|
Name |
Accession |
Description |
Interval |
E-value |
| PH_PLEKHD1 |
cd13281 |
Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH ... |
1-58 |
2.99e-30 |
|
Pleckstrin homology (PH) domain containing, family D (with coiled-coil domains) member 1 PH domain; Human PLEKHD1 (also called UPF0639, pleckstrin homology domain containing, family D (with M protein repeats) member 1) is a single transcript and contains a single PH domain. PLEKHD1 is conserved in human, chimpanzee, , dog, cow, mouse, chicken, zebrafish, and Caenorhabditis elegans. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.
Pssm-ID: 270099 Cd Length: 139 Bit Score: 113.57 E-value: 2.99e-30
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587053 1 MPYAMKISHQDFHGNILLAAESEFEQTQWLEMLQESGKVTWKNAQLGEAMIKSLEAQG 58
Cdd:cd13281 82 KPYAISISHSDFKGNIILAADSEFEQEKWLDMLRESGKITWKNAQLGETMIEELEAQG 139
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
55-293 |
1.94e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 55 EAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQE 134
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 135 KKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQpppsggLHSNLRQIEEKMQQLLEEKLLAEKRMKEN 214
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE------AEEELEEAEAELAEAEEALLEAEAELAEA 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034587053 215 EERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKEER 293
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
42-297 |
5.77e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.57 E-value: 5.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 42 KNAQLGEAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKREL 121
Cdd:COG1196 246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 122 ELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQseqpppsgglhsnLRQIEEKMQQLL 201
Cdd:COG1196 326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE-------------LEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 202 EEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQGL 281
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
250
....*....|....*.
gi 1034587053 282 NSKVRNKEKEERMRAD 297
Cdd:COG1196 473 ALLEAALAELLEELAE 488
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
63-317 |
1.89e-10 |
|
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: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 63 KEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELEltarclkgveQEKKELRHLT 142
Cdd:COG1196 225 LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELE----------EAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 143 ESLQQTLEELSIEKkktlEMLEENENHLQTLANQSEQpppsggLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALE 222
Cdd:COG1196 295 AELARLEQDIARLE----ERRRELEERLEELEEELAE------LEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 223 EEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKEERMRADVSHLK 302
Cdd:COG1196 365 EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
250
....*....|....*
gi 1034587053 303 RFFEECIRNAELEAK 317
Cdd:COG1196 445 EEAAEEEAELEEEEE 459
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
23-265 |
2.46e-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: 62.38 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 23 EFEQTQWLEMLQESGKVTWKNAQLGEAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQ 102
Cdd:TIGR02168 721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 103 FEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSiekkKTLEMLEENENHLQTLanqseqppp 182
Cdd:TIGR02168 801 LREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELS----EDIESLAAEIEELEEL--------- 867
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 183 sgglhsnLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAEREL-KAEVKVRM 261
Cdd:TIGR02168 868 -------IEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLeGLEVRIDN 940
|
....
gi 1034587053 262 DLER 265
Cdd:TIGR02168 941 LQER 944
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
66-293 |
4.84e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.49 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 66 QEYLDKLMEETEELclqREQREELERlnqvlEAEK-QQFEEVVQELRmeqeqiKRELELTARCLKGVEQEKKELRHLTES 144
Cdd:COG1196 185 EENLERLEDILGEL---ERQLEPLER-----QAEKaERYRELKEELK------ELEAELLLLKLRELEAELEELEAELEE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 145 LQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQpppsggLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEE 224
Cdd:COG1196 251 LEAELEELEAELAELEAELEELRLELEELELELEE------AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEE 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034587053 225 REFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKEER 293
Cdd:COG1196 325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
41-297 |
6.41e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.11 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 41 WKNAQLGEAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQReELERLNQVLEAEKQQFEEVVQELRMEQEQIKRE 120
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL-ELEEAQAEEYELLAELARLEQDIARLEERRREL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 121 LELTARclkgVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQpppsggLHSNLRQIEEKMQQL 200
Cdd:COG1196 315 EERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE------AEAELAEAEEELEEL 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 201 LEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQG 280
Cdd:COG1196 385 AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250
....*....|....*..
