNQENERALGAIQ 402
Cdd:TIGR01612 626 KKIIENnnayIDELAKISPYQVPeHLKNKDKIYSTIKSELSKiYEDDIDALYNELSSIVKENAID---NTEDKAKLDDLK 702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 403 RQV-KEINSLQSDFTK----YLTTADSSllQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSrsagktSLVEEA 477
Cdd:TIGR01612 703 SKIdKEYDKIQNMETAtvelHLSNIENK--KNELLDIIVEIKKHIHGEINKDLNKILEDFKNKEKELS------NKINDY 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 478 EKHARSLQELAKQLEEIkRNASGDELvrcavdaatayeNILNaikaaedaanraaSASESALQTVikEDLPRKAKTLSSN 557
Cdd:TIGR01612 775 AKEKDELNKYKSKISEI-KNHYNDQI------------NIDN-------------IKDEDAKQNY--DKSKEYIKTISIK 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 558 SD---KLLNEAKMtqkkLKQEVspaLNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGI-------QRGDIDAMISSAKSMV 627
Cdd:TIGR01612 827 EDeifKIINEMKF----MKDDF---LNKVDKFINFENNCKEKIDSEHEQFAELTNKIkaeisddKLNDYEKKFNDSKSLI 899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 628 RKANDITDEVLDGLNPIQTDVERIKDTygrtqnEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDN--M 705
Cdd:TIGR01612 900 NEINKSIEEEYQNINTLKKVDEYIKIC------ENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNtlI 973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 706 DRIRELiqqarDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSLSLFLQRPNSRENGGTENMFVMYLGNKDASRdyIG 785
Cdd:TIGR01612 974 DKINEL-----DKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLYHQFDEKEKATNDIEQKIEDANKNIPN--IE 1046
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 732170495 786 MAVvdgqLTCVYNLGD-------REAELQVDQILTKSETKEAVMDRVKFQ-RIYQF 833
Cdd:TIGR01612 1047 IAI----HTSIYNIIDeiekeigKNIELLNKEILEEAEINITNFNEIKEKlKHYNF 1098
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
229-576 |
2.87e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.83 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKSQLQGLSASAGLLEQMRhMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQE---KAQVNSR 305
Cdd:PRK03918 365 EEAKAKKEELERLKKRLTGLTPEK-LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgKCPVCGR 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 306 ------KAQTLN------NNVNRATQSAKELDVKIKNVIRNVHM-LNRIRTWQKTHQgenngLANSIR---DSLNEY--- 366
Cdd:PRK03918 444 elteehRKELLEeytaelKRIEKELKEIEEKERKLRKELRELEKvLKKESELIKLKE-----LAEQLKeleEKLKKYnle 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 367 ------------EAKLSDLRARLQEAAAQAKQANGLNQEN---ERALGAIQRQVKEINslqsdfTKYLTTADSSLLQTNI 431
Cdd:PRK03918 519 elekkaeeyeklKEKLIKLKGEIKSLKKELEKLEELKKKLaelEKKLDELEEELAELL------KELEELGFESVEELEE 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 432 ALQLMEKSQKEYeklaASLNEARQELSDKVRELSRSagKTSLVEEAEKHAR---SLQELAKQLEEIKRNASGDElvrcav 508
Cdd:PRK03918 593 RLKELEPFYNEY----LELKDAEKELEREEKELKKL--EEELDKAFEELAEtekRLEELRKELEELEKKYSEEE------ 660
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170495 509 daataYENILNaikaaedaANRAASASESALQTVIKEdLPRKAKTLSSNSDKLLNEaKMTQKKLKQEV 576
Cdd:PRK03918 661 -----YEELRE--------EYLELSRELAGLRAELEE-LEKRREEIKKTLEKLKEE-LEEREKAKKEL 713
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
219-588 |
3.51e-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: 45.34 E-value: 3.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 219 TLLNDLATMGEQLRLVKSQLQGLSAsagLLEQMRHMETQA-------KDLRNQLLNYRSAIsnhgskieglereltDLNQ 291
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQKLQSLCK---ELDILQREQATIdtrtsafRDLQGQLAHAKKQQ---------------ELQQ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 292 EFETLQEKAQVNSRKAQTLNN-NVNRATQSAKELDVKIKNVIRNVHMLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKL 370
Cdd:TIGR00618 438 RYAELCAAAITCTAQCEKLEKiHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPAR 517
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 371 SDL-----RARLQEAAAQAKQANGLNQENERALG-AIQRQVK----EINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQ 440
Cdd:TIGR00618 518 QDIdnpgpLTRRMQRGEQTYAQLETSEEDVYHQLtSERKQRAslkeQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQ 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 441 KEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDE----LVRCAVDAATAYEN 516
Cdd:TIGR00618 598 DLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERvrehALSIRVLPKELLAS 677
