|
Name |
Accession |
Description |
Interval |
E-value |
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
8-700 |
0e+00 |
|
Hamartin protein; This family includes the hamartin protein which is thought to function as a tumour suppressor. The hamartin protein interacts with the tuberin protein pfam03542. Tuberous sclerosis complex (TSC) is an autosomal dominant disorder and is characterized by the presence of hamartomas in many organs, such as brain, skin, heart, lung, and kidney. It is caused by mutation either TSC1 or TSC2 tumour suppressor gene. TSC1 encodes a protein, hamartin, containing two coiled-coil regions, which have been shown to mediate binding to tuberin. The TSC2 gene codes for tuberin pfam03542. These two proteins function within the same pathway(s) regulating cell cycle, cell growth, adhesion, and vesicular trafficking.
Pssm-ID: 461287 [Multi-domain] Cd Length: 730 Bit Score: 817.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 8 VFDLIPLLGSTDLHELEQVKTLLQETLSADKGTMLLNSLVDYFLQTNSSQAVDILSSVREPHDKYLLDKMNECMGKQSCR 87
Cdd:pfam04388 1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDKHLFDKLNECLKKAATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 88 LSTITLLGHVVRKQPPWIHKIARFPLLVSLLKCLKTDSDVVVLITGVLVLITLMPMIPQTNKQLLCDYFDIFGRLAAWNQ 167
Cdd:pfam04388 81 LQALTLLGHVVRRQPTWLHKIANHPLLKSLLKCLKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 168 RHPGHAQGVFAVHLHASVYSLFHRLYGMYPCNFVSYLRAHYSMKENVDTFEEVVKPMLEHVRIHPELITGTKDYEVDPIR 247
Cdd:pfam04388 161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 248 WKRFEPHDIVIECAKISLDSKEASSEEGYSSLAdhiqrravhhsQSCSELSFHEISSVTPIGAICQSLSKSqpyLTVTQD 327
Cdd:pfam04388 241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSSA-----------ADPTASPYTDQQSSYGSSTSTPSSTPR---LQLSSS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 328 SGSSAQTLNNQSDEVKSSGMkeELWSPSSICGMSTPPSSRGMSPTTVSDISLSASHLSGRIPSTPGD-GKWTLSPT---T 403
Cdd:pfam04388 307 SGTSPPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPTTPSELSPSSSHLSSRGSSPPEAaGEATPETTpakD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 404 PSGSSPLPSLSEEIGQAAQNTSS------------TQAKTCKEVKKVTSRSINNSSENGGDaKTPVSLAQLSDIVKRT-- 469
Cdd:pfam04388 385 SPYLKQPPPLSDSHVHRALPASSqpsspprkdgrsQSSFPPLSKQAPTNPNSRGLLEPPGD-KSSVTLSELPDFIKDLal 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 470 ------EGEREDDTINEEILSLTHGKLDF-GSRPGLESSFSGSLDTL--------------------------------- 509
Cdd:pfam04388 464 ssedsvEGAEEEAAISQELSEITTEKNETdCSRGGLDMPFSRTMESLagsqrsrnriasycsstsqsdshgpattpeskp 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 510 ----------------LSSHPNHEQNLVSTPDrveCSAKAGEQQLPRSLWPFTPIENGKHSKCSLSDLTKESMPYEPLFD 573
Cdd:pfam04388 544 salaedglrrtkscsfKQSFTPIEQPIESSDD---CPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLPYEHLFD 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 574 LALPKVASLFLERKTAEAFRRVEGERdhqdemEGEDLSVTSPLEVLDRVIQQGHDTHGKVLKRTfSSPSQSSDphlkgkq 653
Cdd:pfam04388 621 LALPKTASLFVGRKTAELLKKAKGNS------EEDCVSSTSPLEVLDRYIQQGIDAHSKELKRL-PLPSKSAD------- 686
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 528479204 654 hSNKGKGLVPavSDELDMLRSQLLLLHNQLLYERHKREQHALRNRRL 700
Cdd:pfam04388 687 -WTHFGGSAP--SDELTTLRDQLLLLHNQLLYERYKREQHAERNRRL 730
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
714-943 |
1.20e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.27 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 714 NNSMKTQLKLQEVEIQA------VKVSLKEEQRRSVHIQEDREAVVNQLQIQIQQLQKERNDYYSKMQVLKSELQENQTK 787
Cdd:pfam05483 190 NNIEKMILAFEELRVQAenarleMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDK 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 788 AGKME--AELQKANNKVCN--MGHMLSQLS-IKLNNSENM------EQQMAFLNKQLLLLGEANKLYMEEIDRLGPEAHK 856
Cdd:pfam05483 270 ANQLEekTKLQDENLKELIekKDHLTKELEdIKMSLQRSMstqkalEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSF 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 857 ELNMLQASSVREGERLRqsslQQSQRLEAAQQRITDLENQLTKKEQVIREQKKLLDN--VKRQATEQLQASENRYLAQKN 934
Cdd:pfam05483 350 VVTEFEATTCSLEELLR----TEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNkeVELEELKKILAEDEKLLDEKK 425
|
....*....