gi 1034587053 281 LNSKVRNKEKEERMRAD 297
Cdd:COG1196 465 LAELLEEAALLEAALAE 481
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
49-320 |
6.99e-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: 61.23 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 49 AMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQRE----ELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELT 124
Cdd:TIGR02168 687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqisALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 125 ARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTlanqseqpppsggLHSNLRQIEEKMQQLLEEK 204
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-------------LNEEAANLRERLESLERRI 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 205 LLAEKRMKENEERSRALEEEREFYSSQSQALQNS-------LQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSL 277
Cdd:TIGR02168 834 AATERRLEDLEEQIEELSEDIESLAAEIEELEELieeleseLEALLNERASLEEALALLRSELEELSEELRELESKRSEL 913
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034587053 278 EQGL----NSKVRNKEKEERMRADVSHLK-RFFEECIRNAELEAKMPV 320
Cdd:TIGR02168 914 RRELeelrEKLAQLELRLEGLEVRIDNLQeRLSEEYSLTLEEAEALEN 961
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
55-317 |
4.71e-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: 58.53 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 55 EAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQE 134
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 135 KKELRHLTESLQQTLEELSiekkktlEMLEENENHLQTLANQSEQpppsggLHSNLRQIEEKMQQLLEEKLLAEKRMKEN 214
Cdd:TIGR02168 304 KQILRERLANLERQLEELE-------AQLEELESKLDELAEELAE------LEEKLEELKEELESLEAELEELEAELEEL 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 215 EERSRALEEEREFYSS-------QSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRN 287
Cdd:TIGR02168 371 ESRLEELEEQLETLRSkvaqlelQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
250 260 270
....*....|....*....|....*....|..
gi 1034587053 288 K--EKEERMRADVSHLKRFFEEcIRNAELEAK 317
Cdd:TIGR02168 451 ElqEELERLEEALEELREELEE-AEQALDAAE 481
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
74-307 |
3.89e-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: 55.46 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 74 EETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELS 153
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 154 IEKKKTLEMLEENENHLQTLANQSEQ------PPPSGGLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREF 227
Cdd:TIGR02169 751 QEIENVKSELKELEARIEELEEDLHKleealnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEY 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 228 YSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQglnSKVRNKEKEERMRADVSHLKRFFEE 307
Cdd:TIGR02169 831 LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLES---RLGDLKKERDELEAQLRELERKIEE 907
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
59-280 |
5.99e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.92 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 59 LQLAKEKQEYLDKLMEETEELCLQREQREELERLnqvlEAEKQQFEEVVQELRmEQEQIKRELELTARclkgvEQEKKEL 138
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQIELLEPI----RELAERYAAARERLA-ELEYLRAALRLWFA-----QRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 139 RHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQpppSGGlhSNLRQIEEKMQQLLEEKLLAEKRMKENEERS 218
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRG---NGG--DRLEQLEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034587053 219 RALE----EEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQG 280
Cdd:COG4913 369 AALGlplpASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
82-304 |
9.01e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 53.61 E-value: 9.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 82 QREQREELERLNQVLEAEKQQFEEV---VQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKK 158
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALkkeEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 159 TLEMLEEnenHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKLLA-EKRMKENEERSRALEEEREFYSSQSQALQN 237
Cdd:COG4942 102 QKEELAE---LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 238 SLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSL---EQGLNSKVRNKEKEERMRADVSHLKRF 304
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELqqeAEELEALIARLEAEAAAAAERTPAAGF 248
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
17-299 |
3.07e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.75 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 17 LLAAESEFEQTQWLEMLQESGKVTWKNAQLgEAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVL 96
Cdd:TIGR02168 229 LLVLRLEELREELEELQEELKEAEEELEEL-TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 97 EAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLAnq 176
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR-- 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 177 seqpppsgglhSNLRQIEEKMQQLLEEKLLAEKRMKENEER-----SRALEEEREFYSSQSQALQNSLQELTAEKQQAER 251
Cdd:TIGR02168 386 -----------SKVAQLELQIASLNNEIERLEARLERLEDRrerlqQEIEELLKKLEEAELKELQAELEELEEELEELQE 454
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034587053 252 ELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKEERMRADVS 299
Cdd:TIGR02168 455 ELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
63-321 |
3.81e-07 |
|
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: 52.38 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 63 KEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKqqfeevVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLT 142
Cdd:TIGR02169 194 DEKRQQLERLRREREKAERYQALLKEKREYEGYELLKE------KEALERQKEAIERQLASLEEELEKLTEEISELEKRL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 143 ESLQQTLEELSiekKKTLEMLEENENHLQTlanqseqpppsgglhsNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALE 222
Cdd:TIGR02169 268 EEIEQLLEELN---KKIKDLGEEEQLRVKE----------------KIGELEAEIASLERSIAEKERELEDAEERLAKLE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 223 EEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVR-----NKEKEERMRAD 297
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREkleklKREINELKREL 408
|
250 260
....*....|....*....|....
