|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
40-294 |
1.08e-105 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 338.18 E-value: 1.08e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 40 SSRSLHPPYFNLAQAARIWATATCGErdpevsrPRPELFCKLVGgpaaqgsgHTIQGQFCDYCNSEDSRKAHPASHAIDG 119
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 120 SE----RWWQSPPLSSGTQYnqVNLTLDLGQLFHVAYILIKFAnSPRPDLWILERSvDFGSTYSPWQYFAHsrrDCVEQF 195
Cdd:smart00136 68 NNpnnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 196 GQEANMAITQ--DDQMLCVTEYSRIVPLENGEIVVSLINGRPGAKKFAFSDTLREFTKATNIRLRFLRTNTLLGHLISKA 273
Cdd:smart00136 141 GRPPRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR 220
|
250 260
....*....|....*....|.
gi 226423935 274 erdPTVTRRYYYSIKDISVGG 294
Cdd:smart00136 221 ---PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1844-2101 |
2.63e-104 |
|
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: 335.15 E-value: 2.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1844 LQGLSVSTGALEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQVNSRKAQTLYNNIDQT 1923
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1924 IQSAKELDMKIKNIVQNVHILLKQMARPGGEGTDLPVGDWSRELAEAQRMMRDLRSRDFKKHLQEAEAEKMEAQLLLHRI 2003
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2004 RTWLESHQVENNGLLKNIRDSLNDYEDKLQDLRSILQEAAAQAKQATGINHENEGVLGAIQRQMKEMDSLKNDFTKYLAT 2083
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 226423935 2084 ADSSLLQTNNLLQQMDKS 2101
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
44-294 |
5.83e-93 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 301.42 E-value: 5.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 44 LHPPYFNLAQAARIWATATCGERdpevsrpRPELFCKLVGGPAAQGsghtiqgqfCDYCNSEDSRKAHPASHAIDGSER- 122
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLN-------GPERYCILSGLEGGKK---------CFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 123 ---WWQSPPLSSgtQYNQVNLTLDLGQLFHVAYILIKFAnSPRPDLWILERSVDFGSTYSPWQYFAHsrrDCVEQFG-QE 198
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGrPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 199 ANMAITQDDQMLCVTEYSRIVPLENGEIVVSLINGRPGAKKFAFSDTLREFTKATNIRLRFLRTNTLLGHLiskaERDPT 278
Cdd:pfam00055 139 GPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 226423935 279 VTRRYYYSIKDISVGG 294
Cdd:pfam00055 215 VLRKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2284-2412 |
5.93e-51 |
|
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: 177.29 E-value: 5.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2284 AKSMVREANGITSEVLDGLNPIQTDLGRIKDSYESARRE---------DFSKALVDANNSVKKLTRKLPDLFIKIESINQ 2354
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 226423935 2355 QLLPLGNISDNVDRIRELIQQARDAANKVAIPMRFNGKSGVEVRLPNDLEDLKGYTSL 2412
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamB |
smart00281 |
Laminin B domain; |
1509-1638 |
9.89e-47 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 164.74 E-value: 9.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1509 SVHSASWVAPPSYLGDKVSSYGGYLTYHAKSFGLPGDmvLLGKQPDVQLTGQHMSLIHKEPSDPRPDRLHHGRVQVIEGN 1588
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 226423935 1589 FRHEGSSaPVSREELMTVLSRLERLHIRGLHFTETQRLTLGEVGLEEASD 1638
Cdd:smart00281 79 WQYYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1515-1649 |
2.80e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 158.20 E-value: 2.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1515 WVAPPSYLGDKVSSYGGYLTYHAKSFGLPGDmVLLGKQPDVQLTGQHMSLIHKEPSDPRPDR--LHHGRVQVIEGNFRHE 1592
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 226423935 1593 gSSAPVSREELMTVLSRLERLHIRGLHFTETQRLTLGEVGLEEASDTGSGPRAHLVE 1649
Cdd:pfam00052 81 -DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3155-3306 |
3.45e-33 |
|
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: 126.76 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3155 GIYFSqGGGHVVLANSVSLEPALTLTLSIRPRSLTGVLIHIASQS-GEHLSVYMEAGKVTTSMNSeaGGTVTSITPKRSL 3233
Cdd:cd00110 1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNgGDFLALELEDGRLVLRYDL--GSGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226423935 3234 CDGQWHSVTVSIKQHTLHLELDTDNSYTAGQLSFPPN-STRGSLHIGGVPDKLKMLTLPVWNSFFGCLKNIQVN 3306
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2989-3131 |
9.73e-32 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 122.91 E-value: 9.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2989 SPTSHLLFKLPQeLLKPRLQFSLDIQTTSSRGLVFHTGT--RDSFVALYLSEGHVIFALGAGGKKLRLRSKERYHDGKWH 3066
Cdd:cd00110 5 SGSSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSqnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226423935 3067 SVVFGLSGRKVHLVVDGLR-AQEGSLPGNSTISPREQVYLGLSP--SRKSKSLPQHSFVGCLRNFQLD 3131
Cdd:cd00110 84 SVSVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGGLPedLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3008-3133 |
9.84e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 116.28 E-value: 9.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3008 QFSLDIQTTSSRGLVFHTGT--RDSFVALYLSEGHVIFALGAGGKKLRLRSK-ERYHDGKWHSVVFGLSGRKVHLVVDGL 3084
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 3085 RAQEGSLPGNSTI-SPREQVYLGLSPS--RKSKSLPQHSFVGCLRNFQLDSK 3133
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEdlKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3183-3308 |
1.49e-28 |
|
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: 112.90 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3183 IRPRSLTGVLIHIASQSGEHLSVYMEAGKVTTSMNSEAGGTVTSITPKRsLCDGQWHSVTVSIKQHTLHLELDTDNSYTA 3262
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKN-LNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 226423935 3263 GQLSFPPN-STRGSLHIGGVPDKLKMLTLPVWNSFFGCLKNIQVNHI 3308
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
3178-3307 |
2.22e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 109.74 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3178 TLTLSIRPRSLTGVLIHIAS-QSGEHLSVYMEAGKVTTSMNSEAGGTVTSITPKRsLCDGQWHSVTVSIKQHTLHLELDT 3256
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSkGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 3257 DNS-YTAGQLSFPPNSTRGSLHIGGVPDKLKMLTLPVWNSFFGCLKNIQVNH 3307
Cdd:smart00282 80 GNRvSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2598-2738 |
8.11e-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: 102.88 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2598 YFEGTGYARIPTQPN-APFPNFMQTIQTTVDRGLLFFAENQ--DNFISLNIEDGNLMVKYKLNSEPPKekgIRDT--INN 2672
Cdd:cd00110 3 SFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYDLGSGSLV---LSSKtpLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2673 GRDHMILISIGKSQKRMLIN----MNKHSIIIEGEIFDFSTYYLGGIPIAIRERFNISTPAFQGCMKNLK 2738
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDgervVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3015-3133 |
1.09e-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: 93.25 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3015 TTSSRGLVFHTGTRDS-FVALYLSEGHVIFA--LGAGGKKLRLrSKERYHDGKWHSVVFGLSGRKVHLVVDGLRAQEGSL 3091
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 226423935 3092 PGNS-TISPREQVYLG--LSPSRKSKSLPQHSFVGCLRNFQLDSK 3133
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2765-2897 |
1.42e-20 |
|
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: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2765 TASFSRGGQMSFTNLDVPSlDRFQLSFGFQTFQPSGTLL--NHQTRTSSLLVTLEDGHIALSTRDSSSP-IFKSPGTYMD 2841
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPR-TRLSISFSFRTTSPNGLLLyaGSQNGGDFLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226423935 2842 GLLHHVSVISDTSGLRLLIDDQVL--RRNQRLASFSNAQQSLSMGG-------------GYFEGCISNVFV 2897
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGERVveSGSPGGSALLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2617-2738 |
1.06e-19 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 87.78 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2617 NFMQTIQTTVDRGLLFFA--ENQDNFISLNIEDGNLMVKYKLNSEPPKEKGIRDTINNGRDHMILISIGKSQKRMLINMN 2694
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 226423935 2695 KHSIIIEGEIFDF----STYYLGGIPIAIRERFNISTPAFQGCMKNLK 2738
Cdd:smart00282 81 NRVSGESPGGLTIlnldGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1263-1311 |
2.60e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 75.08 E-value: 2.60e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 1263 CECDPAGTAGHHCSPEGGQCPCRPNVIGRQCSRCATGYYGFPYCKPCNC 1311
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2788-2900 |
1.61e-15 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.84 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2788 QLSFGFQTFQPSGTLLNHQT--RTSSLLVTLEDGHIALSTRDSSSPIFKS--PGTYMDGLLHHVSVISDTSGLRLLIDD- 2862
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLGSGPARLTsdPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 2863 -QVLRRNQRLASFSNAQQSLSMGG-------------GYFEGCISNVFVQRM 2900
Cdd:smart00282 81 nRVSGESPGGLTILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1262-1304 |
3.33e-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: 72.00 E-value: 3.33e-15
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 226423935 1262 PCECDPAGTAGHHCSPEGGQCPCRPNVIGRQCSRCATGYYGFP 1304
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1263-1306 |
2.99e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 69.26 E-value: 2.99e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 226423935 1263 CECDPAGTAGHHCSPEGGQCPCRPNVIGRQCSRCATGYYG--FPYC 1306
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2624-2738 |
7.73e-14 |
|
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: 70.53 E-value: 7.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2624 TTVDRGLLFFAENQDN-FISLNIEDGNLMVKYKLNSEPPKEKGIRDTINNGRDHMILISIGKSQKRMLINMNKHSIIIEG 2702
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 226423935 2703 EIFDF----STYYLGGIPIAIRERFNISTPAFQGCMKNLK 2738
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1401-1451 |
4.55e-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: 65.84 E-value: 4.55e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 1401 PCSCNRDGTEPSVCDPETGACMCKENVEGPQCQLCREGsFYLDPTNPKGCT 1451
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
532-574 |
1.28e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 64.68 E-value: 1.28e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 226423935 532 ACQCSTIGSYPVPCDPGNGQCDCLPGITGRQCDRCLSGAYDFP 574
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1353-1398 |
5.66e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.76 E-value: 5.66e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 226423935 1353 CNCSRKGTIEaavSECDRDSGQCRCKPRVTGQQCDKCAPGFYQFPE 1398
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1353-1404 |
6.33e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.76 E-value: 6.33e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 1353 CNCSRKGTieaAVSECDRDSGQCRCKPRVTGQQCDKCAPGFYQFPECVPCSC 1404
Cdd:pfam00053 1 CDCNPHGS---LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1353-1399 |
9.22e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 9.22e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 1353 CNCSRKGTIEaavSECDRDSGQCRCKPRVTGQQCDKCAPGFY--QFPEC 1399
Cdd:smart00180 1 CDCDPGGSAS---GTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
533-576 |
1.52e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.56 E-value: 1.52e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 226423935 533 CQCSTIGSYPVPCDPGNGQCDCLPGITGRQCDRCLSGAYD--FPYC 576
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1402-1450 |
1.93e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.22 E-value: 1.93e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 1402 CSCNRDGTEPSVCDPETGACMCKENVEGPQCQLCREGSFYLDPTNPKGC 1450
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
533-580 |
2.30e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 2.30e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 226423935 533 CQCSTIGSYPVPCDPGNGQCDCLPGITGRQCDRCLSGAYDFPYCQGSG 580
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
422-462 |
4.54e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.06 E-value: 4.54e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 226423935 422 PCSCDPE--RADDCDQGSGHCHCKPNFSGDYCETCADGYYNFP 462
Cdd:cd00055 1 PCDCNGHgsLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1683-1729 |
6.08e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.68 E-value: 6.08e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 1683 PCNCNGH---SNRCQDGSGICInCQHNTAGEHCERCQAGHYGNAIHG-SCR 1729
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| LamG |
smart00282 |
Laminin G domain; |
2431-2566 |
7.50e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 62.36 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2431 FVMYLGNKDaSKDYIGMAVVDGQLTCVYNLGDREAEVQIDQVltesesqeAVMD----RVKFQRIYQFAKL--NYTKEAT 2504
Cdd:smart00282 14 LLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPT--------PLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226423935 2505 STKPkapgvydmesaSSNTLLNLDpenAVFYVGGYPPGFELPRRLRFPPYKGCIELDDLNEN 2566
Cdd:smart00282 85 GESP-----------GGLTILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1836-2193 |
9.15e-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: 68.17 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1836 ELRLVKSKLQG---LSVSTGALEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQE------KA 1906
Cdd:TIGR02169 215 ALLKEKREYEGyelLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrvKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1907 QVNSRKAQ--TLYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARPGGEGTDLPV--GDWSRELAEAQRMMRDLRSRdf 1982
Cdd:TIGR02169 295 KIGELEAEiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrDKLTEEYAELKEELEDLRAE-- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1983 kkhLQEAEAEKMEAQLLLHRIRTWLEShqvennglLKNIRDSLNDYEDKLQDLRSILQEAaaqakqatGINHENEgvLGA 2062
Cdd:TIGR02169 373 ---LEEVDKEFAETRDELKDYREKLEK--------LKREINELKRELDRLQEELQRLSEE--------LADLNAA--IAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2063 IQRQMKEMDSLKNDFTKYLATADSSLLQTNnllQQMDKSQKEYESLAAALNGARQELSDRVRELSRsggkaplvVEAEKH 2142
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQEWKLEQLA---ADLSKYEQELYDLKEEYDRVEKELSKLQRELAE--------AEAQAR 500
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226423935 2143 A--QSLQELAKQLEEIKRNTSG-----DELVRCAVDAATAYE----NILNAIRAAEDAASKA 2193
Cdd:TIGR02169 501 AseERVRGGRAVEEVLKASIQGvhgtvAQLGSVGERYATAIEvaagNRLNNVVVEDDAVAKE 562
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
423-464 |
1.19e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.19e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 226423935 423 CSCDP--ERADDCDQGSGHCHCKPNFSGDYCETCADGYYNFPFC 464
Cdd:pfam00053 1 CDCNPhgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1731-1782 |
1.63e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 1.63e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 1731 CPCPHTNSFATGCAVDGGavRCACKPGYTGTQCERCAPGYFGNPQKfGGSCQ 1782
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
488-535 |
1.94e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 1.94e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 488 CDCNLEGVLPEICDDR-GRCLCRPGVEGPQCDSCRSGSYSFPICQACQC 535
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2793-2897 |
2.34e-10 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 60.90 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2793 FQTFQPSGTLL-NHQTRTSSLLVTLEDGHIALSTRDSSSPI-FKSPGTYM-DGLLHHVSVISDTSGLRLLIDDQVLRRNQ 2869
Cdd:pfam02210 1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLGSGPEsLLSSGKNLnDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 226423935 2870 RLASFS--NAQQSLSMGG-------------GYFEGCISNVFV 2897
Cdd:pfam02210 81 PPGESLllNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1731-1781 |
2.47e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 2.47e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 1731 CPCPHTNSFATGCAVDGGavRCACKPGYTGTQCERCAPGYFGNPQKFGGSC 1781
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1402-1450 |
2.85e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 2.85e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 1402 CSCNRDGTEPSVCDPETGACMCKENVEGPQCQLCREGSFYldpTNPKGC 1450
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
423-463 |
3.75e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 3.75e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 226423935 423 CSCDPERA--DDCDQGSGHCHCKPNFSGDYCETCADGYYNFPF 463
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1731-1774 |
3.97e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 3.97e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 226423935 1731 CPCPHTNSFATGCAVDGGavRCACKPGYTGTQCERCAPGYFGNP 1774
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2386-2564 |
1.17e-09 |
|
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: 59.35 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2386 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPDlRENGgtedmFVMYLGNKDaSKDYIGMAVVDGQLTCVYNLGDREA 2465
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTT-SPNG-----LLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2466 EVQidqvlteseSQEAVMD----RVKFQRIYQFAKL--NYTKEATSTKPkapgvydmesaSSNTLLNLDPEnavFYVGGY 2539
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSP-----------GGSALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 226423935 2540 PPGFELPRRLRFPPYKGCIELDDLN 2564
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
488-528 |
4.16e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.67 E-value: 4.16e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 226423935 488 CDCNLEGVLPEICDDR-GRCLCRPGVEGPQCDSCRSGSYSFP 528
Cdd:cd00055 2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1684-1731 |
9.80e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.51 E-value: 9.80e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 1684 CNCNGH---SNRCQDGSGICInCQHNTAGEHCERCQAGHYGNAIhGSCRVC 1731
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
488-530 |
1.06e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 1.06e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 226423935 488 CDCNLEGVLPEICD-DRGRCLCRPGVEGPQCDSCRSGSY--SFPIC 530
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
628-678 |
1.09e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.51 E-value: 1.09e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 628 CQCHEAGTLSGigECGQEDGDCSCKAHVTGDACDTCEDGFFSLEKSNYFGC 678
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1829-2372 |
1.31e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1829 DLASMGEELRLVKSKLQGLSVSTGALE-QIRHMETQAKDLRNQLLGFRSATSSHGSKMDD-------LEKELSHLNREFE 1900
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEaELEELESRLEELEEQLETLRSKVAQLELQIASlnneierLEARLERLEDRRE 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1901 TLQEKAQVNSRKAQ-----TLYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARPGGEGTDLpvgdwSRELAEAQ---R 1972
Cdd:TIGR02168 418 RLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA-----ERELAQLQarlD 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1973 MMRDLRSRdfKKHLQEAEAEKMEAQLLLHRIRTWL-ESHQVENN----------GLLKNI-RDSLNDYEDKLQDLR---- 2036
Cdd:TIGR02168 493 SLERLQEN--LEGFSEGVKALLKNQSGLSGILGVLsELISVDEGyeaaieaalgGRLQAVvVENLNAAKKAIAFLKqnel 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2037 ---SILQEAAAQAKQATGINHEN----EGVLGAI------------------------------QRQMKEMDSLKNDFTK 2079
Cdd:TIGR02168 571 grvTFLPLDSIKGTEIQGNDREIlkniEGFLGVAkdlvkfdpklrkalsyllggvlvvddldnaLELAKKLRPGYRIVTL 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2080 --YLAT-----------ADSSLLQTNN----LLQQMDKSQKEYESLAAALNGARQELSD----------RVRELSR--SG 2130
Cdd:TIGR02168 651 dgDLVRpggvitggsakTNSSILERRReieeLEEKIEELEEKIAELEKALAELRKELEEleeeleqlrkELEELSRqiSA 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2131 GKAPLVV---EAEKHAQSLQELAKQLEEI---------KRNTSGDELVRCAVDAAT------AYENILNAIRAAEDAASK 2192
Cdd:TIGR02168 731 LRKDLARleaEVEQLEERIAQLSKELTELeaeieeleeRLEEAEEELAEAEAEIEEleaqieQLKEELKALREALDELRA 810
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2193 ATSASKSAFQTVI--KEDLPKRAKTLSSDSEELLNEAKMTQKRLQQVSPALNSLQQT-------LKTVSVQKDLLDANLT 2263
Cdd:TIGR02168 811 ELTLLNEEAANLRerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELieeleseLEALLNERASLEEALA 890
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2264 VARDDLhGIQRGDIDSVvigaKSMVREANGITSEVLDGLNPIQTDLGRIK---DSYESARREDFSKALVDANNSVKKLTR 2340
Cdd:TIGR02168 891 LLRSEL-EELSEELREL----ESKRSELRRELEELREKLAQLELRLEGLEvriDNLQERLSEEYSLTLEEAEALENKIED 965
|
650 660 670
....*....|....*....|....*....|..
