|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
981-1057 |
1.60e-31 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 118.46 E-value: 1.60e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973570 981 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLNDPHNVEKL 1057
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
830-903 |
2.88e-29 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 111.92 E-value: 2.88e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973570 830 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 903
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
491-563 |
2.65e-26 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 103.44 E-value: 2.65e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973570 491 LDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 563
Cdd:pfam02376 5 LDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1107-1163 |
1.26e-14 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 69.45 E-value: 1.26e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767973570 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1163
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1107-1165 |
1.20e-11 |
|
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.
Pssm-ID: 238039 [Multi-domain] Cd Length: 59 Bit Score: 61.11 E-value: 1.20e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767973570 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREM 1165
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1107-1162 |
9.32e-11 |
|
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes
Pssm-ID: 197696 [Multi-domain] Cd Length: 57 Bit Score: 58.42 E-value: 9.32e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767973570 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMR 1162
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
117-317 |
7.80e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 117 QRNEAEK----QKGLQEVQITLAA-RLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASkadevglimtnLEKANQRA 191
Cdd:COG1196 208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 192 EAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASAN 271
Cdd:COG1196 277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767973570 272 QIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLAS 317
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-308 |
2.50e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 111 LTETLLQRNEAEKQKGLQEVQI-TLAARLGEAEEKIKVLHSALKATQAELLELRrkydEEAASKADEVGLIMTNLEKANQ 189
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIeELEAQIEQLKEELKALREALDELRAELTLLN----EEAANLRERLESLERRIAATER 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 190 RAEAAQREVESLREQLASVNSSIrlaccSPQGPSGDKVNFTLCSgprLEAALASKDREILRLLKDVQHLQSSLQELEEas 269
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI-----EELEELIEELESELEA---LLNERASLEEALALLRSELEELSEELRELES-- 908
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767973570 270 anQIADLERQLTAKSEAIEKLEEKLQ-AQSDYEEIKTELS 308
Cdd:TIGR02168 909 --KRSELRRELEELREKLAQLELRLEgLEVRIDNLQERLS 946
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
76-302 |
3.46e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 51.61 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 76 NPELLSPKEQREGTSPAGPTLTEGSRLPGIPGKALLT----ETL--LQR-NEA--EKQKGLQEVQIT-LAARLGEAEEKI 145
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPaeirEKLirLQHeNKMlrLGQEGSYRERLTeLQQLLEDANRRK 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 146 KVLHSALKATQAELLELRRKYDE------EAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccsp 219
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEElqkalqEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQ------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 220 QGPSGDKVNftlcsgpRLEAALASKDREIL----RLLKDVQHLQSSLQELE----EASANQIADLERQLTAKSEAIEKLE 291
Cdd:pfam05622 394 DSNLAQKID-------ELQEALRKKDEDMKameeRYKKYVEKAKSVIKTLDpkqnPASPPEIQALKNQLLEKDKKIEHLE 466
|
250
....*....|....
gi 767973570 292 ---EKLQAQSDYEE 302
Cdd:pfam05622 467 rdfEKSKLQREQEE 480
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
120-313 |
1.39e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 120 EAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKA---TQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQR 196
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 197 EVESLREQLASVNSSIRLAccsPQGPSGDKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQELEEAsanqIADL 276
Cdd:PRK03918 627 ELDKAFEELAETEKRLEEL---RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT----LEKL 699
|
170 180 190
....*....|....*....|....*....|....*..
gi 767973570 277 ERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAM 313
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALERVEELREKVKKYKAL 736
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
157-316 |
2.85e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 157 AELLELRRKYDEEAASKADE---------VGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccspqgpSGDKv 227
Cdd:cd22656 94 AEILELIDDLADATDDEELEeakktikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL----------ETLE- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 228 nftlcsgPRLEAALASKDREILRllKDVQHLQsslQELEEASANQIADLERQLTAKSEAIEKLEEKLQA----QSDYEEI 303
Cdd:cd22656 163 -------KALKDLLTDEGGAIAR--KEIKDLQ---KELEKLNEEYAAKLKAKIDELKALIADDEAKLAAalrlIADLTAA 230
|
170
....*....|....