gi 1034587053 298 VSHLKRFFEECIRNAELEAKMPVI 321
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNAAIAGI 432
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
48-317 |
3.97e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.45 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 48 EAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREEL---------ERLNQVLEAEKQQFEEVVQELRMEQEQIK 118
Cdd:PTZ00121 1474 EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAkkaeeakkaDEAKKAEEAKKADEAKKAEEKKKADELKK 1553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 119 RELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQPPPSGGLHSNLRQIEEkmq 198
Cdd:PTZ00121 1554 AEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE--- 1630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 199 qllEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQElTAEKQQAERELKAEVKVRMDLERRLREAEGAlRSLE 278
Cdd:PTZ00121 1631 ---EKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA-EEDKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAE 1705
|
250 260 270
....*....|....*....|....*....|....*....
gi 1034587053 279 QGLNSKVRNKEKEERMRADVSHLKRFFEECIRNAELEAK 317
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK 1744
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
48-278 |
3.45e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 3.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 48 EAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKREL-----E 122
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLshsriP 794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 123 LTARCLKGVEQEKKELRHLTESLQQTLEELSIEKkktlEMLEENENHLQTLANQSE-QPPPSGGLHSNLRQIEEKMQQLL 201
Cdd:TIGR02169 795 EIQAELSKLEEEVSRIEARLREIEQKLNRLTLEK----EYLEKEIQELQEQRIDLKeQIKSIEKEIENLNGKKEELEEEL 870
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587053 202 EEKllaEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLE 278
Cdd:TIGR02169 871 EEL---EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
48-286 |
6.23e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 6.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 48 EAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARC 127
Cdd:TIGR02169 300 EAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKE 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 128 LKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQseqpppsgglhsnLRQIEEKMQQLLEEKLLA 207
Cdd:TIGR02169 380 FAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAA-------------IAGIEAKINELEEEKEDK 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 208 EKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAEREL---KAEVKVRMDLERRLREAEGALRSLEQGLNSK 284
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaEAQARASEERVRGGRAVEEVLKASIQGVHGT 526
|
..
gi 1034587053 285 VR 286
Cdd:TIGR02169 527 VA 528
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
55-295 |
1.09e-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: 47.66 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 55 EAQGLQLAKEKQEYLDKLMEETEElcLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQE 134
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETEN--LAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 135 KKELRHLTESLQQTLEELSIEKKKTLEMLEEN-ENHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKLLAEKRMKE 213
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVlKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 214 NEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKEER 293
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE 398
|
..
gi 1034587053 294 MR 295
Cdd:pfam02463 399 LK 400
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
48-252 |
1.52e-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: 47.37 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 48 EAMIKSLEAQgLQLAKEKQEYLDKLMEETEELCLQ-REQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTAR 126
Cdd:TIGR02169 811 EARLREIEQK-LNRLTLEKEYLEKEIQELQEQRIDlKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKK 889
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 127 CLKGVEQEKKELRHLTESLQQTLEELSI---EKKKTLEMLEENENHLQTLANQSEQPPPS----GGLHSNLRQIEEKMQQ 199
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKrlsELKAKLEALEEELSEIEDPKGEDEEIPEEelslEDVQAELQRVEEEIRA 969
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034587053 200 LLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERE 252
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFME 1022
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
56-258 |
3.71e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 45.79 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 56 AQGLQLAKEKQ---EYLDKLMEETEELCLQREqrEELERLNQVLEAEKQQFEEVVQELRMEQEQIKReleltarclkgVE 132
Cdd:pfam05667 303 TEKLQFTNEAPaatSSPPTKVETEEELQQQRE--EELEELQEQLEDLESSIQELEKEIKKLESSIKQ-----------VE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 133 QEKKELRHLTESLQQTLEElsieKKKTLEML---EENENHLQTLANQSEQpppsgglhsNLRQIEEKMQQ----LLEE-K 204
Cdd:pfam05667 370 EELEELKEQNEELEKQYKV----KKKTLDLLpdaEENIAKLQALVDASAQ---------RLVELAGQWEKhrvpLIEEyR 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1034587053 205 LLAEKRMKENEERSRALEEEREFYSSQSQAlqnslQELTAEKQQAERELKAEVK 258
Cdd:pfam05667 437 ALKEAKSNKEDESQRKLEEIKELREKIKEV-----AEEAKQKEELYKQLVAEYE 485
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
83-291 |
5.57e-05 |
|
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: 5.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 83 REQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKelrhlTESLQQTLEELSIEkkktLEM 162
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEID-----VASAEREIAELEAE----LER 679
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 163 LEENenhlqtlanqseqpppsgglHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQEL 242
Cdd:COG4913 680 LDAS--------------------SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA 739
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034587053 243 TAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKE 291
Cdd:COG4913 740 EDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| Nucleoporin_FG2 |
pfam15967 |
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of ... |
90-248 |
5.80e-05 |
|
Nucleoporin FG repeated region; Nucleoporin_FG2, or nucleoporin p58/p45, is a family of chordate nucleoporins. The proteins carry many repeats of the FG sequence motif.