gi 226423935 2341 KLPDLFIKIESINQQLLPLGNIsdNVDRIREL 2372
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKELGPV--NLAAIEEY 995
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1835-2244 |
4.19e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1835 EELRLVKSKLQGLSVSTGALEQIRHmetQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQVNSRKAQ 1914
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQE---ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1915 tlYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARpggEGTDLPVGDWsRELAEAQRMMRDLRSRdfkkhLQEAEAEKM 1994
Cdd:COG4717 148 --LEELEERLEELRELEEELEELEAELAELQEELEE---LLEQLSLATE-EELQDLAEELEELQQR-----LAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1995 EAQLLLHRIRTWLEshQVENNGLLKNIRDSLNDYEDKLQDLRSILQEAAAQAKQATGINHenegVLGAIQRQMKEMDSLK 2074
Cdd:COG4717 217 EAQEELEELEEELE--QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT----IAGVLFLVLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2075 NDFTKYLATADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSGGKAP-LVVEAEKHAQSLQ--ELAK 2151
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQeLLREAEELEEELQleELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2152 QLEEI--KRNTSGDELVRCAVDAATAYENILNAIRAAEDAASKATSASKSAFQTVIKEDLPKRAKTLSSDSEELLNEAKM 2229
Cdd:COG4717 371 EIAALlaEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410
....*....|....*
gi 226423935 2230 TQKRLQQVSPALNSL 2244
Cdd:COG4717 451 LREELAELEAELEQL 465
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
628-679 |
6.15e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.20 E-value: 6.15e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 628 CQCHEAGTLSGigECGQEDGDCSCKAHVTGDACDTCEDGFFSLEkSNYFGCQ 679
Cdd:cd00055 2 CDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2078-2409 |
8.04e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.60 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2078 TKYLATADSSLLQTNnlLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSggkaplvvEAEkhaqsLQELAKQLEEIK 2157
Cdd:COG4372 22 TGILIAALSEQLRKA--LFELDKLQEELEQLREELEQAREELEQLEEELEQA--------RSE-----LEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2158 RNTSgdelvrcavDAATAYENILNAIRAAEDAASKAtsasKSAFQTVIKE--DLPKRAKTLSSDSEELLNEAKMTQKRLQ 2235
Cdd:COG4372 87 EQLQ---------AAQAELAQAQEELESLQEEAEEL----QEELEELQKErqDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2236 QVSPALNSLQQTLKTVSVQKDLLDANLTVARddlhgiqrgdidsvvigAKSMVREANG--ITSEVLDGLNPIQTDLGRIK 2313
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALSEAEAEQA-----------------LDELLKEANRnaEKEEELAEAEKLIESLPREL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2314 DSYESARREDFSKALVDANNSVKKLTRKLPDLFIKIESINQQL--LPLGNISDNVDRIRELIQQARDAANKVAIPMrfNG 2391
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEieELELAILVEKDTEEEELEIAALELEALEEAA--LE 294
|
330
....*....|....*...
gi 226423935 2392 KSGVEVRLPNDLEDLKGY 2409
Cdd:COG4372 295 LKLLALLLNLAALSLIGA 312
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
628-678 |
1.38e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.38e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 628 CQCHEAGTLSGigECGQEDGDCSCKAHVTGDACDTCEDGFFsleKSNYFGC 678
Cdd:smart00180 1 CDCDPGGSASG--TCDPDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
295-343 |
3.10e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 49.27 E-value: 3.10e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 295 RCVCNGHAEACSADNPEkQFRCECQHHTCGDTCNRCCAGYNQRRWQPAG 343
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG-TGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1684-1726 |
3.87e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.85 E-value: 3.87e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 226423935 1684 CNCN--GH-SNRCQDGSGICInCQHNTAGEHCERCQAGHYGNAIHG 1726
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
681-724 |
4.07e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.89 E-value: 4.07e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 226423935 681 CQCDIGGALTTMCSGPSGVCQCREHVEGKQCQRPENNYYFPDLH 724
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
681-719 |
8.16e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 8.16e-07
10 20 30
....*....|....*....|....*....|....*....
gi 226423935 681 CQCDIGGALTTMCSGPSGVCQCREHVEGKQCQRPENNYY 719
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1855-2382 |
5.27e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.53 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1855 EQIRHMETQAKDlRNQLLGF----------RSATSSHGSKMDDLEKELSHLNREfetlqekaqvnsrkaQTLYNnIDQTI 1924
Cdd:pfam12128 123 ELGRFMKNAGIQ-RTNLLNTreyrsiiqndRTLLGRERVELRSLARQFALCDSE---------------SPLRH-IDKIA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1925 QS--AKELDMK-IKNIVqnVHILLKQMARPggEGTDLPVGDWSRELAEAQRMMRDLRSRDFKKHLQEAEAEKMEAQLLLH 2001
Cdd:pfam12128 186 KAmhSKEGKFRdVKSMI--VAILEDDGVVP--PKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2002 RIRTWLESHQVENNGLLKNIRDSLNDYEDKLQDLRSILQEAAAQakqatgINHENEGVLGAIQRQMKEMDSLKNDFTKYL 2081
Cdd:pfam12128 262 HLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE------LNGELSAADAAVAKDRSELEALEDQHGAFL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2082 ------ATADSSLL-QTNNLLQQMDKSQKEYE----SLAAALNGARQELSDR-VRELSRSG--------GKAPLVVEAEK 2141
Cdd:pfam12128 336 dadietAAADQEQLpSWQSELENLEERLKALTgkhqDVTAKYNRRRSKIKEQnNRDIAGIKdklakireARDRQLAVAED 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2142 HAQSL-QELAKQLEEIKRNTSGDEL--------VRCAVDAATAYENILNAIRAAEDAASKATSASKSAFQTVikEDLP-- 2210
Cdd:pfam12128 416 DLQALeSELREQLEAGKLEFNEEEYrlksrlgeLKLRLNQATATPELLLQLENFDERIERAREEQEAANAEV--ERLQse 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2211 -KRAKTLSSDSEELLNEAkmtQKRLQQVSPALNSLQQTL--------KTVSVQKDLLDANL--TVARDDLHgiqRGDIDS 2279
Cdd:pfam12128 494 lRQARKRRDQASEALRQA---SRRLEERQSALDELELQLfpqagtllHFLRKEAPDWEQSIgkVISPELLH---RTDLDP 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2280 VVIGAkSMVREAN--GIT--------SEVLDGLNPIQTDLGRIKDSYESAR--REDFSKALVDANNSVKKLTRKLPDLFI 2347
Cdd:pfam12128 568 EVWDG-SVGGELNlyGVKldlkridvPEWAASEEELRERLDKAEEALQSARekQAAAEEQLVQANGELEKASREETFART 646
|
570 580 590
....*....|....*....|....*....|....*.
gi 226423935 2348 KIESINQQLLPLGNISDNV-DRIRELIQQARDAANK 2382
Cdd:pfam12128 647 ALKNARLDLRRLFDEKQSEkDKKNKALAERKDSANE 682
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1827-2246 |
1.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1827 LNDLASMGEELRLVKSKLQGlsvSTGALE---------------QIRHMETQAKDLRN---------QLLGFRSATSShg 1882
Cdd:PRK03918 233 LEELKEEIEELEKELESLEG---SKRKLEekireleerieelkkEIEELEEKVKELKElkekaeeyiKLSEFYEEYLD-- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1883 sKMDDLEKELSHLNREFETLQEKAQvnsrKAQTLYNNIDQTIQSAKELDMKIKNI------VQNVHILLKQMARPGGEGT 1956
Cdd:PRK03918 308 -ELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELeerhelYEEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1957 DLPVGDWSRELAEAQR--------------MMRDLRSR--DFKKHLQEAEAEKME-----AQLLLHRIRTWLESHQVEnn 2015
Cdd:PRK03918 383 GLTPEKLEKELEELEKakeeieeeiskitaRIGELKKEikELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAE-- 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2016 glLKNIRDSLNDYEDKLQDLRSILQeaaaqakqatginhENEGVLGAIQR--QMKEM-DSLKNdftkylatADSSLLQTN 2092
Cdd:PRK03918 461 --LKRIEKELKEIEEKERKLRKELR--------------ELEKVLKKESEliKLKELaEQLKE--------LEEKLKKYN 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2093 nlLQQMDKSQKEYESLAAALNGARQELSDRVRELSRsggKAPLVVEAEKHAQSLQELAKQLEEIKRntsgdELVRCAVDa 2172
Cdd:PRK03918 517 --LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK---LEELKKKLAELEKKLDELEEELAELLK-----ELEELGFE- 585
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226423935 2173 atAYENILNAIRAAEDAASKATSASKSAFQTVIKEDLPKRAKTLSSDSEELLNEAKmtqKRLQQVSPALNSLQQ 2246
Cdd:PRK03918 586 --SVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE---KRLEELRKELEELEK 654
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2062-2379 |
1.20e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.45 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2062 AIQRQMKEMDSLKndftkyLATADSSLLQTN-----NLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSGGKAPLV 2136
Cdd:PRK11281 40 DVQAQLDALNKQK------LLEAEDKLVQQDleqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2137 VEAEKHAQSLQELAKQLEEIKrntsgDELVRCAVDAATAYENILNAIRAAEDAASKATSASKSAFQ--TVIKEDLPKRaK 2214
Cdd:PRK11281 114 TRETLSTLSLRQLESRLAQTL-----DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQirNLLKGGKVGG-K 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2215 TLSSDSEELLN-EAKM--TQKRLQQVSPALNSLQQTLKTvsVQKDLLDANLTVARDDLHGIQRgdidsvVIGAKSM---- 2287
Cdd:PRK11281 188 ALRPSQRVLLQaEQALlnAQNDLQRKSLEGNTQLQDLLQ--KQRDYLTARIQRLEHQLQLLQE------AINSKRLtlse 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2288 --VREAngitsEVLDGLNPIQTD-LgrIKDsyESARREDFSKALVDANNSVKKLTRKlpDLFIK------------I-ES 2351
Cdd:PRK11281 260 ktVQEA-----QSQDEAARIQANpL--VAQ--ELEINLQLSQRLLKATEKLNTLTQQ--NLRVKnwldrltqsernIkEQ 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 226423935 2352 IN---------------QQLLP-LGNISDNVDRIREL------IQQARDA 2379
Cdd:PRK11281 329 ISvlkgslllsrilyqqQQALPsADLIEGLADRIADLrleqfeINQQRDA 378
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
681-719 |
4.92e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.11 E-value: 4.92e-05
10 20 30
....*....|....*....|....*....|....*....
gi 226423935 681 CQCDIGGALTTMCSGPSGVCQCREHVEGKQCQRPENNYY 719
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1986-2328 |
1.88e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1986 LQEAEAEKMEAQLLLHRIRtwLESHQVEnnglLKNIRDSLNDYEDKLQDLRSILqeaaaqakqatginHENEGVLGAIQR 2065
Cdd:TIGR02168 215 YKELKAELRELELALLVLR--LEELREE----LEELQEELKEAEEELEELTAEL--------------QELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2066 QMKEMDSLKNDftkylatADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSggkaplvveAEKHAQS 2145
Cdd:TIGR02168 275 EVSELEEEIEE-------LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK---------LDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2146 LQELAKQLEEIKRNTSG-----DELVRCAVDAATAYENILNAIRAAEDAASKATSASKSAFQTVI-----KEDLPKRAKT 2215
Cdd:TIGR02168 339 LAELEEKLEELKEELESleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErlearLERLEDRRER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2216 LSSDSEELL-----NEAKMTQKRLQQVSPALNSLQQTLKTVSVQKDLLDANLTVARDDLHGIQRG--DIDSVVIGAKSMV 2288
Cdd:TIGR02168 419 LQQEIEELLkkleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaQLQARLDSLERLQ 498
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 226423935 2289 REANGIT---SEVLDGLNPIQTDLGRIKDSYESarREDFSKAL 2328
Cdd:TIGR02168 499 ENLEGFSegvKALLKNQSGLSGILGVLSELISV--DEGYEAAI 539
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2432-2564 |
2.41e-04 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 43.46 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2432 VMYLGNKDAsKDYIGMAVVDGQLTCVYNLGDREAEVQIDQVLTESESQEAVMDRVKFQRIYQFAKLNytkEATSTKPKAP 2511
Cdd:pfam00054 10 LLYNGTQTE-RDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEA---RPTGESPLGA 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 226423935 2512 gvydmesassNTLLNLDpenAVFYVGGYPPGFELPRRLRF-PPYKGCIELDDLN 2564
Cdd:pfam00054 86 ----------TTDLDVD---GPLYVGGLPSLGVKKRRLAIsPSFDGCIRDVIVN 126
|
|
| TNFRSF26 |
cd15837 |
Tumor necrosis factor receptor superfamily member 26 (TNFRSF26), also known as tumor necrosis ... |
1293-1453 |
4.75e-04 |
|
Tumor necrosis factor receptor superfamily member 26 (TNFRSF26), also known as tumor necrosis factor receptor homolog 3 (TNFRH3); TNFRSF26 (also known as tumor necrosis factor receptor homolog 3 (TNFRH3) or TNFRSF24) is predominantly expressed in embryos and lymphoid cell types, along with its closely related TNFRSF22 and TNFRSF23 orthologs, and is developmentally regulated. Unlike TNFRSF22/23, TNFRSF26 does not serve as a TRAIL decoy receptor; it remains an orphan receptor.
Pssm-ID: 276933 [Multi-domain] Cd Length: 118 Bit Score: 42.35 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1293 CSRCATGYYGFpycKPCNcgrrlceevtgkclcPPHTVRpQCEVCEMNSFNFHPvAGCDVCN-CSRKGTIEAAVSECDRD 1371
Cdd:cd15837 13 CQLCPAGHYVS---EPCQ---------------ENHGVG-ECAPCEPGTFTAHP-NGETSCFpCSQCRDDQEVVAECSAT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1372 SG-QCRCKPrvtgqqcdkcapGFYQFPECVPCSCNRdgtepsvcdpetgacmckenvegpqCQLCREGSFYLDPTNPKGC 1450
Cdd:cd15837 73 SDrQCQCKQ------------GHFYCDENCLESCFR-------------------------CSRCPGGRVVLQPCNATRD 115
|
...
gi 226423935 1451 TKC 1453
Cdd:cd15837 116 TVC 118
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
352-420 |
6.25e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.03 E-value: 6.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226423935 352 ACNCHGHAVdcyydpdvehqqaslNSKGVYAGGGVCInCQHNTAGVNCEKCAKGYFRPHGVPvdalHGC 420
Cdd:cd00055 1 PCDCNGHGS---------------LSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG----GGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
296-341 |
7.16e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 7.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 296 CVCN--GHA-EACSADNpekqFRCECQHHTCGDTCNRCCAGYNQRRWQP 341
Cdd:smart00180 1 CDCDpgGSAsGTCDPDT----GQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
353-420 |
1.58e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.87 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226423935 353 CNCHGHAVDcyydpdvehqqaslnSKGVYAGGGVCInCQHNTAGVNCEKCAKGYFrphGVPVDALHGC 420
Cdd:pfam00053 1 CDCNPHGSL---------------SDTCDPETGQCL-CKPGVTGRHCDRCKPGYY---GLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
296-344 |
2.67e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 2.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 296 CVCNGHAEACSADNPEkQFRCECQHHTCGDTCNRCCAGYNQRRWQPAGQ 344
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE-TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1308-1349 |
2.93e-03 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 38.10 E-value: 2.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 226423935 1308 PCNC-----GRRLCEEVTGKCLCPPHTVRPQCEVCEMNSFNFHPVAG 1349
Cdd:cd00055 1 PCDCnghgsLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
384-411 |
4.43e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.68 E-value: 4.43e-03
10 20
....*....|....*....|....*...
gi 226423935 384 GGVCInCQHNTAGVNCEKCAKGYFRPHG 411
Cdd:smart00180 17 TGQCE-CKPNVTGRRCDRCAPGYYGDGP 43
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1968-2234 |
4.47e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1968 AEAQRMMRDLRSRdfkkHLQEAEAEKMEAQLLLHRIRTWLEShqvenngLLKNIRDSLNDYEDKLQDLRSILQEaaaqak 2047
Cdd:NF041483 185 AEAERLAEEARQR----LGSEAESARAEAEAILRRARKDAER-------LLNAASTQAQEATDHAEQLRSSTAA------ 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2048 qatginhENEgvlgAIQRQMKEmdsLKNDFTKYLATADSSLLQTNnllQQMDKSQKEYESLAA-ALNGARQELSDRVR-- 2124
Cdd:NF041483 248 -------ESD----QARRQAAE---LSRAAEQRMQEAEEALREAR---AEAEKVVAEAKEAAAkQLASAESANEQRTRta 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2125 --ELSRsggkapLVVEAEKHAQSLQELAKQLEEIKRnTSGDELVRCAVDAATAyenilnaiRAAEDAASKATSASKSAFQ 2202
Cdd:NF041483 311 keEIAR------LVGEATKEAEALKAEAEQALADAR-AEAEKLVAEAAEKART--------VAAEDTAAQLAKAARTAEE 375
|
250 260 270
....*....|....*....|....*....|....
gi 226423935 2203 TVIK--EDLPKRAKTLSSDSEELLNEAKMTQKRL 2234
Cdd:NF041483 376 VLTKasEDAKATTRAAAEEAERIRREAEAEADRL 409
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LamNT |
smart00136 |
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related ... |
40-294 |
1.08e-105 |
|
Laminin N-terminal domain (domain VI); N-terminal domain of laminins and laminin-related protein such as Unc-6/ netrins.
Pssm-ID: 214532 Cd Length: 238 Bit Score: 338.18 E-value: 1.08e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 40 SSRSLHPPYFNLAQAARIWATATCGErdpevsrPRPELFCKLVGgpaaqgsgHTIQGQFCDYCNSEDSRKAHPASHAIDG 119
Cdd:smart00136 3 RPRSCYPPFVNLAFGREVTATSTCGE-------PGPERYCKLVG--------HTEQGKKCDYCDARNPRRSHPAENLTDG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 120 SE----RWWQSPPLSSGTQYnqVNLTLDLGQLFHVAYILIKFAnSPRPDLWILERSvDFGSTYSPWQYFAHsrrDCVEQF 195
Cdd:smart00136 68 NNpnnpTWWQSEPLSNGPQN--VNLTLDLGKEFHVTYVILKFC-SPRPSLWILERS-DFGKTWQPWQYFSS---DCRRTF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 196 GQEANMAITQ--DDQMLCVTEYSRIVPLENGEIVVSLINGRPGAKKFAFSDTLREFTKATNIRLRFLRTNTLLGHLISKA 273
Cdd:smart00136 141 GRPPRGPITKgnEDEVICTSEYSDIVPLEGGEIAFSLLEGRPSATDFDNSPVLQEWVTATNIRVRLTRLRTLGDELMDDR 220
|
250 260
....*....|....*....|.
gi 226423935 274 erdPTVTRRYYYSIKDISVGG 294
Cdd:smart00136 221 ---PEVTRRYYYAISDIAVGG 238
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1844-2101 |
2.63e-104 |
|
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: 335.15 E-value: 2.63e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1844 LQGLSVSTGALEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQVNSRKAQTLYNNIDQT 1923
Cdd:pfam06008 1 LLSLNSLTGALPAPYKINYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1924 IQSAKELDMKIKNIVQNVHILLKQMARPGGEGTDLPVGDWSRELAEAQRMMRDLRSRDFKKHLQEAEAEKMEAQLLLHRI 2003
Cdd:pfam06008 81 LGHAKELAEAIKNLIDNIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2004 RTWLESHQVENNGLLKNIRDSLNDYEDKLQDLRSILQEAAAQAKQATGINHENEGVLGAIQRQMKEMDSLKNDFTKYLAT 2083
Cdd:pfam06008 161 QTWFQSPQEENKALANALRDSLAEYEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLEETLKT 240
|
250
....*....|....*...
gi 226423935 2084 ADSSLLQTNNLLQQMDKS 2101
Cdd:pfam06008 241 ARDSLDAANLLLQEIDDA 258
|
|
| Laminin_N |
pfam00055 |
Laminin N-terminal (Domain VI); |
44-294 |
5.83e-93 |
|
Laminin N-terminal (Domain VI);
Pssm-ID: 459653 Cd Length: 230 Bit Score: 301.42 E-value: 5.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 44 LHPPYFNLAQAARIWATATCGERdpevsrpRPELFCKLVGGPAAQGsghtiqgqfCDYCNSEDSRKAHPASHAIDGSER- 122
Cdd:pfam00055 1 CYPAFGNLAFGREVSATSTCGLN-------GPERYCILSGLEGGKK---------CFICDSRDPHNSHPPSNLTDSNNGt 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 123 ---WWQSPPLSSgtQYNQVNLTLDLGQLFHVAYILIKFAnSPRPDLWILERSVDFGSTYSPWQYFAHsrrDCVEQFG-QE 198
Cdd:pfam00055 65 netWWQSETGVI--QYENVNLTLDLGKEFHFTYLILKFK-SPRPAAMVLERSTDFGKTWQPYQYFAS---DCRRTFGrPS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 199 ANMAITQDDQMLCVTEYSRIVPLENGEIVVSLINGRPGAKKFAFSDTLREFTKATNIRLRFLRTNTLLGHLiskaERDPT 278
Cdd:pfam00055 139 GPSRGIKDDEVICTSEYSDISPLTGGEVIFSTLEGRPSANIFDYSPELQDWLTATNIRIRLLRLHTLGDEL----LDDPS 214
|
250
....*....|....*.