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732170495 517 ILNAIKAAEDAANRAASASESALQtviKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQQTLN 588
Cdd:TIGR00618 678 RQLALQKMQSEKEQLTYWKEMLAQ---CQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLK 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
358-611 |
9.59e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 9.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 358 SIRDSLNEYEAKLSDLRARLQEAAAQakqangLNQENER--ALGAiqrqvKEINSLQSDFTKylTTADSSLLQTNIAL-- 433
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQL------LEELNKKikDLGE-----EEQLRVKEKIGE--LEAEIASLERSIAEke 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 434 QLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAG-KTSLVEE------------------AEKHARSLQELAK----- 489
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrRDKLTEEyaelkeeledlraeleevDKEFAETRDELKDyrekl 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 490 -----QLEEIKRNAS--GDELVRcavdAATAYENILNAIKAAEDAANRAASASESAlQTVIKEDlPRKAKTLSSNSDKLL 562
Cdd:TIGR02169 395 eklkrEINELKRELDrlQEELQR----LSEELADLNAAIAGIEAKINELEEEKEDK-ALEIKKQ-EWKLEQLAADLSKYE 468
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 732170495 563 NEAKMTQKKLkQEVSPALNNLQQTLNIVTVQKEVIDT-------NLTTLRDGLHGI 611
Cdd:TIGR02169 469 QELYDLKEEY-DRVEKELSKLQRELAEAEAQARASEErvrggraVEEVLKASIQGV 523
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
274-608 |
1.21e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 43.88 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 274 NHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKeldvkiknvIRNVHMLNRIRTWQKTH-QGEN 352
Cdd:TIGR00606 309 NHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQAD---------RHQEHIRARDSLIQSLAtRLEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 353 NGLAnsiRDSLNEYEAK--LSDLRARLQEAAAQAKQANGLNQENERALgaiQRQVKEINSLQSDFTKYLTTADSSLLQTN 430
Cdd:TIGR00606 380 DGFE---RGPFSERQIKnfHTLVIERQEDEAKTAAQLCADLQSKERLK---QEQADEIRDEKKGLGRTIELKKEILEKKQ 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 431 IALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRsAGKTSLVEEAEKHARSLQ-----------ELAKQLEEIKRNA- 498
Cdd:TIGR00606 454 EELKFVIKELQQLEGSSDRILELDQELRKAERELSK-AEKNSLTETLKKEVKSLQnekadldrklrKLDQEMEQLNHHTt 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 499 SGDELVRCAVDAATAYENILNaikaaedaanraASASESALQTVIKEDLPRKaKTLSSNSDKLLNEAKMTQKKLKqEVSP 578
Cdd:TIGR00606 533 TRTQMEMLTKDKMDKDEQIRK------------IKSRHSDELTSLLGYFPNK-KQLEDWLHSKSKEINQTRDRLA-KLNK 598
|
330 340 350
....*....|....*....|....*....|
gi 732170495 579 ALNNLQQTLNIVTVQKEVIDTNLTTLRDGL 608
Cdd:TIGR00606 599 ELASLEQNKNHINNELESKEEQLSSYEDKL 628
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
247-680 |
1.25e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 43.89 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 247 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNnvnraTQSAKELDV 326
Cdd:TIGR01612 756 ILEDFKNKEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDEDAKQNYDKSKEYIK-----TISIKEDEI 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 327 -KIKNVIRNV--HMLNRIRTW---QKTHQGENNG-------LANSIR-----DSLNEYEAKLSDLRARlqeaaaqakqan 388
Cdd:TIGR01612 831 fKIINEMKFMkdDFLNKVDKFinfENNCKEKIDSeheqfaeLTNKIKaeisdDKLNDYEKKFNDSKSL------------ 898
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 389 gLNQENEralgAIQRQVKEINSLQSdFTKYLTTADSS----------------LLQTNIAL----QLMEKSQKeyeklaa 448
Cdd:TIGR01612 899 -INEINK----SIEEEYQNINTLKK-VDEYIKICENTkesiekfhnkqnilkeILNKNIDTikesNLIEKSYK------- 965
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 449 slNEARQELSDKVRELSRSAGKTSLVEEAEKHarslQELAKQLEEIKRN---ASGDELVRCAVDAATAYENILNAIKAAE 525
Cdd:TIGR01612 966 --DKFDNTLIDKINELDKAFKDASLNDYEAKN----NELIKYFNDLKANlgkNKENMLYHQFDEKEKATNDIEQKIEDAN 1039
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 526 DAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKlkqevspaLNNLQQTLNIVTVQKEVIDTNL---- 601
Cdd:TIGR01612 1040 KNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEILEEAEINITN--------FNEIKEKLKHYNFDDFGKEENIkyad 1111
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 602 --TTLRDGLHGIQRgDIDAMISSAKSMVRKANDITDEVLDGLNpiqtDVERIKDTygRTQNEDFKKALTDADNSVNKLTN 679
Cdd:TIGR01612 1112 eiNKIKDDIKNLDQ-KIDHHIKALEEIKKKSENYIDEIKAQIN----DLEDVADK--AISNDDPEEIEKKIENIVTKIDK 1184
|
.
