|
Name |
Accession |
Description |
Interval |
E-value |
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
12-319 |
2.21e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 72.28 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 12 ERIQALEEDLREKEREIATEKKNSLKRDKA-----IQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQ 86
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKLRELEAELEeleaeLEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 87 GSEDYETALSGKEALsaALRSQNLTKSTEnhRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVE 166
Cdd:COG1196 293 LLAELARLEQDIARL--EERRRELEERLE--ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 167 KLRNEVNEREKAMENRYKSLLSESNKKLhNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQncylmAAEDLELRSEGLI 246
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAA-ELAAQLEELEEAEEALLERLERLEEELEELEEA-----LAELEEEEEEEEE 442
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462625355 247 TEKcssqqppgsktifSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDSINNLQAELNKIFALRKQLEQD 319
Cdd:COG1196 443 ALE-------------EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-206 |
7.51e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 7.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQ 81
Cdd:COG1196 299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 82 TQEFQGSEDYETALsgKEALSAALRSQNLTKSTENHRLRRSikKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDL 161
Cdd:COG1196 379 EELEELAEELLEAL--RAAAELAAQLEELEEAEEALLERLE--RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462625355 162 RNEVEKLRNEVNEREKAmENRYKSLLSESNKKLHNQEQVIKHLTE 206
Cdd:COG1196 455 EEEEEALLELLAELLEE-AALLEAALAELLEELAEAAARLLLLLE 498
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-337 |
1.89e-10 |
|
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: 65.86 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSfQERIQALEEDLREKEREIATEKKNSLKRDkaIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQ 83
Cdd:TIGR02169 204 RREREK-AERYQALLKEKREYEGYELLKEKEALERQ--KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 84 EfqgsedyeTALSGKEALsaALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRN 163
Cdd:TIGR02169 281 I--------KDLGEEEQL--RVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 164 EVEKLRNEVNEREKAMEN----------RYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNcylM 233
Cdd:TIGR02169 351 RRDKLTEEYAELKEELEDlraeleevdkEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLN---A 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 234 AAEDLELRSEGLITEKcssqqppgsKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQE-SDSINNLQAELNKIFAL 312
Cdd:TIGR02169 428 AIAGIEAKINELEEEK---------EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRvEKELSKLQRELAEAEAQ 498
|
330 340
....*....|....*....|....*
gi 2462625355 313 RKQLEQDVLSYQNLRKTLEEQISEI 337
Cdd:TIGR02169 499 ARASEERVRGGRAVEEVLKASIQGV 523
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2-192 |
4.27e-10 |
|
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: 63.63 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQ 81
Cdd:COG4942 24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 82 TQ--------EFQGSEDYETALSGKEALSAALRSQNLTKSTENHR------LRRSIKKITQELSDLQQERERLEKDLEEA 147
Cdd:COG4942 104 EElaellralYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARreqaeeLRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2462625355 148 HREKSKgdctIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNK 192
Cdd:COG4942 184 EEERAA----LEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-345 |
5.46e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.69 E-value: 5.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQ 83
Cdd:TIGR02168 732 RKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAE 811
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 84 EFQGSEDYETALSGKEALSAALRS-----QNLTKSTEnhRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTI 158
Cdd:TIGR02168 812 LTLLNEEAANLRERLESLERRIAAterrlEDLEEQIE--ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 159 RDLRNEVEKLRNEVNE-REKAMENRYKslLSESNKKLHnqeQVIKHLTESTNQKDVLLQKFNEKdleviqqncYLMAAED 237
Cdd:TIGR02168 890 ALLRSELEELSEELRElESKRSELRRE--LEELREKLA---QLELRLEGLEVRIDNLQERLSEE---------YSLTLEE 955
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 238 LELRSEGLitekcssqqppgsktifskEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDSINNLQAELNKifalrkQLE 317
Cdd:TIGR02168 956 AEALENKI-------------------EDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTA------QKE 1010
|
330 340
....*....|....*....|....*...
gi 2462625355 318 qDVLSyqnLRKTLEEQISEIRRREEESF 345
Cdd:TIGR02168 1011 -DLTE---AKETLEEAIEEIDREARERF 1034
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
4-216 |
1.42e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 63.03 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKA---REALQKA 80
Cdd:COG1196 280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAeeeLEEAEAE 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 81 QTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLE---KDLEEAHREKSKGDCT 157
Cdd:COG1196 360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEeelEELEEALAELEEEEEE 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462625355 158 IRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQ 216
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2-244 |
2.06e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQ 81
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 82 TQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKgdctIRDL 161
Cdd:COG1196 351 EELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE----LEEL 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 162 RNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELR 241
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGF 506
|
...
gi 2462625355 242 SEG 244
Cdd:COG1196 507 LEG 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1-222 |
2.09e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 62.77 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1 MEHQKERnsFQERIQALEEDLREKEREIATEKKnslKRDKAIQgltmALKSKEKKVEELNSEIEKLSAAFAKAREALQKA 80
Cdd:TIGR02168 300 LEQQKQI--LRERLANLERQLEELEAQLEELES---KLDELAE----ELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 81 QTQEfqgsEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCtird 160
Cdd:TIGR02168 371 ESRL----EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL---- 442
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462625355 161 lrNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKD 222
Cdd:TIGR02168 443 --EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2-174 |
1.32e-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: 60.07 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQ 81
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR 893
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 82 TQEFQGSEDYETALSGKEALSAALRSQNltksTENHRLRRSIKKITQELSDLQQE-RERLEKDLEEAHREKSKGDCTIRD 160
Cdd:TIGR02168 894 SELEELSEELRELESKRSELRRELEELR----EKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEE 969
|
170
....*....|....
gi 2462625355 161 LRNEVEKLRNEVNE 174
Cdd:TIGR02168 970 ARRRLKRLENKIKE 983
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2-352 |
3.88e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 58.59 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLsaafaKAREALQKAQ 81
Cdd:pfam15921 458 ESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITKL-----RSRVDLKLQE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 82 TQEFQGSEDYetaLSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSD-------LQQERERLEKDLEEAHRE---- 150
Cdd:pfam15921 533 LQHLKNEGDH---LRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQhgrtagaMQVEKAQLEKEINDRRLElqef 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 151 ---KSKGDCTIRDLRNEVE-------KLRNEVNEREKAME----------NRYKSLLSESNKKLHNQEQVIKHL------ 204
Cdd:pfam15921 610 kilKDKKDAKIRELEARVSdlelekvKLVNAGSERLRAVKdikqerdqllNEVKTSRNELNSLSEDYEVLKRNFrnksee 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 205 TESTNQKDVLLQKFNEKDLEVIQQNCYLMAAED-----LELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSDYEEliQVL 279
Cdd:pfam15921 690 METTTNKLKMQLKSAQSELEQTRNTLKSMEGSDghamkVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEK--HFL 767
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462625355 280 KKEQDIYTHLVKSLQESDsiNNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISE----IRRREEESFSLYSDQT 352
Cdd:pfam15921 768 KEEKNKLSQELSTVATEK--NKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAEcqdiIQRQEQESVRLKLQHT 842
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
35-338 |
4.58e-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: 58.14 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 35 SLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEfqgsEDYETALSGKEALSAALRSQNLTKST 114
Cdd:TIGR02168 665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL----EQLRKELEELSRQISALRKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 115 ENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENrYKSLLSESNKKL 194
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNEEA 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 195 HNQEQVIKHLTESTNQKdvllqkfnEKDLEVIQQNcylmaAEDLELRSEGLITEKCSSQQPPgsKTIFSKEKKQSSDYEE 274
Cdd:TIGR02168 820 ANLRERLESLERRIAAT--------ERRLEDLEEQ-----IEELSEDIESLAAEIEELEELI--EELESELEALLNERAS 884
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462625355 275 LIQVLKKEQDIYTHLVKSLQESDsiNNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIR 338
Cdd:TIGR02168 885 LEEALALLRSELEELSEELRELE--SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLS 946
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-245 |
8.13e-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: 57.37 E-value: 8.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDL-------REKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAF------ 70
Cdd:TIGR02168 252 EEELEELTAELQELEEKLeelrlevSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLeelesk 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 71 ---AKAREALQKAQTQEFQGS-EDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEE 146
Cdd:TIGR02168 332 ldeLAEELAELEEKLEELKEElESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 147 AHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRyksllsESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVI 226
Cdd:TIGR02168 412 LEDRRERLQQEIEELLKKLEEAELKELQAELEELEE------ELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
250
....*....|....*....
