|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
835-1154 |
2.14e-14 |
|
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: 78.56 E-value: 2.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 835 ERTLELADYKTKCENQSGFILHLKQLLscgntkfEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLE 914
Cdd:TIGR02168 674 ERRREIEELEEKIEELEEKIAELEKAL-------AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 915 KARNDLQTAYEGFVQKLNQQHQtDQTELENRLKEfYTAECEKLQSIyIEEAEKYKTQLQEQFDNLNAAHETTKLEIeASH 994
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEE-RLEEAEEELAE-AEAEIEELEAQ-IEQLKEELKALREALDELRAELTLLNEEA-ANL 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 995 SEKVELLkktyETSLSEIKKSHEMEKKLLENLlNEKQESLEKQINDLKSE--------NDALNERLKSEEQKQLSREKAN 1066
Cdd:TIGR02168 823 RERLESL----ERRIAATERRLEDLEEQIEEL-SEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELE 897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1067 SKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNttlvdkltrFQQENEELKARMDRHMAISRQLSTEQA 1146
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEE 968
|
....*...
gi 2043665167 1147 ALQESLEK 1154
Cdd:TIGR02168 969 EARRRLKR 976
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
871-1157 |
3.02e-13 |
|
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: 74.71 E-value: 3.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 871 LTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGfVQKLNQQHQTDQTELENRLKEF- 949
Cdd:TIGR02168 230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE-LQKELYALANEISRLEQQKQILr 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 950 ------------YTAECEKLQSiYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKSHE 1017
Cdd:TIGR02168 309 erlanlerqleeLEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-----ESRLEELEEQLE 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1018 MEKKLL------ENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNpQVMYLEQELESLKAVLEIKNE 1091
Cdd:TIGR02168 383 TLRSKVaqlelqIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2043665167 1092 KLHQQDLKLMKMEKlvdnnttlvdKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESK 1157
Cdd:TIGR02168 462 ALEELREELEEAEQ----------ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSG 517
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
881-1169 |
3.45e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 74.20 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 881 EREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEgfvqKLNQQHQTDQTELENRLKEFY--TAECEKLQ 958
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELE----ELRLELEELELELEEAQAEEYelLAELARLE 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 959 SIYIEEAEKyKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKSHEMEKKLLENLLNEKQESLEKQI 1038
Cdd:COG1196 302 QDIARLEER-RRELEERLEELEEELAELEEELEELEEELEEL-----EEELEEAEEELEEAEAELAEAEEALLEAEAELA 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1039 NDLKSENDALNERLksEEQKQLSREKANSKNPQVMylEQELESLKAVLEIKNEKLHQQDLKLmkMEKLVDNNTTLVDKLT 1118
Cdd:COG1196 376 EAEEELEELAEELL--EALRAAAELAAQLEELEEA--EEALLERLERLEEELEELEEALAEL--EEEEEEEEEALEEAAE 449
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2043665167 1119 RFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 1169
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
865-1139 |
2.91e-11 |
|
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: 68.16 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 865 NTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKarndlqtayegFVQKLNQQHQTDQTELEN 944
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQ-----------QKQILRERLANLERQLEE 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 945 rlkefYTAECEKLQSiYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKSHEMEKKLL- 1023
Cdd:TIGR02168 321 -----LEAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-----ESRLEELEEQLETLRSKVa 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1024 -----ENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNpQVMYLEQELESLKAVLEIKNEKLHQQDL 1098
Cdd:TIGR02168 390 qlelqIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELRE 468
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2043665167 1099 KLMKMEKLVDnntTLVDKLTRFQQENEELKARMDRHMAISR 1139
Cdd:TIGR02168 469 ELEEAEQALD---AAERELAQLQARLDSLERLQENLEGFSE 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
878-1169 |
4.78e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.40 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 878 LLSEREEALKQHKTLSQELVSLRGELvaasstcEKLEKARNDLQTAYEGFVQKLNQ-------QHQTDQTELENRLKEFy 950
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEEL-------EKLTEEISELEKRLEEIEQLLEElnkkikdLGEEEQLRVKEKIGEL- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 951 TAECEKLQSIY------IEEAEKYKTQLQEQFDNLNAAHETTKLEIE------ASHSEKVELLKKTYETSLSEIKkshEM 1018
Cdd:TIGR02169 300 EAEIASLERSIaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrDKLTEEYAELKEELEDLRAELE---EV 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1019 EKKLLEnlLNEKQESLEKQINDLKSENDAL--NERLKSEEQKQLSREKANSKNpQVMYLEQELESLKAVLEIKNEKLHQQ 1096
Cdd:TIGR02169 377 DKEFAE--TRDELKDYREKLEKLKREINELkrELDRLQEELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKKQ 453
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2043665167 1097 DLKLMkmeklvdnntTLVDKLTRFQQENEELKarmdrhmaisrqlsteqaalqeslEKESKVNKRLSMENEEL 1169
Cdd:TIGR02169 454 EWKLE----------QLAADLSKYEQELYDLK------------------------EEYDRVEKELSKLQREL 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
911-1169 |
7.30e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.02 E-value: 7.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 911 EKLEKARNDLQtayegfvqklnqqhqtdqtELENRLKEFYTAECEKLQsiyieeaekyktQLQeqfdnlnaahettKLEI 990
Cdd:TIGR02169 170 RKKEKALEELE-------------------EVEENIERLDLIIDEKRQ------------QLE-------------RLRR 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 991 EASHSEKV-ELLKKTYETSLSEI---KKSHEMEKKLLENLLNEKQESLEK---QINDLKSENDALNERLK--SEEQKQLS 1061
Cdd:TIGR02169 206 EREKAERYqALLKEKREYEGYELlkeKEALERQKEAIERQLASLEEELEKlteEISELEKRLEEIEQLLEelNKKIKDLG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1062 REKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQE--------NEELKARMDR 1133
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklTEEYAELKEE 365
|
250 260 270
....*....|....*....|....*....|....*.
gi 2043665167 1134 HMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 1169
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREI 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
865-1171 |
1.19e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.11 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 865 NTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLqtayegfvQKLNQQHQTDQTELEN 944
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL--------EERRRELEERLEELEE 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 945 RLKEfytaecEKLQsiyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKSHEMEKKLLE 1024
Cdd:COG1196 324 ELAE------LEEE---LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA-----EAELAEAEEELEELAEELL 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1025 NLLNEKQEsLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqvmyLEQELESLKAVLEIKNEKLHQQDLKLMKME 1104
Cdd:COG1196 390 EALRAAAE-LAAQLEELEEAEEALLERLERLEEELEELEEALAE------LEEEEEEEEEALEEAAEEEAELEEEEEALL 462
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2043665167 1105 KLvdnnttLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELLW 1171
Cdd:COG1196 463 EL------LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
875-1169 |
2.54e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 64.96 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 875 IQHLLSEREEALKqHKTLSQELVSLRGELVAAsstceKLEKARNDLQtayegfvqKLNQQHQTDQTELENRLKEfytaec 954
Cdd:COG1196 202 LEPLERQAEKAER-YRELKEELKELEAELLLL-----KLRELEAELE--------ELEAELEELEAELEELEAE------ 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 955 eklqsiyIEEAEKYKTQLQEQFDNLNaahettkLEIEAsHSEKVELLKKTYETSLSEIKKSHEMEKKLLENL--LNEKQE 1032
Cdd:COG1196 262 -------LAELEAELEELRLELEELE-------LELEE-AQAEEYELLAELARLEQDIARLEERRRELEERLeeLEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1033 SLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqvmyLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTT 1112
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAE------AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2043665167 1113 LVDKLTRFQQENEELKARMDRhmAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 1169
Cdd:COG1196 401 QLEELEEAEEALLERLERLEE--ELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
881-1169 |
1.66e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 62.50 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 881 EREEALKQHKTLSQELVSLRGELVAASstcEKLEKA--RNDLQTAYEGFVQKLNQQHQTDQTELENRL--KEFYTAECEK 956
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAQLAKKE---EELQAAlaRLEEETAQKNNALKKIRELEAQISELQEDLesERAARNKAEK 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 957 LQSIYIEEAEKYKTQLQEQFDNLNAAHE-TTKLEIEASHSEK-VELLKKTYETSLSEIKKSHEME-KKLLENLLNEK--Q 1031
Cdd:pfam01576 293 QRRDLGEELEALKTELEDTLDTTAAQQElRSKREQEVTELKKaLEEETRSHEAQLQEMRQKHTQAlEELTEQLEQAKrnK 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1032 ESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqvmyLEQELESLKAVL-EIKNEKLHQQDlKLMKMEKLVDNN 1110
Cdd:pfam01576 373 ANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKK------LEGQLQELQARLsESERQRAELAE-KLSKLQSELESV 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1111 TTLVD----KLTRFQ----------QENEELKARMDRH-MAIS---RQLSTEQAALQESLEKESK----VNKRLSMENEE 1168
Cdd:pfam01576 446 SSLLNeaegKNIKLSkdvsslesqlQDTQELLQEETRQkLNLStrlRQLEDERNSLQEQLEEEEEakrnVERQLSTLQAQ 525
|
.
gi 2043665167 1169 L 1169
Cdd:pfam01576 526 L 526
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
844-1161 |
4.09e-09 |
|
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: 61.14 E-value: 4.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 844 KTKCENQSGFILHLKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKT-LSQELVSLRGELVAAsstcEKLEKARNDLQT 922
Cdd:pfam02463 699 LEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDeEEEEEEKSRLKKEEK----EEEKSELSLKEK 774
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 923 AYEgfVQKLNQQHQTDQTELENRLKEfYTAECEKLqsiyiEEAEKYKTQLQEQFDNL-NAAHETTKLEIEASHSEKVELL 1001
Cdd:pfam02463 775 ELA--EEREKTEKLKVEEEKEEKLKA-QEEELRAL-----EEELKEEAELLEEEQLLiEQEEKIKEEELEELALELKEEQ 846
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1002 KKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKQinDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELES 1081
Cdd:pfam02463 847 KLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ--KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIK 924
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1082 LKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKR 1161
Cdd:pfam02463 925 EEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEK 1004
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
900-1174 |
3.17e-08 |
|
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: 58.06 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 900 RGELVAASSTcEKLEKARNDLQTAYEGFVQK-LNQQHQTDQTELENrlkefytaECEKLQSIY-IEEAEKYKTQLQEQFD 977
Cdd:TIGR00618 117 RGRILAAKKS-ETEEVIHDLLKLDYKTFTRVvLLPQGEFAQFLKAK--------SKEKKELLMnLFPLDQYTQLALMEFA 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 978 NLNAAHetTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKqindLKSENDALNERLKSEEQ 1057
Cdd:TIGR00618 188 KKKSLH--GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY----LTQKREAQEEQLKKQQL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1058 KQlsrekansknpQVMYLEQELESLKAVLEIKNEKLHQQDLK---LMKMEKLVDNNTTLVDKLTRFQ-QENEELKARMDR 1133
Cdd:TIGR00618 262 LK-----------QLRARIEELRAQEAVLEETQERINRARKAaplAAHIKAVTQIEQQAQRIHTELQsKMRSRAKLLMKR 330
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2043665167 1134 HMAISRQLS-TEQAALQESLEKESKVNKRLSmeNEELLWKLH 1174
Cdd:TIGR00618 331 AAHVKQQSSiEEQRRLLQTLHSQEIHIRDAH--EVATSIREI 370
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
834-1169 |
4.84e-08 |
|
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: 57.34 E-value: 4.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 834 TERTLELADYKTKCENQsgfILHLKQLLSCGNTKFEALtvviQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKL 913
Cdd:TIGR04523 165 KKQKEELENELNLLEKE---KLNIQKNIDKIKNKLLKL----ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 914 EKARNDLQTAYEGFVQKLNQ---QHQTDQTELENRLKEFYTA-----ECEK-LQSIY--IEEAEKYKTQ-----LQEQFD 977
Cdd:TIGR04523 238 QQEINEKTTEISNTQTQLNQlkdEQNKIKKQLSEKQKELEQNnkkikELEKqLNQLKseISDLNNQKEQdwnkeLKSELK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 978 NLNAAHETTKLEIEASHS------EKVELLKKTYETSLSE-IKKSHEMEKK--LLENLLNEKQ------ESLEKQINDLK 1042
Cdd:TIGR04523 318 NQEKKLEEIQNQISQNNKiisqlnEQISQLKKELTNSESEnSEKQRELEEKqnEIEKLKKENQsykqeiKNLESQINDLE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1043 SE-------NDALNERLKSEEQ--KQLSREKANSKNpQVMYLEQELESLK---AVLEIKNEKLH----QQDLKLMKMEKL 1106
Cdd:TIGR04523 398 SKiqnqeklNQQKDEQIKKLQQekELLEKEIERLKE-TIIKNNSEIKDLTnqdSVKELIIKNLDntreSLETQLKVLSRS 476
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2043665167 1107 VDNN-TTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 1169
Cdd:TIGR04523 477 INKIkQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKI 540
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
866-1170 |
4.94e-08 |
|
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: 57.42 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 866 TKFEALTVVIQHLLSEREEALKQHKtlsQELVSLRGELVAASSTCEKLEKARNDLQTAYEGF----------------VQ 929
Cdd:pfam05483 352 TEFEATTCSLEELLRTEQQRLEKNE---DQLKIITMELQKKSSELEEMTKFKNNKEVELEELkkilaedeklldekkqFE 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 930 KLNQQHQTDQTEL----ENRLKEFYTAECE-----KLQSIYIEEAEKYKTQLQEQ---------------FDNLNAAHET 985
Cdd:pfam05483 429 KIAEELKGKEQELifllQAREKEIHDLEIQltaikTSEEHYLKEVEDLKTELEKEklknieltahcdkllLENKELTQEA 508
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 986 TKLEIE-ASHSEKVELLKKTYETSLSEIKKSHEMEKKLlENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREK 1064
Cdd:pfam05483 509 SDMTLElKKHQEDIINCKKQEERMLKQIENLEEKEMNL-RDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEK 587
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1065 A---------------NSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKME-KLVDNNTTLVDKLTRFQQENEELK 1128
Cdd:pfam05483 588 QmkilenkcnnlkkqiENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKEIEDKK 667
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2043665167 1129 ARMDRHMAisrQLSTEQAALQESLEKESKVNKRLSMENEELL 1170
Cdd:pfam05483 668 ISEEKLLE---EVEKAKAIADEAVKLQKEIDKRCQHKIAEMV 706
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
971-1154 |
5.65e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 5.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 971 QLQEQFDNLNAAHETtkLEIEAshsEKVELLK------KTYETSLSEIKKSHEMEKKL-------LENLLNEKQESLEKQ 1037
Cdd:COG4913 229 ALVEHFDDLERAHEA--LEDAR---EQIELLEpirelaERYAAARERLAELEYLRAALrlwfaqrRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1038 INDLKSENDALNERLKSEEQK--QLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQD--LKLMKM------EKLV 1107
Cdd:COG4913 304 LARLEAELERLEARLDALREEldELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEalLAALGLplpasaEEFA 383
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1108 DNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQ---ESLEK 1154
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEaeiASLER 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
835-1170 |
7.58e-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: 57.00 E-value: 7.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 835 ERTLELADYKTKCENQSGFIL----HLKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELvaaSSTC 910
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQselrRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL---SSLE 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 911 EKLEKARNDLQTayegfVQKLNQQHQTDQTELENRLKEFYTAEC-EKLQSI--YIEEAEKYKTQLQEQFDNLNAAHETTK 987
Cdd:TIGR02169 751 QEIENVKSELKE-----LEARIEELEEDLHKLEEALNDLEARLShSRIPEIqaELSKLEEEVSRIEARLREIEQKLNRLT 825
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 988 LEIEASHSEKVELLKKTYETSL---SEIKKSHEMEKKL--LENLLNEKQ---ESLEKQINDLKSENDALNERLKSEEQKQ 1059
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEqikSIEKEIENLNGKKeeLEEELEELEaalRDLESRLGDLKKERDELEAQLRELERKI 905
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1060 lsrEKANSknpQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISR 1139
Cdd:TIGR02169 906 ---EELEA---QIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQ 979
|
330 340 350
....*....|....*....|....*....|.