gi 732170495 680 K 680
Cdd:TIGR01612 1185 K 1185
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
229-509 |
1.31e-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: 43.79 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKSQLQGLSA---SAGLLEQMRHMEtQAKDLRNQLLNYRSA---ISNHGSKIEGLERELTDLN---QEFETLQEK 299
Cdd:COG3096 864 QQLDQLKEQLQLLNKllpQANLLADETLAD-RLEELREELDAAQEAqafIQQHGKALAQLEPLVAVLQsdpEQFEQLQAD 942
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 300 aqvnsrkaqtlnnnVNRATQSAKELDVKI---KNVIRNVHMLNrirtWQKTHQ--GENNGLANSIRDSLNEYEAKLSDLR 374
Cdd:COG3096 943 --------------YLQAKEQQRRLKQQIfalSEVVQRRPHFS----YEDAVGllGENSDLNEKLRARLEQAEEARREAR 1004
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 375 ARLQEAAAQAKQANGLNQENERALGAIQRQVKEinsLQSDFTKYLTTADSSLLqtnialqlmEKSQKEYEKLAASLNEAR 454
Cdd:COG3096 1005 EQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQE---LEQELEELGVQADAEAE---------ERARIRRDELHEELSQNR 1072
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 732170495 455 QELSDKVRELSRSAGK-TSLVEEAEKHARSLQELAKQLEEIKrnASGDELVRCAVD 509
Cdd:COG3096 1073 SRRSQLEKQLTRCEAEmDSLQKRLRKAERDYKQEREQVVQAK--AGWCAVLRLARD 1126
|
|
| TNFRSF6_teleost |
cd13423 |
Tumor necrosis factor receptor superfamily member 6 (TNFRSF6) in teleosts; also known as fas ... |
109-218 |
1.76e-03 |
|
Tumor necrosis factor receptor superfamily member 6 (TNFRSF6) in teleosts; also known as fas cell surface death receptor (FasR); This subfamily of TNFRSF6 (also known as fas cell surface death receptor (FasR) or Fas; APT1; CD95; FAS1; APO-1; FASTM; ALPS1A) is found in teleosts. It contains a death domain and plays a central role in the physiological regulation of programmed cell death. In humans, it has been implicated in the pathogenesis of various malignancies and diseases of the immune system. The receptor interactions with the Fas ligand (FasL), allowing the formation of a death-inducing signaling complex that includes Fas-associated death domain protein (FADD), caspase 8, and caspase 10; autoproteolytic processing of the caspases in the complex triggers a downstream caspase cascade, leading to apoptosis. This receptor has also been shown to activate NF-kappaB, MAPK3/ERK1, and MAPK8/JNK, and is involved in transducing the proliferating signals in normal diploid fibroblast and T cells. In channel catfish and the Japanese rice fish, medaka, homologs of Fas receptor (FasR), as well as FADD and caspase 8, have been identified and characterized, and likely constitute the teleost equivalent of the death-inducing signaling complex (DISC). FasL/FasR are involved in the initiation of apoptosis and suggest that mechanisms of cell-mediated cytotoxicity in teleosts are similar to those used by mammals; presumably, the mechanism of apoptosis induction via death receptors was evolutionarily established during the appearance of vertebrates.