gi 2462625355 227 QQNCYLMAAEDLELRSEGL 245
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGF 504
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
4-284 |
8.18e-08 |
|
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: 57.39 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEEL-----NSEIEKLSAAFAKAREALQ 78
Cdd:TIGR02169 729 EQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEVS 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 79 K--AQTQEFQ---GSEDYETALSGKEaLSAALRSQNLTKSTENHRlRRSIKKITQELSDLQQERERLEKDLEEAHREKSK 153
Cdd:TIGR02169 809 RieARLREIEqklNRLTLEKEYLEKE-IQELQEQRIDLKEQIKSI-EKEIENLNGKKEELEEELEELEAALRDLESRLGD 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 154 GDCTIRDLRNEVEKLRNEVNEREKAMEnRYKSLLSESNKKLHNQEQVIKHLTEstNQKDVLLQKFNEKDLEVIQQNCYLM 233
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQIE-KKRKRLSELKAKLEALEEELSEIED--PKGEDEEIPEEELSLEDVQAELQRV 963
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462625355 234 AAedlELRSEGLITEKCSSQqppgsktiFSKEKKQSSDYEELIQVLKKEQD 284
Cdd:TIGR02169 964 EE---EIRALEPVNMLAIQE--------YEEVLKRLDELKEKRAKLEEERK 1003
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1114-1360 |
2.01e-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: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1114 QDLLMEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIfasgselhSSLTSEIHFLRKQNQALNAMLIKGSR 1193
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL--------ARLEQDIARLEERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1194 DKQ---KENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRcsgQELSRVQEELKLRQQLLS 1270
Cdd:COG1196 324 ELAeleEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE---ELAEELLEALRAAAELAA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1271 QNDKLLQSLRVELKAYEKLDEEHRRLREASGEGWKGQDpfrDLHSLLMEIQALRLQLERSIETSSTLQSRLKEQLARGAE 1350
Cdd:COG1196 401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEE---EEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
|
250
....*....|
gi 2462625355 1351 KAQEGALTLA 1360
Cdd:COG1196 478 ALAELLEELA 487
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
10-229 |
2.48e-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: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 10 FQERIQALEEDLREKEREIATekknsLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQefqgse 89
Cdd:COG3206 180 LEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQ------ 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 90 dyetALSGKEALSAALRSQnltkstenhrlrrSIKKITQELSDLQQERERLEKDLEEAHREkskgdctIRDLRNEVEKLR 169
Cdd:COG3206 249 ----LGSGPDALPELLQSP-------------VIQQLRAQLAELEAELAELSARYTPNHPD-------VIALRAQIAALR 304
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462625355 170 NEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFN--EKDLEVIQQN 229
Cdd:COG3206 305 AQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVAREL 366
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
4-180 |
6.64e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.68 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREI--ATEKKNSLKrdKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQ 81
Cdd:COG3883 22 QKELSELQAELEAAQAELDALQAELeeLNEEYNELQ--AELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 82 TQ-----EFQGSEDYETALSGKEALSAALRSQNltksTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDC 156
Cdd:COG3883 100 GSvsyldVLLGSESFSDFLDRLSALSKIADADA----DLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175
|
170 180
....*....|....*....|....
gi 2462625355 157 TIRDLRNEVEKLRNEVNEREKAME 180
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLA 199
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
12-338 |
2.10e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 12 ERIQALEEDLREKEREIatekknslkrdkaiqgLTMALKSKEKKVEELNSEIEKlsaafakarealqkAQTQEfqgsEDY 91
Cdd:TIGR02168 213 ERYKELKAELRELELAL----------------LVLRLEELREELEELQEELKE--------------AEEEL----EEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 92 ETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNE 171
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 172 VNEREKAME------NRYKSLLSESNKKLHNQEQVIKHL-TESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEG 244
Cdd:TIGR02168 339 LAELEEKLEelkeelESLEAELEELEAELEELESRLEELeEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 245 LITEKCSSQQPPGSKtifsKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQEsdsinnLQAELNKIFALRKQLEQDVLSYQ 324
Cdd:TIGR02168 419 LQQEIEELLKKLEEA----ELKELQAELEELEEELEELQEELERLEEALEE------LREELEEAEQALDAAERELAQLQ 488
|
330
....*....|....
gi 2462625355 325 NLRKTLEEQISEIR 338
Cdd:TIGR02168 489 ARLDSLERLQENLE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1117-1375 |
2.43e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1117 LMEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELhSSLTSEIHFLRKQNQALNAMLikgsRDKQ 1196
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI-EELEAQIEQLKEELKALREAL----DELR 809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1197 KENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLL 1276
Cdd:TIGR02168 810 AELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1277 QSLRvelKAYEKLDEEHRRLREASGEgwkgqdpfrdlhsLLMEIQALRLQLERSIETSSTLQSRLKEQLARGAEKAQega 1356
Cdd:TIGR02168 890 ALLR---SELEELSEELRELESKRSE-------------LRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYS--- 950
|
250
....*....|....*....
gi 2462625355 1357 LTLAVQAVSIPEVPLQPDK 1375
Cdd:TIGR02168 951 LTLEEAEALENKIEDDEEE 969
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
6-193 |
4.06e-06 |
|
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: 51.66 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 6 ERNSFQERIQaLEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVeelnseieklsaafakaREALQKAQTQEF 85
Cdd:pfam17380 345 ERERELERIR-QEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERV-----------------RQELEAARKVKI 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 86 QGSEDYETALSGKEALSAALRSQNLTKSTENHRLR----RSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDl 161
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEeeraREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRD- 485
|
170 180 190
....*....|....*....|....*....|..
gi 2462625355 162 RNEVEKLRNEVNEREkaMENRYKSLLSESNKK 193
Cdd:pfam17380 486 RKRAEEQRRKILEKE--LEERKQAMIEEERKR 515
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-198 |
6.50e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 6.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNsfQERIQALEEDL---REKEREIATEKKnslkrdkAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQ 78
Cdd:PRK02224 226 EEQREQA--RETRDEADEVLeehEERREELETLEA-------EIEDLRETIAETEREREELAEEVRDLRERLEELEEERD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 79 KAQTQEFQGSEDYETALSGKEALSAAL----------RSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAH 148
Cdd:PRK02224 297 DLLAEAGLDDADAEAVEARREELEDRDeelrdrleecRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462625355 149 REKSKGDCTIRDLRNEVEKLRNEVNEREKAMEN--RYKSLLSESNKKLHNQE 198
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNaeDFLEELREERDELRERE 428
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1122-1354 |
6.86e-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: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1122 QEIRTLRKRLEESIKTNEK--LRKQLERQGSEFVQGSTSIFASGSELHSsLTSEIHFLRKQNQALNAMLikgsRDKQKEN 1199
Cdd:TIGR02168 216 KELKAELRELELALLVLRLeeLREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEI----EELQKEL 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1200 DKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQSL 1279
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462625355 1280 RvelKAYEKLDEEHRRLREASGEgwkgqdPFRDLHSLLMEIQALRLQLERSIETSSTLQSRLKEQLARGAEKAQE 1354
Cdd:TIGR02168 371 E---SRLEELEEQLETLRSKVAQ------LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
4-345 |
7.77e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.83 E-value: 7.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIaTEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQ 83
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEI-EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 84 EFQGSEDYETALSGKEALSAALRSQNLTKstENHRLRRSIKKITQELSDLQQER-----ERLEKDLEEAHREKSKGDCTI 158
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELE--ERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 159 RDLRNEVEKLRNEVNEREKAM------------------ENRYKSLLSESNKKLHNQEQVIKHLTESTNQ---KDVLLQK 217
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIeelkkakgkcpvcgreltEEHRKELLEEYTAELKRIEKELKEIEEKERKlrkELRELEK 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 218 FNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCssqqppgsktifskeKKQSSDYEELiqvlkKEqdiythlvKSLQESD 297
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNLEEL---------------EKKAEEYEKL-----KE--------KLIKLKG 539
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2462625355 298 SINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEESF 345
Cdd:PRK03918 540 EIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESV 587
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2-228 |
8.11e-06 |
|
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: 50.79 E-value: 8.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKlsaafakarealQKAQ 81
Cdd:TIGR04523 402 NQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES------------LETQ 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 82 TQEFQGSedYETALSGKEALSAALRSqnltKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDL 161
Cdd:TIGR04523 470 LKVLSRS--INKIKQNLEQKQKELKS----KEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDL 543
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462625355 162 RNEVEKLRNEVNerekamENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQ 228
Cdd:TIGR04523 544 EDELNKDDFELK------KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKE 604
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
5-237 |
9.06e-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: 50.83 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 5 KERNSFQERIQALEEdlREKEREIATEKKNSLKrdKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQE 84
Cdd:TIGR02168 667 KTNSSILERRREIEE--LEEKIEELEEKIAELE--KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEV 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 85 FQGSEDY---ETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDL 161
Cdd:TIGR02168 743 EQLEERIaqlSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462625355 162 RNEVEKLRNEVNEREKAMENryksLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAED 237
Cdd:TIGR02168 823 RERLESLERRIAATERRLED----LEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
4-146 |
1.18e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIATEKKNsLKRDKAIQGltMALKSKEkkVEELNSEIEKLSAAFAKAREALQKAQTQ 83
Cdd:COG1579 44 EARLEAAKTELEDLEKEIKRLELEIEEVEAR-IKKYEEQLG--NVRNNKE--YEALQKEIESLKRRISDLEDEILELMER 118
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462625355 84 EfqgsEDYETALSGKEALSAALRSQNLTKSTEnhrLRRSIKKITQELSDLQQERERLEKDLEE 146
Cdd:COG1579 119 I----EELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAEREELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
12-343 |
1.28e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 12 ERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGS--E 89
Cdd:PRK03918 224 EKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEfyE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 90 DYETALSGKEALSAALRSQN---LTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDcTIRDLR---- 162
Cdd:PRK03918 304 EYLDELREIEKRLSRLEEEIngiEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE-ELERLKkrlt 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 163 -NEVEKLRNEVNEREKAMENRYKSlLSESNKKLHNQEQVIKHLTESTNQkdvllqkfnekdLEVIQQNCYLMAAEDLELR 241
Cdd:PRK03918 383 gLTPEKLEKELEELEKAKEEIEEE-ISKITARIGELKKEIKELKKAIEE------------LKKAKGKCPVCGRELTEEH 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 242 SEGLITE--KCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDiythLVKSLQESDSINNLQAELNKIFAlrKQLEQD 319
Cdd:PRK03918 450 RKELLEEytAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE----LIKLKELAEQLKELEEKLKKYNL--EELEKK 523
|
330 340
....*....|....*....|....
gi 2462625355 320 VLSYQNLRKTLEEQISEIRRREEE 343
Cdd:PRK03918 524 AEEYEKLKEKLIKLKGEIKSLKKE 547
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2-398 |
1.53e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQgltmALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQ 81
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE----AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 82 TQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQEL---------SDLQQERERLEKDLEEAHR--- 149
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAkkadeakkkAEEAKKAEEAKKKAEEAKKade 1474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 150 ------EKSKGDctirDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKhlTESTNQKDVLLQKFNEKDL 223
Cdd:PTZ00121 1475 akkkaeEAKKAD----EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK--AEEAKKADEAKKAEEKKKA 1548
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 224 EVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQssdYEELIQVLKKEQDIYTHLVKSLQE----SDSI 299
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEAR---IEEVMKLYEEEKKMKAEEAKKAEEakikAEEL 1625
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 300 NNLQAELNKIFALRKQLEQDVLSYQNLRKTLEE---QISEIRRREEESfslySDQTSYLSICLEENNRFQVEHFSQEELK 376
Cdd:PTZ00121 1626 KKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkiKAAEEAKKAEED----KKKAEEAKKAEEDEKKAAEALKKEAEEA 1701
|
410 420
....*....|....*....|..