gi 528479204 935 ITQALQTEL 943
Cdd:pfam05483 426 QFEKIAEEL 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
765-951 |
1.12e-05 |
|
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: 48.99 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 765 KERNDYYSKMQVLKSELQENQTKAGKMEAELQKANNKVCNMGHMLSQLSIKLNNSE----NMEQQMAFLNKQLLLLGEAN 840
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaelaELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 841 KLYMEEIDRLGPEAHKELnMLQASSVREGERL----------RQSSL----QQSQRLEAAQQRITDLENQLTKKEQVIRE 906
Cdd:COG4942 107 AELLRALYRLGRQPPLAL-LLSPEDFLDAVRRlqylkylapaRREQAeelrADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 528479204 907 QKKLLDNVKRQATEQLQASENRYLAQKNITQALQTELLELYSKIE 951
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
685-906 |
1.76e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 685 YERHKREQHALRNRRlfGRIVNTTA-LEEQNNSMKTQLKLQEVEIQAVKVSLKEEQRRSVHIQEDREAVVNQLQIQIQQL 763
Cdd:TIGR02168 812 LTLLNEEAANLRERL--ESLERRIAaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 764 QKERNDYYSKMQVLKS----------ELQENQTKAGKMEAELQKANNKvcnmghmLSQLSIKLNNSENMEQQMAfLNKQL 833
Cdd:TIGR02168 890 ALLRSELEELSEELREleskrselrrELEELREKLAQLELRLEGLEVR-------IDNLQERLSEEYSLTLEEA-EALEN 961
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528479204 834 LLLGEANKLYME------EIDRLGPeahkeLNMLqasSVREGErlrqsslQQSQRLEAAQQRITDLENQLTKKEQVIRE 906
Cdd:TIGR02168 962 KIEDDEEEARRRlkrlenKIKELGP-----VNLA---AIEEYE-------ELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
835-963 |
4.85e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.40 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 835 LLGEANKLYMEEIDRLGPEAHKELNMLQASSVREGERLrqssLQQSQRLEAAQQRITDLENQLTKKEQVIREQKKLLDNV 914
Cdd:PRK12705 49 KLEAALLEAKELLLRERNQQRQEARREREELQREEERL----VQKEEQLDARAEKLDNLENQLEEREKALSARELELEEL 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 528479204 915 KRQATEQLQ--ASENRYLAQKNITQALQTElLELYSKIELKNLKTNAPAES 963
Cdd:PRK12705 125 EKQLDNELYrvAGLTPEQARKLLLKLLDAE-LEEEKAQRVKKIEEEADLEA 174
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Hamartin |
pfam04388 |
Hamartin protein; This family includes the hamartin protein which is thought to function as a ... |
8-700 |
0e+00 |
|
Hamartin protein; This family includes the hamartin protein which is thought to function as a tumour suppressor. The hamartin protein interacts with the tuberin protein pfam03542. Tuberous sclerosis complex (TSC) is an autosomal dominant disorder and is characterized by the presence of hamartomas in many organs, such as brain, skin, heart, lung, and kidney. It is caused by mutation either TSC1 or TSC2 tumour suppressor gene. TSC1 encodes a protein, hamartin, containing two coiled-coil regions, which have been shown to mediate binding to tuberin. The TSC2 gene codes for tuberin pfam03542. These two proteins function within the same pathway(s) regulating cell cycle, cell growth, adhesion, and vesicular trafficking.