Pssm-ID: 276928 [Multi-domain] Cd Length: 103 Bit Score: 39.33 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 109 CQEGYYGnavHGSCRACPCPHTNSFATGCVVNGgdvrcsckagyTGTQCERCAPGYFGNPQKFGGSCQPC-SCNSNGQLG 187
Cdd:cd13423 2 CEDGTYQ---HEGLTCCLCPAGQHVEKHCTNNG-----------TDGECEACEDGTYNSHPNSLDSCEPCtSCDPNANLE 67
|
90 100 110
....*....|....*....|....*....|....*
gi 732170495 188 SCHPLTGD----CINQEPKDSSPAEECDDCDSCVM 218
Cdd:cd13423 68 VEERCTPSsdtvCRCKEGHYCDKGEECKVCYPCDT 102
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
229-498 |
1.79e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKSQLQGLSASAGLLEQMRHMEtQAKDLRNQLLNYRSA---ISNHGSKIEGLERELTDLN---QEFETLQEKAQV 302
Cdd:PRK04863 868 EQAKEGLSALNRLLPRLNLLADETLAD-RVEEIREQLDEAEEAkrfVQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQ 946
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 303 NSRKAQTLNNNVnRAtqsakeldvkIKNVIRNVHMLNrirtWQKTHQ--GENNGLANSIRDSLNEYEAKLSDLRARLQEA 380
Cdd:PRK04863 947 AQQTQRDAKQQA-FA----------LTEVVQRRAHFS----YEDAAEmlAKNSDLNEKLRQRLEQAEQERTRAREQLRQA 1011
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 381 AAQAKQANGLNQENERALGAIQRQVKEinsLQSDFTKYLTTADSSLLqtnialqlmEKSQKEYEKLAASLNEARQelsdK 460
Cdd:PRK04863 1012 QAQLAQYNQVLASLKSSYDAKRQMLQE---LKQELQDLGVPADSGAE---------ERARARRDELHARLSANRS----R 1075
|
250 260 270
....*....|....*....|....*....|....*....
gi 732170495 461 VRELSRSAGKTSL-VEEAEKHARSLQELAKQLEEIKRNA 498
Cdd:PRK04863 1076 RNQLEKQLTFCEAeMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
389-668 |
1.80e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 43.02 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 389 GLNQENERALGAIQRQVKEIN-SLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYE-----------KLAASLNEARQE 456
Cdd:COG5185 279 RLNENANNLIKQFENTKEKIAeYTKSIDIKKATESLEEQLAAAEAEQELEESKRETEtgiqnltaeieQGQESLTENLEA 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 457 LSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNA--SGDELVRCAVDAATAYENILNAIKAAEDAANRAASA 534
Cdd:COG5185 359 IKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQrgYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEE 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 535 SESALQTVIKEdLPRKAKTLSSNSDKLLNEAkmtQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRG 614
Cdd:COG5185 439 VSKLLNELISE-LNKVMREADEESQSRLEEA---YDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEG 514
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732170495 615 DIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDT-----------YGRTQNEDFKKALT 668
Cdd:COG5185 515 VRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASnaktdgqaanlRTAVIDELTQYLST 579
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
221-442 |
2.26e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.64 E-value: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 221 LNDLATMGEQLRLVKSQLQGLSASagLLEQMRHMETQAKDLRNQLlnyRSAISNHGSKIEGLERELTDLNQEFEtlqeka 300
Cdd:COG5185 369 EVELSKSSEELDSFKDTIESTKES--LDEIPQNQRGYAQEILATL---EDTLKAADRQIEELQRQIEQATSSNE------ 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 301 qVNSRKAQTLNNNVNRATQSAKElDVKIKNVIRNVHMLNRIRTW-----QKTHQGENN--GLANSIRDSLNEYEAKLSDL 373
Cdd:COG5185 438 -EVSKLLNELISELNKVMREADE-ESQSRLEEAYDEINRSVRSKkedlnEELTQIESRvsTLKATLEKLRAKLERQLEGV 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 732170495 374 RARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSS---LLQTNIALQLMEKSQKE 442
Cdd:COG5185 516 RSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTaviDELTQYLSTIESQQARE 587
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
229-717 |
2.36e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKaqvNSRKaq 308
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK---EERL-- 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 309 tlnnnvnratqsaKELDVKIKNVIRNvhmLNRIRTWQKTHQgenngLANSIRDSLNEYEAKLSDLrarlqeaaaQAKQAN 388
Cdd:PRK03918 341 -------------EELKKKLKELEKR---LEELEERHELYE-----EAKAKKEELERLKKRLTGL---------TPEKLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 389 GLNQENERALGAIQRQVKE----INSLQSDfTKYLTTADSSL-------------LQTNIALQLMEKSQKEYEKLAASLn 451
Cdd:PRK03918 391 KELEELEKAKEEIEEEISKitarIGELKKE-IKELKKAIEELkkakgkcpvcgreLTEEHRKELLEEYTAELKRIEKEL- 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 452 earQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASG---DELVRcavdAATAYENILN-AIKAAEDA 527
Cdd:PRK03918 469 ---KEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKynlEELEK----KAEEYEKLKEkLIKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 528 ANRAASASEsalqtviKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQQTLNivtvQKEVIDTNLTTLRDG 607
Cdd:PRK03918 542 KSLKKELEK-------LEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLK----ELEPFYNEYLELKDA 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 608 LHGIQRgdIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLWRK 687
Cdd:PRK03918 611 EKELER--EEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKR 688
|
490 500 510
....*....|....*....|....*....|...