gi 2043665167 1140 QLSTEQAALQESLEKESKvnkrLSMENEELL 1170
Cdd:TIGR02169 980 EYEEVLKRLDELKEKRAK----LEEERKAIL 1006
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
962-1170 |
1.83e-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: 55.83 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 962 IEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSlseiKKSHEMEKKLLEnlLNEKQESLEKQINDL 1041
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELS----RQISALRKDLAR--LEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1042 KSEndalneRLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEK----LVDNNTTLVDKL 1117
Cdd:TIGR02168 753 SKE------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAeltlLNEEAANLRERL 826
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2043665167 1118 TRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELL 1170
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALL 879
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
844-1127 |
1.87e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.41 E-value: 1.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 844 KTKCENQSGF--ILHLKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQ 921
Cdd:TIGR04523 374 KLKKENQSYKqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 922 TAYEgfvqKLNQQhqtdQTELENRLKEFyTAECEKLQSiyieEAEKYKTQLQE---QFDNLNAahETTKLEieashsEKV 998
Cdd:TIGR04523 454 LIIK----NLDNT----RESLETQLKVL-SRSINKIKQ----NLEQKQKELKSkekELKKLNE--EKKELE------EKV 512
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 999 ELLKKTYETSLSEIKKshemekklLENLLNEKqeslEKQINDLKSENDALNERLKSEEQKqlsrEKANSKNPQVMYLEQE 1078
Cdd:TIGR04523 513 KDLTKKISSLKEKIEK--------LESEKKEK----ESKISDLEDELNKDDFELKKENLE----KEIDEKNKEIEELKQT 576
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2043665167 1079 LESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTR----FQQENEEL 1127
Cdd:TIGR04523 577 QKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKelekAKKENEKL 629
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
867-1102 |
2.18e-07 |
|
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: 54.77 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 867 KFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAyegfVQKLNQQHQTDQTELENRL 946
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 947 KEFYtaecEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLE-IEASHSEKVELLKKTYETsLSEIKKSHEMEKKLLEN 1025
Cdd:COG4942 104 EELA----ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKyLAPARREQAEELRADLAE-LAALRAELEAERAELEA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1026 LLNEKQE---SLEKQINDLKSENDALNERLKsEEQKQLSREKANSKNpqvmyLEQELESLKAVLEIKNEKLHQQDLKLMK 1102
Cdd:COG4942 179 LLAELEEeraALEALKAERQKLLARLEKELA-ELAAELAELQQEAEE-----LEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
958-1188 |
2.38e-07 |
|
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: 54.38 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 958 QSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkktyETSLSEIKKshemekklLENLLNEKQESLEKQ 1037
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL-----ERRIAALAR--------RIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1038 INDLKSENDALNERLKsEEQKQLSR-----EKANSKNPQVMYLEQE--------LESLKAVLEIKNEKLHQQDLKLMKME 1104
Cdd:COG4942 85 LAELEKEIAELRAELE-AQKEELAEllralYRLGRQPPLALLLSPEdfldavrrLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1105 KLVDNNTTLVDKLTRFQQENEE----LKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLsmenEELLWKLHNGDLCS 1180
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEeraaLEALKAERQKLLARLEKELAELAAELAELQQEAEEL----EALIARLEAEAAAA 239
|
....*...
gi 2043665167 1181 PKRSPTSS 1188
Cdd:COG4942 240 AERTPAAG 247
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
956-1169 |
2.75e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 956 KLQSIYIEEAEKYKTQLQEQFDNL------NAAHETTKLE------IEASHSEKVELLKKTYETSLSEIKKSHEMEKKLL 1023
Cdd:COG4717 2 KIKELEIYGFGKFRDRTIEFSPGLnviygpNEAGKSTLLAfiramlLERLEKEADELFKPQGRKPELNLKELKELEEELK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1024 E--------NLLNEKQESLEKQINDLKSENDALNERLKSEEQKQlsrekansknpQVMYLEQELESLKAVLEIKNEKLHQ 1095
Cdd:COG4717 82 EaeekeeeyAELQEELEELEEELEELEAELEELREELEKLEKLL-----------QLLPLYQELEALEAELAELPERLEE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2043665167 1096 QDLKLMKMEklvdnntTLVDKLTRFQQENEELKARMDRHMaisRQLSTE-QAALQESLEKESKVNKRLSMENEEL 1169
Cdd:COG4717 151 LEERLEELR-------ELEEELEELEAELAELQEELEELL---EQLSLAtEEELQDLAEELEELQQRLAELEEEL 215
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
913-1169 |
2.86e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.75 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 913 LEKARNDLQTAYEGFVQKlNQQHQTDQTELENRLKEFYTA-----ECEKLQSIYIEEAEKyktQLQEQFDNLNAAHETT- 986
Cdd:pfam05557 32 LEKKASALKRQLDRESDR-NQELQKRIRLLEKREAEAEEAlreqaELNRLKKKYLEALNK---KLNEKESQLADAREVIs 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 987 --KLEIEASH--SEKVELLKKTYETSLSEIKKSHEMEKKLLENLlNEKQESLEKQINDLKSENDALNE---RLKSEEQKQ 1059
Cdd:pfam05557 108 clKNELSELRrqIQRAELELQSTNSELEELQERLDLLKAKASEA-EQLRQNLEKQQSSLAEAEQRIKElefEIQSQEQDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1060 LSREKANSKNPQVMYLEQELESLK-------------------------------------AVLEIKNEKLHQqdlKLMK 1102
Cdd:pfam05557 187 EIVKNSKSELARIPELEKELERLRehnkhlnenienklllkeevedlkrklereekyreeaATLELEKEKLEQ---ELQS 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1103 MEKLVDNNT-------TLVDKLTRFQQENEELKARMD------RHMAISR-QLSTEQAALQESLEKESKVNKRLSMENEE 1168
Cdd:pfam05557 264 WVKLAQDTGlnlrspeDLSRRIEQLQQREIVLKEENSsltssaRQLEKARrELEQELAQYLKKIEDLNKKLKRHKALVRR 343
|
.
gi 2043665167 1169 L 1169
Cdd:pfam05557 344 L 344
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
875-1174 |
3.34e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 54.68 E-value: 3.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 875 IQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAyEGFV----QKLNQQHqtdqtelENRLKEFY 950
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKA-KGKCpvcgRELTEEH-------RKELLEEY 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 951 TAECEKLQSiYIEEAEKYKTQLQEqfdnlnaahETTKLEIEASHSEKVELLKKTYEtSLSEIKKshEMEKKLLENL--LN 1028
Cdd:PRK03918 458 TAELKRIEK-ELKEIEEKERKLRK---------ELRELEKVLKKESELIKLKELAE-QLKELEE--KLKKYNLEELekKA 524
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1029 EKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqVMYLEQELESLKAVLEIKN-EKLHQQDLKLMKMEKLV 1107
Cdd:PRK03918 525 EEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK---LDELEEELAELLKELEELGfESVEELEERLKELEPFY 601
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2043665167 1108 DNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELLWKLH 1174
Cdd:PRK03918 602 NEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
876-1153 |
4.76e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.41 E-value: 4.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 876 QHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAyegfvqklNQQHQTDQTELENRLKEfytaECE 955
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAAR--------KQELEEILHELESRLEE----EEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 956 KLQSIYIEeaekyKTQLQEQFDNLNAahettKLEIEASHSEKVELLKKTYEtslSEIKKSHE-------------MEKKL 1022
Cdd:pfam01576 90 RSQQLQNE-----KKKMQQHIQDLEE-----QLDEEEAARQKLQLEKVTTE---AKIKKLEEdillledqnsklsKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1023 LENLLNE------KQESLEKQINDLKSENDA----LNERLKSEEQKQLSREKANSK--------NPQVMYLEQELESLKA 1084
Cdd:pfam01576 157 LEERISEftsnlaEEEEKAKSLSKLKNKHEAmisdLEERLKKEEKGRQELEKAKRKlegestdlQEQIAELQAQIAELRA 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2043665167 1085 VLEIKNEKLhqQDLkLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAI-------SRQLSTEQAALQESLE 1153
Cdd:pfam01576 237 QLAKKEEEL--QAA-LARLEEETAQKNNALKKIRELEAQISELQEDLESERAArnkaekqRRDLGEELEALKTELE 309
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
875-1040 |
5.88e-07 |
|
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: 51.85 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 875 IQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAY---EGFVQKLNQQHQTDQTELEN--RLKEF 949
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLGNvrNNKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 950 --YTAECEKLQSIyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEAsHSEKVELLKKTYETSLSEIKKshEMEKkllenlL 1027
Cdd:COG1579 92 eaLQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAE-LEAELEEKKAELDEELAELEA--ELEE------L 161
|
170
....*....|...
gi 2043665167 1028 NEKQESLEKQIND 1040
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
881-1163 |
8.71e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 8.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 881 EREEALKQHKtlsQELVSLRGELVAASSTCEKLEKARNDLQTAYEGfVQKLNQQHQT-DQ-TELENRLKEFYTAECEKlq 958
Cdd:PRK03918 449 HRKELLEEYT---AELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELaEQlKELEEKLKKYNLEELEK-- 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 959 siyieEAEKYKTqLQEQFDNLNAAHETTKLEIEashseKVELLKKTYETSLSEIKKSHEMEKKL---LENLLNEKQESLE 1035
Cdd:PRK03918 523 -----KAEEYEK-LKEKLIKLKGEIKSLKKELE-----KLEELKKKLAELEKKLDELEEELAELlkeLEELGFESVEELE 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1036 KQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLM--KMEKLVDNNTTL 1113
Cdd:PRK03918 592 ERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeEYEELREEYLEL 671
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1114 VDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLS 1163
Cdd:PRK03918 672 SRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
879-1126 |
1.01e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 879 LSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEkarndlqtayegfvqklnqqhqtdqtELENRLKEFYtaecEKLQ 958
Cdd:PRK03918 517 LEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE--------------------------ELKKKLAELE----KKLD 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 959 SIYIEEAEKYKTQLQEQFDNLNAAHETTKlEIEASHSEKVELL--KKTYETSLSEIKKSHEMEKKLLENL--LNEKQESL 1034
Cdd:PRK03918 567 ELEEELAELLKELEELGFESVEELEERLK-ELEPFYNEYLELKdaEKELEREEKELKKLEEELDKAFEELaeTEKRLEEL 645
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1035 EKQINDLKSENDALNERLKSEEQKQLSREKAnSKNPQVMYLEQELESLKAVLE-IKNEK--LHQQDLKLMKMEKLVDNNT 1111
Cdd:PRK03918 646 RKELEELEKKYSEEEYEELREEYLELSRELA-GLRAELEELEKRREEIKKTLEkLKEELeeREKAKKELEKLEKALERVE 724
|
250
....*....|....*
gi 2043665167 1112 TLVDKLTRFQQENEE 1126
Cdd:PRK03918 725 ELREKVKKYKALLKE 739
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
836-1154 |
1.10e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.14 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 836 RTLELADYKTKCENQSGFILHLKQLLScGNTKFEALTVVIQHLLSERE----EALKQHKTLSQELVSLRGELVAASSTCE 911
Cdd:PRK03918 153 QILGLDDYENAYKNLGEVIKEIKRRIE-RLEKFIKRTENIEELIKEKEkeleEVLREINEISSELPELREELEKLEKEVK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 912 KLEKARNDLQTAyegfvQKLNQQHQTDQTELENRLKEFytaecEKlqsiYIEEAEKYKTQLQEQfdnlnaAHETTKLEIE 991
Cdd:PRK03918 232 ELEELKEEIEEL-----EKELESLEGSKRKLEEKIREL-----EE----RIEELKKEIEELEEK------VKELKELKEK 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 992 ASHSEKVELLKKTYETSLSEIKKshemEKKLLENLLNEkqesLEKQINDLKSENDALNERLKSEEqkqlsrekansknpq 1071
Cdd:PRK03918 292 AEEYIKLSEFYEEYLDELREIEK----RLSRLEEEING----IEERIKELEEKEERLEELKKKLK--------------- 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1072 vmyleqELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNT-----TLVDKLTRFQQENEELKARMDRHMAISRQLSTEQA 1146
Cdd:PRK03918 349 ------ELEKRLEELEERHELYEEAKAKKEELERLKKRLTgltpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIK 422
|
....*...
gi 2043665167 1147 ALQESLEK 1154
Cdd:PRK03918 423 ELKKAIEE 430
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
940-1170 |
1.19e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 53.02 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 940 TELENRLkefytaecEKL--QSiyiEEAEKYKtQLQEQFD----NLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIK 1013
Cdd:COG1196 196 GELERQL--------EPLerQA---EKAERYR-ELKEELKeleaELLLLKLRELEAELEELEAELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1014 kshEMEKKLLEnlLNEKQESLEKQINDLKSENDALNERLkSEEQKQLSREKANSKNpqvmyLEQELESLKAVLEIKNEKL 1093
Cdd:COG1196 264 ---ELEAELEE--LRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRE-----LEERLEELEEELAELEEEL 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1094 HQQDLKL---------------MKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKV 1158
Cdd:COG1196 333 EELEEELeeleeeleeaeeeleEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
250
....*....|..
gi 2043665167 1159 NKRLSMENEELL 1170
Cdd:COG1196 413 LERLERLEEELE 424
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
848-1149 |
1.26e-06 |
|
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: 53.20 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 848 ENQSGFILHLKQLLScgNTKFEALTVVIQHLLSEreealkqhktLSQELVSLRGELVAASstcEKLEKARNDLQTAYEgf 927
Cdd:pfam15921 197 EEASGKKIYEHDSMS--TMHFRSLGSAISKILRE----------LDTEISYLKGRIFPVE---DQLEALKSESQNKIE-- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 928 vqKLNQQHQTDQTELENRLKEFYTAECEKLQSIYiEEAEKYKTQL---QEQFDNLNAAHETTKLEIEASHSE-KVEL--L 1001
Cdd:pfam15921 260 --LLLQQHQDRIEQLISEHEVEITGLTEKASSAR-SQANSIQSQLeiiQEQARNQNSMYMRQLSDLESTVSQlRSELreA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1002 KKTYETSLSEIKKS-------------------------HEMEKKLLENL-LNEKQESLEKQ---------------IND 1040
Cdd:pfam15921 337 KRMYEDKIEELEKQlvlanseltearterdqfsqesgnlDDQLQKLLADLhKREKELSLEKEqnkrlwdrdtgnsitIDH 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1041 LKSEND----------ALNERLKSEEQKQLSREKA-----NSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEK 1105
Cdd:pfam15921 417 LRRELDdrnmevqrleALLKAMKSECQGQMERQMAaiqgkNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSER 496
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2043665167 1106 LV-DNNTTLVDKLTRFQQENEE---LKARMDRHMAISRQLSTEQAALQ 1149
Cdd:pfam15921 497 TVsDLTASLQEKERAIEATNAEitkLRSRVDLKLQELQHLKNEGDHLR 544
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
876-1156 |
1.36e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 52.92 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 876 QHLLSEREEALKQHKTLSQeLVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTD----------QTELENR 945
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQ-LPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDiagikdklakIREARDR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 946 LKEFYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKtyETSLSEIKKSHEMEKKLlen 1025
Cdd:pfam12128 409 QLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQL--ENFDERIERAREEQEAA--- 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1026 llNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVM---------YLEQEL----ESLKAVleIKNEK 1092
Cdd:pfam12128 484 --NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLfpqagtllhFLRKEApdweQSIGKV--ISPEL 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1093 LHQQDLKLMKMEKLVDNNTTLVD---KLTRFQ-----QENEELKARMD-----------RHMAISRQLSTEQAALQESLE 1153
Cdd:pfam12128 560 LHRTDLDPEVWDGSVGGELNLYGvklDLKRIDvpewaASEEELRERLDkaeealqsareKQAAAEEQLVQANGELEKASR 639
|
...
gi 2043665167 1154 KES 1156
Cdd:pfam12128 640 EET 642
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
839-1134 |
1.61e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 52.15 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 839 ELADYKTKCENQSGFILHLKQL-------LSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQElvslrGELVAASSTCE 911
Cdd:PRK04778 127 ELQELLESEEKNREEVEQLKDLyrelrksLLANRFSFGPALDELEKQLENLEEEFSQFVELTES-----GDYVEAREILD 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 912 KLEKARN--------------DLQTAYEGFVQKLNQQHQT--------DQTELENRLKEFYTA--ECEK-LQSIYIEEAE 966
Cdd:PRK04778 202 QLEEELAaleqimeeipellkELQTELPDQLQELKAGYRElveegyhlDHLDIEKEIQDLKEQidENLAlLEELDLDEAE 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 967 KYKTQLQEQFDNLNAAHETtklEIEASHseKVELLKKTYETSLSEIKkshEMEKKLLENL--------LN----EKQESL 1034
Cdd:PRK04778 282 EKNEEIQERIDQLYDILER---EVKARK--YVEKNSDTLPDFLEHAK---EQNKELKEEIdrvkqsytLNeselESVRQL 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1035 EKQINDLKSENDALNERLksEEQKQLSREkansknpqvmyLEQELESLKAVL-EIKNEklhQQDLKLMkMEKLVDNNTTL 1113
Cdd:PRK04778 354 EKQLESLEKQYDEITERI--AEQEIAYSE-----------LQEELEEILKQLeEIEKE---QEKLSEM-LQGLRKDELEA 416
|
330 340
....*....|....*....|.