gi 226423935 279 VTRRYYYSIKDISVGG 294
Cdd:pfam00055 215 VLRKYYYAISDISVGG 230
|
|
| Laminin_II |
pfam06009 |
Laminin Domain II; It has been suggested that the domains I and II from laminin A, B1 and B2 ... |
2284-2412 |
5.93e-51 |
|
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: 177.29 E-value: 5.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2284 AKSMVREANGITSEVLDGLNPIQTDLGRIKDSYESARRE---------DFSKALVDANNSVKKLTRKLPDLFIKIESINQ 2354
Cdd:pfam06009 1 SKELAREANETAKEVLEQLAPLSQNLENTSEKLSGINRSleetnelvnDANKALDDAGRSVKKLEELAPDLLDKLKPLKQ 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 226423935 2355 QLLPLGNISDNVDRIRELIQQARDAANKVAIPMRFNGKSGVEVRLPNDLEDLKGYTSL 2412
Cdd:pfam06009 81 LEVNSSSLSDNISRIKELIAQARKAANSIKVSVSFDGDSIVELRPPISVTDLAAYTSL 138
|
|
| LamB |
smart00281 |
Laminin B domain; |
1509-1638 |
9.89e-47 |
|
Laminin B domain;
Pssm-ID: 214597 Cd Length: 127 Bit Score: 164.74 E-value: 9.89e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1509 SVHSASWVAPPSYLGDKVSSYGGYLTYHAKSFGLPGDmvLLGKQPDVQLTGQHMSLIHKEPSDPRPDRLHHGRVQVIEGN 1588
Cdd:smart00281 1 DNEPVYWVAPEQFLGDKVTSYGGKLRYTLSFDGRRGG--THVSAPDVILEGNGLRISHPAEGPPLPDELTTVEVRFREEN 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 226423935 1589 FRHEGSSaPVSREELMTVLSRLERLHIRGLHFTETQRLTLGEVGLEEASD 1638
Cdd:smart00281 79 WQYYGGR-PVTREDLMMVLANLTAILIRATYSQQMAGSRLSDVSLEVAVP 127
|
|
| Laminin_B |
pfam00052 |
Laminin B (Domain IV); |
1515-1649 |
2.80e-44 |
|
Laminin B (Domain IV);
Pssm-ID: 459652 Cd Length: 136 Bit Score: 158.20 E-value: 2.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1515 WVAPPSYLGDKVSSYGGYLTYHAKSFGLPGDmVLLGKQPDVQLTGQHMSLIHKEPSDPRPDR--LHHGRVQVIEGNFRHE 1592
Cdd:pfam00052 2 WSAPEQFLGNKLTSYGGYLTYTVRYEPLPGG-GSLNSEPDVILEGNGLRLSYSSPDQPPPDPgqEQTYSVRLHEENWRDS 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 226423935 1593 gSSAPVSREELMTVLSRLERLHIRGLHFTETQRLTLGEVGLEEASDTGSGPRAHLVE 1649
Cdd:pfam00052 81 -DGAPVSREDFMMVLANLTAILIRATYSTGSGQVSLSNVSLDSAVPGGSGPPASWVE 136
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
3155-3306 |
3.45e-33 |
|
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: 126.76 E-value: 3.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3155 GIYFSqGGGHVVLANSVSLEPALTLTLSIRPRSLTGVLIHIASQS-GEHLSVYMEAGKVTTSMNSeaGGTVTSITPKRSL 3233
Cdd:cd00110 1 GVSFS-GSSYVRLPTLPAPRTRLSISFSFRTTSPNGLLLYAGSQNgGDFLALELEDGRLVLRYDL--GSGSLVLSSKTPL 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226423935 3234 CDGQWHSVTVSIKQHTLHLELDTDNSYTAGQLSFPPN-STRGSLHIGGVPDKLKMLTLPVWNSFFGCLKNIQVN 3306
Cdd:cd00110 78 NDGQWHSVSVERNGRSVTLSVDGERVVESGSPGGSALlNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2989-3131 |
9.73e-32 |
|
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have binding sites for steroids, beta1 integrins, heparin, sulfatides, fibulin-1, and alpha-dystroglycans. Proteins that contain LamG domains serve a variety of purposes including signal transduction via cell-surface steroid receptors, adhesion, migration and differentiation through mediation of cell adhesion molecules.
Pssm-ID: 238058 [Multi-domain] Cd Length: 151 Bit Score: 122.91 E-value: 9.73e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2989 SPTSHLLFKLPQeLLKPRLQFSLDIQTTSSRGLVFHTGT--RDSFVALYLSEGHVIFALGAGGKKLRLRSKERYHDGKWH 3066
Cdd:cd00110 5 SGSSYVRLPTLP-APRTRLSISFSFRTTSPNGLLLYAGSqnGGDFLALELEDGRLVLRYDLGSGSLVLSSKTPLNDGQWH 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226423935 3067 SVVFGLSGRKVHLVVDGLR-AQEGSLPGNSTISPREQVYLGLSP--SRKSKSLPQHSFVGCLRNFQLD 3131
Cdd:cd00110 84 SVSVERNGRSVTLSVDGERvVESGSPGGSALLNLDGPLYLGGLPedLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| LamG |
smart00282 |
Laminin G domain; |
3008-3133 |
9.84e-30 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 116.28 E-value: 9.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3008 QFSLDIQTTSSRGLVFHTGT--RDSFVALYLSEGHVIFALGAGGKKLRLRSK-ERYHDGKWHSVVFGLSGRKVHLVVDGL 3084
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLGSGPARLTSDpTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 3085 RAQEGSLPGNSTI-SPREQVYLGLSPS--RKSKSLPQHSFVGCLRNFQLDSK 3133
Cdd:smart00282 81 NRVSGESPGGLTIlNLDGPLYLGGLPEdlKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3183-3308 |
1.49e-28 |
|
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: 112.90 E-value: 1.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3183 IRPRSLTGVLIHIASQSGEHLSVYMEAGKVTTSMNSEAGGTVTSITPKRsLCDGQWHSVTVSIKQHTLHLELDTDNSYTA 3262
Cdd:pfam02210 1 FRTRQPNGLLLYAGGGGSDFLALELVNGRLVLRYDLGSGPESLLSSGKN-LNDGQWHSVRVERNGNTLTLSVDGQTVVSS 79
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 226423935 3263 GQLSFPPN-STRGSLHIGGVPDKLKMLTLPVWNSFFGCLKNIQVNHI 3308
Cdd:pfam02210 80 LPPGESLLlNLNGPLYLGGLPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| LamG |
smart00282 |
Laminin G domain; |
3178-3307 |
2.22e-27 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 109.74 E-value: 2.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3178 TLTLSIRPRSLTGVLIHIAS-QSGEHLSVYMEAGKVTTSMNSEAGGTVTSITPKRsLCDGQWHSVTVSIKQHTLHLELDT 3256
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSkGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTP-LNDGQWHRVAVERNGRSVTLSVDG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 3257 DNS-YTAGQLSFPPNSTRGSLHIGGVPDKLKMLTLPVWNSFFGCLKNIQVNH 3307
Cdd:smart00282 80 GNRvSGESPGGLTILNLDGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNG 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2598-2738 |
8.11e-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: 102.88 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2598 YFEGTGYARIPTQPN-APFPNFMQTIQTTVDRGLLFFAENQ--DNFISLNIEDGNLMVKYKLNSEPPKekgIRDT--INN 2672
Cdd:cd00110 3 SFSGSSYVRLPTLPApRTRLSISFSFRTTSPNGLLLYAGSQngGDFLALELEDGRLVLRYDLGSGSLV---LSSKtpLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2673 GRDHMILISIGKSQKRMLIN----MNKHSIIIEGEIFDFSTYYLGGIPIAIRERFNISTPAFQGCMKNLK 2738
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDgervVESGSPGGSALLNLDGPLYLGGLPEDLKSPGLPVSPGFVGCIRDLK 149
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
3015-3133 |
1.09e-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: 93.25 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3015 TTSSRGLVFHTGTRDS-FVALYLSEGHVIFA--LGAGGKKLRLrSKERYHDGKWHSVVFGLSGRKVHLVVDGLRAQEGSL 3091
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRydLGSGPESLLS-SGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLP 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 226423935 3092 PGNS-TISPREQVYLG--LSPSRKSKSLPQHSFVGCLRNFQLDSK 3133
Cdd:pfam02210 82 PGESlLLNLNGPLYLGglPPLLLLPALPVRAGFVGCIRDVRVNGE 126
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3013-3136 |
4.46e-21 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 91.61 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3013 IQTTSSRGLVFHTGTRD--SFVALYLSEGHVIFALGAGGKKLRLRSKERYHDGKWHSVVFGLSGRKVHLVVDGLRAQEGS 3090
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTerDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEARPTGE 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 3091 LPGNSTISP--REQVYLGLSPSRKSKSLP---QHSFVGCLRNFQLDSKPLD 3136
Cdd:pfam00054 81 SPLGATTDLdvDGPLYVGGLPSLGVKKRRlaiSPSFDGCIRDVIVNGKPLD 131
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2765-2897 |
1.42e-20 |
|
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: 1.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2765 TASFSRGGQMSFTNLDVPSlDRFQLSFGFQTFQPSGTLL--NHQTRTSSLLVTLEDGHIALSTRDSSSP-IFKSPGTYMD 2841
Cdd:cd00110 1 GVSFSGSSYVRLPTLPAPR-TRLSISFSFRTTSPNGLLLyaGSQNGGDFLALELEDGRLVLRYDLGSGSlVLSSKTPLND 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226423935 2842 GLLHHVSVISDTSGLRLLIDDQVL--RRNQRLASFSNAQQSLSMGG-------------GYFEGCISNVFV 2897
Cdd:cd00110 80 GQWHSVSVERNGRSVTLSVDGERVveSGSPGGSALLNLDGPLYLGGlpedlkspglpvsPGFVGCIRDLKV 150
|
|
| LamG |
smart00282 |
Laminin G domain; |
2617-2738 |
1.06e-19 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 87.78 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2617 NFMQTIQTTVDRGLLFFA--ENQDNFISLNIEDGNLMVKYKLNSEPPKEKGIRDTINNGRDHMILISIGKSQKRMLINMN 2694
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAgsKGGGDYLALELRDGRLVLRYDLGSGPARLTSDPTPLNDGQWHRVAVERNGRSVTLSVDGG 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 226423935 2695 KHSIIIEGEIFDF----STYYLGGIPIAIRERFNISTPAFQGCMKNLK 2738
Cdd:smart00282 81 NRVSGESPGGLTIlnldGPLYLGGLPEDLKLPPLPVTPGFRGCIRNLK 128
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1263-1311 |
2.60e-16 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 75.08 E-value: 2.60e-16
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 1263 CECDPAGTAGHHCSPEGGQCPCRPNVIGRQCSRCATGYYGFPYCKPCNC 1311
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| LamG |
smart00282 |
Laminin G domain; |
2788-2900 |
1.61e-15 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 75.84 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2788 QLSFGFQTFQPSGTLLNHQT--RTSSLLVTLEDGHIALSTRDSSSPIFKS--PGTYMDGLLHHVSVISDTSGLRLLIDD- 2862
Cdd:smart00282 1 SISFSFRTTSPNGLLLYAGSkgGGDYLALELRDGRLVLRYDLGSGPARLTsdPTPLNDGQWHRVAVERNGRSVTLSVDGg 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 2863 -QVLRRNQRLASFSNAQQSLSMGG-------------GYFEGCISNVFVQRM 2900
Cdd:smart00282 81 nRVSGESPGGLTILNLDGPLYLGGlpedlklpplpvtPGFRGCIRNLKVNGK 132
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1262-1304 |
3.33e-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: 72.00 E-value: 3.33e-15
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 226423935 1262 PCECDPAGTAGHHCSPEGGQCPCRPNVIGRQCSRCATGYYGFP 1304
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1263-1306 |
2.99e-14 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 69.26 E-value: 2.99e-14
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 226423935 1263 CECDPAGTAGHHCSPEGGQCPCRPNVIGRQCSRCATGYYG--FPYC 1306
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2624-2738 |
7.73e-14 |
|
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: 70.53 E-value: 7.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2624 TTVDRGLLFFAENQDN-FISLNIEDGNLMVKYKLNSEPPKEKGIRDTINNGRDHMILISIGKSQKRMLINMNKHSIIIEG 2702
Cdd:pfam02210 3 TRQPNGLLLYAGGGGSdFLALELVNGRLVLRYDLGSGPESLLSSGKNLNDGQWHSVRVERNGNTLTLSVDGQTVVSSLPP 82
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 226423935 2703 EIFDF----STYYLGGIPIAIRERFNISTPAFQGCMKNLK 2738
Cdd:pfam02210 83 GESLLlnlnGPLYLGGLPPLLLLPALPVRAGFVGCIRDVR 122
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1401-1451 |
4.55e-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: 65.84 E-value: 4.55e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 1401 PCSCNRDGTEPSVCDPETGACMCKENVEGPQCQLCREGsFYLDPTNPKGCT 1451
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPG-YYGLPSQGGGCQ 50
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
532-574 |
1.28e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 64.68 E-value: 1.28e-12
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 226423935 532 ACQCSTIGSYPVPCDPGNGQCDCLPGITGRQCDRCLSGAYDFP 574
Cdd:cd00055 1 PCDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1353-1398 |
5.66e-12 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 62.76 E-value: 5.66e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 226423935 1353 CNCSRKGTIEaavSECDRDSGQCRCKPRVTGQQCDKCAPGFYQFPE 1398
Cdd:cd00055 2 CDCNGHGSLS---GQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPS 44
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1353-1404 |
6.33e-12 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 62.76 E-value: 6.33e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 1353 CNCSRKGTieaAVSECDRDSGQCRCKPRVTGQQCDKCAPGFYQFPECVPCSC 1404
Cdd:pfam00053 1 CDCNPHGS---LSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1353-1399 |
9.22e-12 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.94 E-value: 9.22e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 1353 CNCSRKGTIEaavSECDRDSGQCRCKPRVTGQQCDKCAPGFY--QFPEC 1399
Cdd:smart00180 1 CDCDPGGSAS---GTCDPDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
533-576 |
1.52e-11 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 61.56 E-value: 1.52e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 226423935 533 CQCSTIGSYPVPCDPGNGQCDCLPGITGRQCDRCLSGAYD--FPYC 576
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYGdgPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1402-1450 |
1.93e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 61.22 E-value: 1.93e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 1402 CSCNRDGTEPSVCDPETGACMCKENVEGPQCQLCREGSFYLDPTNPKGC 1450
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
533-580 |
2.30e-11 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 60.83 E-value: 2.30e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 226423935 533 CQCSTIGSYPVPCDPGNGQCDCLPGITGRQCDRCLSGAYDFPYCQGSG 580
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
422-462 |
4.54e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 60.06 E-value: 4.54e-11
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 226423935 422 PCSCDPE--RADDCDQGSGHCHCKPNFSGDYCETCADGYYNFP 462
Cdd:cd00055 1 PCDCNGHgsLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1683-1729 |
6.08e-11 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 59.68 E-value: 6.08e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 1683 PCNCNGH---SNRCQDGSGICInCQHNTAGEHCERCQAGHYGNAIHG-SCR 1729
Cdd:cd00055 1 PCDCNGHgslSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQGgGCQ 50
|
|
| LamG |
smart00282 |
Laminin G domain; |
2431-2566 |
7.50e-11 |
|
Laminin G domain;
Pssm-ID: 214598 [Multi-domain] Cd Length: 132 Bit Score: 62.36 E-value: 7.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2431 FVMYLGNKDaSKDYIGMAVVDGQLTCVYNLGDREAEVQIDQVltesesqeAVMD----RVKFQRIYQFAKL--NYTKEAT 2504
Cdd:smart00282 14 LLLYAGSKG-GGDYLALELRDGRLVLRYDLGSGPARLTSDPT--------PLNDgqwhRVAVERNGRSVTLsvDGGNRVS 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226423935 2505 STKPkapgvydmesaSSNTLLNLDpenAVFYVGGYPPGFELPRRLRFPPYKGCIELDDLNEN 2566
Cdd:smart00282 85 GESP-----------GGLTILNLD---GPLYLGGLPEDLKLPPLPVTPGFRGCIRNLKVNGK 132
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1836-2193 |
9.15e-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: 68.17 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1836 ELRLVKSKLQG---LSVSTGALEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQE------KA 1906
Cdd:TIGR02169 215 ALLKEKREYEGyelLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrvKE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1907 QVNSRKAQ--TLYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARPGGEGTDLPV--GDWSRELAEAQRMMRDLRSRdf 1982
Cdd:TIGR02169 295 KIGELEAEiaSLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKrrDKLTEEYAELKEELEDLRAE-- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1983 kkhLQEAEAEKMEAQLLLHRIRTWLEShqvennglLKNIRDSLNDYEDKLQDLRSILQEAaaqakqatGINHENEgvLGA 2062
Cdd:TIGR02169 373 ---LEEVDKEFAETRDELKDYREKLEK--------LKREINELKRELDRLQEELQRLSEE--------LADLNAA--IAG 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2063 IQRQMKEMDSLKNDFTKYLATADSSLLQTNnllQQMDKSQKEYESLAAALNGARQELSDRVRELSRsggkaplvVEAEKH 2142
Cdd:TIGR02169 432 IEAKINELEEEKEDKALEIKKQEWKLEQLA---ADLSKYEQELYDLKEEYDRVEKELSKLQRELAE--------AEAQAR 500
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226423935 2143 A--QSLQELAKQLEEIKRNTSG-----DELVRCAVDAATAYE----NILNAIRAAEDAASKA 2193
Cdd:TIGR02169 501 AseERVRGGRAVEEVLKASIQGvhgtvAQLGSVGERYATAIEvaagNRLNNVVVEDDAVAKE 562
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
423-464 |
1.19e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.90 E-value: 1.19e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 226423935 423 CSCDP--ERADDCDQGSGHCHCKPNFSGDYCETCADGYYNFPFC 464
Cdd:pfam00053 1 CDCNPhgSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSD 44
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1731-1782 |
1.63e-10 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 58.52 E-value: 1.63e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 1731 CPCPHTNSFATGCAVDGGavRCACKPGYTGTQCERCAPGYFGNPQKfGGSCQ 1782
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTG--QCECKPNTTGRRCDRCAPGYYGLPSQ-GGGCQ 50
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
488-535 |
1.94e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.52 E-value: 1.94e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 488 CDCNLEGVLPEICDDR-GRCLCRPGVEGPQCDSCRSGSYSFPICQACQC 535
Cdd:pfam00053 1 CDCNPHGSLSDTCDPEtGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2793-2897 |
2.34e-10 |
|
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G subfamily.