gi 732170495 688 IESINQQLLPLGNISDNMDRIR---ELIQQARD 717
Cdd:PRK03918 689 REEIKKTLEKLKEELEEREKAKkelEKLEKALE 721
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-491 |
2.41e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 222 NDLATMGEQLRlvksQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAIsnhgsKIEGLERELTDLNQEFETLQEKAQ 301
Cdd:COG4913 242 EALEDAREQIE----LLEPIRELAERYAAARERLAELEYLRAALRLWFAQR-----RLELLEAELEELRAELARLEAELE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 302 VNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNvhmlnRIRTWQKTHQgennglanSIRDSLNEYEAKLSDLRARLQeaa 381
Cdd:COG4913 313 RLEARLDALREELDELEAQIRGNGGDRLEQLER-----EIERLERELE--------ERERRRARLEALLAALGLPLP--- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 382 aqakqanglnqENERALGAIQRQVKEInslqsdftkyLTTADssllqtnialQLMEKSQKEYEKLAASLNEARQELSDKV 461
Cdd:COG4913 377 -----------ASAEEFAALRAEAAAL----------LEALE----------EELEALEEALAEAEAALRDLRRELRELE 425
|
250 260 270
....*....|....*....|....*....|
gi 732170495 462 RELSRSAGKTSLVEEAEKHARslQELAKQL 491
Cdd:COG4913 426 AEIASLERRKSNIPARLLALR--DALAEAL 453
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
224-502 |
2.47e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.50 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 224 LATMGEQLRLVKSQLQGLSASAGLL-----EQMRHME---TQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLN----- 290
Cdd:pfam10174 242 ISSLERNIRDLEDEVQMLKTNGLLHtedreEEIKQMEvykSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTnqnsd 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 291 --QEFETLQEKAQVNSRKAQTLNNNV----NRATQSAKELDVKIKNvirnvhmLNRIRTWQKTHQGENNGLansiRDSLN 364
Cdd:pfam10174 322 ckQHIEVLKESLTAKEQRAAILQTEVdalrLRLEEKESFLNKKTKQ-------LQDLTEEKSTLAGEIRDL----KDMLD 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 365 EYEAKLSDLRARLqeaaaqakqANGLNQ--ENERALGAIQRQVKeinSLQSdftkylttaDSSllQTNIALQLMEKSQKE 442
Cdd:pfam10174 391 VKERKINVLQKKI---------ENLQEQlrDKDKQLAGLKERVK---SLQT---------DSS--NTDTALTTLEEALSE 447
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 443 YEKLAASLNEARqELSDKVRelsrsagktslVEEAEKHARSLQELAKQLEEIKRNASGDE 502
Cdd:pfam10174 448 KERIIERLKEQR-EREDRER-----------LEELESLKKENKDLKEKVSALQPELTEKE 495
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
390-485 |
3.00e-03 |
|
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: 39.78 E-value: 3.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 390 LNQENERA-LGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKlaasLNEARQELSDKVRELSRsa 468
Cdd:pfam06009 24 QNLENTSEkLSGINRSLEETNELVNDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ----LEVNSSSLSDNISRIKE-- 97
|
90
....*....|....*..
gi 732170495 469 gktsLVEEAEKHARSLQ 485
Cdd:pfam06009 98 ----LIAQARKAANSIK 110
|
|
| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
426-522 |
3.11e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 426 LLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSR------SAGKTSLVEEAEKHARSLQELAKQLEEIKRNAS 499
Cdd:smart00935 10 LQESPAGKAAQKQLEKEFKKRQAELEKLEKELQKLKEKLQKdaatlsEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQ 89
|
90 100
....*....|....*....|...