Pssm-ID: 435043 [Multi-domain] Cd Length: 586 Bit Score: 45.04 E-value: 5.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 90 ERLNQVLEAEKQQFEEVVQELRMEQEQIKReleLTARCLKGVEQEKKELRHL----TESLQQtlEELSIEKKK--TLEML 163
Cdd:pfam15967 243 ENLPPVICQDVENFQKFVKEQKQVQEEISR---MSSKAMLKVQDDIKALKQLlsvaASGLQR--NSLAIDKLKieTAQEL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 164 EENENHLQTLAN----QSEQPPPSGGLHSNLRQIEEKMQQLLEEkllaekrmkeneersraLEEEREFYSSQSQALQNSL 239
Cdd:pfam15967 318 KNADIALRTQKTppglQHENTAPADYFRSLVEQFEVQLQQYRQQ-----------------IEELENHLTTQSSSSHITP 380
|
....*....
gi 1034587053 240 QELTAEKQQ 248
Cdd:pfam15967 381 QDLSLAMQK 389
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
64-290 |
6.75e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 6.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 64 EKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIK---RELELTARCLKGVEQEKKELRH 140
Cdd:PRK03918 218 ELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKkeiEELEEKVKELKELKEKAEEYIK 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 141 LTESLQQTLEELSiEKKKTLEMLEENENHLQTLAnqseqpppsgglhSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRA 220
Cdd:PRK03918 298 LSEFYEEYLDELR-EIEKRLSRLEEEINGIEERI-------------KELEEKEERLEELKKKLKELEKRLEELEERHEL 363
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 221 LEEEREFySSQSQALQNSLQELTAEKqqAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEK 290
Cdd:PRK03918 364 YEEAKAK-KEELERLKKRLTGLTPEK--LEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
48-294 |
1.09e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.63 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 48 EAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAE-----KQQFEEVVQELRMEQEQIKRELE 122
Cdd:TIGR04523 245 TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEisdlnNQKEQDWNKELKSELKNQEKKLE 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 123 LTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQPPPS-GGLHSNLRQIEEKMQQLL 201
Cdd:TIGR04523 325 EIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEiKNLESQINDLESKIQNQE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 202 EEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQGL 281
Cdd:TIGR04523 405 KLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNL 484
|
250
....*....|...
gi 1034587053 282 NSKVRNKEKEERM 294
Cdd:TIGR04523 485 EQKQKELKSKEKE 497
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
62-311 |
1.58e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 62 AKEKQEYLDKLMEETEELClqrEQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKK---EL 138
Cdd:PRK03918 167 LGEVIKEIKRRIERLEKFI---KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieEL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 139 RHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERS 218
Cdd:PRK03918 244 EKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 219 RALEEEREFYSSQSqalqNSLQELTAEKQQAERELkAEVKVRMDLERRLREAEGALRSLEQGLnsKVRNKEKEERMRADV 298
Cdd:PRK03918 324 NGIEERIKELEEKE----ERLEELKKKLKELEKRL-EELEERHELYEEAKAKKEELERLKKRL--TGLTPEKLEKELEEL 396
|
250
....*....|...