gi 2043665167 1114 VDKLTRFQQENEELKARMDRH 1134
Cdd:PRK04778 417 REKLERYRNKLHEIKRYLEKS 437
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
932-1169 |
1.83e-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: 52.33 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 932 NQQHQTDQTELENRLKEfyTAECEKLQSIYIEEAEKYKTQLQEqfdnLNAAHETTKLEIEASHSEKVELLKK--TYETSL 1009
Cdd:TIGR04523 116 KEQKNKLEVELNKLEKQ--KKENKKNIDKFLTEIKKKEKELEK----LNNKYNDLKKQKEELENELNLLEKEklNIQKNI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1010 SEIKKSHEMEKKLLENL--LNEKQESLEKQINDLKSENDALNERLKsEEQKQLSREKA--NSKNPQVMYLEQELESLKAV 1085
Cdd:TIGR04523 190 DKIKNKLLKLELLLSNLkkKIQKNKSLESQISELKKQNNQLKDNIE-KKQQEINEKTTeiSNTQTQLNQLKDEQNKIKKQ 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1086 LEIKNEKLHQQDLKLMKMEKLVDNnttLVDKLTRFQQENEElkarmDRHMAISRQLSTEQAALQESLEKESKVNKRLSME 1165
Cdd:TIGR04523 269 LSEKQKELEQNNKKIKELEKQLNQ---LKSEISDLNNQKEQ-----DWNKELKSELKNQEKKLEEIQNQISQNNKIISQL 340
|
....
gi 2043665167 1166 NEEL 1169
Cdd:TIGR04523 341 NEQI 344
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
873-1170 |
2.31e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.44 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 873 VVIQHLLSEREEALKQHKTLSQELVSLRGELvaaSSTCEKLEKARNDLQTAyegfvqklnqqhQTDQTELENRLKEFYTA 952
Cdd:COG4372 24 ILIAALSEQLRKALFELDKLQEELEQLREEL---EQAREELEQLEEELEQA------------RSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 953 eceklqsiyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELL--KKTYETSLSEIKKSHEMEKKLLENlLNEK 1030
Cdd:COG4372 89 ---------LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEqqRKQLEAQIAELQSEIAEREEELKE-LEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1031 QESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqvmYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNN 1110
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNA-----EKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1111 TTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELL 1170
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAAL 293
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
996-1155 |
2.92e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 2.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 996 EKVELLKKTYETSLSEIKKsheMEKKLLEnlLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYL 1075
Cdd:COG3883 23 KELSELQAELEAAQAELDA---LQAELEE--LNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1076 EQELES-LKAVLEIKNeklhQQDL--KLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESL 1152
Cdd:COG3883 98 SGGSVSyLDVLLGSES----FSDFldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
...
gi 2043665167 1153 EKE 1155
Cdd:COG3883 174 EAQ 176
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
911-1101 |
3.44e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 911 EKLEKARNDLQTAYEGFVQKLNQQHQTDQ--TELENRLKEFYT--AECEKLQSIYieEAEKYKTQLQEQFDNLNAAHEtt 986
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEelEELEAELEELREelEKLEKLLQLL--PLYQELEALEAELAELPERLE-- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 987 klEIEASHSEKVELlkktyETSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKS--EEQKQLSREK 1064
Cdd:COG4717 150 --ELEERLEELREL-----EEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEleEELEEAQEEL 222
|
170 180 190
....*....|....*....|....*....|....*....
gi 2043665167 1065 ANsknpqvmyLEQELESLKAVLEI--KNEKLHQQDLKLM 1101
Cdd:COG4717 223 EE--------LEEELEQLENELEAaaLEERLKEARLLLL 253
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
881-1170 |
3.77e-06 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 50.83 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 881 EREEALKQHKTL-SQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQK-----LNQQHQTDQTELENRLKEFYTAEC 954
Cdd:pfam15742 41 GKNLDLKQHNSLlQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKireleLEVLKQAQSIKSQNSLQEKLAQEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 955 EKLQsiyieEAEKYKTQLQEQfdnLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKkSHEMEKKLLENLLNEKQESL 1034
Cdd:pfam15742 121 SRVA-----DAEEKILELQQK---LEHAHKVCLTDTCILEKKQLEERIKEASENEAKLK-QQYQEEQQKRKLLDQNVNEL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1035 EKQINDLKsENDALNERLKSEEQ----------KQLSREKANS----KNPQ-----VMYLEQELESLKAVLEI------- 1088
Cdd:pfam15742 192 QQQVRSLQ-DKEAQLEMTNSQQQlriqqqeaqlKQLENEKRKSdehlKSNQelsekLSSLQQEKEALQEELQQvlkqldv 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1089 ----KNEKLHQQDLKLMKMEKlvdnnttlvdkltRFQQENEELKARMdrhmaisRQLSTEQAALQESLEKESKVNKRLSM 1164
Cdd:pfam15742 271 hvrkYNEKHHHHKAKLRRAKD-------------RLVHEVEQRDERI-------KQLENEIGILQQQSEKEKAFQKQVTA 330
|
....*.
gi 2043665167 1165 ENEELL 1170
Cdd:pfam15742 331 QNEILL 336
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
834-1138 |
4.06e-06 |
|
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: 51.51 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 834 TERTLELADYKTKCENQsgfILHLKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKL 913
Cdd:pfam02463 222 EEEYLLYLDYLKLNEER---IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 914 EKARNDLQTAYEgfvqKLNQQHQTDQTELENRLKEfytaecEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETT--KLEIE 991
Cdd:pfam02463 299 KSELLKLERRKV----DDEEKLKESEKEKKKAEKE------LKKEKEEIEELEKELKELEIKREAEEEEEEELekLQEKL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 992 ASHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQE--SLEKQINDLKseNDALNERLKSEEQKQLSREKANSKN 1069
Cdd:pfam02463 369 EQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLllELARQLEDLL--KEEKKEELEILEEEEESIELKQGKL 446
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2043665167 1070 PQVmylEQELESLKAVLEIKNEKLHQQDLKLmKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAIS 1138
Cdd:pfam02463 447 TEE---KEELEKQELKLLKDELELKKSEDLL-KETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKV 511
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
867-1165 |
4.40e-06 |
|
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: 50.66 E-value: 4.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 867 KFEALTVVIQHLLSEREEALKQHKtlsqELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTELEnRL 946
Cdd:pfam07888 81 RVAELKEELRQSREKHEELEEKYK----ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELE-RM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 947 KEfytaeceklqsiyieEAEKYKTQLQEQfdnlNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKklLENL 1026
Cdd:pfam07888 156 KE---------------RAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQ--LQDT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1027 LNEKQESLEkQINDLKSENDALNERLKSeeqkqlSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKME-K 1105
Cdd:pfam07888 215 ITTLTQKLT-TAHRKEAENEALLEELRS------LQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTlQ 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1106 LVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSME 1165
Cdd:pfam07888 288 LADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
941-1134 |
4.56e-06 |
|
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: 50.62 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 941 ELENRLKEfYTAECEKLQsiyIEEAEKYKTQLQEQFDNLNAAHETtklEIEASHseKVELLKKTYETSLSEIKKSHEMEK 1020
Cdd:pfam06160 241 QLEEQLEE-NLALLENLE---LDEAEEALEEIEERIDQLYDLLEK---EVDAKK--YVEKNLPEIEDYLEHAEEQNKELK 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1021 KLLENL-----LN----EKQESLEKQINDLKSENDALNERLKSEEQkqlsrekansknPQVMYLEQELESLKAVLEIKNE 1091
Cdd:pfam06160 312 EELERVqqsytLNenelERVRGLEKQLEELEKRYDEIVERLEEKEV------------AYSELQEELEEILEQLEEIEEE 379
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2043665167 1092 klhQQDLK--LMKMEKlvDNNTTLvDKLTRFQQENEELKARMDRH 1134
Cdd:pfam06160 380 ---QEEFKesLQSLRK--DELEAR-EKLDEFKLELREIKRLVEKS 418
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
883-1043 |
5.45e-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: 5.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 883 EEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLN------QQHQTDQTELENRLKEFYTA--EC 954
Cdd:TIGR02168 841 EDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAllrselEELSEELRELESKRSELRREleEL 920
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 955 EKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYEtSLSEIKKShemekklLENL-------- 1026
Cdd:TIGR02168 921 REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARR-RLKRLENK-------IKELgpvnlaai 992
|
170 180
....*....|....*....|..
gi 2043665167 1027 -----LNEKQESLEKQINDLKS 1043
Cdd:TIGR02168 993 eeyeeLKERYDFLTAQKEDLTE 1014
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1009-1162 |
6.06e-06 |
|
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: 48.77 E-value: 6.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1009 LSEIKKSHEMEKKLLENLlNEKQESLEKQINDLKSENDALNERLKSEEQKQlsreKANSKNPQVMYLEQELESLKAVLEI 1088
Cdd:COG1579 33 LAELEDELAALEARLEAA-KTELEDLEKEIKRLELEIEEVEARIKKYEEQL----GNVRNNKEYEALQKEIESLKRRISD 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2043665167 1089 KNEKLhqqdLKLM-KMEKLVDNNTTLVDKLTRFQQENEELKARMDrhmAISRQLSTEQAALQESLEK-ESKVNKRL 1162
Cdd:COG1579 108 LEDEI----LELMeRIEELEEELAELEAELAELEAELEEKKAELD---EELAELEAELEELEAEREElAAKIPPEL 176
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
875-1153 |
7.43e-06 |
|
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: 50.35 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 875 IQHLLSEREEALKQHKTLSQ---ELVSLRGELVAASSTCEKLEKARNDL-----QTAYEGFVQKLNQQHQTDQTELENRL 946
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQlraRIEELRAQEAVLEETQERINRARKAAplaahIKAVTQIEQQAQRIHTELQSKMRSRA 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 947 KEFYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVEL--LKKtyetsLSEIKKSHEMEKKLLE 1024
Cdd:TIGR00618 325 KLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTqhIHT-----LQQQKTTLTQKLQSLC 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1025 NLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKME 1104
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKE 479
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2043665167 1105 KLVDNNT---TLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLE 1153
Cdd:TIGR00618 480 QIHLQETrkkAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQ 531
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
800-1069 |
8.31e-06 |
|
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: 50.44 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 800 RKSLFTAFNSVEKGRQKNPRSLCIQTQTAPdvLSTeRTLELADYKTK---CENQSGFILHLKQLLSCgNTKFEALTVVIQ 876
Cdd:TIGR01612 1575 KKEKFRIEDDAAKNDKSNKAAIDIQLSLEN--FEN-KFLKISDIKKKindCLKETESIEKKISSFSI-DSQDTELKENGD 1650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 877 HLLSERE--EALKQHKtlsQELVSLRGELVAASSTCEKLEKARNDLQTAYE-GFVQKLNQQHQTDQTELENrLKEFYTAE 953
Cdd:TIGR01612 1651 NLNSLQEflESLKDQK---KNIEDKKKELDELDSEIEKIEIDVDQHKKNYEiGIIEKIKEIAIANKEEIES-IKELIEPT 1726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 954 CEKLQSIYI----------EEAEKYKTQLQEQFDNLNAAHE--TTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKK 1021
Cdd:TIGR01612 1727 IENLISSFNtndlegidpnEKLEEYNTEIGDIYEEFIELYNiiAGCLETVSKEPITYDEIKNTRINAQNEFLKIIEIEKK 1806
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2043665167 1022 LLENLLNEKQESLEKQINDLKSENDALNERLKSEEQK------QLSREKANSKN 1069
Cdd:TIGR01612 1807 SKSYLDDIEAKEFDRIINHFKKKLDHVNDKFTKEYSKinegfdDISKSIENVKN 1860
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
984-1169 |
8.69e-06 |
|
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: 50.36 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 984 ETTKLEIEASHSE----KVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQ 1059
Cdd:pfam02463 154 RRLEIEEEAAGSRlkrkKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1060 LSREKANSKNPQVMYLEQELESLKAVLEIKNEKLhQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISr 1139
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL-AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVD- 311
|
170 180 190
....*....|....*....|....*....|
gi 2043665167 1140 qLSTEQAALQESLEKESKVNKRLSMENEEL 1169
Cdd:pfam02463 312 -DEEKLKESEKEKKKAEKELKKEKEEIEEL 340
|
|
| DUF2046 |
pfam09755 |
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues ... |
882-1149 |
9.19e-06 |
|
Uncharacterized conserved protein H4 (DUF2046); This is the conserved N-terminal 350 residues of a family of proteins of unknown function possibly containing a coiled-coil domain.
Pssm-ID: 401633 [Multi-domain] Cd Length: 304 Bit Score: 49.06 E-value: 9.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 882 REEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTELENRLKEFyTAECEKLQSIY 961
Cdd:pfam09755 23 REQLQKRIESLQQENRVLKMELETYKLRCKALQEENRALRQASVNIQAKAEQEEEFISNTLLKKIQAL-KKEKETLAMNY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 962 IEEAEKYKTQLQEQFDNLNaaHETTKLE--IEASHS----------EKVELLKKTYETSLSEIKKshemEKKLLENLLNE 1029
Cdd:pfam09755 102 EQEEEFLTNDLSRKLTQLR--QEKVELEqtLEQEQEyqvnklmrkiEKLEAETLNKQTNLEQLRR----EKVELENTLEQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1030 KQESLE----KQINDLKSENDALNERLK-------SEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQqdl 1098
Cdd:pfam09755 176 EQEALVnrlwKRMDKLEAEKRLLQEKLDqpvsappSPRDSTSEGDTAQNLTAHIQYLRKEVERLRRQLATAQQEHTE--- 252
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2043665167 1099 klmKMEKLVDNNTTLVDKLTRFQQEneeLKARMDRHMAISRQLSTEQAALQ 1149
Cdd:pfam09755 253 ---KMAQYAQEERHIREENLRLQRK---LQLEMERREALCRHLSESESSLE 297
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
941-1058 |
9.46e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.83 E-value: 9.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 941 ELENRLKEfYTAECEKLqsiyIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEM-- 1018
Cdd:PRK00409 527 ELERELEQ-KAEEAEAL----LKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGgy 601
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1019 ----EKKLLENL--LNEKQESLEKQINDLKSENDALNE----RLKSEEQK 1058
Cdd:PRK00409 602 asvkAHELIEARkrLNKANEKKEKKKKKQKEKQEELKVgdevKYLSLGQK 651
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
936-1122 |
9.92e-06 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 48.91 E-value: 9.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 936 QTDQTELENRLKEFyTAECEKLqsiyIEEAEKYKTQLQEQFDNLNAAHETTKleieaSHSEKVELLKKTYETSLSEIKKS 1015
Cdd:cd22656 106 ATDDEELEEAKKTI-KALLDDL----LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLTDEGGA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1016 HEMEKklLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKA---------------NSKNPQVMYLEQ--- 1077
Cdd:cd22656 176 IARKE--IKDLQKELEKLNEEYAAKLKAKIDELKALIADDEAKLAAALRLiadltaadtdldnllALIGPAIPALEKlqg 253
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2043665167 1078 -------ELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQ 1122
Cdd:cd22656 254 awqaiatDLDSLKDLLEDDISKIPAAILAKLELEKAIEKWNELAEKADKFRQ 305
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
962-1169 |
1.24e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.67 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 962 IEEA---EKYKTQLQEQFDNLNAAHET-TKLE-IEASHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKqESLEK 1036
Cdd:TIGR02168 161 FEEAagiSKYKERRKETERKLERTRENlDRLEdILNELERQLKSLERQAEKAERYKELKAELRELELALLVLRL-EELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1037 QINDLKSENDALNERLKS-EEQKQLSREKANSKNPQVMYLEQELESL-KAVLEIKNEklhQQDLKLMKMEkLVDNNTTLV 1114
Cdd:TIGR02168 240 ELEELQEELKEAEEELEElTAELQELEEKLEELRLEVSELEEEIEELqKELYALANE---ISRLEQQKQI-LRERLANLE 315
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2043665167 1115 DKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 1169
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
866-1067 |
1.31e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.38 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 866 TKFEALTVVIQHLLSEREE---ALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEgfvqklnqqhqtdQTEL 942
Cdd:COG4717 71 KELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQE-------------LEAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 943 ENRLKEFytaeCEKLQSIYiEEAEKYKtQLQEQFDNLNAAHETTKLEIEashsEKVELLKKTYETSLSEIKKSHEMekkl 1022
Cdd:COG4717 138 EAELAEL----PERLEELE-ERLEELR-ELEEELEELEAELAELQEELE----ELLEQLSLATEEELQDLAEELEE---- 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2043665167 1023 lenlLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANS 1067
Cdd:COG4717 204 ----LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
883-1100 |
1.36e-05 |
|
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: 49.84 E-value: 1.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 883 EEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTELENRLK--------------- 947
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSaadaavakdrselea 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 948 -------------EFYTAECEKLQSIY--IEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETSLSEI 1012
Cdd:pfam12128 327 ledqhgafldadiETAAADQEQLPSWQseLENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1013 KKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERL------------KSEEQKQL---------SREKANSKNPQ 1071
Cdd:pfam12128 407 DRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLgelklrlnqataTPELLLQLenfderierAREEQEAANAE 486
|
250 260
....*....|....*....|....*....