gi 732170495 500 GDELvrcavdaATAYENILNAIK 522
Cdd:smart00935 90 QEEL-------QKILDKINKAIK 105
|
|
| TSPN |
smart00210 |
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of ... |
1507-1643 |
3.71e-03 |
|
Thrombospondin N-terminal -like domains; Heparin-binding and cell adhesion domain of thrombospondin
Pssm-ID: 214560 Cd Length: 184 Bit Score: 40.42 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 1507 HSVLLGPEFKLVFSIRPR-SLTGILIHI-GSQPGKHLCVYLEAGKVTAS-MDSGAGGTSTSVT-PKQSLCDGQWHSVAVT 1582
Cdd:smart00210 46 FPSGLPEDFSLLTTFRQTpKSRGVLFAIyDAQNVRQFGLEVDGRANTLLlRYQGVDGKQHTVSfRNLPLADGQWHKLALS 125
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 732170495 1583 IKQHILHLELDTDSsytAGQIPFPPAStQEPLHLGGapANLTTLRIPVWKSFFGCLRNIHV 1643
Cdd:smart00210 126 VSGSSATLYVDCNE---IDSRPLDRPG-QPPIDTDG--IEVRGAQAADRKPFQGDLQQLKI 180
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
278-522 |
3.87e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 3.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 278 KIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNN--NVNRATQSAKELDVKIKNVIRnvhmlnRIRTWQKTHQG---EN 352
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQErrEALQRLAEYSWDEIDVASAER------EIAELEAELERldaSS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 353 NGLAnSIRDSLNEYEAKLSDLRARLqeaaaqaKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTnia 432
Cdd:COG4913 685 DDLA-ALEEQLEELEAELEELEEEL-------DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE--- 753
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 433 lqlmeksQKEYEKLAASLNEARQELSDKVRELsrsagktslveeAEKHARSLQELAKQLEEIKR---NASGDelVRCAVD 509
Cdd:COG4913 754 -------RFAAALGDAVERELRENLEERIDAL------------RARLNRAEEELERAMRAFNRewpAETAD--LDADLE 812
|
250
....*....|...
gi 732170495 510 AATAYENILNAIK 522
Cdd:COG4913 813 SLPEYLALLDRLE 825
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
229-488 |
3.97e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 41.98 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKS--QLQGLSASAG---LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLE---RELTDLN---QEFETLQ 297
Cdd:COG0497 133 EHQSLLDPdaQRELLDAFAGleeLLEEYREAYRAWRALKKELEELRADEAERARELDLLRfqlEELEAAAlqpGEEEELE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 298 EKAQVNSRkAQTLNNNVNRATQSAKELDVKIknvirnVHMLNRIRTWQKTHQGENNGLANsIRDSLNEYEAKLSDLRARL 377
Cdd:COG0497 213 EERRRLSN-AEKLREALQEALEALSGGEGGA------LDLLGQALRALERLAEYDPSLAE-LAERLESALIELEEAASEL 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 378 QEAAaqakqaNGLNQENERaLGAIQRQVKEINSLQSdftKYLTTADSSL-LQTNIA--LQLMEKSQKEYEKLAASLNEAR 454
Cdd:COG0497 285 RRYL------DSLEFDPER-LEEVEERLALLRRLAR---KYGVTVEELLaYAEELRaeLAELENSDERLEELEAELAEAE 354
|
250 260 270
....*....|....*....|....*....|....*.
gi 732170495 455 QELSDKVRELS--RSAGKTSLVEEAEKHarsLQELA 488
Cdd:COG0497 355 AELLEAAEKLSaaRKKAAKKLEKAVTAE---LADLG 387
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
425-724 |
4.20e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 425 SLLQTNIALQLMEKS----QKEYEKLAASLNEARQELSDKVRELS-RSAGKTSLVEEAEKHARSLQELAKQLEEIKRnas 499
Cdd:TIGR02169 675 ELQRLRERLEGLKRElsslQSELRRIENRLDELSQELSDASRKIGeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ--- 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 500 gdelvrcavdAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLlneakmtqKKLKQEVSPA 579
Cdd:TIGR02169 752 ----------EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKL--------EEEVSRIEAR 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 580 LNNLQQTLNIVTVQKEVIDTNLTTLRDglhgiQRGDIDAMISSAKsmvrkanditdevldglnpiqtdvERIKDtyGRTQ 659
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQE-----QRIDLKEQIKSIE------------------------KEIEN--LNGK 862
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 732170495 660 NEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQllpLGNISDNMDRIRELIQQARDAASKVAV 724
Cdd:TIGR02169 863 KEELEEELEELEAALRDLESRLGDLKKERDELEAQ---LRELERKIEELEAQIEKKRKRLSELKA 924
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
247-490 |
4.22e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.20 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 247 LLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLnqefetLQEKAQVNSRKaqtlnnnvnratqSAKELDV 326
Cdd:cd22656 126 LLKEAKKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDL------LTDEGGAIARK-------------EIKDLQK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 327 KIKNvirnvhmlnrirtwqkthqgENNGLANSIRDSLNEYEAKLSDLRARLqeaaaqakqanglnQENERALGAIQRQVK 406
Cdd:cd22656 187 ELEK--------------------LNEEYAAKLKAKIDELKALIADDEAKL--------------AAALRLIADLTAADT 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 407 EINSLQSDFTKylttadssllqtniALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQE 486
Cdd:cd22656 233 DLDNLLALIGP--------------AIPALEKLQGAWQAIATDLDSLKDLLEDDISKIPAAILAKLELEKAIEKWNELAE 298
|
....