Pssm-ID: 460494 [Multi-domain] Cd Length: 126 Bit Score: 60.90 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2793 FQTFQPSGTLL-NHQTRTSSLLVTLEDGHIALSTRDSSSPI-FKSPGTYM-DGLLHHVSVISDTSGLRLLIDDQVLRRNQ 2869
Cdd:pfam02210 1 FRTRQPNGLLLyAGGGGSDFLALELVNGRLVLRYDLGSGPEsLLSSGKNLnDGQWHSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 226423935 2870 RLASFS--NAQQSLSMGG-------------GYFEGCISNVFV 2897
Cdd:pfam02210 81 PPGESLllNLNGPLYLGGlppllllpalpvrAGFVGCIRDVRV 123
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1731-1781 |
2.47e-10 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 58.13 E-value: 2.47e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 1731 CPCPHTNSFATGCAVDGGavRCACKPGYTGTQCERCAPGYFGNPQKFGGSC 1781
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETG--QCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1402-1450 |
2.85e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.71 E-value: 2.85e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 1402 CSCNRDGTEPSVCDPETGACMCKENVEGPQCQLCREGSFYldpTNPKGC 1450
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYYG---DGPPGC 46
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
423-463 |
3.75e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 3.75e-10
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 226423935 423 CSCDPERA--DDCDQGSGHCHCKPNFSGDYCETCADGYYNFPF 463
Cdd:smart00180 1 CDCDPGGSasGTCDPDTGQCECKPNVTGRRCDRCAPGYYGDGP 43
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1731-1774 |
3.97e-10 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 57.32 E-value: 3.97e-10
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 226423935 1731 CPCPHTNSFATGCAVDGGavRCACKPGYTGTQCERCAPGYFGNP 1774
Cdd:smart00180 1 CDCDPGGSASGTCDPDTG--QCECKPNVTGRRCDRCAPGYYGDG 42
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
3183-3310 |
5.50e-10 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 59.64 E-value: 5.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3183 IRPRSLTGVLIHIASQS-GEHLSVYMEAGKVTTSMNSEAGGTVTSITPKrsLCDGQWHSVTVSIKQHTLHLELDTDNSYT 3261
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTeRDFLALELRDGRLEVSYDLGSGAAVVRSGDK--LNDGKWHSVELERNGRSGTLSVDGEARPT 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 226423935 3262 A----GQLSFPpnSTRGSLHIGGVP-DKLKMLTLPVWNSFFGCLKNIQVNHIPV 3310
Cdd:pfam00054 79 GesplGATTDL--DVDGPLYVGGLPsLGVKKRRLAISPSFDGCIRDVIVNGKPL 130
|
|
| LamG |
cd00110 |
Laminin G domain; Laminin G-like domains are usually Ca++ mediated receptors that can have ... |
2386-2564 |
1.17e-09 |
|
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: 59.35 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2386 PMRFNGKSGVEVRlpnDLEDLKGYTSLSLFLqRPDlRENGgtedmFVMYLGNKDaSKDYIGMAVVDGQLTCVYNLGDREA 2465
Cdd:cd00110 1 GVSFSGSSYVRLP---TLPAPRTRLSISFSF-RTT-SPNG-----LLLYAGSQN-GGDFLALELEDGRLVLRYDLGSGSL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2466 EVQidqvlteseSQEAVMD----RVKFQRIYQFAKL--NYTKEATSTKPkapgvydmesaSSNTLLNLDPEnavFYVGGY 2539
Cdd:cd00110 70 VLS---------SKTPLNDgqwhSVSVERNGRSVTLsvDGERVVESGSP-----------GGSALLNLDGP---LYLGGL 126
|
170 180
....*....|....*....|....*
gi 226423935 2540 PPGFELPRRLRFPPYKGCIELDDLN 2564
Cdd:cd00110 127 PEDLKSPGLPVSPGFVGCIRDLKVN 151
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1854-2245 |
3.22e-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: 63.21 E-value: 3.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1854 LEQIRHMETQAKDLRNQLlgfRSATSSHGSKMDDLEKELSHLNREF-ETLQEKaqvnsrkaqtlynniDQTIQSAKELDM 1932
Cdd:pfam15921 316 MRQLSDLESTVSQLRSEL---REAKRMYEDKIEELEKQLVLANSELtEARTER---------------DQFSQESGNLDD 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1933 KIKNIVQNVHILLKQMARPGGEGTDLpvgdWSRELAEA---QRMMRDLRSRDFKKHLQEA--EAEKMEAQLLLHRirtWL 2007
Cdd:pfam15921 378 QLQKLLADLHKREKELSLEKEQNKRL----WDRDTGNSitiDHLRRELDDRNMEVQRLEAllKAMKSECQGQMER---QM 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2008 ESHQVENNGLLKnIRDSLNDYEDKLQDLRSILQEAAAQAKQATGINHENEGVLGAIQRQMKEMDSLKNDFTKYLATADSS 2087
Cdd:pfam15921 451 AAIQGKNESLEK-VSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLK 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2088 LLQTNNLLQQMD---KSQKEYESLAAALNGA-------RQELSDR---VRELSRSGG-----KAPLVVEAEKHAQSLQEL 2149
Cdd:pfam15921 530 LQELQHLKNEGDhlrNVQTECEALKLQMAEKdkvieilRQQIENMtqlVGQHGRTAGamqveKAQLEKEINDRRLELQEF 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2150 --------AK-----------QLEEIKRNTSGDELVRCAVDAATAYENILNAIRAAEDAASKATSASKsafqtVIKEDLP 2210
Cdd:pfam15921 610 kilkdkkdAKirelearvsdlELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYE-----VLKRNFR 684
|
410 420 430
....*....|....*....|....*....|....*
gi 226423935 2211 KRAKTLSSDSEELLNEAKMTQKRLQQVSPALNSLQ 2245
Cdd:pfam15921 685 NKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
488-528 |
4.16e-09 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 54.67 E-value: 4.16e-09
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 226423935 488 CDCNLEGVLPEICDDR-GRCLCRPGVEGPQCDSCRSGSYSFP 528
Cdd:cd00055 2 CDCNGHGSLSGQCDPGtGQCECKPNTTGRRCDRCAPGYYGLP 43
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1833-2267 |
7.87e-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: 61.73 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1833 MGEELRLVKSKLQGLSVSTGALEQIR-HMETQAKDLRNQLlgfRSATSSHGSKMDDLEKElsHlNREFETLQEKAQVNSR 1911
Cdd:pfam01576 297 LGEELEALKTELEDTLDTTAAQQELRsKREQEVTELKKAL---EEETRSHEAQLQEMRQK--H-TQALEELTEQLEQAKR 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1912 KAQtlynNIDQTIQSakeldmkIKNIVQNVHILLKQMARPGGEGtdlpvgDWSRELAEAQrmMRDLRSRdfkkhLQEAEA 1991
Cdd:pfam01576 371 NKA----NLEKAKQA-------LESENAELQAELRTLQQAKQDS------EHKRKKLEGQ--LQELQAR-----LSESER 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1992 EKMEAQLLLHRIRTWLEShqveNNGLL-----KNIRDS--LNDYEDKLQDLRSILQEAAAQAKQATGINHENEGVLGAIQ 2064
Cdd:pfam01576 427 QRAELAEKLSKLQSELES----VSSLLneaegKNIKLSkdVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQ 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2065 RQMKEMDSLKNDFTKYLATADSSLLQT-------------------------NNLLQQMDKSQKEYESLAAALNGARQEL 2119
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQAQLSDMkkkleedagtlealeegkkrlqrelEALTQQLEEKAAAYDKLEKTKNRLQQEL 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2120 SDRVRELSRsggKAPLVVEAEKHAQSL-QELAkqlEEikRNTS---GDELVRCAVDAATAYENILNAIRAAEDAaskats 2195
Cdd:pfam01576 583 DDLLVDLDH---QRQLVSNLEKKQKKFdQMLA---EE--KAISaryAEERDRAEAEAREKETRALSLARALEEA------ 648
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226423935 2196 asksafqTVIKEDLPKRAKTLSSDSEELLNEAKMTQKRLQQVSPALNSLQQTLKTVSVQKDLLDANLTVARD 2267
Cdd:pfam01576 649 -------LEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATED 713
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
1684-1731 |
9.80e-09 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.51 E-value: 9.80e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 1684 CNCNGH---SNRCQDGSGICInCQHNTAGEHCERCQAGHYGNAIhGSCRVC 1731
Cdd:pfam00053 1 CDCNPHgslSDTCDPETGQCL-CKPGVTGRHCDRCKPGYYGLPS-DPPQGC 49
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
488-530 |
1.06e-08 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 53.47 E-value: 1.06e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 226423935 488 CDCNLEGVLPEICD-DRGRCLCRPGVEGPQCDSCRSGSY--SFPIC 530
Cdd:smart00180 1 CDCDPGGSASGTCDpDTGQCECKPNVTGRRCDRCAPGYYgdGPPGC 46
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
628-678 |
1.09e-08 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 53.51 E-value: 1.09e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 628 CQCHEAGTLSGigECGQEDGDCSCKAHVTGDACDTCEDGFFSLEKSNYFGC 678
Cdd:pfam00053 1 CDCNPHGSLSD--TCDPETGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQGC 49
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1829-2372 |
1.31e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 61.23 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1829 DLASMGEELRLVKSKLQGLSVSTGALE-QIRHMETQAKDLRNQLLGFRSATSSHGSKMDD-------LEKELSHLNREFE 1900
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLEAELEELEaELEELESRLEELEEQLETLRSKVAQLELQIASlnneierLEARLERLEDRRE 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1901 TLQEKAQVNSRKAQ-----TLYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARPGGEGTDLpvgdwSRELAEAQ---R 1972
Cdd:TIGR02168 418 RLQQEIEELLKKLEeaelkELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA-----ERELAQLQarlD 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1973 MMRDLRSRdfKKHLQEAEAEKMEAQLLLHRIRTWL-ESHQVENN----------GLLKNI-RDSLNDYEDKLQDLR---- 2036
Cdd:TIGR02168 493 SLERLQEN--LEGFSEGVKALLKNQSGLSGILGVLsELISVDEGyeaaieaalgGRLQAVvVENLNAAKKAIAFLKqnel 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2037 ---SILQEAAAQAKQATGINHEN----EGVLGAI------------------------------QRQMKEMDSLKNDFTK 2079
Cdd:TIGR02168 571 grvTFLPLDSIKGTEIQGNDREIlkniEGFLGVAkdlvkfdpklrkalsyllggvlvvddldnaLELAKKLRPGYRIVTL 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2080 --YLAT-----------ADSSLLQTNN----LLQQMDKSQKEYESLAAALNGARQELSD----------RVRELSR--SG 2130
Cdd:TIGR02168 651 dgDLVRpggvitggsakTNSSILERRReieeLEEKIEELEEKIAELEKALAELRKELEEleeeleqlrkELEELSRqiSA 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2131 GKAPLVV---EAEKHAQSLQELAKQLEEI---------KRNTSGDELVRCAVDAAT------AYENILNAIRAAEDAASK 2192
Cdd:TIGR02168 731 LRKDLARleaEVEQLEERIAQLSKELTELeaeieeleeRLEEAEEELAEAEAEIEEleaqieQLKEELKALREALDELRA 810
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2193 ATSASKSAFQTVI--KEDLPKRAKTLSSDSEELLNEAKMTQKRLQQVSPALNSLQQT-------LKTVSVQKDLLDANLT 2263
Cdd:TIGR02168 811 ELTLLNEEAANLRerLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELieeleseLEALLNERASLEEALA 890
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2264 VARDDLhGIQRGDIDSVvigaKSMVREANGITSEVLDGLNPIQTDLGRIK---DSYESARREDFSKALVDANNSVKKLTR 2340
Cdd:TIGR02168 891 LLRSEL-EELSEELREL----ESKRSELRRELEELREKLAQLELRLEGLEvriDNLQERLSEEYSLTLEEAEALENKIED 965
|
650 660 670
....*....|....*....|....*....|..
gi 226423935 2341 KLPDLFIKIESINQQLLPLGNIsdNVDRIREL 2372
Cdd:TIGR02168 966 DEEEARRRLKRLENKIKELGPV--NLAAIEEY 995
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1835-2244 |
4.19e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.01 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1835 EELRLVKSKLQGLSVSTGALEQIRHmetQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQVNSRKAQ 1914
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQE---ELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1915 tlYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARpggEGTDLPVGDWsRELAEAQRMMRDLRSRdfkkhLQEAEAEKM 1994
Cdd:COG4717 148 --LEELEERLEELRELEEELEELEAELAELQEELEE---LLEQLSLATE-EELQDLAEELEELQQR-----LAELEEELE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1995 EAQLLLHRIRTWLEshQVENNGLLKNIRDSLNDYEDKLQDLRSILQEAAAQAKQATGINHenegVLGAIQRQMKEMDSLK 2074
Cdd:COG4717 217 EAQEELEELEEELE--QLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILT----IAGVLFLVLGLLALLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2075 NDFTKYLATADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSGGKAP-LVVEAEKHAQSLQ--ELAK 2151
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQeLLREAEELEEELQleELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2152 QLEEI--KRNTSGDELVRCAVDAATAYENILNAIRAAEDAASKATSASKSAFQTVIKEDLPKRAKTLSSDSEELLNEAKM 2229
Cdd:COG4717 371 EIAALlaEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410
....*....|....*
gi 226423935 2230 TQKRLQQVSPALNSL 2244
Cdd:COG4717 451 LREELAELEAELEQL 465
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
628-679 |
6.15e-08 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 51.20 E-value: 6.15e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 628 CQCHEAGTLSGigECGQEDGDCSCKAHVTGDACDTCEDGFFSLEkSNYFGCQ 679
Cdd:cd00055 2 CDCNGHGSLSG--QCDPGTGQCECKPNTTGRRCDRCAPGYYGLP-SQGGGCQ 50
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2078-2409 |
8.04e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.60 E-value: 8.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2078 TKYLATADSSLLQTNnlLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSggkaplvvEAEkhaqsLQELAKQLEEIK 2157
Cdd:COG4372 22 TGILIAALSEQLRKA--LFELDKLQEELEQLREELEQAREELEQLEEELEQA--------RSE-----LEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2158 RNTSgdelvrcavDAATAYENILNAIRAAEDAASKAtsasKSAFQTVIKE--DLPKRAKTLSSDSEELLNEAKMTQKRLQ 2235
Cdd:COG4372 87 EQLQ---------AAQAELAQAQEELESLQEEAEEL----QEELEELQKErqDLEQQRKQLEAQIAELQSEIAEREEELK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2236 QVSPALNSLQQTLKTVSVQKDLLDANLTVARddlhgiqrgdidsvvigAKSMVREANG--ITSEVLDGLNPIQTDLGRIK 2313
Cdd:COG4372 154 ELEEQLESLQEELAALEQELQALSEAEAEQA-----------------LDELLKEANRnaEKEEELAEAEKLIESLPREL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2314 DSYESARREDFSKALVDANNSVKKLTRKLPDLFIKIESINQQL--LPLGNISDNVDRIRELIQQARDAANKVAIPMrfNG 2391
Cdd:COG4372 217 AEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEieELELAILVEKDTEEEELEIAALELEALEEAA--LE 294
|
330
....*....|....*...
gi 226423935 2392 KSGVEVRLPNDLEDLKGY 2409
Cdd:COG4372 295 LKLLALLLNLAALSLIGA 312
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
628-678 |
1.38e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 50.39 E-value: 1.38e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 628 CQCHEAGTLSGigECGQEDGDCSCKAHVTGDACDTCEDGFFsleKSNYFGC 678
Cdd:smart00180 1 CDCDPGGSASG--TCDPDTGQCECKPNVTGRRCDRCAPGYY---GDGPPGC 46
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1855-2157 |
2.32e-07 |
|
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: 56.95 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1855 EQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQE-----KAQV------NSRKAQTLYN----- 1918
Cdd:TIGR04523 314 SELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQReleekQNEIeklkkeNQSYKQEIKNlesqi 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1919 -----NIDQTIQSAKELDMKIKNIVQNVHILLKQMarpggegTDLpvgdwSRELAEAQRMMRDLRSRDFKKHLQ----EA 1989
Cdd:TIGR04523 394 ndlesKIQNQEKLNQQKDEQIKKLQQEKELLEKEI-------ERL-----KETIIKNNSEIKDLTNQDSVKELIiknlDN 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1990 EAEKMEAQL-----LLHRIRTWLESHQVE---NNGLLKNIRDSLNDYEDKLQDLRSilqeaaAQAKQATGINH-ENEgvl 2060
Cdd:TIGR04523 462 TRESLETQLkvlsrSINKIKQNLEQKQKElksKEKELKKLNEEKKELEEKVKDLTK------KISSLKEKIEKlESE--- 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2061 gaIQRQMKEMDSLKNDFTKylataDSSLLQTNNLLQQMDKSQKEYESLA---AALNGARQELSDRVRELSRSggKAPLVV 2137
Cdd:TIGR04523 533 --KKEKESKISDLEDELNK-----DDFELKKENLEKEIDEKNKEIEELKqtqKSLKKKQEEKQELIDQKEKE--KKDLIK 603
|
330 340
....*....|....*....|
gi 226423935 2138 EAEKHAQSLQELAKQLEEIK 2157
Cdd:TIGR04523 604 EIEEKEKKISSLEKELEKAK 623
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
295-343 |
3.10e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 49.27 E-value: 3.10e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 295 RCVCNGHAEACSADNPEkQFRCECQHHTCGDTCNRCCAGYNQRRWQPAG 343
Cdd:cd00055 1 PCDCNGHGSLSGQCDPG-TGQCECKPNTTGRRCDRCAPGYYGLPSQGGG 48
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2622-2738 |
3.68e-07 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 51.55 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2622 IQTTVDRGLLFFAENQD--NFISLNIEDGNLMVKYKLNSEPPKEkGIRDTINNGRDHMILISigKSQKRMLINMNK-HSI 2698
Cdd:pfam00054 1 FRTTEPSGLLLYNGTQTerDFLALELRDGRLEVSYDLGSGAAVV-RSGDKLNDGKWHSVELE--RNGRSGTLSVDGeARP 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 226423935 2699 IIEGE-----IFDFST-YYLGGIPIAI--RERFNISTPaFQGCMKNLK 2738
Cdd:pfam00054 78 TGESPlgattDLDVDGpLYVGGLPSLGvkKRRLAISPS-FDGCIRDVI 124
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
1684-1726 |
3.87e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.85 E-value: 3.87e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 226423935 1684 CNCN--GH-SNRCQDGSGICInCQHNTAGEHCERCQAGHYGNAIHG 1726
Cdd:smart00180 1 CDCDpgGSaSGTCDPDTGQCE-CKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1883-2254 |
4.05e-07 |
|
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: 56.13 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1883 SKMDDLEKELSHLNREFETLQEKAQVNSRKAQTLYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARpggegtdlpVGD 1962
Cdd:TIGR00618 528 RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVR---------LQD 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1963 WSRELAEAQRMMRDLRSR----------DFKKHLQEAEAEKMEAQLLLHRIRTWLESHQVENNGLLKNIRdslndyEDKL 2032
Cdd:TIGR00618 599 LTEKLSEAEDMLACEQHAllrklqpeqdLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIR------VLPK 672
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2033 QDLRSIlqeaaaqakqatginhenegvlgaiQRQMKEMDSLKNDFTKYLATADSSLLQTNNLLQQMDKSQKEYESLAAAL 2112
Cdd:TIGR00618 673 ELLASR-------------------------QLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS 727
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2113 NGARQELSDRvrelsrsggkaplvveAEKHAQSLQELAKQ-------LEEIKRNTSGDELVRCAVDA--ATAYENILNAI 2183
Cdd:TIGR00618 728 SSLGSDLAAR----------------EDALNQSLKELMHQartvlkaRTEAHFNNNEEVTAALQTGAelSHLAAEIQFFN 791
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226423935 2184 RAAEdaaskatsasksAFQTVIKEDLPKRAKTLSSDSEELLNEAKMTQKRLQQVSPALNSLQQTLKTVSVQ 2254
Cdd:TIGR00618 792 RLRE------------EDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQ 850
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
681-724 |
4.07e-07 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 48.89 E-value: 4.07e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 226423935 681 CQCDIGGALTTMCSGPSGVCQCREHVEGKQCQRPENNYYFPDLH 724
Cdd:cd00055 2 CDCNGHGSLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQ 45
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1962-2274 |
4.72e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 4.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1962 DWSRELAEAQRMMRDLRSRDFKKHLQEAEAEKMEAQLLLHRIRTWLESHQVENNGLLKNIRDSLNDYEDKLQDLRSIlqe 2041
Cdd:COG1196 217 ELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEL--- 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2042 aaaqakqatgiNHENEGVLGAIQRQMKEMDSLKNDFTKYLATADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELSD 2121
Cdd:COG1196 294 -----------LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2122 RVRELSR-SGGKAPLVVEAEKHAQSLQELAKQLEEIKRNTSGDELVrcAVDAATAYENILNAIRAAEDAASKATSASKSA 2200
Cdd:COG1196 363 AEEALLEaEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEA--EEALLERLERLEEELEELEEALAELEEEEEEE 440
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226423935 2201 FQTVIKEDlpKRAKTLSSDSEELLNEAKMTQKRLQQVSPALNSLQQTLKTVSVQKDLLDANLTVARDDLHGIQR 2274
Cdd:COG1196 441 EEALEEAA--EEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKA 512
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
681-719 |
8.16e-07 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 48.08 E-value: 8.16e-07
10 20 30
....*....|....*....|....*....|....*....