Pssm-ID: 461287 [Multi-domain] Cd Length: 730 Bit Score: 817.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 8 VFDLIPLLGSTDLHELEQVKTLLQETLSADKGTMLLNSLVDYFLQTNSSQAVDILSSVREPHDKYLLDKMNECMGKQSCR 87
Cdd:pfam04388 1 VGELFNLLESNDLGELEEIKKVFHEHLNSTKGSWLVNGLVDYYLSTGSQRALEILVSVREPHDKHLFDKLNECLKKAATR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 88 LSTITLLGHVVRKQPPWIHKIARFPLLVSLLKCLKTDSDVVVLITGVLVLITLMPMIPQTNKQLLCDYFDIFGRLAAWNQ 167
Cdd:pfam04388 81 LQALTLLGHVVRRQPTWLHKIANHPLLKSLLKCLKTETDIVVLMTGLLVLITLLPMIPQLVKQYLPDIFEIFGRLASWNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 168 RHPGHAQGVFAVHLHASVYSLFHRLYGMYPCNFVSYLRAHYSMKENVDTFEEVVKPMLEHVRIHPELITGTKDYEVDPIR 247
Cdd:pfam04388 161 KNPGHVPEVYLVHLQASLYSLFHRLYGMYPCNFVSYLRSHYSMKENLETFEETIKPMLEHVRIHPELVTGTKDHELDPTR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 248 WKRFEPHDIVIECAKISLDSKEASSEEGYSSLAdhiqrravhhsQSCSELSFHEISSVTPIGAICQSLSKSqpyLTVTQD 327
Cdd:pfam04388 241 WKKMEPHDVVIECAKFSLDPKEASCEEGYSSSA-----------ADPTASPYTDQQSSYGSSTSTPSSTPR---LQLSSS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 328 SGSSAQTLNNQSDEVKSSGMkeELWSPSSICGMSTPPSSRGMSPTTVSDISLSASHLSGRIPSTPGD-GKWTLSPT---T 403
Cdd:pfam04388 307 SGTSPPYLSPPSIRLKTDSF--PLWSPSSVCGMTTPPTSPGMVPTTPSELSPSSSHLSSRGSSPPEAaGEATPETTpakD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 404 PSGSSPLPSLSEEIGQAAQNTSS------------TQAKTCKEVKKVTSRSINNSSENGGDaKTPVSLAQLSDIVKRT-- 469
Cdd:pfam04388 385 SPYLKQPPPLSDSHVHRALPASSqpsspprkdgrsQSSFPPLSKQAPTNPNSRGLLEPPGD-KSSVTLSELPDFIKDLal 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 470 ------EGEREDDTINEEILSLTHGKLDF-GSRPGLESSFSGSLDTL--------------------------------- 509
Cdd:pfam04388 464 ssedsvEGAEEEAAISQELSEITTEKNETdCSRGGLDMPFSRTMESLagsqrsrnriasycsstsqsdshgpattpeskp 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 510 ----------------LSSHPNHEQNLVSTPDrveCSAKAGEQQLPRSLWPFTPIENGKHSKCSLSDLTKESMPYEPLFD 573
Cdd:pfam04388 544 salaedglrrtkscsfKQSFTPIEQPIESSDD---CPTDEQDGENGLETSILTPSPCKIPSRQKVSTQSGQPLPYEHLFD 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 574 LALPKVASLFLERKTAEAFRRVEGERdhqdemEGEDLSVTSPLEVLDRVIQQGHDTHGKVLKRTfSSPSQSSDphlkgkq 653
Cdd:pfam04388 621 LALPKTASLFVGRKTAELLKKAKGNS------EEDCVSSTSPLEVLDRYIQQGIDAHSKELKRL-PLPSKSAD------- 686
|
730 740 750 760
....*....|....*....|....*....|....*....|....*..
gi 528479204 654 hSNKGKGLVPavSDELDMLRSQLLLLHNQLLYERHKREQHALRNRRL 700
Cdd:pfam04388 687 -WTHFGGSAP--SDELTTLRDQLLLLHNQLLYERYKREQHAERNRRL 730
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
714-943 |
1.20e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 56.27 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 714 NNSMKTQLKLQEVEIQA------VKVSLKEEQRRSVHIQEDREAVVNQLQIQIQQLQKERNDYYSKMQVLKSELQENQTK 787
Cdd:pfam05483 190 NNIEKMILAFEELRVQAenarleMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDK 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 788 AGKME--AELQKANNKVCN--MGHMLSQLS-IKLNNSENM------EQQMAFLNKQLLLLGEANKLYMEEIDRLGPEAHK 856
Cdd:pfam05483 270 ANQLEekTKLQDENLKELIekKDHLTKELEdIKMSLQRSMstqkalEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSF 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 857 ELNMLQASSVREGERLRqsslQQSQRLEAAQQRITDLENQLTKKEQVIREQKKLLDN--VKRQATEQLQASENRYLAQKN 934
Cdd:pfam05483 350 VVTEFEATTCSLEELLR----TEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNkeVELEELKKILAEDEKLLDEKK 425
|
....*....