gi 732170495 487 LAKQ 490
Cdd:cd22656 299 KADK 302
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
268-695 |
4.41e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 41.93 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 268 YRSAISNHGSKIEGLERELtdlnqefETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVhmlnrirtwqkt 347
Cdd:TIGR04523 24 YKNIANKQDTEEKQLEKKL-------KTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQI------------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 348 hqgennglaNSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLL 427
Cdd:TIGR04523 85 ---------KDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 428 QTNIALQLMEKSQKEYE----KLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQ----ELAKQLEEIKRNAS 499
Cdd:TIGR04523 156 KLNNKYNDLKKQKEELEnelnLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLEsqisELKKQNNQLKDNIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 500 --GDELVRCAVDAATAYENILNAIKAaedaanraasasesalQTVIKEDLPRKAKTLSSNSDKLLNEAKMTQkKLKQEVS 577
Cdd:TIGR04523 236 kkQQEINEKTTEISNTQTQLNQLKDE----------------QNKIKKQLSEKQKELEQNNKKIKELEKQLN-QLKSEIS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 578 pALNNlQQTLNIVTVQKEVIDTNLTTLRDglhgIQRgDIDAMISSAKSMVRKANDITDEVLDG----------LNPIQTD 647
Cdd:TIGR04523 299 -DLNN-QKEQDWNKELKSELKNQEKKLEE----IQN-QISQNNKIISQLNEQISQLKKELTNSesensekqreLEEKQNE 371
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 732170495 648 VERIKDtygrtQNEDFKKALTDADNSVNKLTNKLpdlwRKIESINQQL 695
Cdd:TIGR04523 372 IEKLKK-----ENQSYKQEIKNLESQINDLESKI----QNQEKLNQQK 410
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
388-588 |
4.78e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.95 E-value: 4.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 388 NGLNQENERALGAIQRQVKEINSLQSDFTKyLTTADSSLLQTNIALQLM---EKSQKEYEKLAASLNEARQELSDKVRE- 463
Cdd:pfam15905 97 QALEEELEKVEAKLNAAVREKTSLSASVAS-LEKQLLELTRVNELLKAKfseDGTQKKMSSLSMELMKLRNKLEAKMKEv 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 464 -----------------LSRSAGKTSLVEE----AEK-HARSLQELAKQLEEIKR-NASGDELVRCAVDAATAyENILNA 520
Cdd:pfam15905 176 makqegmegklqvtqknLEHSKGKVAQLEEklvsTEKeKIEEKSETEKLLEYITElSCVSEQVEKYKLDIAQL-EELLKE 254
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 732170495 521 IKAAEDAANRAASASESALQTVIKeDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEvspaLNNLQQTLN 588
Cdd:pfam15905 255 KNDEIESLKQSLEEKEQELSKQIK-DLNEKCKLLESEKEELLREYEEKEQTLNAE----LEELKEKLT 317
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
222-670 |
5.61e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 41.38 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 222 NDLATMGEQLRL----VKSQLQGLSAsagLLEQ-MRHME--TQAKD----LRNQLLNYRSAisnHGSKIEGLERELTDLN 290
Cdd:pfam06160 86 KALDEIEELLDDieedIKQILEELDE---LLESeEKNREevEELKDkyreLRKTLLANRFS---YGPAIDELEKQLAEIE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 291 QEFETLQE--------KAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIrnVHMLNRIRTWQKTHQGENNGLA-NSIRD 361
Cdd:pfam06160 160 EEFSQFEEltesgdylEAREVLEKLEEETDALEELMEDIPPLYEELKTEL--PDQLEELKEGYREMEEEGYALEhLNVDK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 362 SLNEYEAKLSDLRARLQEaaaqakqangLNQEN-ERALGAIQrqvKEINSLQSDF-----------------TKYLTTAD 423
Cdd:pfam06160 238 EIQQLEEQLEENLALLEN----------LELDEaEEALEEIE---ERIDQLYDLLekevdakkyveknlpeiEDYLEHAE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 424 SSLLQTNIALQLMEKS----------QKEYEKLAASLNEARQELSDKVRElsRSAGKTSLVEEaekharsLQELAKQLEE 493
Cdd:pfam06160 305 EQNKELKEELERVQQSytlnenelerVRGLEKQLEELEKRYDEIVERLEE--KEVAYSELQEE-------LEEILEQLEE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 494 IK----------RNASGDELVrcAVDAATAYENILNAIKaaedaanraasasesalQTVIKEDLPrkaktlsSNSDKLLN 563