gi 226423935 681 CQCDIGGALTTMCSGPSGVCQCREHVEGKQCQRPENNYY 719
Cdd:smart00180 1 CDCDPGGSASGTCDPDTGQCECKPNVTGRRCDRCAPGYY 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1861-2257 |
8.49e-07 |
|
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: 55.18 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1861 ETQAKDlrNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQvnsrkAQT-LYNnidqtiqSAKELDMKIKNIVQ 1939
Cdd:pfam01576 6 EMQAKE--EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-----AETeLCA-------EAEEMRARLAARKQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1940 NVHILLKQM-ARPGGEGtdlpvgDWSREL-AEAQRMMRDLRsrDFKKHLQEAEA----------------EKMEAQLL-- 1999
Cdd:pfam01576 72 ELEEILHELeSRLEEEE------ERSQQLqNEKKKMQQHIQ--DLEEQLDEEEAarqklqlekvtteakiKKLEEDILll 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2000 ------LHRIRTWLE-------SHQVENNGLLKNIRDSLNDYEDKLQDLRSILQEAAAQAKQATGINHENEGVLGAIQRQ 2066
Cdd:pfam01576 144 edqnskLSKERKLLEeriseftSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2067 MKEM----DSLKNDFTK-------YLATADSSLLQTNNLLQQM---------------------DKSQKEYESLAAALNG 2114
Cdd:pfam01576 224 IAELqaqiAELRAQLAKkeeelqaALARLEEETAQKNNALKKIreleaqiselqedleseraarNKAEKQRRDLGEELEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2115 ARQELSD-----------------RVRELSRSGGKAPLVVEAE------KHAQSLQELAKQLEEIKRNTSGDELVRCAVD 2171
Cdd:pfam01576 304 LKTELEDtldttaaqqelrskreqEVTELKKALEEETRSHEAQlqemrqKHTQALEELTEQLEQAKRNKANLEKAKQALE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2172 AATAyeNILNAIRAAEDAASKATSASKSAFQTVikEDLPKRAktlsSDSE----ELLNEAKMTQKRLQQVSPALNSLQQt 2247
Cdd:pfam01576 384 SENA--ELQAELRTLQQAKQDSEHKRKKLEGQL--QELQARL----SESErqraELAEKLSKLQSELESVSSLLNEAEG- 454
|
490
....*....|
gi 226423935 2248 lKTVSVQKDL 2257
Cdd:pfam01576 455 -KNIKLSKDV 463
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1835-2200 |
1.14e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.56 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1835 EELRLVKSKLQGLSVSTgALEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQVNSRKAQ 1914
Cdd:COG1196 220 EELKELEAELLLLKLRE-LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1915 TLYNNIDQTIQSAKELDMKIKNivqnvhiLLKQMARpggegtdlpvgdWSRELAEAQRMMRDLRSRdfkkhLQEAEAEKM 1994
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEE-------LEEELAE------------LEEELEELEEELEELEEE-----LEEAEEELE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1995 EAQLLLHRIRTWLESHQVENNGLLKNIRDSLNDYEDKLQDLRSILQEAAAQAKQATGINHENEGVLGAIQRQMKEMDSLK 2074
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2075 NDFTKYLATADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSGGKAPLVVEAEKHAQSLQELAKQLE 2154
Cdd:COG1196 435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAAL 514
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 226423935 2155 EIKRN----TSGDELVRCAVDAATAYENIL-----NAIRAAEDAASKATSASKSA 2200
Cdd:COG1196 515 LLAGLrglaGAVAVLIGVEAAYEAALEAALaaalqNIVVEDDEVAAAAIEYLKAA 569
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2060-2237 |
1.53e-06 |
|
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: 53.61 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2060 LGAIQRQMKEMDSLKNDFTKYLATADSSLLQTNNLLQ-----------QMDKSQKEYESLAAALNGARQELSDRVRELSR 2128
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRaleqelaaleaELAELEKEIAELRAELEAQKEELAELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2129 SGGKAPLVV--------EAEKHAQSLQELA----KQLEEIKRNTsgDELVRCAVDAATAYENiLNAIRAAEDAASKATSA 2196
Cdd:COG4942 116 LGRQPPLALllspedflDAVRRLQYLKYLAparrEQAEELRADL--AELAALRAELEAERAE-LEALLAELEEERAALEA 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 226423935 2197 SKSAFQTVIKEdLPKRAKTLSSDSEELLNEAKMTQKRLQQV 2237
Cdd:COG4942 193 LKAERQKLLAR-LEKELAELAAELAELQQEAEELEALIARL 232
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1965-2157 |
1.72e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1965 RELAEAQRMMRDLRSR------------------DFKKHLQEAEAEKMEAQLLLHRIRTWLESH-----QVENNGLLKNI 2021
Cdd:COG3206 189 KELEEAEAALEEFRQKnglvdlseeaklllqqlsELESQLAEARAELAEAEARLAALRAQLGSGpdalpELLQSPVIQQL 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2022 RDSLNDYEDKLQDLRSILqeaaaqakqatGINHEnegVLGAIQRQMKEMDS-LKNDFTKYLATADSSLLQTNNLLQQMDK 2100
Cdd:COG3206 269 RAQLAELEAELAELSARY-----------TPNHP---DVIALRAQIAALRAqLQQEAQRILASLEAELEALQAREASLQA 334
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 226423935 2101 SQKEYESLAAALNGARQELsdrvRELSRsggkaplvvEAEKHAQSLQELAKQLEEIK 2157
Cdd:COG3206 335 QLAQLEARLAELPELEAEL----RRLER---------EVEVARELYESLLQRLEEAR 378
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1828-2154 |
1.77e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 53.37 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1828 NDLASMGEELRLVKSKLQGLSvstgalEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQ 1907
Cdd:COG4372 59 EELEQLEEELEQARSELEQLE------EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1908 VNSRKAQTLYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARPGGEGTDLPVgdwSRELAEAQRMMRDLRSRDFKKHLQ 1987
Cdd:COG4372 133 QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL---DELLKEANRNAEKEEELAEAEKLI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1988 EAEaEKMEAQLLLHRIRTWLESHQVENNGLLknirDSLNDYEDKLQDLRSILQEAAAQAKQATGINHENEGVLGAIQRQM 2067
Cdd:COG4372 210 ESL-PRELAEELLEAKDSLEAKLGLALSALL----DALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2068 KEMDSLKNDfTKYLATADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSGGKAPLVVEAEKHAQSLQ 2147
Cdd:COG4372 285 LEALEEAAL-ELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGA 363
|
....*..
gi 226423935 2148 ELAKQLE 2154
Cdd:COG4372 364 EAGVADG 370
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2081-2385 |
2.36e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2081 LATADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELsdrvRELSRSGGKAPLVVEAEKHAQSLQELAKQLEEIKRnt 2160
Cdd:COG4717 80 LKEAEEKEEEYAELQEELEELEEELEELEAELEELREEL----EKLEKLLQLLPLYQELEALEAELAELPERLEELEE-- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2161 sgdelvrcavdAATAYENILNAIRAAEDAASKAtsasksafQTVIKEDLPKRAKTLSSDSEELLNEAKMTQKRLQQVSPA 2240
Cdd:COG4717 154 -----------RLEELRELEEELEELEAELAEL--------QEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2241 LNSLQQTLKTVSVQKDLLDANLTVArDDLHGIQRGDIDSVVIGA----KSMVREANGITSEVLD------GLNPIQTDLG 2310
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAAllalLGLGGSLLSLILTIAGvlflvlGLLALLFLLL 293
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226423935 2311 RIKDSYESARREDFSKALVDANNSVKKLTRKLPDLFIKIESINQQLLPLgniSDNVDRIRELIQQARDAANKVAI 2385
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEL---LDRIEELQELLREAEELEEELQL 365
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1835-2160 |
2.37e-06 |
|
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: 53.92 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1835 EELRLVKSKLQGLSVSTGALEQ-IRHMETQAKDLRNQLlgfRSATSSHGskmdDLEKELSHLNREFETLQEKAQVNSRKA 1913
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSeLRRIENRLDELSQEL---SDASRKIG----EIEKEIEQLEQEEEKLKERLEELEEDL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1914 QTLYNNIDQTIQSAKELDMKIKNIVQNVHILLKQM----ARPGGEGTDlPVGDWSRELAE--------AQRMMRDLRSRD 1981
Cdd:TIGR02169 747 SSLEQEIENVKSELKELEARIEELEEDLHKLEEALndleARLSHSRIP-EIQAELSKLEEevsriearLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1982 FKKHLQEAEAEKMEAQLLLHRIRTWLESHQVEN--------NGLLKNIRDSLNDYEDKLQDLRSILQeaaaqakqatgiN 2053
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngkkeelEEELEELEAALRDLESRLGDLKKERD------------E 893
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2054 HENEgvLGAIQRQMKEMDS---LKNDFTKYLATADSSLLQTN---------------------NLLQQMDKSQKEYESLA 2109
Cdd:TIGR02169 894 LEAQ--LRELERKIEELEAqieKKRKRLSELKAKLEALEEELseiedpkgedeeipeeelsleDVQAELQRVEEEIRALE 971
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 2110 AALNGARQELSDRVRELSRSGGKAPlVVEAEKhaQSLQELAKQLEEIKRNT 2160
Cdd:TIGR02169 972 PVNMLAIQEYEEVLKRLDELKEKRA-KLEEER--KAILERIEEYEKKKREV 1019
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1826-2178 |
2.90e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.23 E-value: 2.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1826 LLNDLASMGEELRLVKSKLQGLSvstGALEQIRHMETQAKDLRNQL--------LGFRSATSSHGSKMDDLEKELSHLNR 1897
Cdd:COG4717 137 LEAELAELPERLEELEERLEELR---ELEEELEELEAELAELQEELeelleqlsLATEEELQDLAEELEELQQRLAELEE 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1898 EFETLQEK-----AQVNSRKAQTLYNNIDQTIQSAKEL-------------DMKIKNIVQNVH--------------ILL 1945
Cdd:COG4717 214 ELEEAQEEleeleEELEQLENELEAAALEERLKEARLLlliaaallallglGGSLLSLILTIAgvlflvlgllallfLLL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1946 KQMARPGGEGTDLPVGDWSRELAEAQRMMRDLRSRDFKKHLQEAEAEKM-----EAQLLLHRIRTW-----LESHQVENN 2015
Cdd:COG4717 294 AREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELldrieELQELLREAEELeeelqLEELEQEIA 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2016 GLLKNIR-DSLNDYEDKLQDLRSIlqeaaaqakqatginHENEGVLGAIQRQMKEMDSLkndftkylATADSSLLQTNNL 2094
Cdd:COG4717 374 ALLAEAGvEDEEELRAALEQAEEY---------------QELKEELEELEEQLEELLGE--------LEELLEALDEEEL 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2095 LQQMDKSQKEYESLAAALNGARQELSDRVRELSRSGGKAPLVVEAEKHAQSLQELAKQLEEIKRNTSGDELVRcavDAAT 2174
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLE---EARE 507
|
....
gi 226423935 2175 AYEN 2178
Cdd:COG4717 508 EYRE 511
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1855-2382 |
5.27e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.53 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1855 EQIRHMETQAKDlRNQLLGF----------RSATSSHGSKMDDLEKELSHLNREfetlqekaqvnsrkaQTLYNnIDQTI 1924
Cdd:pfam12128 123 ELGRFMKNAGIQ-RTNLLNTreyrsiiqndRTLLGRERVELRSLARQFALCDSE---------------SPLRH-IDKIA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1925 QS--AKELDMK-IKNIVqnVHILLKQMARPggEGTDLPVGDWSRELAEAQRMMRDLRSRDFKKHLQEAEAEKMEAQLLLH 2001
Cdd:pfam12128 186 KAmhSKEGKFRdVKSMI--VAILEDDGVVP--PKSRLNRQQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLS 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2002 RIRTWLESHQVENNGLLKNIRDSLNDYEDKLQDLRSILQEAAAQakqatgINHENEGVLGAIQRQMKEMDSLKNDFTKYL 2081
Cdd:pfam12128 262 HLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDE------LNGELSAADAAVAKDRSELEALEDQHGAFL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2082 ------ATADSSLL-QTNNLLQQMDKSQKEYE----SLAAALNGARQELSDR-VRELSRSG--------GKAPLVVEAEK 2141
Cdd:pfam12128 336 dadietAAADQEQLpSWQSELENLEERLKALTgkhqDVTAKYNRRRSKIKEQnNRDIAGIKdklakireARDRQLAVAED 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2142 HAQSL-QELAKQLEEIKRNTSGDEL--------VRCAVDAATAYENILNAIRAAEDAASKATSASKSAFQTVikEDLP-- 2210
Cdd:pfam12128 416 DLQALeSELREQLEAGKLEFNEEEYrlksrlgeLKLRLNQATATPELLLQLENFDERIERAREEQEAANAEV--ERLQse 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2211 -KRAKTLSSDSEELLNEAkmtQKRLQQVSPALNSLQQTL--------KTVSVQKDLLDANL--TVARDDLHgiqRGDIDS 2279
Cdd:pfam12128 494 lRQARKRRDQASEALRQA---SRRLEERQSALDELELQLfpqagtllHFLRKEAPDWEQSIgkVISPELLH---RTDLDP 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2280 VVIGAkSMVREAN--GIT--------SEVLDGLNPIQTDLGRIKDSYESAR--REDFSKALVDANNSVKKLTRKLPDLFI 2347
Cdd:pfam12128 568 EVWDG-SVGGELNlyGVKldlkridvPEWAASEEELRERLDKAEEALQSARekQAAAEEQLVQANGELEKASREETFART 646
|
570 580 590
....*....|....*....|....*....|....*.
gi 226423935 2348 KIESINQQLLPLGNISDNV-DRIRELIQQARDAANK 2382
Cdd:pfam12128 647 ALKNARLDLRRLFDEKQSEkDKKNKALAERKDSANE 682
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1822-2237 |
6.43e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 6.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1822 CVMTLLNDLASMGEELR-LVKSKLQGLSVST---GALEQIRHME------TQAKDLRN----QLLGFRSATSSHGSKmdd 1887
Cdd:TIGR02168 599 GFLGVAKDLVKFDPKLRkALSYLLGGVLVVDdldNALELAKKLRpgyrivTLDGDLVRpggvITGGSAKTNSSILER--- 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1888 lEKELSHLNREFETLQEKAQVNSRKAQTLYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARPGGEgtdlpvgdwsREL 1967
Cdd:TIGR02168 676 -RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAE----------VEQ 744
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1968 AEAQRMMRDLRSRDFKKHLQEAEAEKMEAQLLLHRirtwLESHQVENNGLLKNIRDSLNDYEDKLQDLRSILQEAAAQAK 2047
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAE----AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAA 820
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2048 QATGINHENEGVLGAIQRQM------------------KEMDSLKNDFTKYLATADSSLLQTNNLLQQMDKSQKEYESLA 2109
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLedleeqieelsedieslaAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2110 AALNGARQELSDRVRELSRSGGKaplVVEAEKHAQSLQELAKQLEEIKRNTSGDELvrcaVDAATAYENILNAIRAAEDA 2189
Cdd:TIGR02168 901 EELRELESKRSELRRELEELREK---LAQLELRLEGLEVRIDNLQERLSEEYSLTL----EEAEALENKIEDDEEEARRR 973
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 226423935 2190 ASKATSASKsAFQTV----IKE--DLPKRAKTLSSDSEElLNEAKmtqKRLQQV 2237
Cdd:TIGR02168 974 LKRLENKIK-ELGPVnlaaIEEyeELKERYDFLTAQKED-LTEAK---ETLEEA 1022
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1854-2155 |
1.09e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 50.29 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1854 LEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQVNSRKAQTLYNNIDQTIQSAKELDMK 1933
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1934 IKNIVQnvhiLLKQMARPGGEGTDLpvgdwSRELAEAQRMM--RDLRSRDFKKHLQ-----EAEAEKMEAQLLLHRirtw 2006
Cdd:COG1340 94 LDELRK----ELAELNKAGGSIDKL-----RKEIERLEWRQqtEVLSPEEEKELVEkikelEKELEKAKKALEKNE---- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2007 lesHQVENNGLLKNIRDSLNDYEDKLQDLRSILQeaaaqakqatgiNHENE--GVLGAIQRQMKEMDSLKNDFTKYLATA 2084
Cdd:COG1340 161 ---KLKELRAELKELRKEAEEIHKKIKELAEEAQ------------ELHEEmiELYKEADELRKEADELHKEIVEAQEKA 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226423935 2085 DssllqtnNLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSggkaplvveaekhaqSLQELAKQLEE 2155
Cdd:COG1340 226 D-------ELHEEIIELQKELRELRKELKKLRKKQRALKREKEKE---------------ELEEKAEEIFE 274
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1827-2246 |
1.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1827 LNDLASMGEELRLVKSKLQGlsvSTGALE---------------QIRHMETQAKDLRN---------QLLGFRSATSShg 1882
Cdd:PRK03918 233 LEELKEEIEELEKELESLEG---SKRKLEekireleerieelkkEIEELEEKVKELKElkekaeeyiKLSEFYEEYLD-- 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1883 sKMDDLEKELSHLNREFETLQEKAQvnsrKAQTLYNNIDQTIQSAKELDMKIKNI------VQNVHILLKQMARPGGEGT 1956
Cdd:PRK03918 308 -ELREIEKRLSRLEEEINGIEERIK----ELEEKEERLEELKKKLKELEKRLEELeerhelYEEAKAKKEELERLKKRLT 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1957 DLPVGDWSRELAEAQR--------------MMRDLRSR--DFKKHLQEAEAEKME-----AQLLLHRIRTWLESHQVEnn 2015
Cdd:PRK03918 383 GLTPEKLEKELEELEKakeeieeeiskitaRIGELKKEikELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAE-- 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2016 glLKNIRDSLNDYEDKLQDLRSILQeaaaqakqatginhENEGVLGAIQR--QMKEM-DSLKNdftkylatADSSLLQTN 2092
Cdd:PRK03918 461 --LKRIEKELKEIEEKERKLRKELR--------------ELEKVLKKESEliKLKELaEQLKE--------LEEKLKKYN 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2093 nlLQQMDKSQKEYESLAAALNGARQELSDRVRELSRsggKAPLVVEAEKHAQSLQELAKQLEEIKRntsgdELVRCAVDa 2172
Cdd:PRK03918 517 --LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK---LEELKKKLAELEKKLDELEEELAELLK-----ELEELGFE- 585
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226423935 2173 atAYENILNAIRAAEDAASKATSASKSAFQTVIKEDLPKRAKTLSSDSEELLNEAKmtqKRLQQVSPALNSLQQ 2246
Cdd:PRK03918 586 --SVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETE---KRLEELRKELEELEK 654
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1828-2256 |
1.19e-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: 51.17 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1828 NDLASMGEELRLVKSKLQglsvstgalEQIRHMETQAKDLRNQLLG---FRSATSSHGSKMDDLEKELSHLNRE------ 1898
Cdd:TIGR04523 162 NDLKKQKEELENELNLLE---------KEKLNIQKNIDKIKNKLLKlelLLSNLKKKIQKNKSLESQISELKKQnnqlkd 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1899 -FETLQEKAQvnsrKAQTLYNNIDQTIQSAKELDMKIKNIVQNvhillKQmarpggegtdlpvgdwsRELAEAQRMMRDL 1977
Cdd:TIGR04523 233 nIEKKQQEIN----EKTTEISNTQTQLNQLKDEQNKIKKQLSE-----KQ-----------------KELEQNNKKIKEL 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1978 rsrdfKKHLQEAEAE-----KMEAQLLLHRIRTWLESHQVE----NNGLLKNIRdSLNDYEDKLQDLRSILqeaaaqakq 2048
Cdd:TIGR04523 287 -----EKQLNQLKSEisdlnNQKEQDWNKELKSELKNQEKKleeiQNQISQNNK-IISQLNEQISQLKKEL--------- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2049 aTGINHENEgvlgAIQRQMKE----MDSLKNDFTKYLATADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELSDRVR 2124
Cdd:TIGR04523 352 -TNSESENS----EKQRELEEkqneIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2125 ELSRsggkapLVVEAEKHAQSLQELAKQLEEIKrntsgdelvrcavdaaTAYENiLNAIRAAEDAASKATSAS-KSafqt 2203
Cdd:TIGR04523 427 EIER------LKETIIKNNSEIKDLTNQDSVKE----------------LIIKN-LDNTRESLETQLKVLSRSiNK---- 479
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 226423935 2204 vIKEDLPKRAKTLSSDSEELLN------EAKMTQKRLQQVSPALNSLQQTLKTVSVQKD 2256
Cdd:TIGR04523 480 -IKQNLEQKQKELKSKEKELKKlneekkELEEKVKDLTKKISSLKEKIEKLESEKKEKE 537
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2062-2379 |
1.20e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 51.45 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2062 AIQRQMKEMDSLKndftkyLATADSSLLQTN-----NLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSGGKAPLV 2136
Cdd:PRK11281 40 DVQAQLDALNKQK------LLEAEDKLVQQDleqtlALLDKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2137 VEAEKHAQSLQELAKQLEEIKrntsgDELVRCAVDAATAYENILNAIRAAEDAASKATSASKSAFQ--TVIKEDLPKRaK 2214
Cdd:PRK11281 114 TRETLSTLSLRQLESRLAQTL-----DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQirNLLKGGKVGG-K 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2215 TLSSDSEELLN-EAKM--TQKRLQQVSPALNSLQQTLKTvsVQKDLLDANLTVARDDLHGIQRgdidsvVIGAKSM---- 2287
Cdd:PRK11281 188 ALRPSQRVLLQaEQALlnAQNDLQRKSLEGNTQLQDLLQ--KQRDYLTARIQRLEHQLQLLQE------AINSKRLtlse 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2288 --VREAngitsEVLDGLNPIQTD-LgrIKDsyESARREDFSKALVDANNSVKKLTRKlpDLFIK------------I-ES 2351
Cdd:PRK11281 260 ktVQEA-----QSQDEAARIQANpL--VAQ--ELEINLQLSQRLLKATEKLNTLTQQ--NLRVKnwldrltqsernIkEQ 328
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 226423935 2352 IN---------------QQLLP-LGNISDNVDRIREL------IQQARDA 2379
Cdd:PRK11281 329 ISvlkgslllsrilyqqQQALPsADLIEGLADRIADLrleqfeINQQRDA 378
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1854-2345 |
1.21e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.22 E-value: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1854 LEQIRHMETQAKDLRNQLLGFRSAT---SSHGSKMDDLEKELSHLNREFETLQEKAQvNSRKaqtlynNIDQTIQSAKEL 1930