gi 528479204 935 ITQALQTEL 943
Cdd:pfam05483 426 QFEKIAEEL 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
765-951 |
1.12e-05 |
|
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: 48.99 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 765 KERNDYYSKMQVLKSELQENQTKAGKMEAELQKANNKVCNMGHMLSQLSIKLNNSE----NMEQQMAFLNKQLLLLGEAN 840
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEaelaELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 841 KLYMEEIDRLGPEAHKELnMLQASSVREGERL----------RQSSL----QQSQRLEAAQQRITDLENQLTKKEQVIRE 906
Cdd:COG4942 107 AELLRALYRLGRQPPLAL-LLSPEDFLDAVRRlqylkylapaRREQAeelrADLAELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 528479204 907 QKKLLDNVKRQATEQLQASENRYLAQKNITQALQTELLELYSKIE 951
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
685-906 |
1.76e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 685 YERHKREQHALRNRRlfGRIVNTTA-LEEQNNSMKTQLKLQEVEIQAVKVSLKEEQRRSVHIQEDREAVVNQLQIQIQQL 763
Cdd:TIGR02168 812 LTLLNEEAANLRERL--ESLERRIAaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 764 QKERNDYYSKMQVLKS----------ELQENQTKAGKMEAELQKANNKvcnmghmLSQLSIKLNNSENMEQQMAfLNKQL 833
Cdd:TIGR02168 890 ALLRSELEELSEELREleskrselrrELEELREKLAQLELRLEGLEVR-------IDNLQERLSEEYSLTLEEA-EALEN 961
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528479204 834 LLLGEANKLYME------EIDRLGPeahkeLNMLqasSVREGErlrqsslQQSQRLEAAQQRITDLENQLTKKEQVIRE 906
Cdd:TIGR02168 962 KIEDDEEEARRRlkrlenKIKELGP-----VNLA---AIEEYE-------ELKERYDFLTAQKEDLTEAKETLEEAIEE 1025
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
695-940 |
1.82e-05 |
|
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: 48.22 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 695 LRNRRLFGRIVNTTALEEQNNSMKTQLKLQEV--EIQAVKVSLKEEQRRSVHIQEDREAV---VNQLQIQIQQLQKERND 769
Cdd:COG4942 1 MRKLLLLALLLALAAAAQADAAAEAEAELEQLqqEIAELEKELAALKKEEKALLKQLAALerrIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 770 YYSKMQVLKSELQENQTKAGKMEAELQKANNKVCNMGHMlSQLSIKLnNSENMEQqmafLNKQLLLLGEANKLYMEEIDR 849
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQ-PPLALLL-SPEDFLD----AVRRLQYLKYLAPARREQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 850 LgpeahkelnmlqASSVREGERLRQSSLQQSQRLEAAQQRitdLENQLTKKEQVIREQKKLLDNVKRQATEQLQASENRY 929
Cdd:COG4942 155 L------------RADLAELAALRAELEAERAELEALLAE---LEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
250
....*....|.
gi 528479204 930 LAQKNITQALQ 940
Cdd:COG4942 220 QEAEELEALIA 230
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
685-959 |
4.20e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.74 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 685 YERHKREQHALRN---------RRLFGRIVNTTALEEQNNSMKTQLKLQEVEIQAVKVSLKEEQ----RRSVHIQEDREA 751
Cdd:TIGR02168 234 LEELREELEELQEelkeaeeelEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsrleQQKQILRERLAN 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 752 VVNQLQIQIQQ---LQKERNDYYSKMQVLKSELQENQTKAGKMEAELQKANNKVCNMghmlsqlsikLNNSENMEQQMAF 828
Cdd:TIGR02168 314 LERQLEELEAQleeLESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL----------ESRLEELEEQLET 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 829 LNKQLLLLGEANKLYMEEIDRLGpeahKELNMLQASSVREGERLR-QSSLQQSQRLEAAQQRITDLENQLTKKEQ---VI 904
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNEIERLE----ARLERLEDRRERLQQEIEeLLKKLEEAELKELQAELEELEEELEELQEeleRL 459
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 528479204 905 REQKKLLDNVKRQATEQLQA---SENRYLAQKNITQALQTELLELYSkiELKNLKTNA 959
Cdd:TIGR02168 460 EEALEELREELEEAEQALDAaerELAQLQARLDSLERLQENLEGFSE--GVKALLKNQ 515
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
689-953 |
4.63e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.62 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 689 KREQHALRNRRLFGRIVNTTALEEQNNSMKTQLKLQEVEIQAVKVSLKEEQRRSVHIQEDREAVV---NQLQIQIQQLQK 765
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEerrRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 766 ERNDYYSKMQVLKSELQENQTKAGKMEAELQKAnnkvcnmghmLSQLSIKLNNSENMEQQMAFLNKQLLllgEANKLYME 845
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEA----------EAELAEAEEALLEAEAELAEAEEELE---ELAEELLE 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 846 EIDRLGPEAHKELNMLQASSVREGERLRQssLQQSQRLEAAQQRITDLENQLTKKEQVIREQKKLLDNVKRQATEQLQAS 925
Cdd:COG1196 391 ALRAAAELAAQLEELEEAEEALLERLERL--EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
250 260
....*....|....*....|....*...