gi 767973570 304 KTEL-SILKAMKLA 316
Cdd:cd22656 231 DTDLdNLLALIGPA 244
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1107-1174 |
3.29e-03 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 39.73 E-value: 3.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973570 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREMLVEGTQDEP 1174
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKKRSGKVEQRPG 119
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
981-1057 |
1.60e-31 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 118.46 E-value: 1.60e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973570 981 MSPELDTYSITKRVKEVLTDNNLGQRLFGESILGLTQGSVSDLLSRPKPWHKLSLKGREpFVRMQLWLNDPHNVEKL 1057
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
830-903 |
2.88e-29 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 111.92 E-value: 2.88e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973570 830 MYREVDTLELTRQVKEKLAKNGICQRIFGEKVLGLSQGSVSDMLSRPKPWSKLTQKGREpFIRMQLWLSDQLGQ 903
Cdd:pfam02376 1 DSEELDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDE 73
|
|
| CUT |
pfam02376 |
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in ... |
491-563 |
2.65e-26 |
|
CUT domain; The CUT domain is a DNA-binding motif which can bind independently or in cooperation with the homeodomain, often found downstream of the CUT domain. Multiple copies of the CUT domain can exist in one protein.
Pssm-ID: 460543 Cd Length: 78 Bit Score: 103.44 E-value: 2.65e-26
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973570 491 LDTAEIAFQVKEQLLKHNIGQRVFGHYVLGLSQGSVSEILARPKPWRKLTVKGKEpFIKMKQFLSDEQNVLAL 563
Cdd:pfam02376 5 LDTKDIADRIKEELKRHKISQAVFAEKVLNRSQGTLSDLLRKPKPWEKLKSGGRT-FIRMYNWLSLPEDERME 76
|
|
| Homeodomain |
pfam00046 |
Homeodomain; |
1107-1163 |
1.26e-14 |
|
Homeodomain;
Pssm-ID: 459649 [Multi-domain] Cd Length: 57 Bit Score: 69.45 E-value: 1.26e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 767973570 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRR 1163
Cdd:pfam00046 1 RRKRTTFTPEQLEELEKEFQENPYPSAEEREELAAQLGLTERQVKVWFQNRRAKWKR 57
|
|
| homeodomain |
cd00086 |
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic ... |
1107-1165 |
1.20e-11 |
|
Homeodomain; DNA binding domains involved in the transcriptional regulation of key eukaryotic developmental processes; may bind to DNA as monomers or as homo- and/or heterodimers, in a sequence-specific manner.
Pssm-ID: 238039 [Multi-domain] Cd Length: 59 Bit Score: 61.11 E-value: 1.20e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 767973570 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREM 1165
Cdd:cd00086 1 RRKRTRFTPEQLEELEKEFEKNPYPSREEREELAKELGLTERQVKIWFQNRRAKLKRSE 59
|
|
| HOX |
smart00389 |
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key ... |
1107-1162 |
9.32e-11 |
|
Homeodomain; DNA-binding factors that are involved in the transcriptional regulation of key developmental processes
Pssm-ID: 197696 [Multi-domain] Cd Length: 57 Bit Score: 58.42 E-value: 9.32e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 767973570 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMR 1162
Cdd:smart00389 2 RRKRTSFTPEQLEELEKEFQKNPYPSREEREELAKKLGLSERQVKVWFQNRRAKWK 57
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
117-317 |
7.80e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 7.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 117 QRNEAEK----QKGLQEVQITLAA-RLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASkadevglimtnLEKANQRA 191
Cdd:COG1196 208 QAEKAERyrelKEELKELEAELLLlKLRELEAELEELEAELEELEAELEELEAELAELEAE-----------LEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 192 EAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASAN 271
Cdd:COG1196 277 EELELELEEAQAEEYELLAELA----------------------RLEQDIARLEERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767973570 272 QIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLAS 317
Cdd:COG1196 335 LEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
111-308 |
2.50e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.91 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 111 LTETLLQRNEAEKQKGLQEVQI-TLAARLGEAEEKIKVLHSALKATQAELLELRrkydEEAASKADEVGLIMTNLEKANQ 189
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIeELEAQIEQLKEELKALREALDELRAELTLLN----EEAANLRERLESLERRIAATER 838
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 190 RAEAAQREVESLREQLASVNSSIrlaccSPQGPSGDKVNFTLCSgprLEAALASKDREILRLLKDVQHLQSSLQELEEas 269
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEI-----EELEELIEELESELEA---LLNERASLEEALALLRSELEELSEELRELES-- 908
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767973570 270 anQIADLERQLTAKSEAIEKLEEKLQ-AQSDYEEIKTELS 308
Cdd:TIGR02168 909 --KRSELRRELEELREKLAQLELRLEgLEVRIDNLQERLS 946
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
108-321 |
2.87e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 56.09 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 108 KALLTetlLQRNEAEKQKgLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEeaasKADEVGLIMTNLEKA 187
Cdd:COG1579 7 RALLD---LQELDSELDR-LEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKR----LELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 188 NQR---------AEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHL 258