gi 2462625355 377 KKVSDLIQLVKELYTDNQHLKK 398
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEELKK 1723
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
12-398 |
1.61e-05 |
|
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: 49.72 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 12 ERIQALEED----LREKEREIA------TEKKNSLK---------RDKAIQgLTMALKSKEKKVEELNSEIEKLSAAFAK 72
Cdd:pfam05483 222 EKIQHLEEEykkeINDKEKQVSllliqiTEKENKMKdltflleesRDKANQ-LEEKTKLQDENLKELIEKKDHLTKELED 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 73 AREALQKAQTQEFQGSEDYETALSGKEALSAALRSQ--NLTKSTENHRLRRSIKKIT----QELsdLQQERERLEKDLEE 146
Cdd:pfam05483 301 IKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQmeELNKAKAAHSFVVTEFEATtcslEEL--LRTEQQRLEKNEDQ 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 147 ahrekskgdctIRDLRNEVEKLRNEVNEREKAMENR------YKSLLSESNKKLHNQEQVIKHLTE--STNQKDVLLQKF 218
Cdd:pfam05483 379 -----------LKIITMELQKKSSELEEMTKFKNNKeveleeLKKILAEDEKLLDEKKQFEKIAEElkGKEQELIFLLQA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 219 NEK---DLEV------IQQNCYLMAAEDL--ELRSEGLITEKCSSQqppgSKTIFSKEKKQSSDYEELIQVLKKEQDIYT 287
Cdd:pfam05483 448 REKeihDLEIqltaikTSEEHYLKEVEDLktELEKEKLKNIELTAH----CDKLLLENKELTQEASDMTLELKKHQEDII 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 288 HLVKslQESDSINNLQAELNKIFALRKQLEqdvlsyqNLRKTLEEQISEIRRREEESfslYSDQTSYLSICLEENNRFQV 367
Cdd:pfam05483 524 NCKK--QEERMLKQIENLEEKEMNLRDELE-------SVREEFIQKGDEVKCKLDKS---EENARSIEYEVLKKEKQMKI 591
|
410 420 430
....*....|....*....|....*....|.
gi 2462625355 368 EHFSQEELKKKVSDLIQLVKELYTDNQHLKK 398
Cdd:pfam05483 592 LENKCNNLKKQIENKNKNIEELHQENKALKK 622
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
21-216 |
1.68e-05 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 48.60 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 21 LREKEREIATEKKNSLKRD-KAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYEtalsgke 99
Cdd:pfam09787 20 LQSKEKLIASLKEGSGVEGlDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSR------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 100 alsaalrsQNLTKSTENHRLRRSIKKITQ-ELSDLQQERERLEkdlEEAHREKSKGDCTIRDLRNEVEKLRNEVNEreka 178
Cdd:pfam09787 93 --------EQLQELEEQLATERSARREAEaELERLQEELRYLE---EELRRSKATLQSRIKDREAEIEKLRNQLTS---- 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 2462625355 179 menryKSLLSESNKKLhnqEQVIKHLTESTNQKDVLLQ 216
Cdd:pfam09787 158 -----KSQSSSSQSEL---ENRLHQLTETLIQKQTMLE 187
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1120-1360 |
1.75e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1120 HIQEIRTLRKRLEESIKTNEKLRKQLERQGSEfvqgstsifasgselhssLTSEIHFLRKQNQALNAMLikgsRDKQKEN 1199
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAE------------------LEAELEELRLELEELELEL----EEAQAEE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1200 DKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELK-LRQQLLSQNDKLLQS 1278
Cdd:COG1196 291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1279 LRVELKAYEKLDEEHRRLREASGEgwkgqdpfrdlhslLMEIQALRLQLERSIETSSTLQSRLKEQLARGAEKAQEGALT 1358
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRA--------------AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEE 436
|
..
gi 2462625355 1359 LA 1360
Cdd:COG1196 437 EE 438
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1047-1370 |
3.35e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.91 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1047 EMNTQNELMERIEEDNLTYQHLLPEspepsashaLSDYETSEKSffsrDQKQDNETEKTSVMVNSFSQDLLMEHIQ-EIR 1125
Cdd:TIGR02169 195 EKRQQLERLRREREKAERYQALLKE---------KREYEGYELL----KEKEALERQKEAIERQLASLEEELEKLTeEIS 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1126 TLRKRLEESIKTNEKLRKQLERQGS-EFVQGSTSIFASGSELhSSLTSEIHFLRKQNQALNAMLIKG--SRDKQK-ENDK 1201
Cdd:TIGR02169 262 ELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEI-ASLERSIAEKERELEDAEERLAKLeaEIDKLLaEIEE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1202 LRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQSLRV 1281
Cdd:TIGR02169 341 LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1282 ELK----AYEKLDEEHRRLREASGEgwkGQDPFRDLHSLLMEIQALRLQLERSIETSSTLQSRLKEQLargAEKAQEGAL 1357
Cdd:TIGR02169 421 ELAdlnaAIAGIEAKINELEEEKED---KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL---SKLQRELAE 494
|
330
....*....|...
gi 2462625355 1358 TLAVQAVSIPEVP 1370
Cdd:TIGR02169 495 AEAQARASEERVR 507
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
4-344 |
3.56e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 48.31 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIA----TEKKNSlkrdKAIQGLtmalkskEKKVEELNSEIEKLSAAFAKAREALQK 79
Cdd:pfam06160 85 KKALDEIEELLDDIEEDIKQILEELDelleSEEKNR----EEVEEL-------KDKYRELRKTLLANRFSYGPAIDELEK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 80 AQTQEFQGSEDYETALSGKEALSAalRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHRE-KSKG---- 154
Cdd:pfam06160 154 QLAEIEEEFSQFEELTESGDYLEA--REVLEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREmEEEGyale 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 155 ----DCTIRDLRNEVEKLRN--------EVNEREKAMENR----YKSLLSESNKK---LHNQEQVIKHLTESTNQKDVLL 215
Cdd:pfam06160 232 hlnvDKEIQQLEEQLEENLAllenleldEAEEALEEIEERidqlYDLLEKEVDAKkyvEKNLPEIEDYLEHAEEQNKELK 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 216 qkfneKDLEVIQQNcYLMAAEDLElrseglitekcSSQQppgsktiFSKE-KKQSSDYEELIQVLKKEQDIYTHLVKSLQ 294
Cdd:pfam06160 312 -----EELERVQQS-YTLNENELE-----------RVRG-------LEKQlEELEKRYDEIVERLEEKEVAYSELQEELE 367
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2462625355 295 ES-DSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEES 344
Cdd:pfam06160 368 EIlEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKLELREIKRLVEKS 418
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2-228 |
3.59e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 48.58 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLsaafakarEALQKAQ 81
Cdd:pfam15921 367 QFSQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRL--------EALLKAM 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 82 TQEFQGS-EDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQErERLEKDLEEAHREKSKGdctIRD 160
Cdd:pfam15921 439 KSECQGQmERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESS-ERTVSDLTASLQEKERA---IEA 514
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 161 LRNEVEKLRNEVNEREKAMENryksllsesnkkLHNQEQvikHLTESTNQKDVLLQKFNEKD--LEVIQQ 228
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQELQH------------LKNEGD---HLRNVQTECEALKLQMAEKDkvIEILRQ 569
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
123-343 |
3.94e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 123 IKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAmenrykslLSESNKKLHNQEQVIK 202
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAE--------EYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 203 HLTESTNQKDVLLQKfNEKDLEVIQQNCYLMAAEDLELRSEGL-ITEKCSSQQppgsKTIFSKEKKQSSDYEELIQVLKK 281
Cdd:COG1196 306 RLEERRRELEERLEE-LEEELAELEEELEELEEELEELEEELEeAEEELEEAE----AELAEAEEALLEAEAELAEAEEE 380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462625355 282 EQDIYTHLVKSLQES----DSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEE 343
Cdd:COG1196 381 LEELAEELLEALRAAaelaAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
5-186 |
4.02e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.84 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 5 KERNSFQERIQALEEDLREKEREIATEKknslkrdKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQe 84
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALE-------ARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 85 fqgsEDYetalsgkEALSAALRSQNLTKSTENHRLRR---SIKKITQELSDLQQERERLEKDLEEAHREKskgDCTIRDL 161
Cdd:COG1579 89 ----KEY-------EALQKEIESLKRRISDLEDEILElmeRIEELEEELAELEAELAELEAELEEKKAEL---DEELAEL 154
|
170 180
....*....|....*....|....*
gi 2462625355 162 RNEVEKLRNEVNEREKAMENRYKSL 186
Cdd:COG1579 155 EAELEELEAEREELAAKIPPELLAL 179
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1121-1363 |
4.63e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.39 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1121 IQEIRTLRKRLEESIKTNEKLRKQLERQGSEfvqgstsifasgselhssLTSEIHFLRKQNQALNAMLikgsRDKQKEND 1200
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEE------------------LEEELEELEEELEEAEEEL----EEAEAELA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1201 KLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQevrcsgQELSRVQEELKLRQQLLSQNDKLLQSLR 1280
Cdd:COG1196 362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE------AEEALLERLERLEEELEELEEALAELEE 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1281 VELKAYEKLDEEHRRLREASGEGWKGQDPFRDLHSLLMEIQALRLQLERSIETSSTLQSRLKEQLARGAEKAQEGALTLA 1360
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
...
gi 2462625355 1361 VQA 1363
Cdd:COG1196 516 LAG 518
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
48-224 |
5.37e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 48 ALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQ--EFQGSEDYETALSGKEALSAALRSqnltKSTENHRLRRS--- 122
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERreALQRLAEYSWDEIDVASAEREIAE----LEAELERLDASsdd 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 123 IKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIK 202
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180
....*....|....*....|....