gi 2043665167 1072 VMYLEQELESLKAVLEIKNEKLHQQDLKL 1100
Cdd:pfam12128 487 VERLQSELRQARKRRDQASEALRQASRRL 515
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
857-1127 |
1.40e-05 |
|
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: 49.58 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 857 LKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVsLRGELVAA----SSTCEKLEKARNDLQTAYEGFVQKLN 932
Cdd:TIGR00618 578 CDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALL-RKLQPEQDlqdvRLHLQQCSQELALKLTALHALQLTLT 656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 933 QQHQTDQ----TELENRLKEFYTAECEKLQSIY------IEEAEKYKTQLQE----------QFDNLNAAHETTKLEIEA 992
Cdd:TIGR00618 657 QERVREHalsiRVLPKELLASRQLALQKMQSEKeqltywKEMLAQCQTLLRElethieeydrEFNEIENASSSLGSDLAA 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 993 SHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQ--ESLEKQINDLKSENDALNER-----LKSEEQKQLSREKA 1065
Cdd:TIGR00618 737 REDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgAELSHLAAEIQFFNRLREEDthllkTLEAEIGQEIPSDE 816
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2043665167 1066 NSKNPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEEL 1127
Cdd:TIGR00618 817 DILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
890-1176 |
1.48e-05 |
|
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: 49.40 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 890 KTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQT-----------------------------DQT 940
Cdd:pfam01576 548 KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLvsnlekkqkkfdqmlaeekaisaryaeerDRA 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 941 ELENRLKEF----YTAECEKLQSIyIEEAEKYKTQLQEQFDNL--------NAAHE------------------TTKLEI 990
Cdd:pfam01576 628 EAEAREKETralsLARALEEALEA-KEELERTNKQLRAEMEDLvsskddvgKNVHElerskraleqqveemktqLEELED 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 991 EASHSEKVELlkkTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDalnerlksEEQKQLSREKANSKNp 1070
Cdd:pfam01576 707 ELQATEDAKL---RLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELE--------DERKQRAQAVAAKKK- 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1071 qvmyLEQELESLKAVLEIKNeKLHQQDLKLMKmeklvdnntTLVDKLTRFQQENEELKARMDRHMAISRQ-------LST 1143
Cdd:pfam01576 775 ----LELDLKELEAQIDAAN-KGREEAVKQLK---------KLQAQMKDLQRELEEARASRDEILAQSKEsekklknLEA 840
|
330 340 350
....*....|....*....|....*....|...
gi 2043665167 1144 EQAALQESLEKESKVNKRLSMENEELLWKLHNG 1176
Cdd:pfam01576 841 ELLQLQEDLAASERARRQAQQERDELADEIASG 873
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
949-1173 |
1.57e-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: 49.30 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 949 FYTAECEKLQSIY--IEEAEKYKTQLQEQFDNL-NAAHETTKlEIEASHSEKVELLKKtyetsLSEIKKSHEMEKKLLEN 1025
Cdd:TIGR02169 668 FSRSEPAELQRLRerLEGLKRELSSLQSELRRIeNRLDELSQ-ELSDASRKIGEIEKE-----IEQLEQEEEKLKERLEE 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1026 LlNEKQESLEKQINDLKSENDALNERLkSEEQKQLSREKANSKNPQVMY-------LEQELESLKAV----------LEI 1088
Cdd:TIGR02169 742 L-EEDLSSLEQEIENVKSELKELEARI-EELEEDLHKLEEALNDLEARLshsripeIQAELSKLEEEvsriearlreIEQ 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1089 KNEKLHQQDLKLMK-MEKLVDNNTTLVDKLTRFQQENEELKAR-------MDRHMAISRQLSTEQAALQESLEKESKVNK 1160
Cdd:TIGR02169 820 KLNRLTLEKEYLEKeIQELQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGDLKKERDELEAQLR 899
|
250
....*....|...
gi 2043665167 1161 RLSMENEELLWKL 1173
Cdd:TIGR02169 900 ELERKIEELEAQI 912
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
852-1087 |
1.86e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 852 GFILHLKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGEL-VAASSTCEKLEKARNDLQTAYEGFVQK 930
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALgLPPDLSPEELLELLDRIEELQELLREA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 931 LNQQHQTDQTELENRLKEFYT-AECEKLQSIY--IEEAEKYKtQLQEQFDNLNAahettklEIEASHSEKVELLKKTYET 1007
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAeAGVEDEEELRaaLEQAEEYQ-ELKEELEELEE-------QLEELLGELEELLEALDEE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1008 SLseikkshemEKKLLEnlLNEKQESLEKQINDLKSENDALNERLKS-EEQKQLSRekansknpqvmyLEQELESLKAVL 1086
Cdd:COG4717 429 EL---------EEELEE--LEEELEELEEELEELREELAELEAELEQlEEDGELAE------------LLQELEELKAEL 485
|
.
gi 2043665167 1087 E 1087
Cdd:COG4717 486 R 486
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
883-1162 |
2.39e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 48.14 E-value: 2.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 883 EEALKQHKTLSQELVSLRGELVAASSTCE----KLEKARNDLQTAYEGFV-QKLNQQHQTDQTE-LENRLKefytAECEK 956
Cdd:pfam19220 58 AQERAAYGKLRRELAGLTRRLSAAEGELEelvaRLAKLEAALREAEAAKEeLRIELRDKTAQAEaLERQLA----AETEQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 957 LQSIYIE------EAEKYKTQLQEQFDNLNAAHETTKLeieasHSEKVELLKKTYETSLSEIKKsHEMEKKLLENLLNEK 1030
Cdd:pfam19220 134 NRALEEEnkalreEAQAAEKALQRAEGELATARERLAL-----LEQENRRLQALSEEQAAELAE-LTRRLAELETQLDAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1031 QESLEKQINDLKSENdALNERLKSEEQKQLSREKAnSKNPQVMYLE----------QELESLKAVLEIKNEKLHQQDLKL 1100
Cdd:pfam19220 208 RARLRALEGQLAAEQ-AERERAEAQLEEAVEAHRA-ERASLRMKLEaltaraaateQLLAEARNQLRDRDEAIRAAERRL 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2043665167 1101 --------MKMEKLVDNNTTLVDKLTRFQqenEELKAR---MDRHMAISRQLSTEQAALQESLEKESKVNKRL 1162
Cdd:pfam19220 286 keasierdTLERRLAGLEADLERRTQQFQ---EMQRARaelEERAEMLTKALAAKDAALERAEERIASLSDRI 355
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
875-1087 |
2.43e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 875 IQHLLSEREEALKQHKTLSQELVSLRGELVAAS-STCEKLEKARNDLQTAYEGFVQKLNQQHqtdqtELENRLKEFytae 953
Cdd:PRK03918 551 LEELKKKLAELEKKLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDAEK-----ELEREEKEL---- 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 954 ceklqsiyieeaEKYKTQLQEQFDNLnaahETTKLEIEASHSEKVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKqES 1033
Cdd:PRK03918 622 ------------KKLEEELDKAFEEL----AETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAEL-EE 684
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2043665167 1034 LEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLE 1087
Cdd:PRK03918 685 LEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
962-1095 |
3.40e-05 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 46.05 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 962 IEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKtyetslseiKKSHEMEKKLLENLlNEKQESLEKQINDL 1041
Cdd:pfam13851 35 IAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQ---------LENYEKDKQSLKNL-KARLKVLEKELKDL 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2043665167 1042 KSENDALNERLK--SEEQKQLSR----------EKANSKNpqvMYLEQELESLKAVLEIKNEKLHQ 1095
Cdd:pfam13851 105 KWEHEVLEQRFEkvERERDELYDkfeaaiqdvqQKTGLKN---LLLEKKLQALGETLEKKEAQLNE 167
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1011-1173 |
3.44e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1011 EIKKSHEMEKKLL------ENLLNEKQESLE---KQINDLKSENDALNERLK--SEEQKQLS--REKANSKNPQVMYLEQ 1077
Cdd:PRK03918 173 EIKRRIERLEKFIkrteniEELIKEKEKELEevlREINEISSELPELREELEklEKEVKELEelKEEIEELEKELESLEG 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1078 ELESLKAVLE-----IKNEKLHQQDLK-----LMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRhmaISRQLSTEQAA 1147
Cdd:PRK03918 253 SKRKLEEKIReleerIEELKKEIEELEekvkeLKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR---LEEEINGIEER 329
|
170 180
....*....|....*....|....*.
gi 2043665167 1148 LQESLEKESKVNKrLSMENEELLWKL 1173
Cdd:PRK03918 330 IKELEEKEERLEE-LKKKLKELEKRL 354
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
857-1181 |
4.83e-05 |
|
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: 47.66 E-value: 4.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 857 LKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAyegfvQKLNQQHQ 936
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL-----RAQEAVLE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 937 TDQTELE-NRLKEFYTAECEKLQSIYiEEAEKYKTQLQEQFDNLNAA-HETTKLEIEASHSEKVELLKKTYETSLSEIKK 1014
Cdd:TIGR00618 281 ETQERINrARKAAPLAAHIKAVTQIE-QQAQRIHTELQSKMRSRAKLlMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRD 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1015 SHEMEKKLLENLlnEKQESLEKQINDLKSENDALNERLKSEEQK--QLSREKAN------SKNPqvmyLEQELESLKAVL 1086
Cdd:TIGR00618 360 AHEVATSIREIS--CQQHTLTQHIHTLQQQKTTLTQKLQSLCKEldILQREQATidtrtsAFRD----LQGQLAHAKKQQ 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1087 EIKNEKLHQQDLKLMK-MEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSME 1165
Cdd:TIGR00618 434 ELQQRYAELCAAAITCtAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHP 513
|
330
....*....|....*.
gi 2043665167 1166 NEELLWKLHNGDLCSP 1181
Cdd:TIGR00618 514 NPARQDIDNPGPLTRR 529
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
874-1168 |
4.93e-05 |
|
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: 47.81 E-value: 4.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 874 VIQH--LLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQ--------KLNQQHQTDQTELE 943
Cdd:pfam17380 277 IVQHqkAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAiyaeqermAMERERELERIRQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 944 NRLKEFYTAECEKLQSIYIEEAEKYKTQLQEQFDN------LNAAHETTKLEIEasHSEKVELLKKTYETSLSEIKKSHE 1017
Cdd:pfam17380 357 ERKRELERIRQEEIAMEISRMRELERLQMERQQKNervrqeLEAARKVKILEEE--RQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1018 MEKKLLEN-----LLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLK-AVLEIKNE 1091
Cdd:pfam17380 435 REVRRLEEerareMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqAMIEEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1092 KlhqqdlKLMKMEkLVDNNTTLVDKLTRFQQENEELKAR-MDRHMAISRQL--STEQAALQESLEKESKVNKRLsMENEE 1168
Cdd:pfam17380 515 R------KLLEKE-MEERQKAIYEEERRREAEEERRKQQeMEERRRIQEQMrkATEERSRLEAMEREREMMRQI-VESEK 586
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1006-1170 |
5.25e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 47.60 E-value: 5.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1006 ETSLSEIK--KSHEMEKKLLENLLNEKQESLEkQINDLKSENDALNERLKS--EEQKQLSREKANSKNPQVMYLEQELES 1081
Cdd:PRK11281 42 QAQLDALNkqKLLEAEDKLVQQDLEQTLALLD-KIDRQKEETEQLKQQLAQapAKLRQAQAELEALKDDNDEETRETLST 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1082 LK-AVLEIK-NEKLHQ-QDLKlmkmEKLVDNNTTLV--------------DKLTRFQQENEELKARMDRHMAISR----Q 1140
Cdd:PRK11281 121 LSlRQLESRlAQTLDQlQNAQ----NDLAEYNSQLVslqtqperaqaalyANSQRLQQIRNLLKGGKVGGKALRPsqrvL 196
|
170 180 190
....*....|....*....|....*....|
gi 2043665167 1141 LSTEQAALQESLEkeskvNKRLSMENEELL 1170
Cdd:PRK11281 197 LQAEQALLNAQND-----LQRKSLEGNTQL 221
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
834-1170 |
5.60e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.51 E-value: 5.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 834 TERTLELADYKTKCENQSGFILHLKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKL 913
Cdd:pfam10174 362 NKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTL 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 914 EKARNDlqtaYEGFVQKLNQQHQTD----QTELENRLKEFYTAEcEKLQSIYIEEAEKYKT--QLQEQFDNLNAAHETTK 987
Cdd:pfam10174 442 EEALSE----KERIIERLKEQREREdrerLEELESLKKENKDLK-EKVSALQPELTEKESSliDLKEHASSLASSGLKKD 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 988 LEIEashSEKVELLKKTYETS--LSEIKKSHEMEKKLLENL-LNEKQESLEKQINDLKSEN-------DALNERLKSEEQ 1057
Cdd:pfam10174 517 SKLK---SLEIAVEQKKEECSklENQLKKAHNAEEAVRTNPeINDRIRLLEQEVARYKEESgkaqaevERLLGILREVEN 593
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1058 KQLSREKANSknpqvmyleqELESLkAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRF--------QQENEELKA 1129
Cdd:pfam10174 594 EKNDKDKKIA----------ELESL-TLRQMKEQNKKVANIKHGQQEMKKKGAQLLEEARRREdnladnsqQLQLEELMG 662
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2043665167 1130 RMDRHM----AISRQLSTEQAALQES--------LEKESKVNKRLSMENEELL 1170
Cdd:pfam10174 663 ALEKTRqeldATKARLSSTQQSLAEKdghltnlrAERRKQLEEILEMKQEALL 715
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
890-1133 |
5.67e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 5.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 890 KTLSQELVSLRGELVAASSTCEKLEKARNDLQT---AYEG-----FVQKLNQQHQTDQTELENRLKEfYTAECEKLQSIY 961
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQErreALQRlaeysWDEIDVASAEREIAELEAELER-LDASSDDLAALE 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 962 --IEEAEKYKTQLQEQFDNLNAAHETTKLEIEAsHSEKVELLKKTYEtSLSEIKKSH---EMEKKL----LENLLNEKQE 1032
Cdd:COG4913 692 eqLEELEAELEELEEELDELKGEIGRLEKELEQ-AEEELDELQDRLE-AAEDLARLElraLLEERFaaalGDAVERELRE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1033 SLEKQINDLKSENDALNERLKSEEQKQLSREKANSKN--PQVMYLEQELESLKavlEIKNEKLHQqdlKLMKMEKLVDNN 1110
Cdd:COG4913 770 NLEERIDALRARLNRAEEELERAMRAFNREWPAETADldADLESLPEYLALLD---RLEEDGLPE---YEERFKELLNEN 843
|
250 260
....*....|....*....|....*
gi 2043665167 1111 TT--LVDKLTRFQQENEELKARMDR 1133
Cdd:COG4913 844 SIefVADLLSKLRRAIREIKERIDP 868
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
964-1157 |
7.13e-05 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 47.05 E-value: 7.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 964 EAEKYKTQLQEQFDNLNAAHETTkLEIEASHSEKVELLKKTYETSLS-EIKKSHEMEKK--LLENLLNEKQESLEKQIND 1040
Cdd:pfam07111 141 ELEEIQRLHQEQLSSLTQAHEEA-LSSLTSKAEGLEKSLNSLETKRAgEAKQLAEAQKEaeLLRKQLSKTQEELEAQVTL 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1041 LKSENDALNERLKSE--------EQKQLS------REKANSKNPQVMYLEQELESLKAVLEIKNEKLHQqdlKLMKMEKL 1106
Cdd:pfam07111 220 VESLRKYVGEQVPPEvhsqtwelERQELLdtmqhlQEDRADLQATVELLQVRVQSLTHMLALQEEELTR---KIQPSDSL 296
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2043665167 1107 VDNNTTLVDKLTRFQQENE-----ELKARMDRHMAISRQLSTEQAALQESLEKESK 1157
Cdd:pfam07111 297 EPEFPKKCRSLLNRWREKVfalmvQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQ 352
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
830-1127 |
7.88e-05 |
|
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: 47.35 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 830 DVLSTERTLELADYKTKCENQSGFILHLK------QLLSCGNTKFEALTVVIQ---HLLSEREEALkqHKTLsQELVSLR 900
Cdd:TIGR01612 688 AIDNTEDKAKLDDLKSKIDKEYDKIQNMEtatvelHLSNIENKKNELLDIIVEikkHIHGEINKDL--NKIL-EDFKNKE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 901 GELvaaSSTCEKLEKARNDLQTaYEGFVQKLnQQHQTDQTELEN----RLKEFYTAECEKLQSIYIEEAEKYKTQLQEQF 976
Cdd:TIGR01612 765 KEL---SNKINDYAKEKDELNK-YKSKISEI-KNHYNDQINIDNikdeDAKQNYDKSKEYIKTISIKEDEIFKIINEMKF 839
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 977 ---DNLNAAHETTKLEieASHSEKVEllkktyetslSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLK 1053
Cdd:TIGR01612 840 mkdDFLNKVDKFINFE--NNCKEKID----------SEHEQFAELTNKIKAEISDDKLNDYEKKFNDSKSLINEINKSIE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1054 SEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHqQDLKLMKMEKLVDN------NTTLVDKLTRFQQENEEL 1127
Cdd:TIGR01612 908 EEYQNINTLKKVDEYIKICENTKESIEKFHNKQNILKEILN-KNIDTIKESNLIEKsykdkfDNTLIDKINELDKAFKDA 986
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
950-1169 |
9.88e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 46.99 E-value: 9.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 950 YTAECEKLQsiYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTY------------ETSLSEIK---- 1013
Cdd:COG5022 815 YLACIIKLQ--KTIKREKKLRETEEVEFSLKAEVLIQKFGRSLKAKKRFSLLKKETiylqsaqrvelaERQLQELKidvk 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1014 -------KSHEMEKKLLEnlLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVL 1086
Cdd:COG5022 893 sisslklVNLELESEIIE--LKKSLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKETS 970
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1087 EIKNEKLHQQDL-------KLMKMEKLVDNNTTLVDKLTRFQQENEELKAR---MDRHMAISRQLSTEQAALQeSLEKES 1156
Cdd:COG5022 971 EEYEDLLKKSTIlvregnkANSELKNFKKELAELSKQYGALQESTKQLKELpveVAELQSASKIISSESTELS-ILKPLQ 1049
|
250
....*....|...