Cdd:COG1579 79 EEQlgnvrnnkeYEALQKEIESLKRRISDLEDEIL----------------------ELMERIEELEEELAELEAELAEL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973570 259 QSSLQELEEASANQIADLERQLTAKSEAIEKLEEKLQAQ--SDYEEIKTELSILKAMKLASSTCS 321
Cdd:COG1579 137 EAELEEKKAELDEELAELEAELEELEAEREELAAKIPPEllALYERIRKRKNGLAVVPVEGGACG 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
113-312 |
3.13e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 58.41 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 113 ETLLQRNEAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAE 192
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 193 AAQREVESLREQLASVNssirlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEAsanQ 272
Cdd:COG1196 387 ELLEALRAAAELAAQLE--------------------------ELEEAEEALLERLERLEEELEELEEALAELEEE---E 437
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767973570 273 IADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKA 312
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
109-317 |
7.88e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 7.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 109 ALLTETLLQRNEAEKQ-KGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVglimTNLEKA 187
Cdd:COG1196 267 AELEELRLELEELELElEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE----EELEEL 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 188 NQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEe 267
Cdd:COG1196 343 EEELEEAEEELEEAEAELAEAEEALL----------------------EAEAELAEAEEELEELAEELLEALRAAAELA- 399
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767973570 268 asaNQIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAMKLAS 317
Cdd:COG1196 400 ---AQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
127-309 |
8.74e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 127 LQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEvglimtnLEKANQRAEAAQREVESLREQLA 206
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ-------LEREIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 207 svnssirlaccspqgpsgdkvnfTLCSgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASANQIADLERQLTAKSEA 286
Cdd:COG4913 366 -----------------------ALLA--ALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420
|
170 180 190
....*....|....*....|....*....|....*
gi 767973570 287 IEKLEEKLQA----QSDY--------EEIKTELSI 309
Cdd:COG4913 421 LRELEAEIASlerrKSNIparllalrDALAEALGL 455
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
115-312 |
1.85e-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: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 115 LLQRNEAEKQKGLQEVQIT--------LAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGlimtNLEK 186
Cdd:COG1196 231 LLKLRELEAELEELEAELEeleaeleeLEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ----DIAR 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 187 ANQRAEAAQREVESLREQLASVNSSIRLAccspqgpsgdkvnftlcsGPRLEAALASKDREILRLLKDVQHLQSSLQELE 266
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEEL------------------EEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767973570 267 EASANQIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKA 312
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
111-310 |
2.18e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 55.41 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 111 LTETLLQRNEAEKQKGLQEVQITLAARLGEAEEKikvlhsaLKATQAELLELRRKYDEEAASkaDEVGLIMTNLEKANQR 190
Cdd:COG3206 157 LAEAYLEQNLELRREEARKALEFLEEQLPELRKE-------LEEAEAALEEFRQKNGLVDLS--EEAKLLLQQLSELESQ 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 191 AEAAQREVESLREQLASVNSSIRLACCSPQGPSGDKVNftlcsgPRLEAALASKDREILRLLK-------DVQHLQSSLQ 263
Cdd:COG3206 228 LAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVI------QQLRAQLAELEAELAELSArytpnhpDVIALRAQIA 301
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767973570 264 ELEEASANQIADLERQLTAKSEAIEKLEEKLQAQsdYEEIKTELSIL 310
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQAREASLQAQ--LAQLEARLAEL 346
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
134-314 |
4.27e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 134 LAARLGEAEEKIKVLHSALKATQAELLELRRKYDEeaasKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIR 213
Cdd:COG3883 21 KQKELSELQAELEAAQAELDALQAELEELNEEYNE----LQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 214 LaccspQGPSGDKVNFTLCSGP------RLEA--ALASKDREILRLLKDvqhLQSSLQELEEASANQIADLERQLTAKSE 285
Cdd:COG3883 97 R-----SGGSVSYLDVLLGSESfsdfldRLSAlsKIADADADLLEELKA---DKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190
....*....|....*....|....*....|
gi 767973570 286 AIEKLEEKL-QAQSDYEEIKTELSILKAMK 314
Cdd:COG3883 169 AKAELEAQQaEQEALLAQLSAEEAAAEAQL 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
108-299 |
7.86e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.91 E-value: 7.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 108 KALLTETLLQRNEAEKQkGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDE---EAASKADEVGLIMTNL 184
Cdd:TIGR02168 331 KLDELAEELAELEEKLE-ELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQlelQIASLNNEIERLEARL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 185 EKANQRAEAAQREVESLREQLASVnssiRLACCSPQGPSGDKVNFTLCSG-PRLEAALASKDREILRLLKDVQHLQSSLQ 263
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEA----ELKELQAELEELEEELEELQEElERLEEALEELREELEEAEQALDAAERELA 485
|
170 180 190
....*....|....*....|....*....|....*.