gi 2462625355 203 HLTESTNQKDVLLQKFN--EKDLE 224
Cdd:COG4913 767 LRENLEERIDALRARLNraEEELE 790
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
134-398 |
5.43e-05 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 48.04 E-value: 5.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 134 QQERERLEKDLEEAHREKSKgdctIRDLRNEVEKLRNEVNEREKAMENRYKSL---LSESNKKLHNQEQVIKHLTESTNQ 210
Cdd:pfam02463 169 RKKKEALKKLIEETENLAEL----IIDLEELKLQELKLKEQAKKALEYYQLKEkleLEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 211 KDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEglitEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLV 290
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE----EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 291 KSLQesdsinNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEESFSLYSDQTSYLSICLEENNRFQVEHF 370
Cdd:pfam02463 321 KEKK------KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260
....*....|....*....|....*...
gi 2462625355 371 SQEELKKKVSDLIQLVKELYTDNQHLKK 398
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLK 422
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
3-125 |
6.15e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 3 HQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQT 82
Cdd:COG4913 329 EAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALA 408
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2462625355 83 QEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKK 125
Cdd:COG4913 409 EAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
37-192 |
7.21e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 7.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 37 KRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRS-------QN 109
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnkeyEA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 110 LTKSTENhrLRRSIKKITQELSDLQQERERLEKDLEEAHREkskgdctIRDLRNEVEKLRNEVNEREKAMENRYKSLLSE 189
Cdd:COG1579 94 LQKEIES--LKRRISDLEDEILELMERIEELEEELAELEAE-------LAELEAELEEKKAELDEELAELEAELEELEAE 164
|
...
gi 2462625355 190 SNK 192
Cdd:COG1579 165 REE 167
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
4-153 |
7.86e-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: 47.07 E-value: 7.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQ------GLTMALKSKE--------KKVEELNSEIEKLSAA 69
Cdd:COG4942 75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgrqpPLALLLSPEDfldavrrlQYLKYLAPARREQAEE 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 70 FAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHR 149
Cdd:COG4942 155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
|
....
gi 2462625355 150 EKSK 153
Cdd:COG4942 235 EAAA 238
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
4-389 |
1.04e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERiQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEI-EKLSAAFAKArEALQKAQT 82
Cdd:PRK01156 335 QKDYNDYIKK-KSRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFIsEILKIQEIDP-DAIKKELN 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 83 QEFQGSEDYETALSGKEALSAALRsQNLTKSTENHRLR--RSI----------KKITQELSDLQQERERLEKDLEEAHRE 150
Cdd:PRK01156 413 EINVKLQDISSKVSSLNQRIRALR-ENLDELSRNMEMLngQSVcpvcgttlgeEKSNHIINHYNEKKSRLEEKIREIEIE 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 151 KSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSEsnkkLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQN- 229
Cdd:PRK01156 492 VKDIDEKIVDLKKRKEYLESEEINKSINEYNKIESARAD----LEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSKr 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 230 ---CYLMAAEDLelrsegLITEKCSSQqppgsktiFSKEKKQSSDYEELIQVLKKE-QDIYTHLVKSLQE-SDSINNLQA 304
Cdd:PRK01156 568 tswLNALAVISL------IDIETNRSR--------SNEIKKQLNDLESRLQEIEIGfPDDKSYIDKSIREiENEANNLNN 633
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 305 ELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEESFSLYSDQTSYLSIcleeNNRFQVEHFSQEELKKKVSDLIQ 384
Cdd:PRK01156 634 KYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKS----RKALDDAKANRARLESTIEILRT 709
|
....*
gi 2462625355 385 LVKEL 389
Cdd:PRK01156 710 RINEL 714
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2-176 |
1.07e-04 |
|
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: 46.81 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDlREKEREIATEKKNSLKRDKA-----IQGLTMALKSKEKKVEEL---NSEIEKLSAAFAKA 73
Cdd:pfam07888 38 ECLQERAELLQAQEAANRQ-REKEKERYKRDREQWERQRRelesrVAELKEELRQSREKHEELeekYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 74 REALQKAQtqefqgsEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREksk 153
Cdd:pfam07888 117 KDALLAQR-------AAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEE--- 186
|
170 180
....*....|....*....|...
gi 2462625355 154 gdctIRDLRNEVEKLRNEVNERE 176
Cdd:pfam07888 187 ----LRSLSKEFQELRNSLAQRD 205
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-403 |
1.11e-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: 46.98 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 118 RLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKL---RNEVNEREKAMENRykslLSESNKKL 194
Cdd:TIGR02169 678 RLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLeqeEEKLKERLEELEED----LSSLEQEI 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 195 HNQEQVIKHLTESTNQKdvllqkfnEKDLEVIQQncylmAAEDLELRSeglitekcssqqppgSKTIFSKEKKQSSDYEE 274
Cdd:TIGR02169 754 ENVKSELKELEARIEEL--------EEDLHKLEE-----ALNDLEARL---------------SHSRIPEIQAELSKLEE 805
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 275 LIQVLKKeqdiythlvkslqesdSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEEsfsLYSDQTSY 354
Cdd:TIGR02169 806 EVSRIEA----------------RLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN---LNGKKEEL 866
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2462625355 355 LSIclEENNRFQVEHFSQE--ELKKKVSDLIQLVKELYTDNQHLKKTIFDL 403
Cdd:TIGR02169 867 EEE--LEELEAALRDLESRlgDLKKERDELEAQLRELERKIEELEAQIEKK 915
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2-400 |
1.24e-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: 46.94 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQ 81
Cdd:TIGR04523 222 ELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLN 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 82 TQEFQGsedyetalsgkeaLSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDL 161
Cdd:TIGR04523 302 NQKEQD-------------WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEK 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 162 RNEVEKLRNEVNEREKAMENryksLLSESNkklhNQEQVIKHLTESTNQKDVLLQKFnEKDLEVIQQNCYLMAAEDLELR 241
Cdd:TIGR04523 369 QNEIEKLKKENQSYKQEIKN----LESQIN----DLESKIQNQEKLNQQKDEQIKKL-QQEKELLEKEIERLKETIIKNN 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 242 SE-GLITEKCSSQQPPGSKTIFSKE--KKQSSDYEELIQVLKKEQDIYT-HLVKSLQESDSINNLQAEL-NKIFALRKQL 316
Cdd:TIGR04523 440 SEiKDLTNQDSVKELIIKNLDNTREslETQLKVLSRSINKIKQNLEQKQkELKSKEKELKKLNEEKKELeEKVKDLTKKI 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 317 EQDVLSYQNLRKTLEEQISEIRRREEESFSLYSDQT-SYLSICLEENNRFQVE-HFSQEELKKKVSDLIQLVKELYTDNQ 394
Cdd:TIGR04523 520 SSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKkENLEKEIDEKNKEIEElKQTQKSLKKKQEEKQELIDQKEKEKK 599
|
....*.
gi 2462625355 395 HLKKTI 400
Cdd:TIGR04523 600 DLIKEI 605
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
54-194 |
1.25e-04 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 44.54 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 54 KKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGK-----EALSAALRSQN------LTKSTENHRLRRS 122
Cdd:pfam08614 14 DRTALLEAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEQLlaqlrEELAELYRSRGelaqrlVDLNEELQELEKK 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462625355 123 IKKITQELSDLQQERERLE---KDLEEAHREKSKGdctIRDLRNEVEKLRNEVNEREKAMENrykslLSESNKKL 194
Cdd:pfam08614 94 LREDERRLAALEAERAQLEeklKDREEELREKRKL---NQDLQDELVALQLQLNMAEEKLRK-----LEKENREL 160
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
49-321 |
1.32e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 49 LKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSEDYETALSGKEALSAALRSqnltKSTENHRLRRSIKKITQ 128
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES----LQEEAEELQEELEELQK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 129 ELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQ--EQVIKHLTE 206
Cdd:COG4372 123 ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEanRNAEKEEEL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 207 STNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIY 286
Cdd:COG4372 203 AEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAA 282
|
250 260 270
....*....|....*....|....*....|....*
gi 2462625355 287 THLVKSLQESDSINNLQAELNKIFALRKQLEQDVL 321
Cdd:COG4372 283 LELEALEEAALELKLLALLLNLAALSLIGALEDAL 317
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
118-340 |
1.53e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.60 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 118 RLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAME--NRYKSLLSESNKKLH 195
Cdd:PRK03918 176 RRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeiEELEKELESLEGSKR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 196 NQEQVIKHLTESTNQKDVLLQKFNEK--DLEVIQQ------------NCYLMAAEDLELRSEGLitekcsSQQPPGSKTI 261
Cdd:PRK03918 256 KLEEKIRELEERIEELKKEIEELEEKvkELKELKEkaeeyiklsefyEEYLDELREIEKRLSRL------EEEINGIEER 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 262 FSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDSINNLQAELNKIFALRK-----QLEQDVLSYQNLRKTLEEQISE 336
Cdd:PRK03918 330 IKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEIEEEISK 409
|
....
gi 2462625355 337 IRRR 340
Cdd:PRK03918 410 ITAR 413
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
42-204 |
1.89e-04 |
|
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: 44.92 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 42 IQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQefqgSEDYETALSGKEALSAALRsQNLTKSTE---NHR 118
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE----LEDLEKEIKRLELEIEEVE-ARIKKYEEqlgNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 119 LRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQE 198
Cdd:COG1579 87 NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*.