gi 2043665167 1157 KVNKRLSMENEEL 1169
Cdd:COG5022 1050 KLKGLLLLENNQL 1062
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
881-1124 |
1.08e-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: 46.64 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 881 EREEALKQHKTLSQELVSLRGELvaaSSTCEKLEKARNDLQTAyegfVQKLNQQHQTDQTELENRLKEFYTAE--CEKL- 957
Cdd:pfam05483 528 QEERMLKQIENLEEKEMNLRDEL---ESVREEFIQKGDEVKCK----LDKSEENARSIEYEVLKKEKQMKILEnkCNNLk 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 958 -----QSIYIEEAEKYKTQLQE----QFDNLNAAH-ETTKLEIE-ASHSEKVELLKKTYETSLsEIKKSHEmeKKLLENL 1026
Cdd:pfam05483 601 kqienKNKNIEELHQENKALKKkgsaENKQLNAYEiKVNKLELElASAKQKFEEIIDNYQKEI-EDKKISE--EKLLEEV 677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1027 LNEK---------QESLEKQINDLKSENDALNERLKSEEQKQLsrEKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQd 1097
Cdd:pfam05483 678 EKAKaiadeavklQKEIDKRCQHKIAEMVALMEKHKHQYDKII--EERDSELGLYKNKEQEQSSAKAALEIELSNIKAE- 754
|
250 260
....*....|....*....|....*..
gi 2043665167 1098 lkLMKMEKLVDNNTTLVDKLTRFQQEN 1124
Cdd:pfam05483 755 --LLSLKKQLEIEKEEKEKLKMEAKEN 779
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
962-1105 |
1.09e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 46.36 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 962 IEEAEKYKTQLQEQFDNLNAAHETtkLEIEA-SHSEKVELLKKTYE---TSLSEIKKS-HEMEKKLLENLlnekQESLEK 1036
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEE--LERELeQKAEEAEALLKEAEklkEELEEKKEKlQEEEDKLLEEA----EKEAQQ 577
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2043665167 1037 QINDLKSENDALNERLKSEEQKQLSREKAnsknpqvmyleQELESLKAVLEIKNEKLHQQDLKLMKMEK 1105
Cdd:PRK00409 578 AIKEAKKEADEIIKELRQLQKGGYASVKA-----------HELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
952-1169 |
1.28e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 952 AECEKLQSIYIEEAEKyktqlqeqfdnlNAAHETTKLEIEAShsEKVELLKKTYEtslseiKKSHEMEKKL--LENLLNE 1029
Cdd:PRK12704 34 KEAEEEAKRILEEAKK------------EAEAIKKEALLEAK--EEIHKLRNEFE------KELRERRNELqkLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1030 KQESLEKQINDLKSENDALNERLKSEEQKQLSREKansknpqvmyLEQELESLKAVLEIKNEK---LHQQDLKLMKMEKL 1106
Cdd:PRK12704 94 KEENLDRKLELLEKREEELEKKEKELEQKQQELEK----------KEEELEELIEEQLQELERisgLTAEEAKEILLEKV 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2043665167 1107 VDNNTTlvDKLTRFQQENEELKARMDRH------MAISRqLSTEQAAlqeslekESKVNkRLSMENEEL 1169
Cdd:PRK12704 164 EEEARH--EAAVLIKEIEEEAKEEADKKakeilaQAIQR-CAADHVA-------ETTVS-VVNLPNDEM 221
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
979-1179 |
1.29e-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: 46.60 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 979 LNAAHETTKLEieaSHSEKVELLKKTYETSLSEIKKshemekklLENLLNEKQESL---EKQINDLKSENDALNERLK-- 1053
Cdd:TIGR02169 667 LFSRSEPAELQ---RLRERLEGLKRELSSLQSELRR--------IENRLDELSQELsdaSRKIGEIEKEIEQLEQEEEkl 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1054 SEEQKQLSRekansknpQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNnttLVDKL--TRFQQENEELKARM 1131
Cdd:TIGR02169 736 KERLEELEE--------DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND---LEARLshSRIPEIQAELSKLE 804
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2043665167 1132 DRHMAISRQL-STEQAALQESLEKESKVNKRLSMENEELLWKLHNGDLC 1179
Cdd:TIGR02169 805 EEVSRIEARLrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIE 853
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
842-1169 |
1.29e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.58 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 842 DYKTKCENQSgFILHLKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELvaaSSTCEKLEKARNDlq 921
Cdd:TIGR00606 686 VFQTEAELQE-FISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEI---PELRNKLQKVNRD-- 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 922 tayegfVQKLNQQHQTDQTELENRLKEFYTAE--------CEKLQsIYIEEAEKYKTQLQEQFDNLNAAHETTKLeieas 993
Cdd:TIGR00606 760 ------IQRLKNDIEEQETLLGTIMPEEESAKvcltdvtiMERFQ-MELKDVERKIAQQAAKLQGSDLDRTVQQV----- 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 994 hSEKVELLKKTYETSLSEIkkshEMEKKLLENLlNEKQESLEKQINDLKSENDALNERL------------KSEEQKQLS 1061
Cdd:TIGR00606 828 -NQEKQEKQHELDTVVSKI----ELNRKLIQDQ-QEQIQHLKSKTNELKSEKLQIGTNLqrrqqfeeqlveLSTEVQSLI 901
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1062 REKANSKN---PQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEElkarmDRHMAIS 1138
Cdd:TIGR00606 902 REIKDAKEqdsPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKD-----DYLKQKE 976
|
330 340 350
....*....|....*....|....*....|.
gi 2043665167 1139 RQLSTEQAALQESLEKESKVNKRLSMENEEL 1169
Cdd:TIGR00606 977 TELNTVNAQLEECEKHQEKINEDMRLMRQDI 1007
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
987-1157 |
1.37e-04 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 45.08 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 987 KLEIEASHSEKVELLKKTY-----ETSLSEIKKSHEMEKKLLENLlNEK--QESLEKQINDLKSENDALNERLKSEEQKQ 1059
Cdd:pfam15294 78 KLQADISELENRELLEQIAefeerEFTSSNKKPNFELNKPKLEPL-NEGggSALLHMEIERLKEENEKLKERLKTLESQA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1060 LSREKANSKnpqvmyLEQELESLKAVL-EIKNEKLHQQDLKlmKMEKLVdnnTTLVDKLTRFQQENEELKARMDRHMAIS 1138
Cdd:pfam15294 157 TQALDEKSK------LEKALKDLQKEQgAKKDVKSNLKEIS--DLEEKM---AALKSDLEKTLNASTALQKSLEEDLAST 225
|
170
....*....|....*....
gi 2043665167 1139 RQlstEQAALQESLEKESK 1157
Cdd:pfam15294 226 KH---ELLKVQEQLEMAEK 241
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
879-1170 |
1.51e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.29 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 879 LSEREEALKQHKT-LSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLnQQHQTDQTELENRLKEFYTAECEKL 957
Cdd:COG1340 6 LSSSLEELEEKIEeLREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEA-QELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 958 QSI--YIEEAEKYKT-------------QLQEQFDNLNAAHETTKLEIEAshsEKvELLKK--TYETSLSEIKKSHEMEK 1020
Cdd:COG1340 85 EKLneLREELDELRKelaelnkaggsidKLRKEIERLEWRQQTEVLSPEE---EK-ELVEKikELEKELEKAKKALEKNE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1021 KLLEnllnekqesLEKQINDLKSENDALNERLKSeeqkqlSREKANSKNPQVMYLEQELESLKAvleiKNEKLHQQDLKL 1100
Cdd:COG1340 161 KLKE---------LRAELKELRKEAEEIHKKIKE------LAEEAQELHEEMIELYKEADELRK----EADELHKEIVEA 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2043665167 1101 M-KMEKLvdnNTTLVDKLTRFQQENEELKARMDRHMAISRQlsTEQAALQ----ESLEKESKvNKRLSMENEELL 1170
Cdd:COG1340 222 QeKADEL---HEEIIELQKELRELRKELKKLRKKQRALKRE--KEKEELEekaeEIFEKLKK-GEKLTTEELKLL 290
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
913-1166 |
1.54e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 913 LEKARNDLQTAYEgFVQKLNQQHQTDQTELENRLKEFYtaecEKLQSIYIEEAEKyktQLQEQFDNLNAAHETTKLEIEA 992
Cdd:COG3206 166 LELRREEARKALE-FLEEQLPELRKELEEAEAALEEFR----QKNGLVDLSEEAK---LLLQQLSELESQLAEARAELAE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 993 ShsekvellkktyETSLSEIKKSHEMEKKLLENLLNEKQ-ESLEKQINDLKSENDALNERLKSEeqkqlsrekanskNPQ 1071
Cdd:COG3206 238 A------------EARLAALRAQLGSGPDALPELLQSPViQQLRAQLAELEAELAELSARYTPN-------------HPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1072 VMYLEQELESLKAvlEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQES 1151
Cdd:COG3206 293 VIALRAQIAALRA--QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370
|
250
....*....|....*..
gi 2043665167 1152 LEK--ESKVNKRLSMEN 1166
Cdd:COG3206 371 LQRleEARLAEALTVGN 387
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
869-1169 |
1.59e-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: 45.87 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 869 EALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQTELE----- 943
Cdd:pfam05483 74 EGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKennat 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 944 ----NRLKEFYTAECEKLQSIYIEEAEKYKT---------QLQEQFDNLNAAHETTKLEIE---ASHSEKVELLKKTYET 1007
Cdd:pfam05483 154 rhlcNLLKETCARSAEKTKKYEYEREETRQVymdlnnnieKMILAFEELRVQAENARLEMHfklKEDHEKIQHLEEEYKK 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1008 SLSEikksHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERlksEEQKQLSREKANSKNPQVMYLEQELESLKAVLE 1087
Cdd:pfam05483 234 EIND----KEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQL---EEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1088 --IKNEKLHQQDLKLMkmeklvdnnTTLVDKLTRFQQ-ENEELKARMDRHMAISRQLSTEQAALQESLEKEskvNKRLSM 1164
Cdd:pfam05483 307 rsMSTQKALEEDLQIA---------TKTICQLTEEKEaQMEELNKAKAAHSFVVTEFEATTCSLEELLRTE---QQRLEK 374
|
....*
gi 2043665167 1165 ENEEL 1169
Cdd:pfam05483 375 NEDQL 379
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
866-1071 |
1.76e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 866 TKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAyegfVQKLNQQHQTDQTELENR 945
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAE----IAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 946 LKEFYTAeceKLQSIYIE---EAEKYkTQLQEQFDNLNAAHETTKLEIEASHSEKVELlkKTYETSLSEIKKSHEMEKKL 1022
Cdd:COG3883 92 ARALYRS---GGSVSYLDvllGSESF-SDFLDRLSALSKIADADADLLEELKADKAEL--EAKKAELEAKLAELEALKAE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2043665167 1023 LENL---LNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQ 1071
Cdd:COG3883 166 LEAAkaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
925-1089 |
2.23e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 44.62 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 925 EGFVQKLNQQHQTDQTELENRLKEFytaecEKLQSIYIEEAEKYKTqLQEQFDNLnaahetTKLEIEAShSEKVELLKKt 1004
Cdd:smart00787 143 EGLKEGLDENLEGLKEDYKLLMKEL-----ELLNSIKPKLRDRKDA-LEEELRQL------KQLEDELE-DCDPTELDR- 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1005 YETSLSEIKKSHEMEKKLLENLLNEKQEsLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpQVMYLEQELESLKA 1084
Cdd:smart00787 209 AKEKLKKLLQEIMIKVKKLEELEEELQE-LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK--EIEKLKEQLKLLQS 285
|
....*
gi 2043665167 1085 VLEIK 1089
Cdd:smart00787 286 LTGWK 290
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
857-1132 |
2.23e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 857 LKQLLSCGNTKFEALTVVIQHLLSEREEALK-QHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQH 935
Cdd:pfam12128 698 HQAWLEEQKEQKREARTEKQAYWQVVEGALDaQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREI 777
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 936 QTDQTELENrlkefytaeCEKLQSiyieEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSE-KVELLKKTYETSLSeiKK 1014
Cdd:pfam12128 778 RTLERKIER---------IAVRRQ----EVLRYFDWYQETWLQRRPRLATQLSNIERAISElQQQLARLIADTKLR--RA 842
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1015 SHEMEKKLLENLLNEKQESLEK------QINDLKSENDAlnerlkseEQKQLSrekANSKNPQVMYLEQELESLKAVLEI 1088
Cdd:pfam12128 843 KLEMERKASEKQQVRLSENLRGlrcemsKLATLKEDANS--------EQAQGS---IGERLAQLEDLKLKRDYLSESVKK 911
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1089 KNEKLHQQDLKLMKM------EKLVDNNTTLVDKLTRFQQENEELKARMD 1132
Cdd:pfam12128 912 YVEHFKNVIADHSGSglaetwESLREEDHYQNDKGIRLLDYRKLVPYLEQ 961
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
911-1168 |
2.27e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 911 EKLEKARNDLQtayegfvQKLNQQHQTDQTELENRLKEfytAE--CEKLQSIYIEEAEKY------KTQLQEQFDNLNAA 982
Cdd:pfam13868 69 EERKRYRQELE-------EQIEEREQKRQEEYEEKLQE---REqmDEIVERIQEEDQAEAeeklekQRQLREEIDEFNEE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 983 HETTK-LEIEAshsEKVELLK-KTYETSLSEIKKSHEMEKKLLE---NLLNEKQESLEKQINDLKSENDALNERLKSEEQ 1057
Cdd:pfam13868 139 QAEWKeLEKEE---EREEDERiLEYLKEKAEREEEREAEREEIEeekEREIARLRAQQEKAQDEKAERDELRAKLYQEEQ 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1058 KQLSREKAnsknpqvmyLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEElKARMDRHMAi 1137
Cdd:pfam13868 216 ERKERQKE---------REEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE-IEQEEAEKR- 284
|
250 260 270
....*....|....*....|....*....|.
gi 2043665167 1138 sRQLSTEQAALQESLEKESKVNKRLSMENEE 1168
Cdd:pfam13868 285 -RMKRLEHRRELEKQIEEREEQRAAEREEEL 314
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
875-1095 |
2.32e-04 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 44.80 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 875 IQHLLSEREEALKQHKTLSQELVSLRGELVAA-------SSTCEKLEKARNDLQTAYEGFVQKL-----NQQHQTDQTEL 942
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAvrektslSASVASLEKQLLELTRVNELLKAKFsedgtQKKMSSLSMEL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 943 ENRLKEFYTAECE----------KLQSI--YIEEAEKYKTQLQEQFDNLNAAHETTKLEIE---------ASHSEKVELL 1001
Cdd:pfam15905 162 MKLRNKLEAKMKEvmakqegmegKLQVTqkNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEklleyitelSCVSEQVEKY 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1002 KKTYeTSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDLksenDALNERLKSEEQKQLSREKANSKNpqvmyLEQELES 1081
Cdd:pfam15905 242 KLDI-AQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDL----NEKCKLLESEKEELLREYEEKEQT-----LNAELEE 311
|
250
....*....|....*..