gi 767973570 264 ELeeasANQIADLERQLTAKSEAIEKLEEKLQAQSD 299
Cdd:TIGR02168 486 QL----QARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
116-358 |
1.01e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.52 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 116 LQRNEAEKQKGLQEVQI---TLAARLGEAEEKIKVLHSALKATQAEL--LELR-RKYDEEAASKADEVGLIMTNLEKANQ 189
Cdd:TIGR02168 251 AEEELEELTAELQELEEkleELRLEVSELEEEIEELQKELYALANEIsrLEQQkQILRERLANLERQLEELEAQLEELES 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 190 RAEAAQREVESLREQLASVNssIRLACCSPQGPSGDKVNFTLCSGPR-LEAALASKDREILRLLKDVQHLQSSLQELEEa 268
Cdd:TIGR02168 331 KLDELAEELAELEEKLEELK--EELESLEAELEELEAELEELESRLEeLEEQLETLRSKVAQLELQIASLNNEIERLEA- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 269 sanQIADLERQLTAKSEAIEKLEEKLQAQsDYEEIKTELSILKAM--KLASSTCSLPQGMAKPEDSLLIAKEAFFPTQKF 346
Cdd:TIGR02168 408 ---RLERLEDRRERLQQEIEELLKKLEEA-ELKELQAELEELEEEleELQEELERLEEALEELREELEEAEQALDAAERE 483
|
250
....*....|..
gi 767973570 347 LLEKPSLLASPE 358
Cdd:TIGR02168 484 LAQLQARLDSLE 495
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
117-313 |
1.66e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 117 QRNEAEKQKG----LQEVQITLAARLGEAEEKIKVL--HSALKATQAELLELRRKYdEEAASKADEVGLIMTNLEKANQR 190
Cdd:COG4717 79 ELKEAEEKEEeyaeLQEELEELEEELEELEAELEELreELEKLEKLLQLLPLYQEL-EALEAELAELPERLEELEERLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 191 AEAAQREVESLREQLASVNSSIRLAccspqgpsgdkvnftlcsgprLEAALASKDREILRLLKDVQHLQSSLQELEEasa 270
Cdd:COG4717 158 LRELEEELEELEAELAELQEELEEL---------------------LEQLSLATEEELQDLAEELEELQQRLAELEE--- 213
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 767973570 271 nQIADLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAM 313
Cdd:COG4717 214 -ELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIA 255
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
120-314 |
3.00e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 52.22 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 120 EAEKQ-KGLQEVQiTLAARLGEAEEKIKVLHSALKATQAELLELR-RKYDEEAASKADEVGLIMTNLEKANQRAEAAQRE 197
Cdd:COG4913 246 DAREQiELLEPIR-ELAERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRAELARLEAELERLEARLDALREE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 198 VESLREQLASvNSSIRLAccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELE---EASANQIA 274
Cdd:COG4913 325 LDELEAQIRG-NGGDRLE--------------------QLEREIERLERELEERERRRARLEALLAALGlplPASAEEFA 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767973570 275 DLERQLTAKSEAIEKLEEKLQ------------AQSDYEEIKTELSILKAMK 314
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEealaeaeaalrdLRRELRELEAEIASLERRK 435
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
76-302 |
3.46e-06 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 51.61 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 76 NPELLSPKEQREGTSPAGPTLTEGSRLPGIPGKALLT----ETL--LQR-NEA--EKQKGLQEVQIT-LAARLGEAEEKI 145
Cdd:pfam05622 241 NEELRCAQLQQAELSQADALLSPSSDPGDNLAAEIMPaeirEKLirLQHeNKMlrLGQEGSYRERLTeLQQLLEDANRRK 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 146 KVLHSALKATQAELLELRRKYDE------EAASKADEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccsp 219
Cdd:pfam05622 321 NELETQNRLANQRILELQQQVEElqkalqEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQ------- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 220 QGPSGDKVNftlcsgpRLEAALASKDREIL----RLLKDVQHLQSSLQELE----EASANQIADLERQLTAKSEAIEKLE 291
Cdd:pfam05622 394 DSNLAQKID-------ELQEALRKKDEDMKameeRYKKYVEKAKSVIKTLDpkqnPASPPEIQALKNQLLEKDKKIEHLE 466
|
250
....*....|....