gi 1034587053 299 SHLKRFFEECIRN 311
Cdd:PRK03918 397 EKAKEEIEEEISK 409
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
51-252 |
1.74e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.85 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 51 IKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREElERLNQVLEAEKQqfEEVVQELRMEQEQIKRELELTAR---- 126
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYDELVEEAKTIKAEIEELTD-ELLNLVMDIEDP--SAALNKLNTAAAKIKSKIEQFQKvikm 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 127 ---------CLKGVEQEKKELRHLTESLQQTLEELSIEKKKtLEMLEENENHLQTLANQSEqpppsgGLHSNLRQIEEKM 197
Cdd:PHA02562 281 yekggvcptCTQQISEGPDRITKIKDKLKELQHSLEKLDTA-IDELEEIMDEFNEQSKKLL------ELKNKISTNKQSL 353
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034587053 198 QQLLEEKLLAEKRMKEneersraLEEEREFYSSQSQALQNSLQELTAEKQQAERE 252
Cdd:PHA02562 354 ITLVDKAKKVKAAIEE-------LQAEFVDNAEELAKLQDELDKIVKTKSELVKE 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
25-245 |
2.01e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 25 EQTQWLEMLQESGKVTWKNAQLGEAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFE 104
Cdd:TIGR02168 821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 105 EVVQELRMEQEQIKRELEltaRCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQpppsg 184
Cdd:TIGR02168 901 EELRELESKRSELRRELE---ELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR----- 972
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587053 185 glhsNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAE 245
Cdd:TIGR02168 973 ----RLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDRE 1029
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
95-233 |
3.05e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 95 VLEAEKQQFEEVV---QELRMEQEQIKRELEltaRCLKGVEQEKKELRHLTESLQQTLEELSIE-----KKKTLEMLEEN 166
Cdd:PRK00409 510 LIGEDKEKLNELIaslEELERELEQKAEEAE---ALLKEAEKLKEELEEKKEKLQEEEDKLLEEaekeaQQAIKEAKKEA 586
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587053 167 ENHLQTLANQSEQPPPSGGLHsnlrQIEEKMQQLLEEKLLAEKRMKENEERSRALEE-EREFYSSQSQ 233
Cdd:PRK00409 587 DEIIKELRQLQKGGYASVKAH----ELIEARKRLNKANEKKEKKKKKQKEKQEELKVgDEVKYLSLGQ 650
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
82-279 |
3.56e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.70 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 82 QREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTArclkgVEQEKKELRHLTESLQQTLEELSIEkkktLE 161
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVD-----LSEEAKLLLQQLSELESQLAEARAE----LA 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 162 MLEENENHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEERE--------------- 226
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAalraqlqqeaqrila 316
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1034587053 227 FYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQ 279
Cdd:COG3206 317 SLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYES 369
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
48-183 |
5.08e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 5.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 48 EAMIKSLEAQGLQLakeKQEYldklmEETEELclqreqREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARc 127
Cdd:PRK00409 519 NELIASLEELEREL---EQKA-----EEAEAL------LKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAK- 583
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587053 128 lKGVEQEKKELRHLteslqQTLEELSIEKKKTLEMLEE-NENHLQTLANQSEQPPPS 183
Cdd:PRK00409 584 -KEADEIIKELRQL-----QKGGYASVKAHELIEARKRlNKANEKKEKKKKKQKEKQ 634
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
60-246 |
5.31e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 5.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 60 QLAKEKQEYLDKLMEETEELCLQREQrEELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELE-LTARCLKgVEQEKKEL 138
Cdd:PRK12705 30 RLAKEAERILQEAQKEAEEKLEAALL-EAKELLLRERNQQRQEARREREELQREEERLVQKEEqLDARAEK-LDNLENQL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 139 RHLTESLQQTLEELSIEKKktlemleENENHLQTLANQSEQpppsgglhsnlrQIEEKMQQLLEEKLLAEK--RMKENEE 216
Cdd:PRK12705 108 EEREKALSARELELEELEK-------QLDNELYRVAGLTPE------------QARKLLLKLLDAELEEEKaqRVKKIEE 168
|
170 180 190
....*....|....*....|....*....|
gi 1034587053 217 RSRaLEEEREFYSSQSQALQNSLQELTAEK 246
Cdd:PRK12705 169 EAD-LEAERKAQNILAQAMQRIASETASDL 197
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
33-318 |
5.49e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.37 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 33 LQESGKVTWKNAQLGE--AMIKSLEaqglqlakeKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQEL 110