gi 528479204 926 ENRYLAQKNITQALQTELLELYSKIELK 953
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLL 496
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
835-963 |
4.85e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 47.40 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 835 LLGEANKLYMEEIDRLGPEAHKELNMLQASSVREGERLrqssLQQSQRLEAAQQRITDLENQLTKKEQVIREQKKLLDNV 914
Cdd:PRK12705 49 KLEAALLEAKELLLRERNQQRQEARREREELQREEERL----VQKEEQLDARAEKLDNLENQLEEREKALSARELELEEL 124
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 528479204 915 KRQATEQLQ--ASENRYLAQKNITQALQTElLELYSKIELKNLKTNAPAES 963
Cdd:PRK12705 125 EKQLDNELYrvAGLTPEQARKLLLKLLDAE-LEEEKAQRVKKIEEEADLEA 174
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
746-989 |
2.93e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.44 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 746 QEDREAVVNQLQIQIQQLQKERNDYYSKMQVLKSELQENQTKAGKMEAELQKANNKvcnmghmLSQLSIKLN-NSENMEQ 824
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE-------IAEAEAEIEeRREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 825 QMAFLNKQLLLLGEANKLYMEE-----IDRlgpeahkeLNMLQASSVREGERLRQSSlQQSQRLEAAQQRITDLENQLTK 899
Cdd:COG3883 91 RARALYRSGGSVSYLDVLLGSEsfsdfLDR--------LSALSKIADADADLLEELK-ADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 900 KEQVIREQKKLLDNVKRQATE---QLQASENRYLAQKnitQALQTELLELYSKIELKNLKTNAPAESISDPSSPTNQRPN 976
Cdd:COG3883 162 LKAELEAAKAELEAQQAEQEAllaQLSAEEAAAEAQL---AELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
250
....*....|...
gi 528479204 977 GNSAGPSAPSLPA 989
Cdd:COG3883 239 AAAAAASAAGAGA 251
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
820-951 |
3.07e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 820 ENMEQQMAFLNKQLLLlgEANklymEEIDRLGPEAHKELNMLQASSVREGERLRQ--SSL-QQSQRLEAAQQRITDLENQ 896
Cdd:PRK12704 45 EEAKKEAEAIKKEALL--EAK----EEIHKLRNEFEKELRERRNELQKLEKRLLQkeENLdRKLELLEKREEELEKKEKE 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 528479204 897 LTKKEQVIREQKKLLDNVKRQATEQLQ------ASENRYLAQKNITQALQTELLELYSKIE 951
Cdd:PRK12704 119 LEQKQQELEKKEEELEELIEEQLQELErisgltAEEAKEILLEKVEEEARHEAAVLIKEIE 179
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
696-958 |
4.56e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 696 RNRRLFGRIVNttaLEEQNNSMKTQLKLQEVEIQAVK----------VSLKEEQRRSVHIQEDREAVVNQLQIQIQQLQK 765
Cdd:TIGR04523 212 KNKSLESQISE---LKKQNNQLKDNIEKKQQEINEKTteisntqtqlNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEK 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 766 ERNDYYSKMQVL------------KSELQENQTKAGKMEAELQKANNKVCNMGHMLSQLSIKLNNSEN----MEQQMAFL 829
Cdd:TIGR04523 289 QLNQLKSEISDLnnqkeqdwnkelKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESenseKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 830 NKQLLLLGEANKLYMEEIDRLGPE------------------------AHKELNMLQassvREGERLRQSSLQQSQRLEA 885
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKNLESQindleskiqnqeklnqqkdeqikkLQQEKELLE----KEIERLKETIIKNNSEIKD 444
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 528479204 886 AQQRITDLENQLTKKEQVIREQKKLLDNVKRQATEQLQASENRylaQKNITQALQtELLELysKIELKNLKTN 958
Cdd:TIGR04523 445 LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK---QKELKSKEK-ELKKL--NEEKKELEEK 511
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
782-951 |
5.89e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 782 QENQTKAGKMEAELQKANNKvcnmghmLSQLSIKLnnsENMEQQMAFLNKQLLLLGEANKLYMEEIDRLGPEAH-----K 856
Cdd:COG4913 606 FDNRAKLAALEAELAELEEE-------LAEAEERL---EALEAELDALQERREALQRLAEYSWDEIDVASAEREiaeleA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 857 ELNMLQASSV------REGERLRQSSLQQSQRLEAAQQRITDLENQLTKKEQVIREQKKLLDNVKRQATEQLQASENRYL 930
Cdd:COG4913 676 ELERLDASSDdlaaleEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERF 755
|
170 180
....*....|....*....|.