gi 767973570 292 ---EKLQAQSDYEE 302
Cdd:pfam05622 467 rdfEKSKLQREQEE 480
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
122-314 |
5.36e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 5.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 122 EKQKGLQEVQITLAA-RLGEAEEKIKVLHSALKATQAELLELRRKYDEeAASKADEVGLIMTNLEKanqRAEAAQREVES 200
Cdd:TIGR02168 217 ELKAELRELELALLVlRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEE---EIEELQKELYA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 201 LREQLASVNSSIRLAccspqgpsGDKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQELE---EASANQIADLE 277
Cdd:TIGR02168 293 LANEISRLEQQKQIL--------RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKeelESLEAELEELE 364
|
170 180 190
....*....|....*....|....*....|....*..
gi 767973570 278 RQLTAKSEAIEKLEEKLQAQSDyEEIKTELSILKAMK 314
Cdd:TIGR02168 365 AELEELESRLEELEEQLETLRS-KVAQLELQIASLNN 400
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
107-368 |
5.57e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 50.29 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 107 GKALLTETLLQRNEAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRrkydEEAASKADEVGLIMTNLEK 186
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLE----EELEQARSELEQLEEELEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 187 ANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELE 266
Cdd:COG4372 85 LNEQLQAAQAELAQAQEELESLQEEAE----------------------ELQEELEELQKERQDLEQQRKQLEAQIAELQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 267 EASAN---QIADLERQLTAKSEAIEKLEEKLQAQSDyEEIKTELSILK--AMKLASSTCSLPQGMAKPEDSLLIAKEAFF 341
Cdd:COG4372 143 SEIAEreeELKELEEQLESLQEELAALEQELQALSE-AEAEQALDELLkeANRNAEKEEELAEAEKLIESLPRELAEELL 221
|
250 260
....*....|....*....|....*..
gi 767973570 342 PTQKFLLEKPSLLASPEEDPSEDDSIK 368
Cdd:COG4372 222 EAKDSLEAKLGLALSALLDALELEEDK 248
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
120-313 |
1.39e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 120 EAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKA---TQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQR 196
Cdd:PRK03918 547 ELEKLEELKKKLAELEKKLDELEEELAELLKELEElgfESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEE 626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 197 EVESLREQLASVNSSIRLAccsPQGPSGDKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQELEEAsanqIADL 276
Cdd:PRK03918 627 ELDKAFEELAETEKRLEEL---RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT----LEKL 699
|
170 180 190
....*....|....*....|....*....|....*..
gi 767973570 277 ERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILKAM 313
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALERVEELREKVKKYKAL 736
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
121-312 |
2.47e-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: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 121 AEKQKGLQEVQITLAA---RLGEAEEKIKVLHSALKATQAELLELRRKYDEeaasKADEVGLIMTNLEKANQRAEAAQRE 197
Cdd:COG4942 23 AEAEAELEQLQQEIAElekELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 198 VESLREQLASVnssIRLACCSPQGPsgdKVNFTLCSGPRLEAA-----LASKDREILRLLKDVQHLQSSLQELEEASANQ 272
Cdd:COG4942 99 LEAQKEELAEL---LRALYRLGRQP---PLALLLSPEDFLDAVrrlqyLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767973570 273 IADLERQLTAKSEAIEKLEEKLQAQ--------SDYEEIKTELSILKA 312
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERqkllarleKELAELAAELAELQQ 220
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
138-302 |
2.65e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 138 LGEAEEKIKVL-HSALKATQAELLELRRKYDEEAASKADEVglimTNLEKANQraeaaQREvESLREQLASVNssirlac 216
Cdd:PRK12704 44 LEEAKKEAEAIkKEALLEAKEEIHKLRNEFEKELRERRNEL----QKLEKRLL-----QKE-ENLDRKLELLE------- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 217 cspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQsslQELEEASANQIADLER--QLT---AKSEAIEKLE 291
Cdd:PRK12704 107 -------------------KREEELEKKEKELEQKQQELEKKE---EELEELIEEQLQELERisGLTaeeAKEILLEKVE 164
|
170
....*....|....*.
gi 767973570 292 EKLQAQS-----DYEE 302
Cdd:PRK12704 165 EEARHEAavlikEIEE 180
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
141-308 |
3.58e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 3.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 141 AEEKIKVLhsalkatQAELLELRRKydeeaaskadevglimtnLEKANQRAEAAQREVESLREQLASVNssiRLAccspq 220
Cdd:COG4913 608 NRAKLAAL-------EAELAELEEE------------------LAEAEERLEALEAELDALQERREALQ---RLA----- 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 221 gpsgdKVNFTLCSGPRLEAALASKDREILRLLK---DVQHLQSSLQELEEasanQIADLERQLTAKSEAIEKLEEKL-QA 296
Cdd:COG4913 655 -----EYSWDEIDVASAEREIAELEAELERLDAssdDLAALEEQLEELEA----ELEELEEELDELKGEIGRLEKELeQA 725
|
170
....*....|..