gi 2462625355 199 QVIKHL 204
Cdd:COG1579 167 ELAAKI 172
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
10-388 |
1.93e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 46.26 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 10 FQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLT--------MALKSKEKKVEELNSE--------IEKLSAAFAKA 73
Cdd:pfam15921 215 FRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKsesqnkieLLLQQHQDRIEQLISEheveitglTEKASSARSQA 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 74 ---REALQKAQTQEFQGSEDYETALSGKEALSAALRSQnltkstenhrLRRSIKKITQELSDLQQERERLEKDLEEAHRE 150
Cdd:pfam15921 295 nsiQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSE----------LREAKRMYEDKIEELEKQLVLANSELTEARTE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 151 KSKGDCTIRDLRNEVEKLRNEVNEREKAMenrykSLLSESNKKLHNQEqvikhlTESTNQKDVLLQKFNEKDLEVIQQNC 230
Cdd:pfam15921 365 RDQFSQESGNLDDQLQKLLADLHKREKEL-----SLEKEQNKRLWDRD------TGNSITIDHLRRELDDRNMEVQRLEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 231 YLMAaedLELRSEGLITEKCSSQQppGSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESD-SINNLQAELNKi 309
Cdd:pfam15921 434 LLKA---MKSECQGQMERQMAAIQ--GKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSErTVSDLTASLQE- 507
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462625355 310 faLRKQLEQDVLSYQNLRKTLEEQISEIRRREEESFSLYSDQTSYLSICLEENNRFQVehfsQEELKKKVSDLIQLVKE 388
Cdd:pfam15921 508 --KERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKV----IEILRQQIENMTQLVGQ 580
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2-181 |
2.01e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIAT--EKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQK 79
Cdd:COG4717 85 EKEEEYAELQEELEELEEELEELEAELEElrEELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 80 AQTQEfqgsedyETALSGKEALSAALRSQNLTKStenhrlrrsikkitQELSDLQQERERLEKDLEEAHREkskgdctIR 159
Cdd:COG4717 165 LEELE-------AELAELQEELEELLEQLSLATE--------------EELQDLAEELEELQQRLAELEEE-------LE 216
|
170 180
....*....|....*....|..
gi 2462625355 160 DLRNEVEKLRNEVNEREKAMEN 181
Cdd:COG4717 217 EAQEELEELEEELEQLENELEA 238
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-174 |
3.01e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.68 E-value: 3.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKE-KKVEELNSEIEKLSAAFAKAREALQKa 80
Cdd:COG4913 285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRAR- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 81 qtqefqgsedyetalsgkeaLSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKskgdctiRD 160
Cdd:COG4913 364 --------------------LEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAAL-------RD 416
|
170
....*....|....
gi 2462625355 161 LRNEVEKLRNEVNE 174
Cdd:COG4913 417 LRRELRELEAEIAS 430
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
2-229 |
3.31e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.81 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKERE---IATEKKNSLKRDKAIQGLTMAlkskekkVEELNSEIEKLSAAFAKAREALQ 78
Cdd:TIGR01612 1552 EIKDAHKKFILEAEKSEQKIKEIKKEkfrIEDDAAKNDKSNKAAIDIQLS-------LENFENKFLKISDIKKKINDCLK 1624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 79 KAQTQEfqgsedyetalsgKEALSAALRSQNlTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEahrekskgdcti 158
Cdd:TIGR01612 1625 ETESIE-------------KKISSFSIDSQD-TELKENGDNLNSLQEFLESLKDQKKNIEDKKKELDE------------ 1678
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462625355 159 rdLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKdvLLQKFNEKDLEVIQQN 229
Cdd:TIGR01612 1679 --LDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKEEIESIKELIEPTIEN--LISSFNTNDLEGIDPN 1745
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
14-341 |
3.43e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 45.42 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 14 IQALEEDLREKEREIATE--KKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQ-GSEd 90
Cdd:TIGR00606 794 MERFQMELKDVERKIAQQaaKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElKSE- 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 91 yETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQErerLEKDLEEAHREKSKGDCTIRDLRNEVEKLRN 170
Cdd:TIGR00606 873 -KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETF---LEKDQQEKEELISSKETSNKKAQDKVNDIKE 948
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 171 EVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNekdleviqqncylmaaEDLELRSEGLITEKC 250
Cdd:TIGR00606 949 KVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKIN----------------EDMRLMRQDIDTQKI 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 251 SSQQPPGSKTIFSKEKKQSSDYEELIQVLKK-EQDIYTHLVKSLQE-SDSINNLQAELNKIFALRKQLEQDVLSYQNLRK 328
Cdd:TIGR00606 1013 QERWLQDNLTLRKRENELKEVEEELKQHLKEmGQMQVLQMKQEHQKlEENIDLIKRNHVLALGRQKGYEKEIKHFKKELR 1092
|
330
....*....|...
gi 2462625355 329 TLEEQISEIRRRE 341
Cdd:TIGR00606 1093 EPQFRDAEEKYRE 1105
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
22-403 |
4.38e-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: 45.01 E-value: 4.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 22 REKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLsaafakarealqkaqtqefqgsEDYETALSGKEAL 101
Cdd:TIGR04523 36 KQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKIL----------------------EQQIKDLNDKLKK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 102 SaalrSQNLTKSTEN-HRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAME 180
Cdd:TIGR04523 94 N----KDKINKLNSDlSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 181 NrYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLL---QKFNEKDLEVIQQncylmaAEDLELRSEGLITEKCSSQQppg 257
Cdd:TIGR04523 170 E-LENELNLLEKEKLNIQKNIDKIKNKLLKLELLLsnlKKKIQKNKSLESQ------ISELKKQNNQLKDNIEKKQQ--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 258 skTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDSINNLQAELNK--------IFALRKQLEQDVLSY-QNLRK 328
Cdd:TIGR04523 240 --EINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKqlnqlkseISDLNNQKEQDWNKElKSELK 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462625355 329 TLEEQISEIRRREEESFSLYSDQTSYLSICLEENNRFQVEHFS-QEELKKKVSDLIQLVKElytdNQHLKKTIFDL 403
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEkQRELEEKQNEIEKLKKE----NQSYKQEIKNL 389
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
4-171 |
4.53e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 4.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQ 83
Cdd:pfam01576 151 SKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQ 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 84 efqgSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERlekdlEEAHREKSKGDCtiRDLRN 163
Cdd:pfam01576 231 ----IAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLES-----ERAARNKAEKQR--RDLGE 299
|
....*...
gi 2462625355 164 EVEKLRNE 171
Cdd:pfam01576 300 ELEALKTE 307
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1-388 |
4.66e-04 |
|
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: 45.10 E-value: 4.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1 MEHQKERNSFQE--RIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQ 78
Cdd:pfam05483 384 MELQKKSSELEEmtKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIK 463
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 79 KAQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENhrlrrsiKKITQELSDLQQERERLEKDLEEAHREKSKGDCTI 158
Cdd:pfam05483 464 TSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN-------KELTQEASDMTLELKKHQEDIINCKKQEERMLKQI 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 159 RDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFN--EKDLEVIQQNCYLMAAE 236
Cdd:pfam05483 537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNnlKKQIENKNKNIEELHQE 616
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 237 DLELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKK--------EQDIYTHLVKSLQESDSINNLQAELN- 307
Cdd:pfam05483 617 NKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKeiedkkisEEKLLEEVEKAKAIADEAVKLQKEIDk 696
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 308 ----KIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEESFSLYSDQTSYLSICLEE----NNRFQVEHFSQEELKKKV 379
Cdd:pfam05483 697 rcqhKIAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAEllslKKQLEIEKEEKEKLKMEA 776
|
....*....
gi 2462625355 380 SDLIQLVKE 388
Cdd:pfam05483 777 KENTAILKD 785
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
53-340 |
5.67e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 53 EKKVEELNSEIEKLSAAFAKAREALQKAQTQefqgsedyetalsgKEALSAalRSQNLTKSTENHRLRRSIKKITQELSD 132
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAE--------------LDALQE--RREALQRLAEYSWDEIDVASAEREIAE 672
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 133 LQQERERLEK---DLEEAHREKSKgdctIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKhltestN 209
Cdd:COG4913 673 LEAELERLDAssdDLAALEEQLEE----LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAED------L 742
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 210 QKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLitekcssqqppgsktifskEKKQSSDYEELIQVLKKEQDIYTHL 289
Cdd:COG4913 743 ARLELRALLEERFAAALGDAVERELRENLEERIDAL-------------------RARLNRAEEELERAMRAFNREWPAE 803
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462625355 290 VKSLQES-DSINNLQAELNKI-----------F--ALRKQLEQDVLsyqNLRKTLEEQISEIRRR 340
Cdd:COG4913 804 TADLDADlESLPEYLALLDRLeedglpeyeerFkeLLNENSIEFVA---DLLSKLRRAIREIKER 865
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
19-206 |
5.69e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 19 EDLREKEREIATEKKNSLKRDKAIQGLTMALKSK---EKKVEELNSEIEKLSAafaKAREALQKAQTQEFQGSEDYETAL 95
Cdd:PRK03918 518 EELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKKLDELEE---ELAELLKELEELGFESVEELEERL 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 96 SGKEALsaalrsqnltkstenHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNER 175
Cdd:PRK03918 595 KELEPF---------------YNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEE 659
|
170 180 190
....*....|....*....|....*....|..
gi 2462625355 176 E-KAMENRYKSLLSESNKKLHNQEQVIKHLTE 206
Cdd:PRK03918 660 EyEELREEYLELSRELAGLRAELEELEKRREE 691
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2-147 |
5.97e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.52 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIA---TEKKNSLKRDkaIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQ 78
Cdd:COG4913 306 RLEAELERLEARLDALREELDELEAQIRgngGDRLEQLERE--IERLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462625355 79 KAQTQefqgsedYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEA 147
Cdd:COG4913 384 ALRAE-------AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLAL 445
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
67-225 |
6.13e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 6.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 67 SAAFAKAR------EALQKAQTQEFQGSEDYETALSGKEALSAALRsqnlTKSTENHRLRRSIKKITQELSD----LQQE 136
Cdd:PRK00409 488 SNAFEIAKrlglpeNIIEEAKKLIGEDKEKLNELIASLEELERELE----QKAEEAEALLKEAEKLKEELEEkkekLQEE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 137 RERLEKDLEEAHRE-----KSKGDCTIRDLRNEVEKLRNEVNERE-----KAMENRYKSLLSESNKKLHNQEQV-----I 201
Cdd:PRK00409 564 EDKLLEEAEKEAQQaikeaKKEADEIIKELRQLQKGGYASVKAHEliearKRLNKANEKKEKKKKKQKEKQEELkvgdeV 643
|
170 180
....*....|....*....|....