gi 528479204 931 AQKNITQALQTELLELYSKIE 951
Cdd:COG4913 756 AAALGDAVERELRENLEERID 776
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
710-951 |
7.53e-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: 43.89 E-value: 7.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 710 LEEQNNSMKTQLKLQEVEIQAVKVSLKE-----EQRRSVHIQEDREavVNQLQIQIQQLQKERNDYYSKMQVLKSELQEN 784
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEEleeelEQLRKELEELSRQ--ISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 785 QTKAGKMEAELQKANnkvcnmghmlSQLSIKLNNSENMEQQMAFLNKQLLLLGEAnklymeeIDRLgPEAHKELNMLQAS 864
Cdd:TIGR02168 760 EAEIEELEERLEEAE----------EELAEAEAEIEELEAQIEQLKEELKALREA-------LDEL-RAELTLLNEEAAN 821
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 865 SVREGERLRQSSLQQSQRLEAAQQRITDLENQLTKKEQVIREQKKLLDnvkrQATEQLQASENRYLAQKNITQALQTELL 944
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIE----ELESELEALLNERASLEEALALLRSELE 897
|
....*..
gi 528479204 945 ELYSKIE 951
Cdd:TIGR02168 898 ELSEELR 904
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
765-981 |
1.05e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 765 KERNDYYSKMQVLKSELQENQTKAGKMEAELQKANNKvcnmghmLSQLSIKLnnsENMEQQMAFLNKQLLLLGEANKLYM 844
Cdd:COG4372 45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEE-------LEELNEQL---QAAQAELAQAQEELESLQEEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 845 EEIDRLGpeahKELNMLQASSVR---EGERLRQSSLQQSQRLEAAQQRITDLENQLTKKEQVIREQKKL-----LDNVKR 916
Cdd:COG4372 115 EELEELQ----KERQDLEQQRKQleaQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaeqaLDELLK 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528479204 917 QATEQLQASENRYLAQKNITQALQTELLELYSKIELKNLKTNAPAESISDPSSPTNQRPNGNSAG 981
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
652-962 |
2.21e-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: 42.35 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 652 KQHSNKGKGLVPAVSDELDMLRSQLLLLHNQLLYERhKREQHALRNRRLFGRIVNTTALEEQNNSMKTQLKLQEVEIQAV 731
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEA-EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 732 KVSLKEE-QRRSVHIQEDREAVVNqlqiqiqqlqkerndyyskmqvLKSELQENQTKAGKMEAELQKANNKVCNMGHMLS 810
Cdd:TIGR02168 784 IEELEAQiEQLKEELKALREALDE----------------------LRAELTLLNEEAANLRERLESLERRIAATERRLE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 811 QLSiklNNSENMEQQMAFLNKQllllgeanklyMEEIDRLGPEAHKELNMLQ--------------------ASSVREGE 870
Cdd:TIGR02168 842 DLE---EQIEELSEDIESLAAE-----------IEELEELIEELESELEALLnerasleealallrseleelSEELRELE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 871 ----RLRQSSLQQSQRLEAAQQRITDLENQLTKKEQVIREQKKLLdnvkrqateqLQASENRYLAQKNITQALQTELLEL 946
Cdd:TIGR02168 908 skrsELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLT----------LEEAEALENKIEDDEEEARRRLKRL 977
|
330
....*....|....*..
gi 528479204 947 YSKI-ELKNLKTNAPAE 962
Cdd:TIGR02168 978 ENKIkELGPVNLAAIEE 994
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
853-956 |
2.55e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 853 EAHKELNMLQAssvrEGERLRQSSLQQSQRLEAAQQRITDLENQLTKKEQVIREQKKLLDNVKR---QATEQLQASENRY 929
Cdd:COG1196 257 ELEAELAELEA----ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEErleELEEELAELEEEL 332
|
90 100
....*....|....*....|....*..