gi 767973570 297 QSDYEEIKTELS 308
Cdd:COG4913 726 EEELDELQDRLE 737
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
121-299 |
6.88e-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: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 121 AEKQKGLQEVQITLAarlgEAEEKIKVLHSALKATQAELLELRRKYDEeaaskadevglIMTNLEKANQRAEAAQREVES 200
Cdd:TIGR02168 666 AKTNSSILERRREIE----ELEEKIEELEEKIAELEKALAELRKELEE-----------LEEELEQLRKELEELSRQISA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 201 LREQLASVNSSIRLACCSPQgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEASAN---QIADLE 277
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIA---------------QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEleaQIEQLK 795
|
170 180
....*....|....*....|..
gi 767973570 278 RQLTAKSEAIEKLEEKLQAQSD 299
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNE 817
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
116-208 |
9.46e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 116 LQRNEAEKQKGLQEVQitlaARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGLIMTNLEKANQRAEAAQ 195
Cdd:COG4913 343 LEREIERLERELEERE----RRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLR 418
|
90
....*....|...
gi 767973570 196 REVESLREQLASV 208
Cdd:COG4913 419 RELRELEAEIASL 431
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
121-300 |
1.15e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 121 AEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRR------------KYDEEAASKADEVGLIMTN---LE 185
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeidvaSAEREIAELEAELERLDASsddLA 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 186 KANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSS---- 261
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIG----------------------RLEKELEQAEEELDELQDRLEAAEDLarle 746
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767973570 262 ---------LQELEEASANQI-ADLERQLTAKSEAIEKLEEKL-QAQSDY 300
Cdd:COG4913 747 lralleerfAAALGDAVERELrENLEERIDALRARLNRAEEELeRAMRAF 796
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
120-311 |
2.22e-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: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 120 EAEKQKGLQEvqitlaarLGEAEEKIKVLHSALKATQAELLELRR------KYDEEAASKAD-EVGLIMTNLEKANQRAE 192
Cdd:TIGR02169 169 DRKKEKALEE--------LEEVEENIERLDLIIDEKRQQLERLRRerekaeRYQALLKEKREyEGYELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 193 AAQREVESLREQLASVNSSIrlaccspqgpsgDKVNFTLcsgPRLEAALASKDREILRLLKDVQ-HLQSSLQELEeasaN 271
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEI------------SELEKRL---EEIEQLLEELNKKIKDLGEEEQlRVKEKIGELE----A 301
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 767973570 272 QIADLERQLTAKSEAIEKLEEKL-QAQSDYEEIKTELSILK 311
Cdd:TIGR02169 302 EIASLERSIAEKERELEDAEERLaKLEAEIDKLLAEIEELE 342
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
127-369 |
2.22e-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: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 127 LQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKAdEVGLIMTNLEK--ANQRAEAAQREVESLREQ 204
Cdd:TIGR02169 728 LEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLH-KLEEALNDLEArlSHSRIPEIQAELSKLEEE 806
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 205 LASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDVQHLQSSLQELEEasanQIADLERQ---LT 281
Cdd:TIGR02169 807 VSRIEARLR----------------------EIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE----QIKSIEKEienLN 860
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 282 AKSEAIEKLEEKLQAQ-----SDYEEIKTELSILKA----MKLASSTCSLPQGMAKPEDSLLIAKEAFFPTQKFLLEKPs 352
Cdd:TIGR02169 861 GKKEELEEELEELEAAlrdleSRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDP- 939
|
250
....*....|....*..