Cdd:COG5022 799 LQPLLSLLGSRKEYRSylACIIKLQ---------KTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETI 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 111 RmeqEQIKRELELTARCLKGVEQEKKELRHLTEsLQQTLEELSIEKKKTLEMLEENENhlqtlanqseqpppsgglhsnl 190
Cdd:COG5022 870 Y---LQSAQRVELAERQLQELKIDVKSISSLKL-VNLELESEIIELKKSLSSDLIENL---------------------- 923
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 191 rqieekmqQLLEEKLLAEKRMKENEERSRALEEERefyssQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREA 270
Cdd:COG5022 924 --------EFKTELIARLKKLLNNIDLEEGPSIEY-----VKLPELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKA 990
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034587053 271 EGALRSLEQGLNSKVRNKEKEERmradvsHLKRFFEECIRNAELEAKM 318
Cdd:COG5022 991 NSELKNFKKELAELSKQYGALQE------STKQLKELPVEVAELQSAS 1032
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
51-313 |
6.01e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.21 E-value: 6.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 51 IKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEkQQFEEVVQELRmEQEQIKRELELTARCLKG 130
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-IDVASAEREIA-ELEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 131 VEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQPPPSGGLHSNLRqIEEKMQQLLEEKLLAEKR 210
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL-LEERFAAALGDAVERELR 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 211 mKENEERSRALEEEREfysSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEgalrslEQGLnskVRNKEK 290
Cdd:COG4913 769 -ENLEERIDALRARLN---RAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLE------EDGL---PEYEER 835
|
250 260
....*....|....*....|....*...
gi 1034587053 291 -----EERMRADVSHLKRFFEECIRNAE 313
Cdd:COG4913 836 fkellNENSIEFVADLLSKLRRAIREIK 863
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
48-258 |
6.17e-04 |
|
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: 6.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 48 EAMIKSLEAQGLQLAKEKQEYLDKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARC 127
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 128 L-KGVEQEKKELRHLTESLQQT------LEELSIEKKKTLEMLEENENHLQTLANQSEQpppsgglhsNLRQIEEKMQQL 200
Cdd:COG4942 113 LyRLGRQPPLALLLSPEDFLDAvrrlqyLKYLAPARREQAEELRADLAELAALRAELEA---------ERAELEALLAEL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587053 201 LEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVK 258
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
77-297 |
6.55e-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: 42.08 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 77 EELCLQREQREELERLNQVLEAEKQQFEEvvqELRMEQEQIKRELELTArclkgveqEKKELRHLTESLQQTLEELSIEK 156
Cdd:pfam01576 12 EELQKVKERQQKAESELKELEKKHQQLCE---EKNALQEQLQAETELCA--------EAEEMRARLAARKQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 157 KKTLEMLEENENHLQTLANQSEQPppSGGLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQ 236
Cdd:pfam01576 81 ESRLEEEEERSQQLQNEKKKMQQH--IQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNSKLSKERKLLE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587053 237 NSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQGLNSKVRNKEKEERMRAD 297
Cdd:pfam01576 159 ERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTD 219
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
45-153 |
9.53e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 41.30 E-value: 9.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 45 QLGEAMIKSLEAQGLQLAKE-----KQEYLDKLMEETEELclqREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKR 119
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEalleaKEEIHKLRNEFEKEL---RERRNELQKLEKRLLQKEENLDRKLELLEKREEELEK 114
|
90 100 110
....*....|....*....|....*....|....
gi 1034587053 120 ELELTARCLKGVEQEKKELRHLTESLQQTLEELS 153
Cdd:PRK12704 115 KEKELEQKQQELEKKEEELEELIEEQLQELERIS 148
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
70-315 |
1.43e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 40.88 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 70 DKLMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQEL------------RMEQEQIKRELELTARCLKGVEQEK-K 136
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQermamerereleRIRQEERKRELERIRQEEIAMEISRmR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 137 ELRHLTESLQQTLEELSIE-----KKKTLEMLEENENHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKLLAEKRM 211
Cdd:pfam17380 379 ELERLQMERQQKNERVRQEleaarKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQER 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 212 KENEERSRALEEEREfyssqsqalqnsLQELTAEKQQAERELkAEVKVRMDLERRLREAEGALrsLEQGLNSKVRNKEKE 291
Cdd:pfam17380 459 QQQVERLRQQEEERK------------RKKLELEKEKRDRKR-AEEQRRKILEKELEERKQAM--IEEERKRKLLEKEME 523
|
250 260
....*....|....*....|....