gi 528479204 930 LAQKNITQALQTELLELYSKIELKNLK 956
Cdd:COG1196 333 EELEEELEELEEELEEAEEELEEAEAE 359
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
777-954 |
3.52e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 777 LKSELQENQTKAGKMEAELQ--KANNKVCNMGHMLSQLSIKLNNSEN----MEQQMAFLNKQLLLLGEANKLYMEEIDRL 850
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESqlaeARAELAEAEARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 851 G-----PEAHKELNMLQAssvrEGERLRQSSLQQSQRLEAAQQRITDLENQLTKKEQVIREQKKLLDNVKRQATEQLQAS 925
Cdd:COG3206 260 LqspviQQLRAQLAELEA----ELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQ 335
|
170 180
....*....|....*....|....*....
gi 528479204 926 ENRYLAQKNITQALQTELLELYSKIELKN 954
Cdd:COG3206 336 LAQLEARLAELPELEAELRRLEREVEVAR 364
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
779-944 |
4.07e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 41.26 E-value: 4.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 779 SELQEnQTKAGKMEAEL--QKANNKVCNMghmlsQLSIKLNNSENMEQqmAFLNKQLLLLGEANKLYME---EIDRLGPE 853
Cdd:pfam17380 285 SERQQ-QEKFEKMEQERlrQEKEEKAREV-----ERRRKLEEAEKARQ--AEMDRQAAIYAEQERMAMErerELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 854 AHKELN--------MLQASSVREGERLRQSSLQQSQR----LEAA-QQRITDLENQLTKKEQV-----IREQKKLLDNVK 915
Cdd:pfam17380 357 ERKRELerirqeeiAMEISRMRELERLQMERQQKNERvrqeLEAArKVKILEEERQRKIQQQKvemeqIRAEQEEARQRE 436
|
170 180
....*....|....*....|....*....
gi 528479204 916 RQATEQLQASENRYLAQKNITQALQTELL 944
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQERQQQVERL 465
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
761-959 |
4.22e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 40.90 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 761 QQLQKERNDYYSKMQVLKSELQENQTKAGKMEAELQKANNKvcnmghmLSQLSIKLNnseNMEQQMAFLNKQLLLLGEAN 840
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE-------LAALEAELA---ELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 841 KLYMEEIDRLGPEAHKELNMLQAS---SVREGERLRQSSLQQSQRLEAAQQRITDLEnqltKKEQVIREQKKLLDNVKRQ 917
Cdd:COG4942 107 AELLRALYRLGRQPPLALLLSPEDfldAVRRLQYLKYLAPARREQAEELRADLAELA----ALRAELEAERAELEALLAE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 528479204 918 ATEQLQASENRYLAQKNITQALQTELLELysKIELKNLKTNA 959
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAEL--AAELAELQQEA 222
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
772-985 |
4.23e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 772 SKMQVLKSELQENQTKAGKMEAELQKANNKVCN----MGHMLSQLSIK---------LNNSENMEQqmaFLNKQLLL--L 836
Cdd:COG3883 51 EEYNELQAELEALQAEIDKLQAEIAEAEAEIEErreeLGERARALYRSggsvsyldvLLGSESFSD---FLDRLSALskI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 837 GEANKLYMEEIDrlgpEAHKELNMLQASSVREGERLRQSSLQQSQRLEAAQQRITDLE---NQLTKKEQVIREQKKLLDN 913
Cdd:COG3883 128 ADADADLLEELK----ADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEallAQLSAEEAAAEAQLAELEA 203
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528479204 914 VKRQATEQLQASENRYLAQKNITQALQTELLELYSKIELKNLKTNAPAESISDPSSPTNQRPNGNSAGPSAP 985
Cdd:COG3883 204 ELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAG 275
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
710-1027 |
6.95e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 40.26 E-value: 6.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 710 LEEQNNSMKTQLKLQEVEIQavkvSLKEEQRRSVHIQEDREAVVNQLQIQIQQLQKERNDYYSKMQVLKSELQENQTKA- 788
Cdd:pfam07888 134 LEEDIKTLTQRVLERETELE----RMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVl 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 789 ------GKMEAELQKANNKVCNMGHMLSQLSIKLNNSENMEQQMAFLNKQLLLLGEANKLYMEEIDRLGPEAHKELNMLQ 862
Cdd:pfam07888 210 qlqdtiTTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLA 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 863 ASSV--REG------ERlrqSSLQQSqrLEAAQQRITDLENQLTKKEQVIREQK----KL--------------LDNVKR 916