gi 2043665167 1082 LKAVLEIK---NEKLHQ 1095
Cdd:pfam15905 312 LKEKLTLEeqeHQKLQQ 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
854-1070 |
2.40e-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: 44.75 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 854 ILHLKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQ 933
Cdd:COG4942 36 IAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 934 QHQTDQTELENRLKEFYTAEcekLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYE--TSLSE 1011
Cdd:COG4942 116 LGRQPPLALLLSPEDFLDAV---RRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEerAALEA 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2043665167 1012 IKKshemEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNP 1070
Cdd:COG4942 193 LKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
972-1169 |
2.45e-04 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 43.51 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 972 LQEQFDNLNAAHETTKLEIEASHSEKVELLK--KTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALN 1049
Cdd:pfam05010 13 ARNEIEEKELEINELKAKYEELRRENLEMRKivAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQALADLNSVEKSFS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1050 ERLK-SEEQKQ-LSREKANSknpqvmyleqelESLKAVLE-----IKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQ 1122
Cdd:pfam05010 93 DLFKrYEKQKEvISGYKKNE------------ESLKKCAQdylarIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1123 ENEELKArmdrhmaisrQLSTEQ---AALQESLEKESKvnkrlsmENEEL 1169
Cdd:pfam05010 161 ETAALQA----------SLRKEQmkvQSLERQLEQKTK-------ENEEL 193
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
857-1130 |
2.91e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 857 LKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQT---AYEGFVQKLNQ 933
Cdd:COG4372 64 LEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQqrkQLEAQIAELQS 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 934 QHQTDQTELENRLKEFYTAEcEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEAshSEKVELLKKTYETSLSEIK 1013
Cdd:COG4372 144 EIAEREEELKELEEQLESLQ-EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE--LAEAEKLIESLPRELAEEL 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1014 KSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKL 1093
Cdd:COG4372 221 LEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
250 260 270
....*....|....*....|....*....|....*..
gi 2043665167 1094 HQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKAR 1130
Cdd:COG4372 301 LLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
867-1058 |
4.36e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 43.20 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 867 KFEALtvviQHLLSEREEALKQHKTLSQELVSLRGELVAA-SSTCEKLEKARNDLQTAYEGFVQKLNQQHQ-----TDQT 940
Cdd:cd00176 41 KHEAL----EAELAAHEERVEALNELGEQLIEEGHPDAEEiQERLEELNQRWEELRELAEERRQRLEEALDlqqffRDAD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 941 ELENRLKEfytAECEKLQSIYIEEAEKYKTQLQEqfdnlnaaHETTKLEIEAsHSEKVELLKKTYEtslseikkshemek 1020
Cdd:cd00176 117 DLEQWLEE---KEAALASEDLGKDLESVEELLKK--------HKELEEELEA-HEPRLKSLNELAE-------------- 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 2043665167 1021 KLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQK 1058
Cdd:cd00176 171 ELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKK 208
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
951-1170 |
5.03e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 5.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 951 TAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHSEkvellkktyetsLSEIKKshEMEKklLENLLNEK 1030
Cdd:COG4372 22 TGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE------------LEQARS--ELEQ--LEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1031 QESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQvmyLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNN 1110
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD---LEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2043665167 1111 TTLVDKLTRFQQ--ENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELL 1170
Cdd:COG4372 163 QEELAALEQELQalSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
883-1169 |
6.06e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.36 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 883 EEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQT-----ELENRLKEFYTAECEKL 957
Cdd:PTZ00121 1339 EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAkkkaeEDKKKADELKKAAAAKK 1418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 958 QSiyiEEAEKYKTQLQEQFDNLNAAHETTK---LEIEASHSEKVELLKKTYEtslsEIKKSHEMEKKLLEnllNEKQESL 1034
Cdd:PTZ00121 1419 KA---DEAKKKAEEKKKADEAKKKAEEAKKadeAKKKAEEAKKAEEAKKKAE----EAKKADEAKKKAEE---AKKADEA 1488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1035 EKQINDLKSENDALneRLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQDlKLMKMEKlvdnnttlV 1114
Cdd:PTZ00121 1489 KKKAEEAKKKADEA--KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD-ELKKAEE--------L 1557
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2043665167 1115 DKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEEL 1169
Cdd:PTZ00121 1558 KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
920-1131 |
6.20e-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: 43.73 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 920 LQTAYEGFVQKLNQQHQTDQTELENRLKEFYTAECEKlqsiyiEEAEKYKTQLQEQFDNLNAAHETTKleieashsEKVE 999
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDR------EQWERQRRELESRVAELKEELRQSR--------EKHE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1000 LLKKTYEtslsEIKKSHEMEKKLLENLLNEKQES------LEKQINDL---KSENDALNERLKSEEQK---QLSREKANS 1067
Cdd:pfam07888 98 ELEEKYK----ELSASSEELSEEKDALLAQRAAHearireLEEDIKTLtqrVLERETELERMKERAKKagaQRKEEEAER 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2043665167 1068 KNPQVMYL--EQELESLKAVLEIKNEKLHQQDLKLMKmekLVDNNTTLVDKLTRFQQ---ENEELKARM 1131
Cdd:pfam07888 174 KQLQAKLQqtEEELRSLSKEFQELRNSLAQRDTQVLQ---LQDTITTLTQKLTTAHRkeaENEALLEEL 239
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
989-1142 |
6.75e-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: 44.27 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 989 EIEAShsekvelLKKTYETSLSEIKKSHEMEKKLLENllNEKQESLEKQINDLksendaLNERLKSEEQkqlsrekansk 1068
Cdd:TIGR01612 541 EIEAG-------LKESYELAKNWKKLIHEIKKELEEE--NEDSIHLEKEIKDL------FDKYLEIDDE----------- 594
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2043665167 1069 NPQVMYLEQEL-ESLKAVLEiKNEKLHqqdlKLMKMEKLVDNNTTLVDKLTRFQ--QENEELKARMDRHMAISRQLS 1142
Cdd:TIGR01612 595 IIYINKLKLELkEKIKNISD-KNEYIK----KAIDLKKIIENNNAYIDELAKISpyQVPEHLKNKDKIYSTIKSELS 666
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
987-1132 |
6.83e-04 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 41.14 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 987 KLEIEASHsEKVELLKktyetslsEIKKSHEMEKKLLENLLNekqeSLEKQINDLKSENDALNERLKseEQKQLSREKAN 1066
Cdd:pfam12718 6 KLEAENAQ-ERAEELE--------EKVKELEQENLEKEQEIK----SLTHKNQQLEEEVEKLEEQLK--EAKEKAEESEK 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2043665167 1067 SK------NPQVMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKlvdnnttlvdKLTRFQQENEELKARMD 1132
Cdd:pfam12718 71 LKtnnenlTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLER----------KVQALEQERDEWEKKYE 132
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
999-1145 |
6.95e-04 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 41.01 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 999 ELLKKTYETSLSEIKKSHEMEkklLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNpQVMYLEQE 1078
Cdd:pfam12474 6 EQQKDRFEQERQQLKKRYEKE---LEQLERQQKQQIEKLEQRQTQELRRLPKRIRAEQKKRLKMFRESLKQ-EKKELKQE 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2043665167 1079 LESLKavleikneKLHQQDLKLMKMEKLvdnnttlvdKLTRFQQENEELKARMDRHMAISRQLSTEQ 1145
Cdd:pfam12474 82 VEKLP--------KFQRKEAKRQRKEEL---------ELEQKHEELEFLQAQSEALERELQQLQNEK 131
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
898-1036 |
7.04e-04 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 42.20 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 898 SLRGELVAASSTCEKLEKARNDLQTAYEGFVQKLnQQHQTDQTELENRLKEFytaecEKLQSIYIEEAEKYKtQLQEQFD 977
Cdd:pfam13851 30 SLKEEIAELKKKEERNEKLMSEIQQENKRLTEPL-QKAQEEVEELRKQLENY-----EKDKQSLKNLKARLK-VLEKELK 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2043665167 978 NLNAAHETTKLEIEASHSEKVELLKKtYETSLSEIKKSHEMEKKLLENLLNEKQESLEK 1036
Cdd:pfam13851 103 DLKWEHEVLEQRFEKVERERDELYDK-FEAAIQDVQQKTGLKNLLLEKKLQALGETLEK 160
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
881-1152 |
8.86e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 43.75 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 881 EREEALKQH-----KTLSQ---ELVSLRGELVAASSTC----------EKLEKARNDLQTAYEGFVQkLNQQHQTDQTEL 942
Cdd:PRK11281 80 EETEQLKQQlaqapAKLRQaqaELEALKDDNDEETRETlstlslrqleSRLAQTLDQLQNAQNDLAE-YNSQLVSLQTQP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 943 ENRLKEFYTAEceklqsiyieeaekykTQLQE---QFDNLNAAHETTkleieaSHSEKVELlkktyETSLSEIKKSHEME 1019
Cdd:PRK11281 159 ERAQAALYANS----------------QRLQQirnLLKGGKVGGKAL------RPSQRVLL-----QAEQALLNAQNDLQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1020 KKLLEN-------------LLNEKQESLEKQINDLKsenDALNE-RLK-SEEQ--KQLSREKANS--KNPqvmYLEQELE 1080
Cdd:PRK11281 212 RKSLEGntqlqdllqkqrdYLTARIQRLEHQLQLLQ---EAINSkRLTlSEKTvqEAQSQDEAARiqANP---LVAQELE 285
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2043665167 1081 slkavleiKNEKLHQQDLKlmkmeklvdnnTTlvDKLTRFQQENEELKARMDRHMAISRQLStEQ-AALQESL 1152
Cdd:PRK11281 286 --------INLQLSQRLLK-----------AT--EKLNTLTQQNLRVKNWLDRLTQSERNIK-EQiSVLKGSL 336
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
1017-1133 |
9.74e-04 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 42.05 E-value: 9.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1017 EMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSknpqvmyLEQELESLKAVLEIKNEKLHQQ 1096
Cdd:PRK14160 4 ECKDAKHENMEEDCCKENENKEEDKGKEEDLEFEEIEKEEIIEDSEESNEV-------KIEELKDENNKLKEENKKLENE 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2043665167 1097 dlklmkMEklvdnntTLVDKLTRFQQENEELKARMDR 1133
Cdd:PRK14160 77 ------LE-------ALKDRLLRTVAEYDNYRKRTAK 100
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1017-1178 |
9.86e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 9.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1017 EMEKKLLENLLNEKQEsLEKQINDLKSENDALNERLKSeeqkqlSREKANSKNPQVMYLEQELESLKavlEIKNEklhqq 1096
Cdd:COG1340 4 DELSSSLEELEEKIEE-LREEIEELKEKRDELNEELKE------LAEKRDELNAQVKELREEAQELR---EKRDE----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1097 dlklmkmeklvdnnttLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLsmenEELLWKLHNG 1176
Cdd:COG1340 69 ----------------LNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEI----ERLEWRQQTE 128
|
..
gi 2043665167 1177 DL 1178
Cdd:COG1340 129 VL 130
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
971-1170 |
9.93e-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: 43.50 E-value: 9.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 971 QLQEQFDNLNAAHETTKleieashseKVELLKKTYETSLSEIKkSHEMEKKLLENLLN------------EKQESLEKQI 1038
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIK---------ALETLRQVRQTQGQKVQ-EHQMELKYLKQYKEkaceirdqitskEAQLESSREI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1039 NDLK-SENDALNERLKSEEQKQLSrekansknpqVMYLEQELESLKAVlEIKNEKLHQQdLKLmKMEKLvdnnttlvdkl 1117
Cdd:TIGR00606 240 VKSYeNELDPLKNRLKEIEHNLSK----------IMKLDNEIKALKSR-KKQMEKDNSE-LEL-KMEKV----------- 295
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2043665167 1118 trFQQENEELKARMDRHMAISRQLSTEQAALQESLEKESKVNKRLSMENEELL 1170
Cdd:TIGR00606 296 --FQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELL 346
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
948-1169 |
1.01e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 42.70 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 948 EFYTAECEKLQSiYIEEAEKYKTQLQEQFDNLN--------AAHETTKLEIEashsEKVELLKKTYETslsEIKKS-HEM 1018
Cdd:smart00787 66 ELYQFSCKELKK-YISEGRDLFKEIEEETLINNpplfkeyfSASPDVKLLMD----KQFQLVKTFARL---EAKKMwYEW 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1019 EKKLLENL----------LNEKQESLEKQINDLKSENDALNERLKS-----EEQKQLSREKANSKNPQVMYLEQELESLK 1083
Cdd:smart00787 138 RMKLLEGLkegldenlegLKEDYKLLMKELELLNSIKPKLRDRKDAleeelRQLKQLEDELEDCDPTELDRAKEKLKKLL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1084 AVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLTrfQQENEELKARMDRHMAISRQLSTEQAALQeSLEKESKVnKRLS 1163
Cdd:smart00787 218 QEIMIKVKKLEELEEELQELESKIEDLTNKKSELN--TEIAEAEKKLEQCRGFTFKEIEKLKEQLK-LLQSLTGW-KITK 293
|
....*.
gi 2043665167 1164 MENEEL 1169
Cdd:smart00787 294 LSGNTL 299
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
961-1169 |
1.06e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 961 YIEEAEKYKTQLQEQFDNLnaahettkLEIEASHSEKVELLKKTYEtslseikkshEMEKKLLEN---------LLNEKQ 1031
Cdd:PRK04778 113 LLDLIEEDIEQILEELQEL--------LESEEKNREEVEQLKDLYR----------ELRKSLLANrfsfgpaldELEKQL 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1032 ESLE---KQINDLKSEND---------ALNERLKSEEQK-----QLSREKANSknpqvmyLEQELESLKAVL-EIKNEKL 1093
Cdd:PRK04778 175 ENLEeefSQFVELTESGDyveareildQLEEELAALEQImeeipELLKELQTE-------LPDQLQELKAGYrELVEEGY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1094 HQQDLKLMKM-----EKLVDNNTTLVD-KLTRFQQENEELKARMD------RHMAISRQ-LSTEQAALQESLEKESKVNK 1160
Cdd:PRK04778 248 HLDHLDIEKEiqdlkEQIDENLALLEElDLDEAEEKNEEIQERIDqlydilEREVKARKyVEKNSDTLPDFLEHAKEQNK 327
|
....*....
gi 2043665167 1161 RLSMENEEL 1169
Cdd:PRK04778 328 ELKEEIDRV 336
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
997-1169 |
1.13e-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: 42.96 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 997 KVELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQ------ESLEKQINDLKSENDALNERLKSEEQKQlsrEKANSKNP 1070
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKErykrdrEQWERQRRELESRVAELKEELRQSREKH---EELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1071 QVMYLEQELESLKAVLeiknekLHQQDLKLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISRQLSTEQAALQE 1150
Cdd:pfam07888 105 ELSASSEELSEEKDAL------LAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQA 178
|
170
....*....|....*....
gi 2043665167 1151 SLEKESKVNKRLSMENEEL 1169
Cdd:pfam07888 179 KLQQTEEELRSLSKEFQEL 197
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
848-1091 |
1.25e-03 |
|
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: 43.11 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 848 ENQSGFILHLKQLLScgntKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEGF 927
Cdd:TIGR00606 853 QDQQEQIQHLKSKTN----ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEEL 928
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 928 VQKLNQQHQTDQTELENRLKE-----FYTAECEKlqsiYIEEA-EKYKTQLQEQFDNLNAahettKLEIEASHSEKVEll 1001
Cdd:TIGR00606 929 ISSKETSNKKAQDKVNDIKEKvknihGYMKDIEN----KIQDGkDDYLKQKETELNTVNA-----QLEECEKHQEKIN-- 997
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1002 kKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQ----LSREKANSKNPQVMYLEQ 1077
Cdd:TIGR00606 998 -EDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQehqkLEENIDLIKRNHVLALGR 1076
|
250
....*....|....