gi 1034587053 292 ERMRADVSHLKRFFEECIRNAELE 315
Cdd:pfam17380 524 ERQKAIYEEERRREAEEERRKQQE 547
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
63-269 |
1.52e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 63 KEKQEYLDKLMEETEE-LCLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHL 141
Cdd:PRK02224 515 EERREDLEELIAERREtIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERI 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 142 TESL----------------QQTLEELSIEKKKTLEMLEE---------NENHLQTLANQSEQpppsggLHSNLRQIEEK 196
Cdd:PRK02224 595 RTLLaaiadaedeierlrekREALAELNDERRERLAEKRErkreleaefDEARIEEAREDKER------AEEYLEQVEEK 668
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034587053 197 MQQLLEEK--LLAEKRMKENE-ERSRALEEEREFYSSQSQALQnSLQELTAEKQQAERELKAEVKVR--MDLERRLRE 269
Cdd:PRK02224 669 LDELREERddLQAEIGAVENElEELEELRERREALENRVEALE-ALYDEAEELESMYGDLRAELRQRnvETLERMLNE 745
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
76-301 |
2.11e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 76 TEELCLQREQREELERLNQVLEAEKQqfeEVVQELRMEQEQIKREL-ELTARCLKGVEQEKKELRHLTEsLQQTLEELSI 154
Cdd:PHA02562 194 QQQIKTYNKNIEEQRKKNGENIARKQ---NKYDELVEEAKTIKAEIeELTDELLNLVMDIEDPSAALNK-LNTAAAKIKS 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 155 EKK---KTLEMLEENENHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQ 231
Cdd:PHA02562 270 KIEqfqKVIKMYEKGGVCPTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELKNKISTN 349
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587053 232 SQALQNSLQEltAEKQQAE-RELKAEVKVRmdlerrlREAEGALRSLEQGLNSKVRNKEKEERMRADVSHL 301
Cdd:PHA02562 350 KQSLITLVDK--AKKVKAAiEELQAEFVDN-------AEELAKLQDELDKIVKTKSELVKEKYHRGIVTDL 411
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
52-335 |
2.31e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 52 KSLEAQGLQLAKEKQEYLDKLMEE---TEELCLQREQREELERLNQVLEAEKQQFEEV---------VQELRMEQEQIK- 118
Cdd:PTZ00121 1445 KADEAKKKAEEAKKAEEAKKKAEEakkADEAKKKAEEAKKADEAKKKAEEAKKKADEAkkaaeakkkADEAKKAEEAKKa 1524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 119 RELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQpppsgglhsnLRQIEEKMQ 198
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE----------AKKAEEARI 1594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 199 QLLEEKLLAEKRMKENEERSralEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLE 278
Cdd:PTZ00121 1595 EEVMKLYEEEKKMKAEEAKK---AEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE 1671
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034587053 279 QGLNSKVRNKEKEERMRADVSHLKRFFEECIRNAELEAKMPVIMKNSVYIHKAATRR 335
Cdd:PTZ00121 1672 EDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEN 1728
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
72-289 |
3.02e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 39.49 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 72 LMEETEELCLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEE 151
Cdd:pfam07888 40 LQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 152 LSIEKKKTLEMLEENENHLQTLANQSEQpppsggLHSNLRQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQ 231
Cdd:pfam07888 120 LLAQRAAHEARIRELEEDIKTLTQRVLE------RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034587053 232 SQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREAEGA---LRSLEQGLNSKVRNKE 289
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALleeLRSLQERLNASERKVE 254
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
82-260 |
3.11e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 39.92 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 82 QREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLE 161
Cdd:COG1196 661 SLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 162 MLEENENHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKLLAEkrmkenEErSRALEEEREFYSSQSQALQNSLQE 241
Cdd:COG1196 741 LLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAI------EE-YEELEERYDFLSEQREDLEEARET 813
|
170
....*....|....*....