gi 2462625355 202 KHLteSTNQKDVLLQKFNEKDLEV 225
Cdd:PRK00409 644 KYL--SLGQKGEVLSIPDDKEAIV 665
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
9-170 |
7.52e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.08 E-value: 7.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 9 SFQERIQALEEDLREKEREiaTEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALqkaqtqefqgs 88
Cdd:COG2433 377 SIEEALEELIEKELPEEEP--EAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERI----------- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 89 EDYETALSgkealsaalrsqnLTKSTENHRLRRSikkitQELSDLQQERERLEKDLEEAHREkskgdctIRDLRNEVEKL 168
Cdd:COG2433 444 ERLERELS-------------EARSEERREIRKD-----REISRLDREIERLERELEEERER-------IEELKRKLERL 498
|
..
gi 2462625355 169 RN 170
Cdd:COG2433 499 KE 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
4-181 |
7.95e-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: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLrekeREIATEKKNSLKRDKAIQGLTMA------LKSKEKKVEELNSEIEKLSAA---FAKAR 74
Cdd:COG4913 616 EAELAELEEELAEAEERL----EALEAELDALQERREALQRLAEYswdeidVASAEREIAELEAELERLDASsddLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 75 EALQKAQtQEFQGSEDYETALSGKEAlsaalrsqnlTKSTENHRLRRSIKKITQELSDL-----QQERERLEKDLEEAHR 149
Cdd:COG4913 692 EQLEELE-AELEELEEELDELKGEIG----------RLEKELEQAEEELDELQDRLEAAedlarLELRALLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|..
gi 2462625355 150 EKSKGDcTIRDLRNEVEKLRNEVNEREKAMEN 181
Cdd:COG4913 761 DAVERE-LRENLEERIDALRARLNRAEEELER 791
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
5-318 |
8.40e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 44.04 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 5 KER--NSFQERIQALEEDLREKEREIATEKK-------NSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKARE 75
Cdd:pfam10174 392 KERkiNVLQKKIENLQEQLRDKDKQLAGLKErvkslqtDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 76 AL--------QKAQTQEFQGSEDYETALSGKEALSaALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEkDLEEA 147
Cdd:pfam10174 472 SLkkenkdlkEKVSALQPELTEKESSLIDLKEHAS-SLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAH-NAEEA 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 148 HREKSKGDCTIRDLRNEVEKLRNEVNEREKAMEnRYKSLLSESNKKLHNQEQVIKHLtESTNQKDVLLQKFNEKDLEVIQ 227
Cdd:pfam10174 550 VRTNPEINDRIRLLEQEVARYKEESGKAQAEVE-RLLGILREVENEKNDKDKKIAEL-ESLTLRQMKEQNKKVANIKHGQ 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 228 QNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQssdyeeliQVLKKEQDIYTHLVKSLQESDSI-NNLQAEl 306
Cdd:pfam10174 628 QEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKTR--------QELDATKARLSSTQQSLAEKDGHlTNLRAE- 698
|
330
....*....|..
gi 2462625355 307 nkifaLRKQLEQ 318
Cdd:pfam10174 699 -----RRKQLEE 705
|
|
| ALIX_LYPXL_bnd |
pfam13949 |
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV ... |
57-210 |
1.17e-03 |
|
ALIX V-shaped domain binding to HIV; The binding of the LYPxL motif of late HIV p6Gag and EIAV p9Gag to this domain is necessary for viral budding.This domain is generally central between an N-terminal Bro1 domain, pfam03097 and a C-terminal proline-rich domain. The retroviruses thus used this domain to hijack the ESCRT system of the cell.
Pssm-ID: 464053 [Multi-domain] Cd Length: 294 Bit Score: 42.99 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 57 EELNSEIEKLSAAFAKAREALQKAQtQEFQGSEDYETALSG-KEALSAALRSQNLTKSTEN-HRLRRSIKKITQELSDLQ 134
Cdd:pfam13949 75 ATLRAEIRKYREILEQASESDSQVR-SKFREHEEDLELLSGpDEDLEAFLPSSRRAKNSPSvEEQVAKLRELLNKLNELK 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 135 QERERLEKDLeeahREKSKGDctirDLRNEV--EKLRNEVNEREKAMENR----YKSLLSESNKKLHNQEQVIKHLTEST 208
Cdd:pfam13949 154 REREQLLKDL----KEKARND----DISPKLllEKARLIAPNQEEQLFEEelekYDPLQNRLEQNLHKQEELLKEITEAN 225
|
..
gi 2462625355 209 NQ 210
Cdd:pfam13949 226 NE 227
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2-79 |
1.37e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 1.37e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSaafAKAREALQK 79
Cdd:PRK12704 72 EFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI---EEQLQELER 146
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1081-1295 |
1.41e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 43.57 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1081 LSDYETSEKSFfsRDQKQDNETEKTSVMVNSFSQDLLMEHIQEIRTLRKRLEESIKT-NEKLRKQLERQGSEfVQGSTSI 1159
Cdd:pfam15921 383 LADLHKREKEL--SLEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAmKSECQGQMERQMAA-IQGKNES 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1160 FASGSELHSSLTSEIHFLRKQNQALNAmlikgsrdKQKENDKLRESLSRKTVSLEHLQReyaSVKEENERLQKEGSEKER 1239
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTA--------KKMTLESSERTVSDLTASLQEKER---AIEATNAEITKLRSRVDL 528
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2462625355 1240 HNQQLiQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQSLRVELKAYEKLDEEHRR 1295
Cdd:pfam15921 529 KLQEL-QHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGR 583
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
4-196 |
1.50e-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: 43.51 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQT- 82
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVr 937
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 83 -QEFQG--SEDYETALSGKEALSAALrsqnltkSTENHRLRRSIKKITQELSDL-----------QQERERLEKDLEEah 148
Cdd:TIGR02168 938 iDNLQErlSEEYSLTLEEAEALENKI-------EDDEEEARRRLKRLENKIKELgpvnlaaieeyEELKERYDFLTAQ-- 1008
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462625355 149 rekskgdctIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHN 196
Cdd:TIGR02168 1009 ---------KEDLTEAKETLEEAIEEIDREARERFKDTFDQVNENFQR 1047
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1051-1299 |
1.52e-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: 43.52 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1051 QNELmERIEEDNLTYQHLLPESPE--PSASHALSDYETSEKSFFSRDQKQDNETEKTSVMVNSFSQDLLMEHIQEIRTLR 1128
Cdd:TIGR02169 722 EKEI-EQLEQEEEKLKERLEELEEdlSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAEL 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1129 KRLEESIKTNEKLRKQLERQgsefvqgstsifasgselHSSLTSEIHFLRKQNQALNAMLI-----KGSRDKQKENDKLR 1203
Cdd:TIGR02169 801 SKLEEEVSRIEARLREIEQK------------------LNRLTLEKEYLEKEIQELQEQRIdlkeqIKSIEKEIENLNGK 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1204 -----ESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLL-- 1276
Cdd:TIGR02169 863 keeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKge 942
|
250 260
....*....|....*....|....
gi 2462625355 1277 -QSLRVELKAYEKLDEEHRRLREA 1299
Cdd:TIGR02169 943 dEEIPEEELSLEDVQAELQRVEEE 966
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
4-152 |
1.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREI--ATEKKNSLKRDKAIQGLTmALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQ 81
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLdaLREELDELEAQIRGNGGD-RLEQLEREIERLERELEERERRRARLEALLAALG 372
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462625355 82 TQEFQGSEDYEtalsgkeALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEEAHREKS 152
Cdd:COG4913 373 LPLPASAEEFA-------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| V_Alix_like |
cd08915 |
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains ... |
11-219 |
1.93e-03 |
|
Protein-interacting V-domain of mammalian Alix and related domains; This superfamily contains the V-shaped (V) domain of mammalian Alix (apoptosis-linked gene-2 interacting protein X), His-Domain type N23 protein tyrosine phosphatase (HD-PTP, also known as PTPN23), Bro1 and Rim20 (also known as PalA) from Saccharomyces cerevisiae, and related domains. Alix, HD-PTP, Bro1, and Rim20 all interact with the ESCRT (Endosomal Sorting Complexes Required for Transport) system. Alix, also known as apoptosis-linked gene-2 interacting protein 1 (AIP1), participates in membrane remodeling processes during the budding of enveloped viruses, vesicle budding inside late endosomal multivesicular bodies (MVBs), and the abscission reactions of mammalian cell division. It also functions in apoptosis. HD-PTP functions in cell migration and endosomal trafficking, Bro1 in endosomal trafficking, and Rim20 in the response to the external pH via the Rim101 pathway. The Alix V-domain contains a binding site, partially conserved in this superfamily, for the retroviral late assembly (L) domain YPXnL motif. The Alix V-domain is also a dimerization domain. Members of this superfamily have an N-terminal Bro1-like domain, which binds components of the ESCRT-III complex. The Bro1-like domains of Alix and HD-PTP can also bind human immunodeficiency virus type 1 (HIV-1) nucleocapsid. Many members, including Alix, HD-PTP, and Bro1, also have a proline-rich region (PRR), which binds multiple partners in Alix, including Tsg101 (tumor susceptibility gene 101, a component of ESCRT-1) and the apoptotic protein ALG-2. The C-terminal portion (V-domain and PRR) of Bro1 interacts with Doa4, a ubiquitin thiolesterase needed to remove ubiquitin from MVB cargoes; it interacts with a YPxL motif in Doa4s catalytic domain to stimulate its deubiquitination activity. Rim20 may bind the ESCRT-III subunit Snf7, bringing the protease Rim13 (a YPxL-containing transcription factor) into proximity with Rim101, and promoting the proteolytic activation of Rim101. HD-PTP is encoded by the PTPN23 gene, a tumor suppressor gene candidate often absent in human kidney, breast, lung, and cervical tumors. HD-PTP has a C-terminal catalytically inactive tyrosine phosphatase domain.