gi 2043665167 1078 ELESLKAVLEIKNE 1091
Cdd:TIGR00606 1077 QKGYEKEIKHFKKE 1090
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1020-1157 |
1.31e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.84 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1020 KKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKA------NSKNPQVMYLEQELESLKAVLEIKNEKL 1093
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNefekelRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2043665167 1094 HQQDLKLMKMEKLVDNNTTLVDKLtrfQQENEELKARMDRHMAISRQLSTEQA--ALQESLEKESK 1157
Cdd:PRK12704 106 EKREEELEKKEKELEQKQQELEKK---EEELEELIEEQLQELERISGLTAEEAkeILLEKVEEEAR 168
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
962-1157 |
1.41e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 962 IEEAEKYKTQLQEQFDNLNAAHETTKLEIEAShSEKVELLKKTYETSLSEIKKshemekklLENLLNEKQESLEKQINDL 1041
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNEL-QAELEALQAEIDKLQAEIAE--------AEAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1042 K---SENDALNERLKSEE-----QKQLSREKANSKNPQVMyleQELESLKAVLEIKNEKLHQqdlklmKMEKLVDNNTTL 1113
Cdd:COG3883 96 YrsgGSVSYLDVLLGSESfsdflDRLSALSKIADADADLL---EELKADKAELEAKKAELEA------KLAELEALKAEL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2043665167 1114 VDKLTRFQQENEELKARMDrhmaisrQLSTEQAALQESLEKESK 1157
Cdd:COG3883 167 EAAKAELEAQQAEQEALLA-------QLSAEEAAAEAQLAELEA 203
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
878-1089 |
1.46e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 42.61 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 878 LLSEREEALKQHKTLSQELVSLRGELVAASStcEKLEKARNDLQTAYEGFVQKLNQQHQtDQTELENRLKEF--YTAECE 955
Cdd:PRK05771 51 LLTKLSEALDKLRSYLPKLNPLREEKKKVSV--KSLEELIKDVEEELEKIEKEIKELEE-EISELENEIKELeqEIERLE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 956 KLQSIYIEEAEKYKTQL---------QEQFDNLNAAHETTKLEIEASHSEKVEL----LKKTYETSLSEIKKsHEMEKKL 1022
Cdd:PRK05771 128 PWGNFDLDLSLLLGFKYvsvfvgtvpEDKLEELKLESDVENVEYISTDKGYVYVvvvvLKELSDEVEEELKK-LGFERLE 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2043665167 1023 LEN--LLNEKQESLEKQINDLKSENDALNERLKSEEQKqLSREKANSKNpqvmYLEQELESLKAVLEIK 1089
Cdd:PRK05771 207 LEEegTPSELIREIKEELEEIEKERESLLEELKELAKK-YLEELLALYE----YLEIELERAEALSKFL 270
|
|
| COG5391 |
COG5391 |
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function ... |
857-1097 |
1.63e-03 |
|
Phox homology (PX) domain protein [Intracellular trafficking and secretion / General function prediction only];
Pssm-ID: 227680 [Multi-domain] Cd Length: 524 Bit Score: 42.48 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 857 LKQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASStceKLEKARNDLqtayegfVQKLNQQHQ 936
Cdd:COG5391 292 TSKAIHNILSIFSLFEKILIQLESEEESLTRLLESLNNLLLLVLNFSGVFAK---RLEQNQNSI-------LNEGVVQAE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 937 TDQTELENRLKEFYTAECEKLQSIYIEEA-EKYKTQLQEQFDNLNAAHETT---KLEIEASHSEKVELLKKTYETSLsei 1012
Cdd:COG5391 362 TLRSSLKELLTQLQDEIKSRESLILTDSNlEKLTDQNLEDVEELSRSLRKNssqRAVVSQQPEGLTSFSKLSYKLRD--- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1013 kKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEK 1092
Cdd:COG5391 439 -FVQEKSRSKSIESLQQDKEKLEEQLAIAEKDAQEINEELKNELKFFFSVRNSDLEKILKSVADSHIEWAEENLEIWKSV 517
|
....*
gi 2043665167 1093 LHQQD 1097
Cdd:COG5391 518 KEQLD 522
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
913-1150 |
1.73e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 41.83 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 913 LEKARNDLQTayegfvqKLNQQHQTDQTElENRLKEFYTAECEKLQSiYIEEAEKYKTQLQEQFDNLNAAHET--TKLEI 990
Cdd:pfam00038 23 LEQQNKLLET-------KISELRQKKGAE-PSRLYSLYEKEIEDLRR-QLDTLTVERARLQLELDNLRLAAEDfrQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 991 EASHSE-------------------KVELLKKtYETSLSEI---KKSHEMEKKLLENLLNEKQESLEKQIN---DLKSen 1045
Cdd:pfam00038 94 ELNLRTsaendlvglrkdldeatlaRVDLEAK-IESLKEELaflKKNHEEEVRELQAQVSDTQVNVEMDAArklDLTS-- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1046 dALNE-RLKSEEQKQLSREKANsknpqvMYLEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDNNTTLVDKLtRFQQEN 1124
Cdd:pfam00038 171 -ALAEiRAQYEEIAAKNREEAE------EWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSL-KKQKAS 242
|
250 260 270
....*....|....*....|....*....|..
gi 2043665167 1125 -----EELKARMDRHMA-ISRQLSTEQAALQE 1150
Cdd:pfam00038 243 lerqlAETEERYELQLAdYQELISELEAELQE 274
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
922-1167 |
2.10e-03 |
|
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: 42.73 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 922 TAYEGFVQKLNQQHQTDQTELENRLKEFytaecekLQSIYIEEAE-KYKTQ-LQEQFDNLNAAHETTKLEIEASHSEKVE 999
Cdd:TIGR01612 656 KIYSTIKSELSKIYEDDIDALYNELSSI-------VKENAIDNTEdKAKLDdLKSKIDKEYDKIQNMETATVELHLSNIE 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1000 LLKKTYETSLSEIKKSHEME-----KKLLENLLNeKQESLEKQINDLKSENDALN------ERLKSEEQKQLSREKANSK 1068
Cdd:TIGR01612 729 NKKNELLDIIVEIKKHIHGEinkdlNKILEDFKN-KEKELSNKINDYAKEKDELNkykskiSEIKNHYNDQINIDNIKDE 807
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1069 NPQVMYlEQELESLKAVlEIKNEKLHQ--QDLKLMKMEKLvdnntTLVDKLTRFQQENEE-LKARMDRHMAISRQLSTEQ 1145
Cdd:TIGR01612 808 DAKQNY-DKSKEYIKTI-SIKEDEIFKiiNEMKFMKDDFL-----NKVDKFINFENNCKEkIDSEHEQFAELTNKIKAEI 880
|
250 260
....*....|....*....|..
gi 2043665167 1146 AALQESlEKESKVNKRLSMENE 1167
Cdd:TIGR01612 881 SDDKLN-DYEKKFNDSKSLINE 901
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
840-1094 |
2.18e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 840 LADYKTKCEN-QSGFILHLKQ----LLSCGNTKFEaltvviqhLLSEREEALKQHKTLSQELVSLRgelvaasstcEKLE 914
Cdd:PTZ00440 747 LEVYKHQIINrKNEFILHLYEndkdLPDGKNTYEE--------FLQYKDTILNKENKISNDINILK----------ENKK 808
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 915 KARNDLQTaYEGFVQKLnQQHQTDQTELENRLKEFYTAECE-----KLQSIYIEEAEKYKT---QLQEQFDNLNA----- 981
Cdd:PTZ00440 809 NNQDLLNS-YNILIQKL-EAHTEKNDEELKQLLQKFPTEDEnlnlkELEKEFNENNQIVDNiikDIENMNKNINIiktln 886
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 982 ----AHETTKLEIEASHSEKVELLKKTyETSLSEIKKSH---EMEKKLLENLLNEKQESLEKQ-----INDLKSENDALN 1049
Cdd:PTZ00440 887 iainRSNSNKQLVEHLLNNKIDLKNKL-EQHMKIINTDNiiqKNEKLNLLNNLNKEKEKIEKQlsdtkINNLKMQIEKTL 965
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1050 ERLKSEEQKQLSR-----EKANSKNPQVMYLEQELESLKAVLEIKNEKLH 1094
Cdd:PTZ00440 966 EYYDKSKENINGNdgthlEKLDKEKDEWEHFKSEIDKLNVNYNILNKKID 1015
|
|
| Wtap |
pfam17098 |
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and ... |
1019-1169 |
2.24e-03 |
|
WTAP/Mum2p family; The Wtap family includes female-lethal(2)D from Drosophila and pre-mRNA-splicing regulator WTAP from mammals. The former is required for female-specific splicing of Sex-lethal RNA, and the latter is a regulatory subunit of the RNA N6-methyladenosine methyltransferase. The family also includes the yeast Mum2p protein which is part of the Mis complex.
Pssm-ID: 465345 [Multi-domain] Cd Length: 155 Bit Score: 39.97 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1019 EKKLLENLLNEKQESLEKQINDLKSENDalneRLKSeeqkqlSREKANSKNPQVMY---LEQELESLKAVLEIKNEKLHQ 1095
Cdd:pfam17098 1 ESKRRENLLLARLAEKEQEIQELKAQLQ----DLKQ------SLQPPSSQLRSLLLdpaVNLEFLRLKKELEEKKKKLKE 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2043665167 1096 QDLKLMKMEKLVDNNTT--LVDKLTRFQQENEELkarmdrhmaiSRQLSTEQAA-LQESLEKESKVNKRLSMENEEL 1169
Cdd:pfam17098 71 AQLELAAWKFTPDSTTGkrLMAKCRLLQQENEEL----------GRQLSEGRIAkLEIELALQKKVVEELKKSLEEL 137
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
857-1126 |
2.40e-03 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 41.51 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 857 LKQLLSCGNTKFEALTVVIQHLLSEREEAlKQHK-TLSQELVSLRGELVAASSTCEKLEKARNDLQTAYegfvQKLNQQH 935
Cdd:pfam14915 54 LTKTVFQYNGQLNVLKAENTMLNSKLENE-KQNKeRLETEVESYRSRLAAAIQDHEQSQTSKRDLELAF----QRERDEW 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 936 QtdqtelenRLKEFYTAECEKLqsiyIEEAEKYKTQLQE---QFDNL-NAAHETT-KLEIEASHSEKVELLKKTYETSLS 1010
Cdd:pfam14915 129 L--------RLQDKMNFDVSNL----RDENEILSQQLSKaesKANSLeNELHRTRdALREKTLLLESVQRDLSQAQCQKK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1011 EIKKSHEMEKKLLENLLnEKQESLEKQINDLKSENDALnerlkseeQKQLS--REKANSKNPQVMYLEQELESLKAVLEI 1088
Cdd:pfam14915 197 ELEHMYQNEQDKVNKYI-GKQESLEERLAQLQSENMLL--------RQQLEdaQNKADAKEKTVIDIQDQFQDIVKKLQA 267
|
250 260 270
....*....|....*....|....*....|....*....
gi 2043665167 1089 KNEKlhqQDLKLM-KMEKLVDNNTTLVDKLTRFQQENEE 1126
Cdd:pfam14915 268 ESEK---QVLLLEeRNKELINECNHLKERLYQYEKEKAE 303
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
866-1080 |
2.41e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.36 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 866 TKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELvaasstcEKLEKARNDLQTAYEGFVQKLNQQHQtDQTELENR 945
Cdd:TIGR02169 357 EEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-------EKLKREINELKRELDRLQEELQRLSE-ELADLNAA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 946 lkefytaeceklqsiyIEEAEKYKTQLQEqfdnlnaAHETTKLEIEAShsekvellkktyETSLSEIKKSHEMEKKLLEN 1025
Cdd:TIGR02169 429 ----------------IAGIEAKINELEE-------EKEDKALEIKKQ------------EWKLEQLAADLSKYEQELYD 473
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2043665167 1026 lLNEKQESLEKQINDLKSENDALnerlksEEQKQLSREKANSKNPQVMYLEQELE 1080
Cdd:TIGR02169 474 -LKEEYDRVEKELSKLQRELAEA------EAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| K-box |
pfam01486 |
K-box region; The K-box region is commonly found associated with SRF-type transcription ... |
1030-1132 |
2.74e-03 |
|
K-box region; The K-box region is commonly found associated with SRF-type transcription factors see pfam00319. The K-box is a possible coiled-coil structure. Possible role in multimer formation.
Pssm-ID: 460228 [Multi-domain] Cd Length: 91 Bit Score: 38.21 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1030 KQESLEKQINDLKSENDALNErlkseEQKQLSREKANSKNPQ-VMYLEQELE-SLKAVLEIKNEKLHQQDLKLMKMEKLV 1107
Cdd:pfam01486 5 EQENWQQEAAKLKKEIENLQR-----SQRQLLGEDLSSLSLKeLQQLEQQLEkSLKRIRSRKNQLLLEQIEELKKKERIL 79
|
90 100
....*....|....*....|....*
gi 2043665167 1108 dnnttlvdkltrfQQENEELKARMD 1132
Cdd:pfam01486 80 -------------QEENKELRKKLE 91
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
876-1096 |
2.93e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.93 E-value: 2.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 876 QHLLSEREEALKQHKTLSQELVSLRGELvaasstcEKLEKARNDLQTAYEGFVQKLNQQHQTDQ-TELENRLkefytaec 954
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-------EEAEAALEEFRQKNGLVDLSEEAKLLLQQlSELESQL-------- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 955 EKLQSIyIEEAEKYKTQLQEQFDNLNAAhettklEIEASHSEKVELLKKTYETSLSEIKkshEMEKKLLEN-----LLNE 1029
Cdd:COG3206 229 AEARAE-LAEAEARLAALRAQLGSGPDA------LPELLQSPVIQQLRAQLAELEAELA---ELSARYTPNhpdviALRA 298
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2043665167 1030 KQESLEKQIN--------DLKSENDALNERLKSEEQkQLSREKANSKN-PQvmyLEQELESLKAVLEIkNEKLHQQ 1096
Cdd:COG3206 299 QIAALRAQLQqeaqrilaSLEAELEALQAREASLQA-QLAQLEARLAElPE---LEAELRRLEREVEV-ARELYES 369
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
858-1174 |
2.95e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 41.82 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 858 KQLLSCGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELvaasstcEKLEKARNDLQTAYEGFVQKLNQQ--- 934
Cdd:pfam15964 374 KELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQV-------EKVTREKNSLVSQLEEAQKQLASQemd 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 935 ---------HQTDQT-----ELENRLKEFYTAECEKLQsIYIEEAEKYKTQL--------QEQFDNLNAAHETTKLEIEA 992
Cdd:pfam15964 447 vtkvcgemrYQLNQTkmkkdEAEKEHREYRTKTGRQLE-IKDQEIEKLGLELseskqrleQAQQDAARAREECLKLTELL 525
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 993 SHSEK----VELLKKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALnerlkseeqkqlsrekANSK 1068
Cdd:pfam15964 526 GESEHqlhlTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSL----------------LTSQ 589
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1069 NPQVMYLEQELESLKAVLEIKNEKLHQqdlklmKMEKLVDNNTTLVDKLTRFQQENEELK------ARMDRHMAIS-RQL 1141
Cdd:pfam15964 590 NTFIAKLKEECCTLAKKLEEITQKSRS------EVEQLSQEKEYLQDRLEKLQKRNEELEeqcvqhGRMHERMKQRlRQL 663
|
330 340 350
....*....|....*....|....*....|....
gi 2043665167 1142 STE-QAALQESLEKESKVNKrLSMENEELLWKLH 1174
Cdd:pfam15964 664 DKHcQATAQQLVQLLSKQNQ-LFKERQNLTEEVQ 696
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
931-1123 |
3.02e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 41.54 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 931 LNQQHQTdQTELENRLKEFYTAECEKLQSIYIEEAEKYKT------QLQEQFDNLNAAHET-----TKLEIE-ASHSEKV 998
Cdd:PHA02562 193 IQQQIKT-YNKNIEEQRKKNGENIARKQNKYDELVEEAKTikaeieELTDELLNLVMDIEDpsaalNKLNTAaAKIKSKI 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 999 ELLKK-------------------TYETSLSEIK-KSHEMEKKLleNLLNEKQESLEK---QINDLKSENDALNERLKSE 1055
Cdd:PHA02562 272 EQFQKvikmyekggvcptctqqisEGPDRITKIKdKLKELQHSL--EKLDTAIDELEEimdEFNEQSKKLLELKNKISTN 349
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2043665167 1056 EQkQLSREKANSKNpqvmyLEQELESLKAVLEIKNEKLhqqdlklmkmEKLVDNNTTLVDKLTRFQQE 1123
Cdd:PHA02562 350 KQ-SLITLVDKAKK-----VKAAIEELQAEFVDNAEEL----------AKLQDELDKIVKTKSELVKE 401
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
875-1169 |
3.24e-03 |
|
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: 41.38 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 875 IQHLLSEREEALKQHKTLSQELVSLRgelvaasstcEKLEKARNDLQT---AYEGFVQKLNQQHQtdqtELENRLKEFYT 951
Cdd:pfam06160 102 IKQILEELDELLESEEKNREEVEELK----------DKYRELRKTLLAnrfSYGPAIDELEKQLA----EIEEEFSQFEE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 952 A------------------ECEKLQSiYIEEA----EKYKTQLQEQFDNLNAAHEttKLEIEASHSEKVELLKktyetsl 1009
Cdd:pfam06160 168 LtesgdylearevlekleeETDALEE-LMEDIpplyEELKTELPDQLEELKEGYR--EMEEEGYALEHLNVDK------- 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1010 sEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENDALnerlkseeQKQLSREKaNSKNpqvmYLEQELESLKAVLEik 1089
Cdd:pfam06160 238 -EIQQLEEQLEENLALLENLELDEAEEALEEIEERIDQL--------YDLLEKEV-DAKK----YVEKNLPEIEDYLE-- 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1090 neklHQQDLKLMKMEKL--VDNNTTLVDK-LTRFQQENEELKARMDRHMAISRQLSTEQAA---LQESLEKESKVNKRLS 1163
Cdd:pfam06160 302 ----HAEEQNKELKEELerVQQSYTLNENeLERVRGLEKQLEELEKRYDEIVERLEEKEVAyseLQEELEEILEQLEEIE 377
|
....*.