gi 1034587053 242 LtaekQQAERELKAEVKVR 260
Cdd:COG1196 814 L----EEAIEEIDRETRER 828
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
56-327 |
3.64e-03 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 39.72 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 56 AQGLQLAKEKQEYLDKLMEETEELCLQREQREELE-RLNQVLEAEKQQFEEvvqelRMEQEQIKRELElTARCLKGVEQE 134
Cdd:pfam17380 337 AEQERMAMERERELERIRQEERKRELERIRQEEIAmEISRMRELERLQMER-----QQKNERVRQELE-AARKVKILEEE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 135 K-KELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQpppsgglhSNLRQIEEKMQQLLEEKLLAEKRMKE 213
Cdd:pfam17380 411 RqRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQ--------ERQQQVERLRQQEEERKRKKLELEKE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 214 NEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRlREAEGALRS---------LEQGLNSK 284
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERR-REAEEERRKqqemeerrrIQEQMRKA 561
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1034587053 285 VRNKEKEERMRADVSHLKRFFEECIRNAELEAKMPVIMKNSVY 327
Cdd:pfam17380 562 TEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIKPIY 604
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
94-256 |
4.12e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 39.38 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 94 QVLEAEkQQFEEVVQELRMEQEQIKRELELTARclkgveQEKKELRHLTEslqqtlEELSIEKKKtlemLEENENHLQtl 173
Cdd:PRK12704 32 KIKEAE-EEAKRILEEAKKEAEAIKKEALLEAK------EEIHKLRNEFE------KELRERRNE----LQKLEKRLL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 174 anQSEQpppsgglhsnlrQIEEKMQQLLEEKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQE---LTAEK---- 246
Cdd:PRK12704 93 --QKEE------------NLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERisgLTAEEakei 158
|
170
....*....|..
gi 1034587053 247 --QQAERELKAE 256
Cdd:PRK12704 159 llEKVEEEARHE 170
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
81-279 |
4.76e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 38.98 E-value: 4.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 81 LQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARcLKGVEQEKKELRHLTESLQQTLEELSIEKK--K 158
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQllP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 159 TLEMLEENENHLQTLANQSEQpppsggLHSNLRQIEEKMQQLLEeklLAEKRMKENEERSRALEEEREFYSSQSQALQNS 238
Cdd:COG4717 130 LYQELEALEAELAELPERLEE------LEERLEELRELEEELEE---LEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1034587053 239 LQELTAEKQQAERELKAEVKVRMDLERRLREAEGALRSLEQ 279
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
62-270 |
5.74e-03 |
|
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: 39.18 E-value: 5.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 62 AKEKQEYLDKLMEETEE------LCLQREQREELERLNQVLEAEKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEK 135
Cdd:pfam02463 206 AKKALEYYQLKEKLELEeeyllyLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 136 KELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQPPPSGGLHSNLRQIEEKMQQLLEEKLLAEKRMKENE 215
Cdd:pfam02463 286 EELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQ 365
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1034587053 216 ERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKAEVKVRMDLERRLREA 270
Cdd:pfam02463 366 EKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDL 420
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
20-152 |
6.51e-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: 38.59 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 20 AESEFEQTQWLEMLQESGKVTWKNAQLGEAMIKsLEAQGLQLAKEKQEYLDKLMEETEELCLQ-REQREELERLNQVLEA 98
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLALL-LSPEDFLDAVRRLQYLKYLAPARREQAEElRADLAELAALRAELEA 171
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034587053 99 EKQQFEEVVQELRMEQEQIKRELELTARCLKGVEQEKKELRHLTESLQQTLEEL 152
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
178-258 |
6.59e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 38.78 E-value: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 178 EQPPPSGGLHSNLRQIEEKMQQLLE---EKLLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELK 254
Cdd:PRK11448 136 PPEDPENLLHALQQEVLTLKQQLELqarEKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERK 215
|
....
gi 1034587053 255 AEVK 258
Cdd:PRK11448 216 QKRK 219
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
125-297 |
7.26e-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: 38.90 E-value: 7.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 125 ARCLKGVEQEKKELRHLTESLQQTLEELSIEKKKTLEMLEENENHLQTLANQSEQpppsggLHSNLRQIEEKMQQLLEEK 204
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSD------ASRKIGEIEKEIEQLEQEE 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034587053 205 LLAEKRMKENEERSRALEEEREFYSSQSQALQNSLQELTAEKQQAERELKA-EVKVRM-----------DLERRLREAEG 272
Cdd:TIGR02169 733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDlEARLSHsripeiqaelsKLEEEVSRIEA 812
|
170 180
....*....|....*....|....*
gi 1034587053 273 ALRSLEQGLNSKVRNKEKEERMRAD 297
Cdd:TIGR02169 813 RLREIEQKLNRLTLEKEYLEKEIQE 837
|
|
| |