Pssm-ID: 185746 [Multi-domain] Cd Length: 342 Bit Score: 42.33 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 11 QERIQALEEDLREKEREIatekknslKRDKAIQGLTMA-LKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQEFQGSE 89
Cdd:cd08915 90 EELLQECEELLEEEAAED--------DQLRAKFGTLRWrRPSSDEAAKELYEKVTKLRGYLEQASNSDNEVLQCYESIDP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 90 DYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKDLEeahrEKSKGDCTIRDLRNEVEKLR 169
Cdd:cd08915 162 NLVLLCGGYKELKAFIPSPYPALDPEVSEVVSSLRPLLNEVSELEKERERFISELE----IKSRNNDILPKLITEYKKNG 237
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2462625355 170 NEVNER--EKAMENrYKSLLSESNKKLHNQEQVIKHLTEStNQKDVLLQKFN 219
Cdd:cd08915 238 TTEFEDlfEEHLKK-FDKDLTYVEKTKKKQIELIKEIDAA-NQEFSQVKNSN 287
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1-388 |
2.01e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 42.90 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1 MEHQKERNSFQERIQALEEDLREKEREIATEKKnslkrdkaiqgltmalkskeKKVEELNSEIEKLSAAFAKAREALQKA 80
Cdd:pfam12128 268 KSDETLIASRQEERQETSAELNQLLRTLDDQWK--------------------EKRDELNGELSAADAAVAKDRSELEAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 81 QTQEFQ-GSEDYETALSGKEALSaALRSQNLTKSTENHRLRRSIKKITQELSDLQQER--------ERLEKDLEEAHREK 151
Cdd:pfam12128 328 EDQHGAfLDADIETAAADQEQLP-SWQSELENLEERLKALTGKHQDVTAKYNRRRSKIkeqnnrdiAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 152 SKGDCTIRD--------LRNEVEKLRNEVNEREKamenRYKSLLSESNKKLhNQEQVIKHLTESTNQKDVLLQKFNEKdL 223
Cdd:pfam12128 407 DRQLAVAEDdlqaleseLREQLEAGKLEFNEEEY----RLKSRLGELKLRL-NQATATPELLLQLENFDERIERAREE-Q 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 224 EVIQQNCYLMAAEDLELRSE--------GLITEKCSSQQP----------PGSKTIFSKEKKQSSDYEELI-QVLKKEQD 284
Cdd:pfam12128 481 EAANAEVERLQSELRQARKRrdqasealRQASRRLEERQSaldelelqlfPQAGTLLHFLRKEAPDWEQSIgKVISPELL 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 285 IYTHLVKSLQESDSinnlqAELNKIFALRKQLEQ-DVLSYQNLRKTLEEQISEIRR---REEESFSLYSDQTSYLSICLE 360
Cdd:pfam12128 561 HRTDLDPEVWDGSV-----GGELNLYGVKLDLKRiDVPEWAASEEELRERLDKAEEalqSAREKQAAAEEQLVQANGELE 635
|
410 420
....*....|....*....|....*...
gi 2462625355 361 ENNRfqVEHFSQEELKKKVSDLIQLVKE 388
Cdd:pfam12128 636 KASR--EETFARTALKNARLDLRRLFDE 661
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1118-1299 |
2.66e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1118 MEHIQEIRTLRKRLEESIKTNEKLRKQLERQGSEFVqgstsiFASGSELHSSLTSEIHFLRKQNQALNAMliKGSRDKQK 1197
Cdd:PRK03918 548 LEKLEELKKKLAELEKKLDELEEELAELLKELEELG------FESVEELEERLKELEPFYNEYLELKDAE--KELEREEK 619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1198 ENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNqqLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQ 1277
Cdd:PRK03918 620 ELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
170 180
....*....|....*....|..
gi 2462625355 1278 SLRVELKAYEKLDEEHRRLREA 1299
Cdd:PRK03918 698 KLKEELEEREKAKKELEKLEKA 719
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2-347 |
2.94e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.36 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALEEDLREKEReiATEKKNSLKRDKA------IQGLTMALKSKEKKVEELNSEIEKLSAAFA--KA 73
Cdd:PRK03918 342 ELKKKLKELEKRLEELEERHELYEE--AKAKKEELERLKKrltgltPEKLEKELEELEKAKEEIEEEISKITARIGelKK 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 74 REALQKAQTQEFQGSEDyETALSGKEaLSAALRSQNLTKST-ENHRLRRSIKKITQELSDLQQERERLEKDLEEAHR--- 149
Cdd:PRK03918 420 EIKELKKAIEELKKAKG-KCPVCGRE-LTEEHRKELLEEYTaELKRIEKELKEIEEKERKLRKELRELEKVLKKESElik 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 150 EKSKGDcTIRDLRNEVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNE-----KDLE 224
Cdd:PRK03918 498 LKELAE-QLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDEleeelAELL 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 225 VIQQNCYLMAAEDLELRSEGL-------ITEKCSSQQPPGSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQ--- 294
Cdd:PRK03918 577 KELEELGFESVEELEERLKELepfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEkky 656
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 295 ---ESDSINNLQAELNK-IFALRKQLEQDVLSYQNLRKTLE---EQISEIRRREEESFSL 347
Cdd:PRK03918 657 seeEYEELREEYLELSReLAGLRAELEELEKRREEIKKTLEklkEELEEREKAKKELEKL 716
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1122-1354 |
3.38e-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: 41.67 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1122 QEIRTLRKRLEESIKTNEKLRKQLERQGSEfvqgstsifasgselHSSLTSEIHFLRKQNQALNAMLikgsRDKQKENDK 1201
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKE---------------EKALLKQLAALERRIAALARRI----RALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1202 LRESLSRKTVSLEHLQREYASVKEEnerLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQLLSQNDKLLQSLRV 1281
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEE---LAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462625355 1282 ELKAYEKLDEEHRRLREasgegwkgqdpfrDLHSLLMEIQALRLQLERSIETSSTLQSRLKEQLARGAEKAQE 1354
Cdd:COG4942 158 DLAELAALRAELEAERA-------------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
124-346 |
3.63e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 3.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 124 KKITQELSDLQQERERLEK---DLEEAHREKSKGDCTIRDLRNEVEKLRnevNEREKAMenRYKSLLSESNK-----KLH 195
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKaleELEEVEENIERLDLIIDEKRQQLERLR---REREKAE--RYQALLKEKREyegyeLLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 196 NQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKKQSSdYEEL 275
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIAS-LERS 309
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462625355 276 IQVLKKEQdiythlvKSLQEsdSINNLQAELNKIFALRKQLEQDVLSYQNLRKTLEEQISEIRRREEESFS 346
Cdd:TIGR02169 310 IAEKEREL-------EDAEE--RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
99-216 |
3.98e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 41.99 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 99 EAlSAALRSQNLTKSTEnhrlrrsIKKITQELSDLQQERERLEKDLEEAHREKskgdctIRDLRNEVEKLRNEVN----- 173
Cdd:COG0542 397 EA-AARVRMEIDSKPEE-------LDELERRLEQLEIEKEALKKEQDEASFER------LAELRDELAELEEELEalkar 462
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2462625355 174 -EREKAMENRYKSL---LSESNKKLHNQEQVIKHLTESTNQKDVLLQ 216
Cdd:COG0542 463 wEAEKELIEEIQELkeeLEQRYGKIPELEKELAELEEELAELAPLLR 509
|
|
| HlpA |
COG2825 |
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope ... |
4-86 |
4.31e-03 |
|
Periplasmic chaperone for outer membrane proteins, Skp family [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442073 [Multi-domain] Cd Length: 171 Bit Score: 39.82 E-value: 4.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIATEKKNsLKRDKAiqglTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQ 83
Cdd:COG2825 42 KAAQKKLEKEFKKRQAELQKLEKELQALQEK-LQKEAA----TLSEEERQKKERELQKKQQELQRKQQEAQQDLQKRQQE 116
|
...
gi 2462625355 84 EFQ 86
Cdd:COG2825 117 LLQ 119
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2-215 |
4.49e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 41.95 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 2 EHQKERNSFQERIQALE------EDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKARE 75
Cdd:PRK02224 479 ELEAELEDLEEEVEEVEerleraEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKRE 558
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 76 AlqkAQTQEFQGSEDYETAlsgkealsAALRSQNLTKSTENHRLRRsIKKITQELSDLQQERERLekdleeahREKSKGD 155
Cdd:PRK02224 559 A---AAEAEEEAEEAREEV--------AELNSKLAELKERIESLER-IRTLLAAIADAEDEIERL--------REKREAL 618
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462625355 156 CTIRDLRNevEKLRnEVNEREKAME-----NRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLL 215
Cdd:PRK02224 619 AELNDERR--ERLA-EKRERKRELEaefdeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQ 680
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
53-343 |
4.58e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 53 EKKVEELNSEIEKLSAAFAKAREALQKAQT-QEFQGSEDYETALSGKEALSAALRSQNLTKSTenhrLRRSIKKITQELS 131
Cdd:PRK05771 35 DLKEELSNERLRKLRSLLTKLSEALDKLRSyLPKLNPLREEKKKVSVKSLEELIKDVEEELEK----IEKEIKELEEEIS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 132 DLQQERERLEKDLEeahrekskgdctirdlrnEVEKLRN----EVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTES 207
Cdd:PRK05771 111 ELENEIKELEQEIE------------------RLEPWGNfdldLSLLLGFKYVSVFVGTVPEDKLEELKLESDVENVEYI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 208 TNQKD------VLLQKFNEKDLEVIQQNCYlmaaEDLELRSEGLITEKCSSqqppgsktIFSKEKKQSSDYEELIQVLKK 281
Cdd:PRK05771 173 STDKGyvyvvvVVLKELSDEVEEELKKLGF----ERLELEEEGTPSELIRE--------IKEELEEIEKERESLLEELKE 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462625355 282 EQDIYTHLVKSLQESDSINNLQAEL-------NKIFALR--------KQLEQDVLSYQNLRKTLEeqISEIRRREEE 343
Cdd:PRK05771 241 LAKKYLEELLALYEYLEIELERAEAlskflktDKTFAIEgwvpedrvKKLKELIDKATGGSAYVE--FVEPDEEEEE 315
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
100-340 |
5.44e-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: 5.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 100 ALSAALRSQNLTKSTEN--HRLRRSIKKITQELSDLQQERERLEKDLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREK 177
Cdd:COG4942 11 LALAAAAQADAAAEAEAelEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 178 AMEnryksllsESNKKLHNQEQVIKHLTES---TNQKDVLLQKFNEKDLEVIQQNCYLMA--AEDLELRSEGLITEKcss 252
Cdd:COG4942 91 EIA--------ELRAELEAQKEELAELLRAlyrLGRQPPLALLLSPEDFLDAVRRLQYLKylAPARREQAEELRADL--- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 253 qqppgsKTIFSKEKKQSSDYEELIQVLKKEQDIYTHLVKSLQESDS-INNLQAELNKIFALRKQLEQDVLSYQNLRKTLE 331
Cdd:COG4942 160 ------AELAALRAELEAERAELEALLAELEEERAALEALKAERQKlLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
....*....