gi 767973570 353 lLASPEEDPSEDDSIKD 369
Cdd:TIGR02169 940 -KGEDEEIPEEELSLED 955
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
116-310 |
2.68e-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: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 116 LQRNEAEKQKGLQEVQITLA---ARLGEAEEKIKVLH--------------SALKATQAELLELRRKYDEEAASKA---D 175
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAkleAEIDKLLAEIEELEreieeerkrrdkltEEYAELKEELEDLRAELEEVDKEFAetrD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 176 EVGLIMTNLEKANQRAEAAQREVESLREQLasVNSSIRLAccspqgpsgdkvnftlcsgpRLEAALASKDREILRLLKDV 255
Cdd:TIGR02169 386 ELKDYREKLEKLKREINELKRELDRLQEEL--QRLSEELA--------------------DLNAAIAGIEAKINELEEEK 443
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767973570 256 QHLQSSLQELE---EASANQIADLERQLTAKSEAIEKLEEKL-QAQSDYEEIKTELSIL 310
Cdd:TIGR02169 444 EDKALEIKKQEwklEQLAADLSKYEQELYDLKEEYDRVEKELsKLQRELAEAEAQARAS 502
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
100-314 |
4.42e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 100 SRLPGIPGKALLTETLLQRNEAEKQKgLQEVQITLAARLGEA---EEKIKVLHSALKATQAELLELRRKYDE--EAASKA 174
Cdd:PRK03918 214 SELPELREELEKLEKEVKELEELKEE-IEELEKELESLEGSKrklEEKIRELEERIEELKKEIEELEEKVKElkELKEKA 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 175 DEVGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcSGPRLEAALASKDREILRLLKD 254
Cdd:PRK03918 293 EEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-------------------ELEEKEERLEELKKKLKELEKR 353
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973570 255 VQHLQSSLQELEEASA--NQIADLERQLTAKSeaIEKLEEKLQ-AQSDYEEIKTELSILKAMK 314
Cdd:PRK03918 354 LEELEERHELYEEAKAkkEELERLKKRLTGLT--PEKLEKELEeLEKAKEEIEEEISKITARI 414
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
118-311 |
5.33e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 118 RNEAEkqkGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRK---YDEEAASKADEVGLIMTNLEKANQRAEAA 194
Cdd:PRK02224 341 NEEAE---SLREDADDLEERAEELREEAAELESELEEAREAVEDRREEieeLEEEIEELRERFGDAPVDLGNAEDFLEEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 195 QREVESLREQLASVNSSIRlaccspqgpsgdKVNFTLCSGPRLEAalASKDREILRLLKDVQHLqSSLQELEEasanQIA 274
Cdd:PRK02224 418 REERDELREREAELEATLR------------TARERVEEAEALLE--AGKCPECGQPVEGSPHV-ETIEEDRE----RVE 478
|
170 180 190
....*....|....*....|....*....|....*..
gi 767973570 275 DLERQLTAKSEAIEKLEEKLQAQSDYEEIKTELSILK 311
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLE 515
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
108-312 |
8.20e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 8.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 108 KALLTETLLQRNEAEKQKGLQEVQIT-LAARLG--------EAEEKIKVLhSALKATQAELLELRRKYDEEAASKADEVG 178
Cdd:COG4717 297 KASLGKEAEELQALPALEELEEEELEeLLAALGlppdlspeELLELLDRI-EELQELLREAEELEEELQLEELEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 179 LI---MTNLEKANQRAEAAQREVEsLREQLASVNSSIRLAccspqgpsgdkvnftlcsGPRLEAALASKDREilRLLKDV 255
Cdd:COG4717 376 LAeagVEDEEELRAALEQAEEYQE-LKEELEELEEQLEEL------------------LGELEELLEALDEE--ELEEEL 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767973570 256 QHLQSSLQELEEasanQIADLERQLTAKSEAIEKLEEklqaQSDYEEIKTELSILKA 312
Cdd:COG4717 435 EELEEELEELEE----ELEELREELAELEAELEQLEE----DGELAELLQELEELKA 483
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
108-293 |
1.12e-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: 43.21 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 108 KALLTETLLQRNEAEKQKGLQEVQI-TLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAA------------SKA 174
Cdd:COG4942 40 EKELAALKKEEKALLKQLAALERRIaALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEelaellralyrlGRQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 175 DEVGLIM--TNLEKANQRAEAAQREVESLREQLASVNSSIRlaccspqgpsgdkvnftlcsgpRLEAALASKDREILRLL 252
Cdd:COG4942 120 PPLALLLspEDFLDAVRRLQYLKYLAPARREQAEELRADLA----------------------ELAALRAELEAERAELE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767973570 253 KDVQHLQSSLQELEEASANQ---IADLERQLTAKSEAIEKLEEK 293
Cdd:COG4942 178 ALLAELEEERAALEALKAERqklLARLEKELAELAAELAELQQE 221
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
127-297 |
1.77e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 127 LQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAAS------KADEVGLIM--TNLEKANQRAEAAQREV 198
Cdd:COG3883 49 LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAlyrsggSVSYLDVLLgsESFSDFLDRLSALSKIA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 199 ESLREQLASVNSSIRLAccspqgpsgdkvnftlcsgPRLEAALASKDREILRLLKDVQHLQSSLQELEEASANQIADLER 278
Cdd:COG3883 129 DADADLLEELKADKAEL-------------------EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170
....*....|....*....