Cdd:pfam06160 376 IEeeqeefkeslQSLRKDELE--AREKLDEFKLELREIK-----------------RLVEKSNLP-------GLPESYLD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 564 EAKMTQKKLkQEVSPALNNLQqtLNIVTVQKEVIDTnlttlrdglhgiqRGDIDAMISSAKSMVRKANdITDEVldglnp 643
Cdd:pfam06160 430 YFFDVSDEI-EDLADELNEVP--LNMDEVNRLLDEA-------------QDDVDTLYEKTEELIDNAT-LAEQL------ 486
|
490 500 510
....*....|....*....|....*....|
gi 732170495 644 IQtdverikdtYG---RTQNEDFKKALTDA 670
Cdd:pfam06160 487 IQ---------YAnryRSSNPEVAEALTEA 507
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
229-710 |
8.56e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKSQLQGLSaSAGLLEQMRHMETQAKDLRNQLLNY----RSAISNHGSKIEGLER------ELTDLNQEFETLQE 298
Cdd:PRK02224 187 GSLDQLKAQIEEKE-EKDLHERLNGLESELAELDEEIERYeeqrEQARETRDEADEVLEEheerreELETLEAEIEDLRE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 299 KAQVNSRKAQTLNNNVNRATQSAKEL-------------------------------DVKIKNVIRNVhmlnriRTWQKT 347
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELeeerddllaeaglddadaeavearreeledrDEELRDRLEEC------RVAAQA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 348 HQGENNGLANSI----------RDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTK 417
Cdd:PRK02224 340 HNEEAESLREDAddleeraeelREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 418 YLTTADSSLLQTNIALQLMEKSQKEYEKL------------------AASLNEARQELSDKVRELSRSAGKTSLVEEAEK 479
Cdd:PRK02224 420 ERDELREREAELEATLRTARERVEEAEALleagkcpecgqpvegsphVETIEEDRERVEELEAELEDLEEEVEEVEERLE 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 480 HARSLQELAKQLEEIKRNASG-DELVrcAVDAATAYENILNAikaaedaANRAASASESALQTVIKEDlprKAKTLSSNS 558
Cdd:PRK02224 500 RAEDLVEAEDRIERLEERREDlEELI--AERRETIEEKRERA-------EELRERAAELEAEAEEKRE---AAAEAEEEA 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 559 DKLLNEAKMTQKKLkQEVSPALNNLQqtlNIVTVQKEV--IDTNLTTLRDglhgiQRGDIDAMISSAKSMVRKANDITDE 636
Cdd:PRK02224 568 EEAREEVAELNSKL-AELKERIESLE---RIRTLLAAIadAEDEIERLRE-----KREALAELNDERRERLAEKRERKRE 638
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 732170495 637 VLDGLNPiqtdvERIKDTygRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDNMDRIRE 710
Cdd:PRK02224 639 LEAEFDE-----ARIEEA--REDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALEN 705
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
392-574 |
9.89e-03 |
|
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: 40.13 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 392 QENERALGAIQRQV----KEINSLQS---DFTKYLTTADSSLLQTNIALQLMEKS-----------QKEYEKLAASLNEA 453
Cdd:COG4942 23 AEAEAELEQLQQEIaeleKELAALKKeekALLKQLAALERRIAALARRIRALEQElaaleaelaelEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 454 RQELSDKVRELSRSAGKTSLV-----EEAEKHARSL-------QELAKQLEEIKRNAsgDELVRCAVDAATAYENiLNAI 521
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLAlllspEDFLDAVRRLqylkylaPARREQAEELRADL--AELAALRAELEAERAE-LEAL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 732170495 522 KAAEDAANRAASASESALQTVIKEdLPRKAKTLSSNSDKLLNEAKMTQKKLKQ 574
Cdd:COG4942 180 LAELEEERAALEALKAERQKLLAR-LEKELAELAAELAELQQEAEELEALIAR 231
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
229-323 |
9.96e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.00 E-value: 9.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 732170495 229 EQLRLVKSQLQGLSASAGLLEQ-----MRHMETQAKDLRNQLLNYRSAISNHGSKIEglerELTDLNQEFETLQEKAQVN 303
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAqlqklQEDLEKQAEIAREAQQNYERELVLHAEDIK----ALQALREELNELKAEIAEL 76
|
90 100
....*....|....*....|
gi 732170495 304 SRKAQTLNNNVNRATQSAKE 323
Cdd:pfam07926 77 KAEAESAKAELEESEESWEE 96
|
|
| |