gi 2043665167 1164 MENEEL 1169
Cdd:pfam06160 378 EEQEEF 383
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
961-1050 |
3.49e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 38.77 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 961 YIEEAEKYKTQLQEQFDNLNAAHEttKLEIE-ASHSEKVELLKKTYETSLSEIKKSHEMEKKL---------LENLLNEK 1030
Cdd:pfam07926 20 AEAQLQKLQEDLEKQAEIAREAQQ--NYERElVLHAEDIKALQALREELNELKAEIAELKAEAesakaeleeSEESWEEQ 97
|
90 100
....*....|....*....|
gi 2043665167 1031 QESLEKQINDLKSENDALNE 1050
Cdd:pfam07926 98 KKELEKELSELEKRIEDLNE 117
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
882-1133 |
3.92e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 41.48 E-value: 3.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 882 REEALKQHKTLSQELVSLRGELVAA-SSTCEKLE--KARNDLQTAYEgfvQKLNQQHQTD-QTELENRLKEFYT------ 951
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQfENTKEKIAeyTKSIDIKKATE---SLEEQLAAAEaEQELEESKRETETgiqnlt 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 952 AECEKLQSIYIEEAEKYK------------TQLQEQFDNLNAAHETTKLEIEASHSEKVELLKKTYETsLSEIKKSHEME 1019
Cdd:COG5185 343 AEIEQGQESLTENLEAIKeeienivgevelSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAT-LEDTLKAADRQ 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1020 KKLLENLLNEKQESLE---KQINDLKSENDALNERLKSEEQKQLS----------REKANSKNPQVMYLEQELESLKAVL 1086
Cdd:COG5185 422 IEELQRQIEQATSSNEevsKLLNELISELNKVMREADEESQSRLEeaydeinrsvRSKKEDLNEELTQIESRVSTLKATL 501
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2043665167 1087 EIKNEKLHQQdlkLMKMEKLVDNNTTLVDKLTRFQQENEELKARMDR 1133
Cdd:COG5185 502 EKLRAKLERQ---LEGVRSKLDQVAESLKDFMRARGYAHILALENLI 545
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
866-1173 |
4.02e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 41.70 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 866 TKFEALTVVIQHLLSEREEALKQHKTLSQELVSLRGELVAASSTCEKLEKARNDLQTAYEgfvqklnqQHQTDQTELENR 945
Cdd:pfam01576 636 TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE--------EMKTQLEELEDE 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 946 LKEfytAECEKLQ----------------SIYIEEAEKYKTQLQEQFDNLNAahettklEIEASHSEKVELL--KKTYET 1007
Cdd:pfam01576 708 LQA---TEDAKLRlevnmqalkaqferdlQARDEQGEEKRRQLVKQVRELEA-------ELEDERKQRAQAVaaKKKLEL 777
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1008 SLSEIKKSHEMEKKLLENLLneKQ-ESLEKQINDLKSENDALneRLKSEEQKQLSRE---KANSKNPQVMYLEQEL---E 1080
Cdd:pfam01576 778 DLKELEAQIDAANKGREEAV--KQlKKLQAQMKDLQRELEEA--RASRDEILAQSKEsekKLKNLEAELLQLQEDLaasE 853
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1081 SLKAVLEIKNEKLhQQDLK--LMKMEKLVDNNTTLVDKLTRFQQENEE-------LKARMDRHMAISRQLSTEQAALQES 1151
Cdd:pfam01576 854 RARRQAQQERDEL-ADEIAsgASGKSALQDEKRRLEARIAQLEEELEEeqsntelLNDRLRKSTLQVEQLTTELAAERST 932
|
330 340
....*....|....*....|..
gi 2043665167 1152 LEKESKVNKRLSMENEELLWKL 1173
Cdd:pfam01576 933 SQKSESARQQLERQNKELKAKL 954
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
933-1097 |
4.62e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 933 QQHQTDQTELENRLKefyTAEcEKLQSIY--IEEAEKYKTQLQEQFDNLNAAHETTKLEIEASHS---EKVELLKK---- 1003
Cdd:COG3883 19 QAKQKELSELQAELE---AAQ-AELDALQaeLEELNEEYNELQAELEALQAEIDKLQAEIAEAEAeieERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1004 TYE--------------TSLSE-------IKKSHEMEKKLLENL------LNEKQESLEKQINDLKSENDALNERLKSEE 1056
Cdd:COG3883 95 LYRsggsvsyldvllgsESFSDfldrlsaLSKIADADADLLEELkadkaeLEAKKAELEAKLAELEALKAELEAAKAELE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2043665167 1057 QKQLSREKANSK-NPQVMYLEQELESLKAVLEIKNEKLHQQD 1097
Cdd:COG3883 175 AQQAEQEALLAQlSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
887-1136 |
4.87e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 40.01 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 887 KQHKTLSQELVSLRGELVAASSTCEKLEKARNDLqtayEGFVQKLNQQHQTDQTELEnRLKEFYTAECEKLqsiyiEEAE 966
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRAEKA----EAEVAALNRRIQLLEEELE-RTEERLAEALEKL-----EEAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 967 KYKtqlqEQFDNLNAAHETTKLEIEashsEKVELLkktyETSLSEIK--------KSHEMEKKL--LENLLN---EKQES 1033
Cdd:pfam00261 71 KAA----DESERGRKVLENRALKDE----EKMEIL----EAQLKEAKeiaeeadrKYEEVARKLvvVEGDLEraeERAEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1034 LEKQINDLKSENDALNERLKSEEqkqLSREKANSKNPQVmylEQELESLKAVLEIKNEKLHQQDLKLMKMEKLVDnntTL 1113
Cdd:pfam00261 139 AESKIVELEEELKVVGNNLKSLE---ASEEKASEREDKY---EEQIRFLTEKLKEAETRAEFAERSVQKLEKEVD---RL 209
|
250 260
....*....|....*....|...
gi 2043665167 1114 VDKLTRFQQENEELKARMDRHMA 1136
Cdd:pfam00261 210 EDELEAEKEKYKAISEELDQTLA 232
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
932-1171 |
4.89e-03 |
|
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: 41.58 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 932 NQQHQTDQTEL---ENRLKEFYTAECEKLQSIYIEEAEK---------YKTQLQEQ-------FDNLNAA-------HET 985
Cdd:TIGR01612 1857 NVKNSTDENLLfdiLNKTKDAYAGIIGKKYYSYKDEAEKifinisklaNSINIQIQnnsgidlFDNINIAilssldsEKE 1936
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 986 TKLEIEASHSEKVELLKK---TYETSLSEIKKSHEMEKKLLE--NLLNEKQESLEK--QINDLK--------SENDALNE 1050
Cdd:TIGR01612 1937 DTLKFIPSPEKEPEIYTKirdSYDTLLDIFKKSQDLHKKEQDtlNIIFENQQLYEKiqASNELKdtlsdlkyKKEKILND 2016
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1051 -RL---KSEEQKQLSREKAN-------SKNPQVMY----LEQELESLKAVLEIK-NEKLHQQDLKlmKMEKLVDNNTTLV 1114
Cdd:TIGR01612 2017 vKLllhKFDELNKLSCDSQNydtilelSKQDKIKEkidnYEKEKEKFGIDFDVKaMEEKFDNDIK--DIEKFENNYKHSE 2094
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2043665167 1115 DKLTRFQQENEELKARMDRHMAISRQLSTEQAALQES-LEKESKVNKRLSMENEELLW 1171
Cdd:TIGR01612 2095 KDNHDFSEEKDNIIQSKKKLKELTEAFNTEIKIIEDKiIEKNDLIDKLIEMRKECLLF 2152
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
901-1153 |
5.34e-03 |
|
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: 41.19 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 901 GELVAASSTCEKLEKARNDLQTAYEGFVQKLNQQHQTDQT-------ELENRLKEFYTAeceklqSIYIEEAEKYKtQLQ 973
Cdd:TIGR00606 123 GEKVSLSSKCAEIDREMISHLGVSKAVLNNVIFCHQEDSNwplsegkALKQKFDEIFSA------TRYIKALETLR-QVR 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 974 EQFDNLNAAHETTKLEIEASHSEKVEL-----LKKTYETSLSEIKKSHEMEKKLLENLLNEKQESLEKqINDLKSEndal 1048
Cdd:TIGR00606 196 QTQGQKVQEHQMELKYLKQYKEKACEIrdqitSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSK-IMKLDNE---- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1049 nerLKSEEQKQLSREKANSKNPQVM---YLEQElESLKAVLEIKNEKLHQQDLKLM----KMEKLVDNNTTLVDKLTRFQ 1121
Cdd:TIGR00606 271 ---IKALKSRKKQMEKDNSELELKMekvFQGTD-EQLNDLYHNHQRTVREKERELVdcqrELEKLNKERRLLNQEKTELL 346
|
250 260 270
....*....|....*....|....*....|..
gi 2043665167 1122 QENEELKARMDRHMAISRQLSTEQAALQESLE 1153
Cdd:TIGR00606 347 VEQGRLQLQADRHQEHIRARDSLIQSLATRLE 378
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
879-1169 |
5.70e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 5.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 879 LSEREEALKQHKTLSQE----LVSLRGELVAASSTCEKLEKARNDLQTAYEgFVQKLNQQHQTDQTELENrlkefyTAEC 954
Cdd:PRK04863 357 LEELEERLEEQNEVVEEadeqQEENEARAEAAEEEVDELKSQLADYQQALD-VQQTRAIQYQQAVQALER------AKQL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 955 EKLQSIYIEEA----EKYKTQLQEQFDNLNAAHetTKLEI-EASHS--EKV-ELLKK-TYETSLSEikkSHEMEKKLLEN 1025
Cdd:PRK04863 430 CGLPDLTADNAedwlEEFQAKEQEATEELLSLE--QKLSVaQAAHSqfEQAyQLVRKiAGEVSRSE---AWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1026 LlnEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLKAVLEIKNEKLHQQdlklmkMEK 1105
Cdd:PRK04863 505 L--REQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES------VSE 576
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1106 LVDNNTTLvdkltrfQQENEELKARMDRHMAISRQLSTEQAAL---------------------QESLEKEskvnKRLSM 1164
Cdd:PRK04863 577 ARERRMAL-------RQQLEQLQARIQRLAARAPAWLAAQDALarlreqsgeefedsqdvteymQQLLERE----RELTV 645
|
....*
gi 2043665167 1165 ENEEL 1169
Cdd:PRK04863 646 ERDEL 650
|
|
| PI3K_P85_iSH2 |
pfam16454 |
Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain; This domain is found ... |
929-1044 |
5.86e-03 |
|
Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain; This domain is found between the two SH2 domains in phosphatidylinositol 3-kinase regulatory subunit P85. It forms a complex with the adaptor-binding domain of phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha.
Pssm-ID: 465121 [Multi-domain] Cd Length: 161 Bit Score: 38.79 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 929 QKLNQQHQTDQTELEnRLKEFYTAECEKLQSiyieeaekyKTQLQEQFDNLNA-----AHETTKLEIEASHSEKvELLKK 1003
Cdd:pfam16454 20 IEIHKQYLEKSREYD-RLYEEYNKTSQEIQM---------KRQALEAFNEAIKmfeeqIKLQERFSKEAQPHEI-ERLLE 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2043665167 1004 TYETSLSEIKKSHEMEKKLLENLLNEKQES--LEKQINDLKSE 1044
Cdd:pfam16454 89 NYELLKSRLKELHDSKEQLEEDLKTQKEYNreLEREMNSLKPE 131
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
974-1116 |
5.86e-03 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 38.75 E-value: 5.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 974 EQFDNLNAAHETTKLEIEAShSEKVELLKKTYETSlSEIKKSHEMEKKLLENLLNEKQESLEKQINDLKSENdalnerlk 1053
Cdd:pfam09744 36 ELLESLASRNQEHNVELEEL-REDNEQLETQYERE-KALRKRAEEELEEIEDQWEQETKDLLSQVESLEEEN-------- 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2043665167 1054 seeqKQLSREKANSknpqvmyleqeLESLKAVLEIKNEKLHQQDLKLMKmeKLVDnnttLVDK 1116
Cdd:pfam09744 106 ----RRLEADHVSR-----------LEEKEAELKKEYSKLHERETEVLR--KLKE----VVDR 147
|
|
| Ctf13_LRR_LRR-insertion |
cd19611 |
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein ... |
1008-1095 |
6.42e-03 |
|
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein complex CBF3 subunit C (Ctf13); Ctf13, is an F-box protein of the leucine-rich-repeat superfamily; it is a component of CEN binding factor 3 (CBF3), a complex that recognizes point centromeres found in budding yeast, associating specifically with the third centromere DNA element (CDEIII) DNA. CBF3 is comprised of two homodimers of Cep3 and Ndc10, and a Ctf13-Skp1 heterodimer. The Skp1-Ctf13 heterodimer interacts with Cep3, Ndc10 and CDEIII at a completely conserved G, centrally positioned between the TGC/CCG sites. The eight leucine-rich repeat (LRR) motifs of Ctf13 (LRR 1-8) form a solenoid structure. At the N-terminus of the Ctf13 LRR is an expanded F-box, and at the C-terminal end, an alpha-beta domain formed by insertions within the latter LRRs of Ctf13 (LRR insertion domain). This domain model includes the LLR domain and the LRR insertion domain.
Pssm-ID: 381623 Cd Length: 290 Bit Score: 40.01 E-value: 6.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1008 SLSEIKK-SHEMEKKLLENLLNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKNPQVMYLEQELESLK--A 1084
Cdd:cd19611 14 NPNMVKKiLKVLEKKELLDLVSEVFFGQDEEESDEEDEDDSSKNDRKKLTDDDVKEKSYKLNDPSIIRIISSLESMKnlR 93
|
90
....*....|.
gi 2043665167 1085 VLEIKNEKLHQ 1095
Cdd:cd19611 94 KLSVRGDNLYE 104
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1003-1160 |
6.68e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.38 E-value: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1003 KTYETSLSEIKKSHEMEKKLLENL----------LNEKQESLEKQINDLKSENDALNERLKSEEQKQLSREKANSKnpqv 1072
Cdd:PHA02562 184 QTLDMKIDHIQQQIKTYNKNIEEQrkkngeniarKQNKYDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNK---- 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1073 myLEQELESLKAVLEI--KNEKLHQ---------QDLKLM--KMEKLVDNNTTLVDKLTRFQQENEELKARMDRHMAISR 1139
Cdd:PHA02562 260 --LNTAAAKIKSKIEQfqKVIKMYEkggvcptctQQISEGpdRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSK 337
|
170 180
....*....|....*....|....*...
gi 2043665167 1140 -------QLSTEQAALQESLEKESKVNK 1160
Cdd:PHA02562 338 kllelknKISTNKQSLITLVDKAKKVKA 365
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
946-1168 |
7.86e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 7.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 946 LKEFYTAECEKLQSIYIEEAEKYKTQLQEQFDNLNAAHETTKLEIEashSEKVELLKKTYEtslSEIKKSHEMEKKLLEN 1025
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE---KKKVEQLKKKEA---EEKKKAEELKKAEEEN 1659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 1026 LLNEKQESLEKQINDLKSEndalnERLKSEEQKQLSREKansknpqvmyLEQELESLKAVLEIKnEKLHQQDLKLMKMEK 1105
Cdd:PTZ00121 1660 KIKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEA----------LKKEAEEAKKAEELK-KKEAEEKKKAEELKK 1723
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2043665167 1106 LVDNNTTLVDKLTRFQQEN----EELKARMDRHMAISRQLSTEQAALQE-SLEKESKVNKRLSMENEE 1168
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEEDkkkaEEAKKDEEEKKKIAHLKKEEEKKAEEiRKEKEAVIEEELDEEDEK 1791
|
|
| COG6 |
pfam06419 |
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi ... |
956-1051 |
8.60e-03 |
|
Conserved oligomeric complex COG6; COG6 is a component of the conserved oligomeric golgi complex, which is composed of eight different subunits and is required for normal golgi morphology and localization.
Pssm-ID: 461904 Cd Length: 611 Bit Score: 40.28 E-value: 8.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 956 KLQSIYIEEAEKYKTQLQ---EQFDNLNAAHETTKLEIEASHSEKVELLKKTyeTSLSEIKKSHEMEKKLLENLLNEKQE 1032
Cdd:pfam06419 30 KINGEFLKEFGPVVEQLKrieTDVEKLNNSCDEMRKRLSAAKEDTAPLLEEA--SSLQEQKKKIELKQKLLDAFLDKFTL 107
|
90
....*....|....*....
gi 2043665167 1033 SlEKQINDLKSENDALNER 1051
Cdd:pfam06419 108 S-EEEEAALTSGEEPVNDE 125
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
879-1056 |
8.71e-03 |
|
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: 38.76 E-value: 8.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 879 LSEREEALKQHKTlsqelvSLRGELVAASSTCEKLEKARNDLQTAYegfVQKLNQQHQTDQTELEnrlkefytaeceklq 958
Cdd:pfam08614 12 LLDRTALLEAENA------KLQSEPESVLPSTSSSKLSKASPQSAS---IQSLEQLLAQLREELA--------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043665167 959 siyieEAEKYKTQLQEQFDNLNAAHETTKLEIEAShSEKVELLKKTyETSLSEIKKSHEME----KKLLENL------LN 1028
Cdd:pfam08614 68 -----ELYRSRGELAQRLVDLNEELQELEKKLRED-ERRLAALEAE-RAQLEEKLKDREEElrekRKLNQDLqdelvaLQ 140
|
170 180 190
....*....|....*....|....*....|.
gi 2043665167 1029 EKQESLEKQINDLKSENDALNERL---KSEE 1056
Cdd:pfam08614 141 LQLNMAEEKLRKLEKENRELVERWmkrKGQE 171
|
|
| |