Cdd:PRK03918 206 LREINEISSELPELREELEKLEKEVkelEELKEEIEELEKELESLEGSKRKLEEKIR-ELEE------RIEELKKEIEEL 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1931 DMKIKNI------VQNVHILLKQMARPGGEGTDLPV--GDWSRELAEAQRMMRDLRSRdfKKHLQEAEAEKMEAQLLLHR 2002
Cdd:PRK03918 279 EEKVKELkelkekAEEYIKLSEFYEEYLDELREIEKrlSRLEEEINGIEERIKELEEK--EERLEELKKKLKELEKRLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2003 IRTWLEshqvenngllknirdslndyedKLQDLRSIlqeaaaqakqatginhenegvlgaiqrqMKEMDSLKNDFTKYla 2082
Cdd:PRK03918 357 LEERHE----------------------LYEEAKAK----------------------------KEELERLKKRLTGL-- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2083 tadsSLLQTNNLLQQMDKSQKEYE-------SLAAALNGARQELSDRVRELSRSGGKAPL-----------------VVE 2138
Cdd:PRK03918 385 ----TPEKLEKELEELEKAKEEIEeeiskitARIGELKKEIKELKKAIEELKKAKGKCPVcgrelteehrkelleeyTAE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2139 AEKHAQSLQELAKQLEEIKRNTSGDELVRCAVDAATAYENILNAIRAAEDAASKatsasksafqtVIKEDLpKRAKTLSS 2218
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKK-----------YNLEEL-EKKAEEYE 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2219 DSEELLNEAKMTQKRLQQVSPALNSLQQTLKTVSVQKDLLDANLTVARDDLHGIQRGDIDSVvigaKSMVREANGITSEV 2298
Cdd:PRK03918 529 KLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEEL----EERLKELEPFYNEY 604
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 226423935 2299 LDgLNPIQTDLGRIKDSYESARRE--DFSKALVDANNSVKKLTRKLPDL 2345
Cdd:PRK03918 605 LE-LKDAEKELEREEKELKKLEEEldKAFEELAETEKRLEELRKELEEL 652
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2060-2267 |
1.29e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2060 LGAIQRQMKEMDSLKNDFTKYLATADSSLLQTNNLLQ-----------QMDKSQKEYESLAAALNGARQELSDRVRELSR 2128
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNelqaelealqaEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2129 SGGKAPLvVEAEKHAQSLQELAKQLEeikrntsgdelvrcAVDAATAYEN-ILNAIRAAEDAASKATSASKSAfqtviKE 2207
Cdd:COG3883 98 SGGSVSY-LDVLLGSESFSDFLDRLS--------------ALSKIADADAdLLEELKADKAELEAKKAELEAK-----LA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 226423935 2208 DLPKRAKTLSSDSEELlnEAKMTQKR--LQQVSPALNSLQQTLKTVSVQKDLLDANLTVARD 2267
Cdd:COG3883 158 ELEALKAELEAAKAEL--EAQQAEQEalLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1826-2249 |
1.59e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1826 LLNDLASMGEELRLVKSKLQGLSVSTgALEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHL---------- 1895
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGLTPEK-LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELkkakgkcpvc 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1896 NREFETLQEKAQVNSRKAQTlyNNIDQTIQSAKELDMKIKNIVQNVHILLKqmarpgGEGTDLPVgdwsRELAEaqrMMR 1975
Cdd:PRK03918 442 GRELTEEHRKELLEEYTAEL--KRIEKELKEIEEKERKLRKELRELEKVLK------KESELIKL----KELAE---QLK 506
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1976 DLRSRDFKKHLQEAEAEKMEAQLLLHRIRTwLEShqvENNGLLKNIRdSLNDYEDKLQDLRSILqeaaaqakqatginHE 2055
Cdd:PRK03918 507 ELEEKLKKYNLEELEKKAEEYEKLKEKLIK-LKG---EIKSLKKELE-KLEELKKKLAELEKKL--------------DE 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2056 NEGVLGAIQRQMKEMdslkndftkylatADSSLLQTNNLLQQMDKSQKEYESLAaalnGARQELSDRVRELSRSGGKapl 2135
Cdd:PRK03918 568 LEEELAELLKELEEL-------------GFESVEELEERLKELEPFYNEYLELK----DAEKELEREEKELKKLEEE--- 627
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2136 VVEAEKHAQ----SLQELAKQLEEIKRNTSGDElvrcavdaataYENILNAIRAAEDAASKATSAsksafqtviKEDLPK 2211
Cdd:PRK03918 628 LDKAFEELAetekRLEELRKELEELEKKYSEEE-----------YEELREEYLELSRELAGLRAE---------LEELEK 687
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 226423935 2212 RAKTLSSDSEEL------LNEAKMTQKRLQQVSPALNSLQQTLK 2249
Cdd:PRK03918 688 RREEIKKTLEKLkeeleeREKAKKELEKLEKALERVEELREKVK 731
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1935-2322 |
3.05e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 49.74 E-value: 3.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1935 KNIVQNVHILLKQMARpggegtdlpvgDWSRELAEAQR----MMRDL-----RSRDFKKH---LQEAEAEKMEAQlllhr 2002
Cdd:pfam05557 8 KARLSQLQNEKKQMEL-----------EHKRARIELEKkasaLKRQLdresdRNQELQKRirlLEKREAEAEEAL----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2003 irtwleSHQVENNGLLKNIRDS----LNDYEDKLQDLRSILqeaaaqakqaTGINHEnegvLGAIQRQMKEMDSlkndft 2078
Cdd:pfam05557 72 ------REQAELNRLKKKYLEAlnkkLNEKESQLADAREVI----------SCLKNE----LSELRRQIQRAEL------ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2079 kYLATADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELSD---RVRELSR--------------SGGKAPLVVEAEK 2141
Cdd:pfam05557 126 -ELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEaeqRIKELEFeiqsqeqdseivknSKSELARIPELEK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2142 HAQSLQELAKQLEEIKRNTS-------------------GDELVRCAVDAA------TAYENI-----LNaIRAAEDAAS 2191
Cdd:pfam05557 205 ELERLREHNKHLNENIENKLllkeevedlkrklereekyREEAATLELEKEkleqelQSWVKLaqdtgLN-LRSPEDLSR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2192 KatsasksaFQTVIKEDLPKRAKTLSSDSE---------ELLNE-----AKMT--QKRLQQVSPALNSLQQTLKTVSVQK 2255
Cdd:pfam05557 284 R--------IEQLQQREIVLKEENSSLTSSarqlekarrELEQElaqylKKIEdlNKKLKRHKALVRRLQRRVLLLTKER 355
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226423935 2256 DLLDANLTVARDDL----HGIQRGDidsVVIGAKSMVREANGITSEVLDGLNPIQTDLGRIKDSYESARRE 2322
Cdd:pfam05557 356 DGYRAILESYDKELtmsnYSPQLLE---RIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQQAQTLERE 423
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
681-719 |
4.92e-05 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 43.11 E-value: 4.92e-05
10 20 30
....*....|....*....|....*....|....*....
gi 226423935 681 CQCDIGGALTTMCSGPSGVCQCREHVEGKQCQRPENNYY 719
Cdd:pfam00053 1 CDCNPHGSLSDTCDPETGQCLCKPGVTGRHCDRCKPGYY 39
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1854-2156 |
6.43e-05 |
|
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: 49.05 E-value: 6.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1854 LEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQVNSRKAQtlynniDQTIQSAKELdmk 1933
Cdd:pfam10174 407 QEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERL------EELESLKKEN--- 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1934 iKNIVQNVHILLKQMARPGGEGTDLPvgdwSRELAEAQRMMR---DLRSRDFKKHLQEAEAEKMEAQL------------ 1998
Cdd:pfam10174 478 -KDLKEKVSALQPELTEKESSLIDLK----EHASSLASSGLKkdsKLKSLEIAVEQKKEECSKLENQLkkahnaeeavrt 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1999 ---LLHRIRTwLE----SHQVENN----------GLLKNIRDSLNDYEDKLQDLRS-ILQEAAAQAKQATGINH----EN 2056
Cdd:pfam10174 553 npeINDRIRL-LEqevaRYKEESGkaqaeverllGILREVENEKNDKDKKIAELESlTLRQMKEQNKKVANIKHgqqeMK 631
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2057 EGVLGAIQRQMKEMDSLKndftkylatADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELSDRvrelsrsggkaplv 2136
Cdd:pfam10174 632 KKGAQLLEEARRREDNLA---------DNSQQLQLEELMGALEKTRQELDATKARLSSTQQSLAEK-------------- 688
|
330 340
....*....|....*....|.
gi 226423935 2137 veaEKHAQSL-QELAKQLEEI 2156
Cdd:pfam10174 689 ---DGHLTNLrAERRKQLEEI 706
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2002-2264 |
1.09e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2002 RIRTWLESHqvennglLKNIRDSLNDYEDKLQDLRSilqeaaaqakqatginhENEGVlgAIQRQMKEMDSLKNDFTKYL 2081
Cdd:COG3206 175 KALEFLEEQ-------LPELRKELEEAEAALEEFRQ-----------------KNGLV--DLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2082 ATADSSLLQTNNLLQQMDKSQKEYESLAAALNG------ARQELSDRVREL----SRSGGKAPLVVEAEkhaQSLQELAK 2151
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQspviqqLRAQLAELEAELaelsARYTPNHPDVIALR---AQIAALRA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2152 QL-EEIKRntsgdelvrcavdAATAYENILNAIRAAEDAASKATSASKSAFQTvikedLPKRAKTLSsdseELLNEAKMT 2230
Cdd:COG3206 306 QLqQEAQR-------------ILASLEAELEALQAREASLQAQLAQLEARLAE-----LPELEAELR----RLEREVEVA 363
|
250 260 270
....*....|....*....|....*....|....
gi 226423935 2231 QKRLQQvspalnsLQQTLKTVSVQKDLLDANLTV 2264
Cdd:COG3206 364 RELYES-------LLQRLEEARLAEALTVGNVRV 390
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2090-2361 |
1.30e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2090 QTNNLLQQMDK--SQKEYESLAAALNGARQELSDRVRELSR----------SGGKAPLVVEA-EKHAQSLQELAKQLEEI 2156
Cdd:PRK02224 184 DQRGSLDQLKAqiEEKEEKDLHERLNGLESELAELDEEIERyeeqreqareTRDEADEVLEEhEERREELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2157 KRNTSGDELVRcavdaATAYENILNAIRAAEDAASKATSA-SKSAFQTVIKEDLPKRAKTLSSDSEELlneakmtQKRLQ 2235
Cdd:PRK02224 264 RETIAETERER-----EELAEEVRDLRERLEELEEERDDLlAEAGLDDADAEAVEARREELEDRDEEL-------RDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2236 QVSPALNSLQQTLKTVSVQKDLLDANLTVARDdlhgiQRGDIDSVVIGAKSMVREANGITSEVLDGLNPIQTDLGRIKDS 2315
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADDLEERAEELRE-----EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVD 406
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 226423935 2316 YESA--RREDFSKALVDANNSVKKLTRKLPDLFIKIESiNQQLLPLGN 2361
Cdd:PRK02224 407 LGNAedFLEELREERDELREREAELEATLRTARERVEE-AEALLEAGK 453
|
|
| Laminin_G_3 |
pfam13385 |
Concanavalin A-like lectin/glucanases superfamily; This domain belongs to the Concanavalin ... |
3014-3135 |
1.40e-04 |
|
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: 44.68 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 3014 QTTSSRGLVFHTGTRDSFVALYLSEGHVIFALGAGGKKLR-LRSKERYHDGKWHSVVFGLSGRKVHLVVDGLRAQEGSLP 3092
Cdd:pfam13385 29 SLPGWARAIISSSGGGGYSLGLDGDGRLRFAVNGGNGGWDtVTSGASVPLGQWTHVAVTYDGGTLRLYVNGVLVGSSTLT 108
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 226423935 3093 GNSTISPREQVYLGLSPSRKSkslpqhSFVGCLRNFQLDSKPL 3135
Cdd:pfam13385 109 GGPPPGTGGPLYIGRSPGGDD------YFNGLIDEVRIYDRAL 145
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1855-2235 |
1.60e-04 |
|
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: 47.54 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1855 EQIRHMETQAKDLRNQLLGFRSatsSHGSKMDDLEKELSHLNREF---ETLQEKAQVNsrKAQTLYNNIDQTIQSAKELD 1931
Cdd:pfam06160 121 EEVEELKDKYRELRKTLLANRF---SYGPAIDELEKQLAEIEEEFsqfEELTESGDYL--EAREVLEKLEEETDALEELM 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1932 MKIKNIVQNVHILL-----------KQMARpggEGTDLPVGDWSRELAEAQRMMRDLRSRDFKKHLQEAEA--EKMEAQL 1998
Cdd:pfam06160 196 EDIPPLYEELKTELpdqleelkegyREMEE---EGYALEHLNVDKEIQQLEEQLEENLALLENLELDEAEEalEEIEERI 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1999 --LLHRIRTWLESHQ-VENNglLKNIRDSLNDYEDKLQDLRSILQEAAAQAkqatGINHENEGVLGAIQRQMKEMDSLKN 2075
Cdd:pfam06160 273 dqLYDLLEKEVDAKKyVEKN--LPEIEDYLEHAEEQNKELKEELERVQQSY----TLNENELERVRGLEKQLEELEKRYD 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2076 DFTKYLATADS--SLLQTN--NLLQQMDKSQKEYESLAAALNGARQElsdrvrelsrsggkaplvveaEKHAQ-SLQELA 2150
Cdd:pfam06160 347 EIVERLEEKEVaySELQEEleEILEQLEEIEEEQEEFKESLQSLRKD---------------------ELEAReKLDEFK 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2151 KQLEEIKR-----NTSG-----DELVRCAVDAATAYENILNAIRAAEDAASKATSASKSAFQTVIKEdlpkraktlssdS 2220
Cdd:pfam06160 406 LELREIKRlveksNLPGlpesyLDYFFDVSDEIEDLADELNEVPLNMDEVNRLLDEAQDDVDTLYEK------------T 473
|
410
....*....|....*
gi 226423935 2221 EELLNEAKMTQKRLQ 2235
Cdd:pfam06160 474 EELIDNATLAEQLIQ 488
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1833-2251 |
1.78e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 47.73 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1833 MGEELRLVKSKLQGLSVS---TGALEQIRHMETQAKDLRNQLLGFRSATSShgskmddLEKELSHLNREFETLQE---KA 1906
Cdd:TIGR00606 524 MEQLNHHTTTRTQMEMLTkdkMDKDEQIRKIKSRHSDELTSLLGYFPNKKQ-------LEDWLHSKSKEINQTRDrlaKL 596
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1907 QVNSRKAQTLYNNIDQTIQSAKELDMKIKNIVQNVhillkqmarPGGEGTDLPVGDWSRELAEA--QRMMRDLRSRDFKK 1984
Cdd:TIGR00606 597 NKELASLEQNKNHINNELESKEEQLSSYEDKLFDV---------CGSQDEESDLERLKEEIEKSskQRAMLAGATAVYSQ 667
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1985 HLQEAEAEKMEAQLLLHRI-RTwleshQVENNGLLKNIRDSLNDYEDKLQDLRSILQEAAAQAKQATGINHENEGVLGAI 2063
Cdd:TIGR00606 668 FITQLTDENQSCCPVCQRVfQT-----EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLK 742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2064 QRQMKE-----------MDSLKNDFTK---YLATADSSL-----LQTN-----NLLQQMDKSQKEYESLAAALNGA---- 2115
Cdd:TIGR00606 743 EKEIPElrnklqkvnrdIQRLKNDIEEqetLLGTIMPEEesakvCLTDvtimeRFQMELKDVERKIAQQAAKLQGSdldr 822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2116 -----RQELSDRVRELSRsggkapLVVEAEKHAQSLQELAKQLEEIKRNTS--GDELVRCAVDAA----------TAYEN 2178
Cdd:TIGR00606 823 tvqqvNQEKQEKQHELDT------VVSKIELNRKLIQDQQEQIQHLKSKTNelKSEKLQIGTNLQrrqqfeeqlvELSTE 896
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226423935 2179 ILNAIRAAEDAASKAtsaskSAFQTVIKEDLPKRAKTLSSDSEellnEAKMTQKRLQQVSPALNSLQQTLKTV 2251
Cdd:TIGR00606 897 VQSLIREIKDAKEQD-----SPLETFLEKDQQEKEELISSKET----SNKKAQDKVNDIKEKVKNIHGYMKDI 960
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1986-2328 |
1.88e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1986 LQEAEAEKMEAQLLLHRIRtwLESHQVEnnglLKNIRDSLNDYEDKLQDLRSILqeaaaqakqatginHENEGVLGAIQR 2065
Cdd:TIGR02168 215 YKELKAELRELELALLVLR--LEELREE----LEELQEELKEAEEELEELTAEL--------------QELEEKLEELRL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2066 QMKEMDSLKNDftkylatADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSggkaplvveAEKHAQS 2145
Cdd:TIGR02168 275 EVSELEEEIEE-------LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESK---------LDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2146 LQELAKQLEEIKRNTSG-----DELVRCAVDAATAYENILNAIRAAEDAASKATSASKSAFQTVI-----KEDLPKRAKT 2215
Cdd:TIGR02168 339 LAELEEKLEELKEELESleaelEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIErlearLERLEDRRER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2216 LSSDSEELL-----NEAKMTQKRLQQVSPALNSLQQTLKTVSVQKDLLDANLTVARDDLHGIQRG--DIDSVVIGAKSMV 2288
Cdd:TIGR02168 419 LQQEIEELLkkleeAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERElaQLQARLDSLERLQ 498
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 226423935 2289 REANGIT---SEVLDGLNPIQTDLGRIKDSYESarREDFSKAL 2328
Cdd:TIGR02168 499 ENLEGFSegvKALLKNQSGLSGILGVLSELISV--DEGYEAAI 539
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1829-2269 |
2.25e-04 |
|
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: 47.09 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1829 DLASMGEELRLVKSKLQ-----GLSVSTgaleQIRHMETQAKDLRNQLLGFRSAT-------SSHGSKMDDLEKELSHLN 1896
Cdd:pfam01576 462 DVSSLESQLQDTQELLQeetrqKLNLST----RLRQLEDERNSLQEQLEEEEEAKrnverqlSTLQAQLSDMKKKLEEDA 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1897 REFETLQEKAQVNSRKAQTLYNNIDQTIQSAKELDmKIKNIVQnvhillkqmarpgGEGTDLPVG-DWSRELAEAQrmmr 1975
Cdd:pfam01576 538 GTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE-KTKNRLQ-------------QELDDLLVDlDHQRQLVSNL---- 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1976 DLRSRDFKKHLqeAEAEKMEAQLLLHRIRTWLESHQVENNGL-----LKNIRDSLNDYEDKLQDLRSILQEAAAQAKQaT 2050
Cdd:pfam01576 600 EKKQKKFDQML--AEEKAISARYAEERDRAEAEAREKETRALslaraLEEALEAKEELERTNKQLRAEMEDLVSSKDD-V 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2051 GIN-HENEGVLGAIQRQMKEM----DSLKNDFTkylATADSSL-LQTNnlLQQMdKSQKEYEslaaaLNGARQELSDRVR 2124
Cdd:pfam01576 677 GKNvHELERSKRALEQQVEEMktqlEELEDELQ---ATEDAKLrLEVN--MQAL-KAQFERD-----LQARDEQGEEKRR 745
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2125 ELSRSggkaplvveaekhaqsLQELAKQLEEIKRNTSGdelvrcAVDAATAYENILNAIRAAEDAASKA-TSASKS--AF 2201
Cdd:pfam01576 746 QLVKQ----------------VRELEAELEDERKQRAQ------AVAAKKKLELDLKELEAQIDAANKGrEEAVKQlkKL 803
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226423935 2202 QTVIKeDLPKRAKTLSSDSEELLNEAKMTQKRLQQVSPALNSLQQTLKTVSVQKDLLDANltvaRDDL 2269
Cdd:pfam01576 804 QAQMK-DLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQE----RDEL 866
|
|
| Laminin_G_1 |
pfam00054 |
Laminin G domain; |
2432-2564 |
2.41e-04 |
|
Laminin G domain;
Pssm-ID: 395008 [Multi-domain] Cd Length: 131 Bit Score: 43.46 E-value: 2.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2432 VMYLGNKDAsKDYIGMAVVDGQLTCVYNLGDREAEVQIDQVLTESESQEAVMDRVKFQRIYQFAKLNytkEATSTKPKAP 2511
Cdd:pfam00054 10 LLYNGTQTE-RDFLALELRDGRLEVSYDLGSGAAVVRSGDKLNDGKWHSVELERNGRSGTLSVDGEA---RPTGESPLGA 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 226423935 2512 gvydmesassNTLLNLDpenAVFYVGGYPPGFELPRRLRF-PPYKGCIELDDLN 2564
Cdd:pfam00054 86 ----------TTDLDVD---GPLYVGGLPSLGVKKRRLAIsPSFDGCIRDVIVN 126
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1831-2498 |
2.71e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 2.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1831 ASMGEELRLVKSKLQGLSVSTGALEQIRHMETQAKDLRNQLLGFRSAtsshgskmddlEKELSHLNREFETLQEKA-QVN 1909
Cdd:TIGR00606 231 AQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSR-----------KKQMEKDNSELELKMEKVfQGT 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1910 SRKAQTLYNNIDQTIQSAKEldmKIKNIVQNVHILLKQMARPGGEGTDLPVgDWSRELAEAQRMMRDLRSRDFkkhLQEA 1989
Cdd:TIGR00606 300 DEQLNDLYHNHQRTVREKER---ELVDCQRELEKLNKERRLLNQEKTELLV-EQGRLQLQADRHQEHIRARDS---LIQS 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1990 EAEKMEAQLLLH------RIRTWLESHQVENNGLLKNIRDSLNDYEDKLQdlrsilqeaaAQAKQATGINHENEGVLGAI 2063
Cdd:TIGR00606 373 LATRLELDGFERgpfserQIKNFHTLVIERQEDEAKTAAQLCADLQSKER----------LKQEQADEIRDEKKGLGRTI 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2064 QRQM----KEMDSLKNdFTKYLATADSSLLQTNNLLQQMDKSQKEyesLAAALNGARQElSDRVRELSRSGGKAPLVvea 2139
Cdd:TIGR00606 443 ELKKeileKKQEELKF-VIKELQQLEGSSDRILELDQELRKAERE---LSKAEKNSLTE-TLKKEVKSLQNEKADLD--- 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2140 ekhaQSLQELAKQLEEIKRNT-SGDELVRCAVDAATAYENIL-NAIRAAEDAASKATsasksafqtvikeDLPKRaKTLS 2217
Cdd:TIGR00606 515 ----RKLRKLDQEMEQLNHHTtTRTQMEMLTKDKMDKDEQIRkIKSRHSDELTSLLG-------------YFPNK-KQLE 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2218 SDSEELLNEAKMTQKRLQQVSPALNSLQQTLKTVSVQKDLLDANLTVARDDLHgiqrgdidsvvigaksmvrEANGITSE 2297
Cdd:TIGR00606 577 DWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLF-------------------DVCGSQDE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2298 vldglnpiQTDLGRIKDSYESARRE------------DFSKALVDANNS------------------VKKL---TRKLPD 2344
Cdd:TIGR00606 638 --------ESDLERLKEEIEKSSKQramlagatavysQFITQLTDENQSccpvcqrvfqteaelqefISDLqskLRLAPD 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2345 -------LFIKIESINQQLLPLGNISDN-VDRIRELIQQARDAANKVAIPMRfngksgvevRLPNDLEdlKGYTSLSLFL 2416
Cdd:TIGR00606 710 klkstesELKKKEKRRDEMLGLAPGRQSiIDLKEKEIPELRNKLQKVNRDIQ---------RLKNDIE--EQETLLGTIM 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2417 QRPDLRENGGTeDMFVM---YLGNKDASKDYIGMAV----VDGQLTCV-YNLGDREAEVQIDQVLTESE-SQEAVMDRVK 2487
Cdd:TIGR00606 779 PEEESAKVCLT-DVTIMerfQMELKDVERKIAQQAAklqgSDLDRTVQqVNQEKQEKQHELDTVVSKIElNRKLIQDQQE 857
|
730
....*....|.