gi 2462625355 332 EQISEIRRR 340
Cdd:COG4942 234 AEAAAAAER 242
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
4-246 |
6.06e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 6.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQ 83
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 84 efqgSEDYETALSGKEALSAALRSQNLTKSTENHRLRRSIKKITQELSDLQQERERLEKdlEEAHREKSKGDCTIRDLRN 163
Cdd:COG4372 124 ----RQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSE--AEAEQALDELLKEANRNAE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 164 EVEKLRNEVNEREKAMENRYKSLLSESNKKLHNQEQVIKHLTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSE 243
Cdd:COG4372 198 KEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEE 277
|
...
gi 2462625355 244 GLI 246
Cdd:COG4372 278 LEI 280
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
6-181 |
6.34e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.15 E-value: 6.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 6 ERNSFQERI---QALEEDLREKEREIATEKKNslKRDKA---IQGLTMALKSKEKKVEELNSEIEKLSAAFAKAREALQK 79
Cdd:PHA02562 189 KIDHIQQQIktyNKNIEEQRKKNGENIARKQN--KYDELveeAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAK 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 80 AQTQEFQGSEDYETALSGKEALSAalrSQNLtkSTENHRL---RRSIKKITQELSDLQQERERLEKDLEEAhREKSKgdc 156
Cdd:PHA02562 267 IKSKIEQFQKVIKMYEKGGVCPTC---TQQI--SEGPDRItkiKDKLKELQHSLEKLDTAIDELEEIMDEF-NEQSK--- 337
|
170 180 190
....*....|....*....|....*....|..
gi 2462625355 157 TIRDLRNEVEK-------LRNEVNEREKAMEN 181
Cdd:PHA02562 338 KLLELKNKISTnkqslitLVDKAKKVKAAIEE 369
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
49-388 |
6.41e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.49 E-value: 6.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 49 LKSKEKKVEELNSEIEKLSAAFAKAREAlqKAQTQEFQGSEDYETALSGKEALSAALRSQNLTKSTENhrLRRSIKKITQ 128
Cdd:TIGR00618 158 LKAKSKEKKELLMNLFPLDQYTQLALME--FAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQV--LEKELKHLRE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 129 ELSDLQQERERLEKdLEEAHREKSKGDCTIRDLRNEVEKLRNEVNEREKAMENRYKS-----LLSESNKKLHNQEQVIKH 203
Cdd:TIGR00618 234 ALQQTQQSHAYLTQ-KREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaapLAAHIKAVTQIEQQAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 204 LTESTNQKDVLLQKFNEKDLEVIQQNCYLMAAEDLELRSEGLITEKCSSQQPPGSKTIFSKEKkqssdyeELIQVLKKEQ 283
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQH-------TLTQHIHTLQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 284 DIYTHLVKSLQESDSI-NNLQAELNKIFALrkQLEQDVLSYQNLRKTLEEQISEIRRREEESFSLYSDQtsylsiCLEEN 362
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKElDILQREQATIDTR--TSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ------CEKLE 457
|
330 340
....*....|....*....|....*..
gi 2462625355 363 NRFQVEHF-SQEELKKKVSDLIQLVKE 388
Cdd:TIGR00618 458 KIHLQESAqSLKEREQQLQTKEQIHLQ 484
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
4-344 |
6.68e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIATEKKNSLKRDKAIQGLtmalkskEKKVEELNSEIEKLSAAFAKAREALQK---- 79
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLESEEKNREEVEQL-------KDLYRELRKSLLANRFSFGPALDELEKqlen 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 80 -----AQTQEFQGSEDYETAlsgKEALSAAlrsqnltkSTENHRLRRSIKKITQELSDLQQE-RERLEkDLEEAHRE-KS 152
Cdd:PRK04778 177 leeefSQFVELTESGDYVEA---REILDQL--------EEELAALEQIMEEIPELLKELQTElPDQLQ-ELKAGYRElVE 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 153 KG--------DCTIRDLRNEVEKLRN--------EVNEREKAMENR----YKSLLSE---SNKKLHNQEQVIKHLTESTN 209
Cdd:PRK04778 245 EGyhldhldiEKEIQDLKEQIDENLAlleeldldEAEEKNEEIQERidqlYDILEREvkaRKYVEKNSDTLPDFLEHAKE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 210 QKDVLLQKfnekdLEVIQQNcYLMAAEDLELrseglitekcssqqppgSKTIFSKEKKQSSDYEELIQVLKKEQDIYTHL 289
Cdd:PRK04778 325 QNKELKEE-----IDRVKQS-YTLNESELES-----------------VRQLEKQLESLEKQYDEITERIAEQEIAYSEL 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2462625355 290 VKSLQES----DSINNLQAELNKifALrKQLEQDVLSYQNLRKTLEEQISEIRRREEES 344
Cdd:PRK04778 382 QEELEEIlkqlEEIEKEQEKLSE--ML-QGLRKDELEAREKLERYRNKLHEIKRYLEKS 437
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1100-1301 |
6.86e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.91 E-value: 6.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1100 NETEKTSVMvnSFSQDLLMEHIQ-EIRTLRK-------RLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELhSSLT 1171
Cdd:COG4717 32 NEAGKSTLL--AFIRAMLLERLEkEADELFKpqgrkpeLNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL-EELE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1172 SEIHFLRKQNQALNAMLikGSRDKQKENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCS 1251
Cdd:COG4717 109 AELEELREELEKLEKLL--QLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462625355 1252 G-----------QELSRVQEELKLRQQLLSQNDKLLQSLRVELKAYEK---LDEEHRRLREASG 1301
Cdd:COG4717 187 SlateeelqdlaEELEELQQRLAELEEELEEAQEELEELEEELEQLENeleAAALEERLKEARL 250
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1122-1329 |
8.39e-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: 40.81 E-value: 8.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1122 QEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELhSSLTSEIHFLRKQNQALNAmLIKGSRDKQKENDK 1201
Cdd:TIGR02168 302 QQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKL-EELKEELESLEAELEELEA-ELEELESRLEELEE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1202 LRESLSRKTVSLEhlqREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVqeELKLRQQLLSQNDKLLQSLRV 1281
Cdd:TIGR02168 380 QLETLRSKVAQLE---LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELEELQE 454
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2462625355 1282 ELKAYEKLDEEHRRLREASGEgwKGQDPFRDLHSLLMEIQALRLQLER 1329
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQ--ALDAAERELAQLQARLDSLERLQEN 500
|
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| OmpH |
smart00935 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
4-86 |
8.90e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 214922 [Multi-domain] Cd Length: 140 Bit Score: 38.33 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 4 QKERNSFQERIQALEEDLREKEREIATEKKNsLKRDKAiqglTMALKSKEKKVEELNSEIEKLSAAFAKAREALQKAQTQ 83
Cdd:smart00935 17 KAAQKQLEKEFKKRQAELEKLEKELQKLKEK-LQKDAA----TLSEAAREKKEKELQKKVQEFQRKQQKLQQDLQKRQQE 91
|
...
gi 2462625355 84 EFQ 86
Cdd:smart00935 92 ELQ 94
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1122-1299 |
8.98e-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: 40.52 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1122 QEIRTLRKRLEESIKTNEKLRKQLERQGSEFVQGSTSIFASGSELH------SSLTSEIHFLRKQNQALNAMLIK--GSR 1193
Cdd:COG4942 34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAaleaelAELEKEIAELRAELEAQKEELAEllRAL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1194 DKQKENDKLR-----ESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEELKLRQQL 1268
Cdd:COG4942 114 YRLGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL 193
|
170 180 190
....*....|....*....|....*....|....*
gi 2462625355 1269 LSQNDKLLQSLRVELKAYEK----LDEEHRRLREA 1299
Cdd:COG4942 194 KAERQKLLARLEKELAELAAelaeLQQEAEELEAL 228
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1193-1360 |
8.98e-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: 40.52 E-value: 8.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1193 RDKQKENDKLRESLSRKTVSLEHLQREYASVKEENERLQKEGSEKERHNQQLIQEVRCSGQELSRVQEEL-KLRQQLLSQ 1271
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIaELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462625355 1272 NDKLLQSLRV-----------ELKAYEKLDEEHRRLREASGEGWKGQDPFRDLHSLLMEIQALRLQLERSIETSSTLQSR 1340
Cdd:COG4942 103 KEELAELLRAlyrlgrqpplaLLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180
....*....|....*....|
gi 2462625355 1341 LKEQLARGAEKAQEGALTLA 1360
Cdd:COG4942 183 LEEERAALEALKAERQKLLA 202
|
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