gi 767973570 279 QLTAKSEAIEKLEEKLQAQ 297
Cdd:COG3883 190 EEAAAEAQLAELEAELAAA 208
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
117-296 |
2.12e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 41.52 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 117 QRNEAEKQKGLQEVQITLA--ARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASKADEVGLIMTNL--EKANQRAE 192
Cdd:pfam12795 9 KLDEAAKKKLLQDLQQALSllDKIDASKQRAAAYQKALDDAPAELRELRQELAALQAKAEAAPKEILASLslEELEQRLL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 193 AAQREVESLREQLASVNSSIRLACCSPQGPSG---------DKVNFTLCSGPRLEAALASKDREILRLLKDVQHLQSSLQ 263
Cdd:pfam12795 89 QTSAQLQELQNQLAQLNSQLIELQTRPERAQQqlsearqrlQQIRNRLNGPAPPGEPLSEAQRWALQAELAALKAQIDML 168
|
170 180 190
....*....|....*....|....*....|....
gi 767973570 264 ELEEASANQIADLER-QLTAKSEAIEKLEEKLQA 296
Cdd:pfam12795 169 EQELLSNNNRQDLLKaRRDLLTLRIQRLEQQLQA 202
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
157-316 |
2.85e-03 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 41.59 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 157 AELLELRRKYDEEAASKADE---------VGLIMTNLEKANQRAEAAQREVESLREQLASVNSSIrlaccspqgpSGDKv 227
Cdd:cd22656 94 AEILELIDDLADATDDEELEeakktikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKDQTAL----------ETLE- 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 228 nftlcsgPRLEAALASKDREILRllKDVQHLQsslQELEEASANQIADLERQLTAKSEAIEKLEEKLQA----QSDYEEI 303
Cdd:cd22656 163 -------KALKDLLTDEGGAIAR--KEIKDLQ---KELEKLNEEYAAKLKAKIDELKALIADDEAKLAAalrlIADLTAA 230
|
170
....*....|....
gi 767973570 304 KTEL-SILKAMKLA 316
Cdd:cd22656 231 DTDLdNLLALIGPA 244
|
|
| COG5576 |
COG5576 |
Homeodomain-containing transcription factor [Transcription]; |
1107-1174 |
3.29e-03 |
|
Homeodomain-containing transcription factor [Transcription];
Pssm-ID: 227863 [Multi-domain] Cd Length: 156 Bit Score: 39.73 E-value: 3.29e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973570 1107 KKPRVVLAPEEKEALRKAYQLEPYPSQQTIELLSFQLNLKTNTVINWFHNYRSRMRREMLVEGTQDEP 1174
Cdd:COG5576 52 KSKRRRTTDEQLMVLEREFEINPYPSSITRIKLSLLLNMPPKSVQIWFQNKRAKEKKKRSGKVEQRPG 119
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
245-312 |
3.71e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 40.68 E-value: 3.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973570 245 DREILRLLKDVQHLQSSLQELEEASAN---QIADLERQLTAKSEAIEKLEEKL-QAQSDYEEIKTELSILKA 312
Cdd:COG1579 2 MPEDLRALLDLQELDSELDRLEHRLKElpaELAELEDELAALEARLEAAKTELeDLEKEIKRLELEIEEVEA 73
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
113-207 |
5.79e-03 |
|
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: 41.31 E-value: 5.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 113 ETLLQRNEAEKQKGLQEVQITLAARLGEAEEKIKVLHSALKATQAELLELRRKYDEEAASkadevgliMTNLEKANQRae 192
Cdd:pfam01576 480 ETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGT--------LEALEEGKKR-- 549
|
90
....*....|....*
gi 767973570 193 aAQREVESLREQLAS 207
Cdd:pfam01576 550 -LQRELEALTQQLEE 563
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
159-306 |
6.28e-03 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 38.45 E-value: 6.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973570 159 LLELRRKYDEEAAskadevglimTNLEKANQRAEAAQREVESLREQL----ASVNSSIRlaccspQGPSGdkvnftlcsg 234
Cdd:TIGR02473 7 LLDLREKEEEQAK----------LELAKAQAEFERLETQLQQLIKYReeyeQQALEKVG------AGTSA---------- 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973570 235 prleAALASKDREILRLLKDVQHLQSSLQELEeasaNQIADLERQLTAKS---EAIEKLEEKLQAQSDYEEIKTE 306
Cdd:TIGR02473 61 ----LELSNYQRFIRQLDQRIQQQQQELALLQ----QEVEAKRERLLEARrelKALEKLKEKKQKEYRAEEAKRE 127
|
|
|