gi 226423935 2488 FQRIYQfAKLN 2498
Cdd:TIGR00606 858 QIQHLK-SKTN 867
|
|
| Laminin_G_2 |
pfam02210 |
Laminin G domain; This family includes the Thrombospondin N-terminal-like domain, a Laminin G ... |
2433-2559 |
2.92e-04 |
|
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: 43.18 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2433 MYLGNKdaSKDYIGMAVVDGQLTCVYNLGDREAEVqidqvlteSESQEAVMD----RVKFQRIYQFAKLNYTKEATSTKP 2508
Cdd:pfam02210 11 LYAGGG--GSDFLALELVNGRLVLRYDLGSGPESL--------LSSGKNLNDgqwhSVRVERNGNTLTLSVDGQTVVSSL 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 226423935 2509 KAPGVYDMESassntllnldpeNAVFYVGGYPPGFELPRRLRFPPYKGCIE 2559
Cdd:pfam02210 81 PPGESLLLNL------------NGPLYLGGLPPLLLLPALPVRAGFVGCIR 119
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1853-2189 |
3.02e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1853 ALEQIRHMETQAKDLRNQLLGFRsatsshgSKMDDLEKELSHLNREFETLQEKAQVNSRKAQTLYNNIDQTIQSAKELDM 1932
Cdd:COG4372 36 ALFELDKLQEELEQLREELEQAR-------EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1933 KIKNIVQNVHILLKQMArpggegtDLpvgdwsreLAEAQRMMRDLRSRDFKKHLQEAEAEKMEAQllLHRIRTWLESHQV 2012
Cdd:COG4372 109 EAEELQEELEELQKERQ-------DL--------EQQRKQLEAQIAELQSEIAEREEELKELEEQ--LESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2013 ENNGLlknirdSLNDYEDKLQDLRSILqeaaaQAKQATGINHENEGVLGAIQRQMKEMDSLKNDFTKYLATADSSLLQTN 2092
Cdd:COG4372 172 ELQAL------SEAEAEQALDELLKEA-----NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2093 NLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSGGKAPLVVEAEKHAQSLQELAKQLEEIKRNTSGDELVRCAVDA 2172
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAA 320
|
330
....*....|....*..
gi 226423935 2173 ATAYENILNAIRAAEDA 2189
Cdd:COG4372 321 LLELAKKLELALAILLA 337
|
|
| ATG17_like |
pfam04108 |
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ... |
1960-2252 |
3.19e-04 |
|
Autophagy protein ATG17-like domain; This domain is found in the autophagy-related proteins ATG17 and ATG11, conserved across eukaryotes. ATG17 forms a complex with ATG29 and ATG31, critical for both PAS (preautophagosomal structure) formation and autophagy. Together with ATG13, it is required for ATG1 kinase activation. ATG11 is a scaffold protein required for the cytoplasm-to-vacuole targeting (Cvt) pathway during starvation and to recruit ATG proteins to the pre-autophagosome. It is also required for ATG1 kinase activation. In many eukaryotes, ATG11 (the orthologue in mammals is RB1-inducible coiled-coil protein 1 (RB1CC1) and in S. pombe is Taz1-interacting factor 1 (taf1)) is essential for bulk autophagy, except in S.cerevisiae. ATG17 and ATG11 are large similar proteins, both predicted to be almost entirely helical, containing conserved coiled-coil regions and lack obvious functional motifs.
Pssm-ID: 427715 [Multi-domain] Cd Length: 360 Bit Score: 45.84 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1960 VGDWSRELAE-AQRMMRDLRSRDFK-----KHLQEAEAekmeaqlLLHRIRTWLESHQVEN----NGLLKNIRDSLNDYE 2029
Cdd:pfam04108 8 LCRWANELLTdARSLLEELVVLLAKiaflrRGLSVQLA-------NLEKVREGLEKVLNELkkdfKQLLKDLDAALERLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2030 DKLQDLRSILqeaaaqakqatginhenegVLGAIQRQMKEMDSLKnDFtkyLATADSSLLQtNNLLQQMDKSQKEYESLA 2109
Cdd:pfam04108 81 ETLDKLRNTP-------------------VEPALPPGEEKQKTLL-DF---IDEDSVEILR-DALKELIDELQAAQESLD 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2110 AALNGARQELSDRVRELSRSGGKAPLVVEAEKHAQSLQELAKQLEEIkrntsGDELVRcavdaatAYENILNAIRAAEDA 2189
Cdd:pfam04108 137 SDLKRFDDDLRDLQKELESLSSPSESISLIPTLLKELESLEEEMASL-----LESLTN-------HYDQCVTAVKLTEGG 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226423935 2190 askatsasKSAFQTVIKED---LPKRAKTLSSDSEELLNEAKMTQKRLQQVSPALNSLQQTLKTVS 2252
Cdd:pfam04108 205 --------RAEMLEVLENDareLDDVVPELQDRLDEMENNYERLQKLLEQKNSLIDELLSALQLIA 262
|
|
| Gp58 |
pfam07902 |
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage ... |
2094-2303 |
3.68e-04 |
|
gp58-like protein; Sequences found in this family are derived from a number of bacteriophage and prophage proteins. They are similar to gp58, a minor structural protein of Lactococcus delbrueckii bacteriophage LL-H.
Pssm-ID: 369586 [Multi-domain] Cd Length: 594 Bit Score: 46.10 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2094 LLQQMDKSQKEYESLAAALNGARQELSDRVRELSRS------GGKAPLVVEAEKHAQSLQELAKQL-----EEIKRNTSg 2162
Cdd:pfam07902 134 ATRISEDTDKKLALINETISGIRREYQDADRQLSSSyqagieGLKATMASDKIGLQAEIQASAQGLsqrydNEIRKLSA- 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2163 dELVRCAVDAATAYENILNAIRAAEDAASKAT--------SASKSAFQTVIKEdLPKRAKTLSSDSEELLNEAKMTQKRL 2234
Cdd:pfam07902 213 -KITTTSSGTTEAYESKLDDLRAEFTRSNQGMrteleskiSGLQSTQQSTAYQ-ISQEISNREGAVSRVQQDLDSYQRRL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2235 QQVSPALNSLQQTLK----TVSVQKDLLDANLT---------VARDDLHGIQRGDIDSVVIGAKSMVREANGITSEVLDG 2301
Cdd:pfam07902 291 QDAEKNYSSLTQTVKglqsTVSDPNSKLESRITqlaglieqkVTRGDVESIIRQSGDSIMLAIKAKLPQSKMSGSEIISA 370
|
..
gi 226423935 2302 LN 2303
Cdd:pfam07902 371 IN 372
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
2087-2258 |
4.28e-04 |
|
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: 44.60 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2087 SLLQTNNLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSGGKAPLVVEAEKHAQSLQELAKQLEEIKrntsgDELV 2166
Cdd:pfam12795 21 DLQQALSLLDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLSLEELEQRLLQTS-----AQLQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2167 RCAVDAATaYENILNAIRAAEDAASKATSASKSAFQTvIKEDLpkrakTLSSDSEELLNEAKMTQKRLQQVspALNS--- 2243
Cdd:pfam12795 96 ELQNQLAQ-LNSQLIELQTRPERAQQQLSEARQRLQQ-IRNRL-----NGPAPPGEPLSEAQRWALQAELA--ALKAqid 166
|
170
....*....|....*.
gi 226423935 2244 -LQQTLKTVSVQKDLL 2258
Cdd:pfam12795 167 mLEQELLSNNNRQDLL 182
|
|
| TNFRSF26 |
cd15837 |
Tumor necrosis factor receptor superfamily member 26 (TNFRSF26), also known as tumor necrosis ... |
1293-1453 |
4.75e-04 |
|
Tumor necrosis factor receptor superfamily member 26 (TNFRSF26), also known as tumor necrosis factor receptor homolog 3 (TNFRH3); TNFRSF26 (also known as tumor necrosis factor receptor homolog 3 (TNFRH3) or TNFRSF24) is predominantly expressed in embryos and lymphoid cell types, along with its closely related TNFRSF22 and TNFRSF23 orthologs, and is developmentally regulated. Unlike TNFRSF22/23, TNFRSF26 does not serve as a TRAIL decoy receptor; it remains an orphan receptor.
Pssm-ID: 276933 [Multi-domain] Cd Length: 118 Bit Score: 42.35 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1293 CSRCATGYYGFpycKPCNcgrrlceevtgkclcPPHTVRpQCEVCEMNSFNFHPvAGCDVCN-CSRKGTIEAAVSECDRD 1371
Cdd:cd15837 13 CQLCPAGHYVS---EPCQ---------------ENHGVG-ECAPCEPGTFTAHP-NGETSCFpCSQCRDDQEVVAECSAT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1372 SG-QCRCKPrvtgqqcdkcapGFYQFPECVPCSCNRdgtepsvcdpetgacmckenvegpqCQLCREGSFYLDPTNPKGC 1450
Cdd:cd15837 73 SDrQCQCKQ------------GHFYCDENCLESCFR-------------------------CSRCPGGRVVLQPCNATRD 115
|
...
gi 226423935 1451 TKC 1453
Cdd:cd15837 116 TVC 118
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2062-2269 |
5.39e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2062 AIQRQMKEMDSLKNDFTKYLATADSSLLQT--NNLLQQMDKSQKEYESLAAALNGARQELSDRVRELSRSGGkaplvvea 2139
Cdd:COG4913 266 AARERLAELEYLRAALRLWFAQRRLELLEAelEELRAELARLEAELERLEARLDALREELDELEAQIRGNGG-------- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2140 ekhaQSLQELAKQLEEIKRntsgdELVRCAvDAATAYENILNAIRAAEDAaskatsaSKSAFQTVIKE--DLPKRAKTLS 2217
Cdd:COG4913 338 ----DRLEQLEREIERLER-----ELEERE-RRRARLEALLAALGLPLPA-------SAEEFAALRAEaaALLEALEEEL 400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 226423935 2218 SDSEELLNEAKMTQKRLQQvspALNSLQQTLKTVSVQKDLLDANLTVARDDL 2269
Cdd:COG4913 401 EALEEALAEAEAALRDLRR---ELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
352-420 |
6.25e-04 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 40.03 E-value: 6.25e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226423935 352 ACNCHGHAVdcyydpdvehqqaslNSKGVYAGGGVCInCQHNTAGVNCEKCAKGYFRPHGVPvdalHGC 420
Cdd:cd00055 1 PCDCNGHGS---------------LSGQCDPGTGQCE-CKPNTTGRRCDRCAPGYYGLPSQG----GGC 49
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1834-2385 |
6.48e-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: 45.83 E-value: 6.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1834 GEELRLVKSKLQGLSVSTGALE-QIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQVNSRK 1912
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLErSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1913 AQTLYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARPGGEGTDLpvGDWSRELAEAQRMMR-DLRsrDFKKHLQEAEA 1991
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRL--QEELQRLSEELADLNaAIA--GIEAKINELEE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1992 EKMEAQLLLHRIRTWLESHQVENNGL---LKNIRDSLNDYEDKLQDLRSIL-----------QEAAAQAKQATGINHENE 2057
Cdd:TIGR02169 442 EKEDKALEIKKQEWKLEQLAADLSKYeqeLYDLKEEYDRVEKELSKLQRELaeaeaqaraseERVRGGRAVEEVLKASIQ 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2058 GVLGAIqRQMKEMDS------------------LKNDFT-----KYL-------AT-----------ADSSLLQTN---- 2092
Cdd:TIGR02169 522 GVHGTV-AQLGSVGEryataievaagnrlnnvvVEDDAVakeaiELLkrrkagrATflplnkmrderRDLSILSEDgvig 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2093 ---NLLQQMDKSQKEY----------ESLAAAlngarQELSDRVR------EL----------SRSGGKAPLVVEAEKha 2143
Cdd:TIGR02169 601 favDLVEFDPKYEPAFkyvfgdtlvvEDIEAA-----RRLMGKYRmvtlegELfeksgamtggSRAPRGGILFSRSEP-- 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2144 QSLQELAKQLEEIKRntsgdELVRCAVDAATAyENILNAIRAAEDAASKATsasksafqtvikEDLPKRAKTLSSDSEEL 2223
Cdd:TIGR02169 674 AELQRLRERLEGLKR-----ELSSLQSELRRI-ENRLDELSQELSDASRKI------------GEIEKEIEQLEQEEEKL 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2224 LNEAKMTQKRLQQVSPALNSLQQTLKTVSVQKDLLDANLTVARDDLHGIQRGDIDSVVigaKSMVREANGITSEV--LDG 2301
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI---PEIQAELSKLEEEVsrIEA 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2302 -LNPIQTDLGR--IKDSYESARREDFSKALVDANNSVKKLTRKLPDLFIKIESINQQLLP-----------LGNISDNVD 2367
Cdd:TIGR02169 813 rLREIEQKLNRltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEEleaalrdlesrLGDLKKERD 892
|
650
....*....|....*...
gi 226423935 2368 RIRELIQQARDAANKVAI 2385
Cdd:TIGR02169 893 ELEAQLRELERKIEELEA 910
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1805-1937 |
6.81e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1805 QEPKDGSPAEEcddcdscvMTLLNDLASMGEELRLVKSKLQGLSVSTGALEQIRHMETQAKDLRNQLLGFRSATSSHGSK 1884
Cdd:COG1340 125 QQTEVLSPEEE--------KELVEKIKELEKELEKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 226423935 1885 MDDLEKELSHLNREFETLQEKAQVNSRKAQTLYNNIDQTIQSAKELDMKIKNI 1937
Cdd:COG1340 197 MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKL 249
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
296-341 |
7.16e-04 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 39.60 E-value: 7.16e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 296 CVCN--GHA-EACSADNpekqFRCECQHHTCGDTCNRCCAGYNQRRWQP 341
Cdd:smart00180 1 CDCDpgGSAsGTCDPDT----GQCECKPNVTGRRCDRCAPGYYGDGPPG 45
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1893-2264 |
7.45e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 45.28 E-value: 7.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1893 SHLNREFETLQEKAQVNSRKAQTLYNN--IDQTI-QSAKELDMKIKNIVQNV---HILLKQmarpgGEGTDLPVGDWSR- 1965
Cdd:PRK01156 77 GHVYQIRRSIERRGKGSRREAYIKKDGsiIAEGFdDTTKYIEKNILGISKDVflnSIFVGQ-----GEMDSLISGDPAQr 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1966 -----ELAEAQRMMRD-LRSRDFKKHLQEAEAEkmeaqllLHRIRTWLESHQVEnnglLKNIRDSLNDYEDKLQD-LRSI 2038
Cdd:PRK01156 152 kkildEILEINSLERNyDKLKDVIDMLRAEISN-------IDYLEEKLKSSNLE----LENIKKQIADDEKSHSItLKEI 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2039 LQEAAAQAKQATGINHENEgvlgaiqrQMKEMDSLKNDFTKY---LATADSSL---LQTNNLLQQMDKSQKEYESLAAAL 2112
Cdd:PRK01156 221 ERLSIEYNNAMDDYNNLKS--------ALNELSSLEDMKNRYeseIKTAESDLsmeLEKNNYYKELEERHMKIINDPVYK 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2113 NgaRQELSDRVRELSRSGGKAPLVVEAEKHAQSLQELAKQLEE--------IKRNTSGDELVRCAVDAATAYENILNAIR 2184
Cdd:PRK01156 293 N--RNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVlqkdyndyIKKKSRYDDLNNQILELEGYEMDYNSYLK 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2185 AAEDAASKATSASKSafQTVIKEDLPKRAKTLSSDSEELLNEAKMTQKRLQQVSPALNSLQQTLKTVSVQKDLLDANLTV 2264
Cdd:PRK01156 371 SIESLKKKIEEYSKN--IERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEM 448
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
2068-2236 |
8.66e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 43.86 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2068 KEMDSLKNDftkyLATADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQ---ELSDRVRElsRSGGKAPLVVEAEKHAQ 2144
Cdd:pfam00261 1 KKMQQIKEE----LDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQlleEELERTEE--RLAEALEKLEEAEKAAD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2145 SLQELAKQLEEikRNTSGDELVRcavdaatAYENILN-AIRAAEDAASKATSASKSAfqTVIKEDLPK---RAKTLSSDS 2220
Cdd:pfam00261 75 ESERGRKVLEN--RALKDEEKME-------ILEAQLKeAKEIAEEADRKYEEVARKL--VVVEGDLERaeeRAELAESKI 143
|
170
....*....|....*.
gi 226423935 2221 EELLNEAKMTQKRLQQ 2236
Cdd:pfam00261 144 VELEEELKVVGNNLKS 159
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2062-2390 |
8.83e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 8.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2062 AIQRQMKEMDSLKNDFTKYLATADSSLLQTNNLLQQMDKSQKEYESLAAALNGARQELSDRVRELsrsggkaplvveaEK 2141
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL-------------AQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2142 HAQSLQELAKQLEEIKRntsgdELvrcavdaatayENILNAIRAAEDAASKATSASKSAFQTVIKEDlpKRAKTLSSDSE 2221
Cdd:COG4372 99 AQEELESLQEEAEELQE-----EL-----------EELQKERQDLEQQRKQLEAQIAELQSEIAERE--EELKELEEQLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2222 ELLNEAKMTQKRLQQVSPA-----LNSLQQTLKTVSVQKDLLDANLTVARDDLHGIQRGDIDSVVIGAKSMVREANGITS 2296
Cdd:COG4372 161 SLQEELAALEQELQALSEAeaeqaLDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2297 EVLDGLNPIQTDLGRIKDSYESARREDFSKALVDANNSVKKLTRKLPDLFIKIESINQQLLPLgniSDNVDRIRELIQQA 2376
Cdd:COG4372 241 ALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLN---LAALSLIGALEDAL 317
|
330
....*....|....