Cdd:pfam07888 290 DASLalREGrarwaqER---ETLQQS--AEADKDRIEKLSAELQRLEERLQEERmereKLevelgrekdcnrvqLSESRR 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 917 QATEqLQASENRYLAQKNITQALQTELLELYSKIELKNLK------TNAPAESISDPSSPTNQRPNGNsagPSAPSLPAD 990
Cdd:pfam07888 365 ELQE-LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETvadakwSEAALTSTERPDSPLSDSEDEN---PEALQPPRP 440
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 528479204 991 LMKR---EEGAHVCVNGEISAASPQTPTALINGSQEEDLS 1027
Cdd:pfam07888 441 LGHYslcEQGQPDSLLLATPPPSPRDPESTVVISQPAPLS 480
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
820-943 |
7.16e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 820 ENMEQQMAFLNKQLLLLGEANKLYmEEIDrlgpEAHKELNMLQAssvregERLRQSSLQQSQRLEAAQQRITDLENQLTK 899
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELA-ERYA----AARERLAELEY------LRAALRLWFAQRRLELLEAELEELRAELAR 306
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 528479204 900 KEQVIREQKKLLDnvkrQATEQLQASENRYLAQKNIT-QALQTEL 943
Cdd:COG4913 307 LEAELERLEARLD----ALREELDELEAQIRGNGGDRlEQLEREI 347
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
689-966 |
7.69e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 40.48 E-value: 7.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 689 KREQHALRNRRLFGRIVnTTALEEQNNSMKTQLKL---QEVEIQAVKVSLKEEQ--------------------RRSVHI 745
Cdd:pfam05483 366 RTEQQRLEKNEDQLKII-TMELQKKSSELEEMTKFknnKEVELEELKKILAEDEklldekkqfekiaeelkgkeQELIFL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 746 QEDREAVVNQLQIQIQQLQKERNDYYSKMQVLKSELQENQTK-------AGKMEAELQKANNKVCNMGHMLSQLSIKLNN 818
Cdd:pfam05483 445 LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKnieltahCDKLLLENKELTQEASDMTLELKKHQEDIIN 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 819 SENMEQQMAflnKQLLLLGEANKLYMEEIDrlgpeahkelnmlqasSVRegERLRQSSLQQSQRLEAAQQRITDLENQLT 898
Cdd:pfam05483 525 CKKQEERML---KQIENLEEKEMNLRDELE----------------SVR--EEFIQKGDEVKCKLDKSEENARSIEYEVL 583
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528479204 899 KKEQVIREQKKLLDNVKRQA------TEQLQaSENRYLAQKNITQALQTELLEL-YSKIELKNLKTNAPAESISD 966
Cdd:pfam05483 584 KKEKQMKILENKCNNLKKQIenknknIEELH-QENKALKKKGSAENKQLNAYEIkVNKLELELASAKQKFEEIID 657
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
709-959 |
7.78e-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: 40.44 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 709 ALEEQNNSMKTQLKLQEV-EIQAVKVSLKEEQRRSVHIQEDREAVVNQLQIQIQQLQKERNDYYSKMQVLKS-------E 780
Cdd:TIGR02169 776 KLEEALNDLEARLSHSRIpEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEqiksiekE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 781 LQENQTKAGKMEAELQKANNKVCNMGHMLSQLSIKLnnsENMEQQMAflnkqllllgeanklymeeidrlgpEAHKELNM 860
Cdd:TIGR02169 856 IENLNGKKEELEEELEELEAALRDLESRLGDLKKER---DELEAQLR-------------------------ELERKIEE 907
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 861 LQAssvrEGERLRQSSLQQSQRLEAAQQRITDLEN----------------QLTKKEQVIREQKKLLDNVKRQATEQLQA 924
Cdd:TIGR02169 908 LEA----QIEKKRKRLSELKAKLEALEEELSEIEDpkgedeeipeeelsleDVQAELQRVEEEIRALEPVNMLAIQEYEE 983
|
250 260 270
....*....|....*....|....*....|....*.
gi 528479204 925 SENRYLAQKNITQALQTELLELYSKIE-LKNLKTNA 959
Cdd:TIGR02169 984 VLKRLDELKEKRAKLEEERKAILERIEeYEKKKREV 1019
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
825-943 |
7.81e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 39.95 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528479204 825 QMAFLNkQLLLLGEANKLYMEeiDRLGpEAHKELNMLQAssvrEGERLRQSSLQQSQRLEAAQQRITDLENQLTKKEQVI 904
Cdd:PRK09039 61 QIAELA-DLLSLERQGNQDLQ--DSVA-NLRASLSAAEA----ERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQVS 132
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 528479204 905 RE---QKKLLDN----VKRQ--ATEQ-LQASENRYLAQKNITQALQTEL 943
Cdd:PRK09039 133 ARalaQVELLNQqiaaLRRQlaALEAaLDASEKRDRESQAKIADLGRRL 181
|
|
| |