gi 226423935 2377 RDAANKVAIPMRFN 2390
Cdd:COG4372 318 LAALLELAKKLELA 331
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1829-2418 |
1.04e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.21 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1829 DLASMGEELRLVK-SKLQGLSVSTGALEQI----RH-METQAKDLRNQLLGFRSATSSHGSKMD----------DLEKEL 1892
Cdd:pfam12128 391 DIAGIKDKLAKIReARDRQLAVAEDDLQALeselREqLEAGKLEFNEEEYRLKSRLGELKLRLNqatatpelllQLENFD 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1893 SHLNREFETL------QEKAQVNSRKAQTLYNNIDQTIQSAKELDMKIKNIVQNVHILLKQMARPGGEGTDLPVGDWSRE 1966
Cdd:pfam12128 471 ERIERAREEQeaanaeVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHFLRKEAPDWEQS 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1967 LAeaqrmmrdlrsrdfkkhlqeaeaeKMEAQLLLHRI----RTWLESHQVENN--GL---LKNIrdSLNDYEDKLQDLRS 2037
Cdd:pfam12128 551 IG------------------------KVISPELLHRTdldpEVWDGSVGGELNlyGVkldLKRI--DVPEWAASEEELRE 604
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2038 ILQEAAAQAKQATGINHENEGVLGAIQRQMKEMDSLKNDFTKYLATADSSLLQTNNLLQQM------------DKSQKEY 2105
Cdd:pfam12128 605 RLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEkdkknkalaerkDSANERL 684
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2106 ESLAAALN-------GARQELSDRVRELSRSGGKAPLVVEAEKHAQS---LQELAKQLEEIKRNTSG------DELVRCA 2169
Cdd:pfam12128 685 NSLEAQLKqldkkhqAWLEEQKEQKREARTEKQAYWQVVEGALDAQLallKAAIAARRSGAKAELKAletwykRDLASLG 764
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2170 VDAATAYE---NILNAIRAAEDAA---SKATSASKSAFQTVIKEDlPKRAKTLsSDSEELLNEAKMTQKRLQQ-VSPALN 2242
Cdd:pfam12128 765 VDPDVIAKlkrEIRTLERKIERIAvrrQEVLRYFDWYQETWLQRR-PRLATQL-SNIERAISELQQQLARLIAdTKLRRA 842
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2243 SLQQTLKTVSVQKDLLDANLTVARDDLHGIQRGDIDsvvigakSMVREANGITSEVLDGLNpiqtDLGRIKDsYESarrE 2322
Cdd:pfam12128 843 KLEMERKASEKQQVRLSENLRGLRCEMSKLATLKED-------ANSEQAQGSIGERLAQLE----DLKLKRD-YLS---E 907
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2323 DFSKALVDANNSVKKLTRKLPDLFikIESINQQLLPLGNISDNVDRIRELIQQARDAANKVAIPMRFNGKSGVEVrLPND 2402
Cdd:pfam12128 908 SVKKYVEHFKNVIADHSGSGLAET--WESLREEDHYQNDKGIRLLDYRKLVPYLEQWFDVRVPQSIMVLREQVSI-LGVD 984
|
650
....*....|....*.
gi 226423935 2403 LEDLkgYTSLSLFLQR 2418
Cdd:pfam12128 985 LTEF--YDVLADFDRR 998
|
|
| TNFRSF16 |
cd13416 |
Tumor necrosis factor receptor superfamily member 16 (TNFRSF16), also known as p75 ... |
1641-1799 |
1.27e-03 |
|
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: 42.29 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1641 SGPRAHLVEMC-ACPPDY--------TGDSCQGCRPGY-YWDNKSLpVGRCVPCNcnghsnRCQDGSGICINCQ--HNTa 1708
Cdd:cd13416 5 SGQYTSSGECCeQCPPGEgvarpcgdNQTVCEPCLDGVtFSDVVSH-TEPCQPCT------RCPGLMSMRAPCTatHDT- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1709 geHCErCQAGHYGNAIHGSCRVCpcphtnsfaTGCAVDGGAVRcACKPGyTGTQCERCAPGYFGNPQKFGGSCQPCN-CN 1787
Cdd:cd13416 77 --VCE-CAYGYYLDEDSGTCEPC---------TVCPPGQGVVQ-SCGPN-QDTVCEACPEGTYSDEDSSTDPCLPCTvCE 142
|
170
....*....|...
gi 226423935 1788 SNG-QLGPCDPLT 1799
Cdd:cd13416 143 DGEvELRECTPVS 155
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1855-2128 |
1.37e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1855 EQIRHMETQAKDLRNQLLGFRSATS-----------SHGSKMDDLEKELSHLNREFETLQEKaqvnsrkaQTLYNNIDQT 1923
Cdd:PRK01156 483 EKIREIEIEVKDIDEKIVDLKKRKEyleseeinksiNEYNKIESARADLEDIKIKINELKDK--------HDKYEEIKNR 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1924 IQSAKELDMKIKNIvqnvhillkqmarpggegtdlpvgDWSRelAEAQRMMRDL-----RSRDFKKHLQEAEAEkmeaql 1998
Cdd:PRK01156 555 YKSLKLEDLDSKRT------------------------SWLN--ALAVISLIDIetnrsRSNEIKKQLNDLESR------ 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1999 lLHRIRTWLESHQVENNGLLKNIRDSLNDYEDK---LQDLRSILqeaaaqakqatginHENEGVLGAIQRQMKEMDSLKN 2075
Cdd:PRK01156 603 -LQEIEIGFPDDKSYIDKSIREIENEANNLNNKyneIQENKILI--------------EKLRGKIDNYKKQIAEIDSIIP 667
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2076 DftkyLATADSSLLQTNNLLQQMDK-------SQKEYESLAAALNGARQELSDRVRELSR 2128
Cdd:PRK01156 668 D----LKEITSRINDIEDNLKKSRKalddakaNRARLESTIEILRTRINELSDRINDINE 723
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
353-420 |
1.58e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.87 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 226423935 353 CNCHGHAVDcyydpdvehqqaslnSKGVYAGGGVCInCQHNTAGVNCEKCAKGYFrphGVPVDALHGC 420
Cdd:pfam00053 1 CDCNPHGSL---------------SDTCDPETGQCL-CKPGVTGRHCDRCKPGYY---GLPSDPPQGC 49
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1966-2323 |
1.59e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1966 ELAEAQRMMRDLRSRdfkkhLQEAEAEKMEAQLLLHRIRTWLEshQVENNglLKNIRDSLNDYEDKLQDLRSILQEaaaq 2045
Cdd:COG4372 39 ELDKLQEELEQLREE-----LEQAREELEQLEEELEQARSELE--QLEEE--LEELNEQLQAAQAELAQAQEELES---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2046 akqatgINHENEGVLGAIQRQMKEMDSLKNdftkylatadssllQTNNLLQQMDKSQKEYESLAAALNGARQELSDRVRE 2125
Cdd:COG4372 106 ------LQEEAEELQEELEELQKERQDLEQ--------------QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2126 LSRSGgkapLVVEAEKHAQSLQELAKQLEEIKRNTSGDELVRCAVDAATAYENILNAIRAAEDAASKATSASKSAFQTVI 2205
Cdd:COG4372 166 LAALE----QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2206 KEDLPKRAKTLSSDS----EELLNEAKMTQKRLQQVSPALNSLQQTLKTVSVQKDLLDANLTVARDDLHGIQRGD--IDS 2279
Cdd:COG4372 242 LELEEDKEELLEEVIlkeiEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDAllAAL 321
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 226423935 2280 VVIGAKSMVREANGITSEVLDGLNPIQTDLGRIKDSYESARRED 2323
Cdd:COG4372 322 LELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEA 365
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2029-2271 |
1.68e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.28 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2029 EDKLQDLRSILQEAAaqakqatGINH----------------EN----EGVLGAIQRQMK-------------------- 2068
Cdd:TIGR02168 151 EAKPEERRAIFEEAA-------GISKykerrketerklertrENldrlEDILNELERQLKslerqaekaerykelkaelr 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2069 --EMDSLKNDFTKYLATADSSLLQTNNLLQQMDKSQ---KEYESLAAALNGARQELSDRVREL-----SRSGGKAPLVVE 2138
Cdd:TIGR02168 224 elELALLVLRLEELREELEELQEELKEAEEELEELTaelQELEEKLEELRLEVSELEEEIEELqkelyALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2139 AEKHAQSLQELAKQLEEI---------KRNTSGDELVRCAVDAATAyENILNAIRAAEDAASKATSASKSAFqtvikEDL 2209
Cdd:TIGR02168 304 KQILRERLANLERQLEELeaqleelesKLDELAEELAELEEKLEEL-KEELESLEAELEELEAELEELESRL-----EEL 377
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226423935 2210 PKRAKTLSSDSEELLNEAKMTQKRLQQVSPALNSLQQTL-KTVSVQKDLLDANLTVARDDLHG 2271
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRReRLQQEIEELLKKLEEAELKELQA 440
|
|
| Tar |
COG0840 |
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms]; |
1854-2384 |
2.16e-03 |
|
Methyl-accepting chemotaxis protein (MCP) [Signal transduction mechanisms];
Pssm-ID: 440602 [Multi-domain] Cd Length: 533 Bit Score: 43.86 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1854 LEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQVNSRKAQTLYNNIDQTIQSAKELDMK 1933
Cdd:COG0840 1 LLILLLLLALLLALLLLALSLLALLAAALLILLALLLAALTALALLLLLSLLALLLLLLLLALALLLVLLALLLLLALVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1934 IKNIVQNVHILLKQMARPGGEGTDLPVGDWSRELAEAQRMMRDLRSRDFKKHLQEAEAEKMEAQLLLHRIRTWLESHQVE 2013
Cdd:COG0840 81 LLALLLALLLLLLALLALALAALALLAALAALLALLELLLAALLAALAIALLALAALLALAALALALLALALLAAAAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2014 NNGLLKNIRDSLNDYEDKLQDLRSILQEAAAQAKQATGINHENEGVLGAIQRQMKEMDSL-KNDFTKYLATadssllqtn 2092
Cdd:COG0840 161 AALAALLEAAALALAAAALALALLAAALLALVALAIILALLLSRSITRPLRELLEVLERIaEGDLTVRIDV--------- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2093 nllqqmdKSQKEYESLAAALNGARQELSDRVRELSRSGGKapLVVEAEKHAQSLQELAKQLEEIKRNTSgdelvrcavDA 2172
Cdd:COG0840 232 -------DSKDEIGQLADAFNRMIENLRELVGQVRESAEQ--VASASEELAASAEELAAGAEEQAASLE---------ET 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2173 ATAYENILNAIRAAEDAASKATSASKSAFQTvikedlpkrAKTLSSDSEELLNEAKMTQKRLQQVSPALNSL----QQTL 2248
Cdd:COG0840 294 AAAMEELSATVQEVAENAQQAAELAEEASEL---------AEEGGEVVEEAVEGIEEIRESVEETAETIEELgessQEIG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2249 KTVSVQKD------LLDANLTV--ARDDLHGiqRG--------------------DIDSVVIGAKSMVREANGITSEVLD 2300
Cdd:COG0840 365 EIVDVIDDiaeqtnLLALNAAIeaARAGEAG--RGfavvadevrklaersaeatkEIEELIEEIQSETEEAVEAMEEGSE 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2301 glnpiqtdlgRIKDSYESArrEDFSKALVDANNSVKKLTrklpDLFIKI-ESINQQLLPLGNISDNVDRIRELIQQARDA 2379
Cdd:COG0840 443 ----------EVEEGVELV--EEAGEALEEIVEAVEEVS----DLIQEIaAASEEQSAGTEEVNQAIEQIAAAAQENAAS 506
|
....*
gi 226423935 2380 ANKVA 2384
Cdd:COG0840 507 VEEVA 511
|
|
| Laminin_EGF |
pfam00053 |
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six. |
296-344 |
2.67e-03 |
|
Laminin EGF domain; This family is like pfam00008 but has 8 conserved cysteines instead of six.
Pssm-ID: 395007 Cd Length: 49 Bit Score: 38.10 E-value: 2.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 226423935 296 CVCNGHAEACSADNPEkQFRCECQHHTCGDTCNRCCAGYNQRRWQPAGQ 344
Cdd:pfam00053 1 CDCNPHGSLSDTCDPE-TGQCLCKPGVTGRHCDRCKPGYYGLPSDPPQG 48
|
|
| EGF_Lam |
cd00055 |
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous ... |
1308-1349 |
2.93e-03 |
|
Laminin-type epidermal growth factor-like domain; laminins are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation; the laminin-type epidermal growth factor-like module occurs in tandem arrays; the domain contains 4 disulfide bonds (loops a-d) the first three resemble epidermal growth factor (EGF); the number of copies of this domain in the different forms of laminins is highly variable ranging from 3 up to 22 copies
Pssm-ID: 238012 Cd Length: 50 Bit Score: 38.10 E-value: 2.93e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 226423935 1308 PCNC-----GRRLCEEVTGKCLCPPHTVRPQCEVCEMNSFNFHPVAG 1349
Cdd:cd00055 1 PCDCnghgsLSGQCDPGTGQCECKPNTTGRRCDRCAPGYYGLPSQGG 47
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1854-2156 |
4.04e-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: 43.09 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1854 LEQIRHMETQAKDLRNQLLGFRSATSSHGSKMDDLEKELSHLNREFETLQEKAQVNSRKAQTLYNNIDQTIQSAKELDMK 1933
Cdd:TIGR04523 432 KETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1934 IKNIVQNVHILLKQmarpggegtdlpVGDWSRELAEAQRMMRDLRSR----DFKKHLQEAEAEKMEAQlllHRIRtwlES 2009
Cdd:TIGR04523 512 VKDLTKKISSLKEK------------IEKLESEKKEKESKISDLEDElnkdDFELKKENLEKEIDEKN---KEIE---EL 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2010 HQvENNGLLKN---IRDSLNDYEDKLQDLRSILQEAAAQAKQATG----INHENEgvlgAIQRQMKEMDSLKNDFTKYLA 2082
Cdd:TIGR04523 574 KQ-TQKSLKKKqeeKQELIDQKEKEKKDLIKEIEEKEKKISSLEKelekAKKENE----KLSSIIKNIKSKKNKLKQEVK 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2083 TADSSLLQTNNLLQQMDKSQKEYESLaaaLNGARQELSDRVRELSRSGGKA----------PLVVEAEKHAQS----LQE 2148
Cdd:TIGR04523 649 QIKETIKEIRNKWPEIIKKIKESKTK---IDDIIELMKDWLKELSLHYKKYitrmirikdlPKLEEKYKEIEKelkkLDE 725
|
....*...
gi 226423935 2149 LAKQLEEI 2156
Cdd:TIGR04523 726 FSKELENI 733
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1876-2214 |
4.25e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1876 SATSSHGSKMDDLEKELSHLNREFETLQEK-AQVNSrKAQTLYNNIDQTIQSAKELdmkiknivqnvhillkqmarpgge 1954
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKrDELNE-ELKELAEKRDELNAQVKEL------------------------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1955 gtdlpvgdwsRELAEAQRMMRDLRSRDFKKHLQEAEAEKMEAQLLLHRIRTWLESHQVEN--NGLLKNIRDSLNDYEDKL 2032
Cdd:COG1340 56 ----------REEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNkaGGSIDKLRKEIERLEWRQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2033 QdlRSILqeaaaqakqatGINHENEgvlgaIQRQMKEMDSLKNDftkylatadssllqtnnlLQQMDKSQKEYESLAAAL 2112
Cdd:COG1340 126 Q--TEVL-----------SPEEEKE-----LVEKIKELEKELEK------------------AKKALEKNEKLKELRAEL 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2113 NGARQELSDRVRELSRsggkapLVVEAEKHAQSLQELAKQLEEIKRntSGDELVRCAVDAATAYENI----------LNA 2182
Cdd:COG1340 170 KELRKEAEEIHKKIKE------LAEEAQELHEEMIELYKEADELRK--EADELHKEIVEAQEKADELheeiielqkeLRE 241
|
330 340 350
....*....|....*....|....*....|..
gi 226423935 2183 IRAAEDAASKATSASKSafqTVIKEDLPKRAK 2214
Cdd:COG1340 242 LRKELKKLRKKQRALKR---EKEKEELEEKAE 270
|
|
| EGF_Lam |
smart00180 |
Laminin-type epidermal growth factor-like domai; |
384-411 |
4.43e-03 |
|
Laminin-type epidermal growth factor-like domai;
Pssm-ID: 214543 Cd Length: 46 Bit Score: 37.68 E-value: 4.43e-03
10 20
....*....|....*....|....*...
gi 226423935 384 GGVCInCQHNTAGVNCEKCAKGYFRPHG 411
Cdd:smart00180 17 TGQCE-CKPNVTGRRCDRCAPGYYGDGP 43
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1968-2234 |
4.47e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 42.89 E-value: 4.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1968 AEAQRMMRDLRSRdfkkHLQEAEAEKMEAQLLLHRIRTWLEShqvenngLLKNIRDSLNDYEDKLQDLRSILQEaaaqak 2047
Cdd:NF041483 185 AEAERLAEEARQR----LGSEAESARAEAEAILRRARKDAER-------LLNAASTQAQEATDHAEQLRSSTAA------ 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2048 qatginhENEgvlgAIQRQMKEmdsLKNDFTKYLATADSSLLQTNnllQQMDKSQKEYESLAA-ALNGARQELSDRVR-- 2124
Cdd:NF041483 248 -------ESD----QARRQAAE---LSRAAEQRMQEAEEALREAR---AEAEKVVAEAKEAAAkQLASAESANEQRTRta 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2125 --ELSRsggkapLVVEAEKHAQSLQELAKQLEEIKRnTSGDELVRCAVDAATAyenilnaiRAAEDAASKATSASKSAFQ 2202
Cdd:NF041483 311 keEIAR------LVGEATKEAEALKAEAEQALADAR-AEAEKLVAEAAEKART--------VAAEDTAAQLAKAARTAEE 375
|
250 260 270
....*....|....*....|....*....|....
gi 226423935 2203 TVIK--EDLPKRAKTLSSDSEELLNEAKMTQKRL 2234
Cdd:NF041483 376 VLTKasEDAKATTRAAAEEAERIRREAEAEADRL 409
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2063-2246 |
6.45e-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: 41.72 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2063 IQRQMKEM----DSLKNDFT-----KYLATADSSLLQTNNllqQMDKSQKEY----ESLAAALNGARQELSDRVRELSRS 2129
Cdd:pfam15905 127 LEKQLLELtrvnELLKAKFSedgtqKKMSSLSMELMKLRN---KLEAKMKEVmakqEGMEGKLQVTQKNLEHSKGKVAQL 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2130 GGKapLVVEAEKHAQSLQELAKQLEEIKR-NTSGDELVRCAVDAATAYENILNAIRAAEDAASKaTSASKSAFQTVIKeD 2208
Cdd:pfam15905 204 EEK--LVSTEKEKIEEKSETEKLLEYITElSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQS-LEEKEQELSKQIK-D 279
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 226423935 2209 LPKRAKTLSSDSEELLNEAK-----------MTQKRLQQVSPALNSLQQ 2246
Cdd:pfam15905 280 LNEKCKLLESEKEELLREYEekeqtlnaeleELKEKLTLEEQEHQKLQQ 328
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1906-2322 |
7.15e-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: 42.36 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1906 AQVNSRKAQTLyNNIDQTIQSAKELDMKIKnivqnvhILLKQMARPGGEgtdlpvgdwsRELAEAQRMMRDlRSRDFKKH 1985
Cdd:TIGR02169 166 AEFDRKKEKAL-EELEEVEENIERLDLIID-------EKRQQLERLRRE----------REKAERYQALLK-EKREYEGY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 1986 LQEAEAEKMEAQLllHRIRTWLESHQVENNGLLKNIRDSLNDYEDKLQDLRSIlqeaaaqakqATGINHENEGVLGAIQR 2065
Cdd:TIGR02169 227 ELLKEKEALERQK--EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL----------NKKIKDLGEEEQLRVKE 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2066 QMKEmdslkndFTKYLATADSSLLQTNNLLQQMDKSQKEYESLaaalngaRQELSDRVRELSRSggkaplvveaekhaqs 2145
Cdd:TIGR02169 295 KIGE-------LEAEIASLERSIAEKERELEDAEERLAKLEAE-------IDKLLAEIEELERE---------------- 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2146 LQELAKQLEEIKrntsgdelvrcavdaatayenilnairaAEDAASKATsasksafqtviKEDLPKRAKTLSSDSEELLN 2225
Cdd:TIGR02169 345 IEEERKRRDKLT----------------------------EEYAELKEE-----------LEDLRAELEEVDKEFAETRD 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226423935 2226 EAKMTQKRLQQVSPALNSLQQTLKTVSVQKDLLDANLTVARDDLHGIQRG--DIDSVVIGAKSMVREANG---ITSEVLD 2300
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKinELEEEKEDKALEIKKQEWkleQLAADLS 465
|
410 420
....*....|....*....|....*.
gi 226423935 2301 G----LNPIQTDLGRIKDSYESARRE 2322
Cdd:TIGR02169 466 KyeqeLYDLKEEYDRVEKELSKLQRE 491
|
|
| |
