|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
820-1020 |
8.12e-101 |
|
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: 315.08 E-value: 8.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 820 FQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQA 899
Cdd:pfam05010 1 YSQKDMDAALEKARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKDQA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 900 LADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQ 979
Cdd:pfam05010 81 LADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRSKAKA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 11119414 980 EQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDELI 1020
Cdd:pfam05010 161 ETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
753-1021 |
4.66e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 753 AQKLQEELEfaIMRIEALKLARQIALASRSHQDAKREAahptdvsisktalysrigtaevekpagllfqqpdLDSALQIA 832
Cdd:COG1196 215 YRELKEELK--ELEAELLLLKLRELEAELEELEAELEE----------------------------------LEAELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 833 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKsvshQTVQQLVLEKEQALADLNSVEKSLAD 912
Cdd:COG1196 259 EAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE----ERRRELEERLEELEEELAELEEELEE 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 913 LfrrYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQ 992
Cdd:COG1196 335 L---EEELEELEEELEEAEEELEEAEAE-LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
250 260
....*....|....*....|....*....
gi 11119414 993 LRVDALERTLEQKNKEIEELTKICDELIA 1021
Cdd:COG1196 411 ALLERLERLEEELEELEEALAELEEEEEE 439
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
825-1014 |
1.04e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 53.14 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 825 LDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKT---IAQMIEDEQREKsvshqtvQQLVLEKEQALA 901
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKElyaLANEISRLEQQK-------QILRERLANLER 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 902 DLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVH---AEEKLDRANAEIAQVRGKAQ 978
Cdd:TIGR02168 317 QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRleeLEEQLETLRSKVAQLELQIA 396
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 11119414 979 qeqaahqaSLRKEQLRVDA----LERTLEQKNKEIEELTK 1014
Cdd:TIGR02168 397 --------SLNNEIERLEArlerLEDRRERLQQEIEELLK 428
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
825-1023 |
2.35e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 825 LDSALQIARAEIITKE-REVSEWKDKYEESRREVMEMRKIVAEYEKtiaqmIEDEQREKSVSHQTVQQLVLEKEQALADL 903
Cdd:COG4717 47 LLERLEKEADELFKPQgRKPELNLKELKELEEELKEAEEKEEEYAE-----LQEELEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 904 nSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRvkkeEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAA 983
Cdd:COG4717 122 -EKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL----EEELEELEAELAELQEELEELLEQLSLATEEELQD 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 11119414 984 HQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAKM 1023
Cdd:COG4717 197 LAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
754-1022 |
3.15e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 51.48 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 754 QKLQEELEFAIMRIEALKLARQIALASRSHQDAKREAAhptdvsisKTALYSRigTAEVEkpagllfqqpDLDSALQIAR 833
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEEL--------RLELEEL--ELELE----------EAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 834 AEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKsvshQTVQQLVLEKEQALADLNSVEKSLADL 913
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE----EELEEAEEELEEAEAELAEAEEALLEA 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 914 FRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRG--KAQQEQAAHQASLRKE 991
Cdd:COG1196 371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAEleEEEEEEEEALEEAAEE 450
|
250 260 270
....*....|....*....|....*....|.
gi 11119414 992 QLRVDALERTLEQKNKEIEELTKICDELIAK 1022
Cdd:COG1196 451 EAELEEEEEALLELLAELLEEAALLEAALAE 481
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
818-1014 |
7.43e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 7.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 818 LLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSV--SHQTVQQLVLE 895
Cdd:PRK03918 184 FIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLegSKRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 896 KEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEEKLDRANA------- 968
Cdd:PRK03918 264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDE-LREIEKRLSRLEEEINGIEERIKELEEkeerlee 342
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 11119414 969 ----------EIAQVRGKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTK 1014
Cdd:PRK03918 343 lkkklkelekRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
773-1018 |
8.59e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 50.14 E-value: 8.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 773 ARQIALASRSHQDAKREAAHPTD----VSISKTALYSRigTAEVEKPAGLLFQQPDLDSALQIARAEIITKEREV--SEW 846
Cdd:PTZ00121 1139 ARKAEEARKAEDAKRVEIARKAEdarkAEEARKAEDAK--KAEAARKAEEVRKAEELRKAEDARKAEAARKAEEErkAEE 1216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 847 KDKYEESRR-----EVMEMRKIVAEYEKTIAQMIEDEQR---EKSVSHQTVQQLVL---EKEQALADLNSVEKSLADLFR 915
Cdd:PTZ00121 1217 ARKAEDAKKaeavkKAEEAKKDAEEAKKAEEERNNEEIRkfeEARMAHFARRQAAIkaeEARKADELKKAEEKKKADEAK 1296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 916 RYEKMKEVLEGFRKNEEvlKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQeqaahqasLRKEQLRV 995
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADE--------AEAAEEKA 1366
|
250 260
....*....|....*....|...
gi 11119414 996 DALERTLEQKNKEIEELTKICDE 1018
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAEE 1389
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
821-1022 |
9.98e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.99 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 821 QQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIaqmiedEQREKSVSHQTVQQLVLEKEQAL 900
Cdd:COG4942 49 EEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL------EAQKEELAELLRALYRLGRQPPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 901 ADLNSVEkSLADLFRRYEKMKEVLEGFRKNEEVLKRcAQEYLSRVKKEEQRyqalkvhAEEKLDRANAEIAQVRGKAQQE 980
Cdd:COG4942 123 ALLLSPE-DFLDAVRRLQYLKYLAPARREQAEELRA-DLAELAALRAELEA-------ERAELEALLAELEEERAALEAL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 11119414 981 QAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDELIAK 1022
Cdd:COG4942 194 KAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
839-1012 |
1.35e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 839 KEREVSEWKDKYEESRREVMEMRKIVAEYEktiaQMIEDEQREKSVSHQTVQQLVL---EKEQALADLNSVEKSLADLFR 915
Cdd:TIGR02168 223 RELELALLVLRLEELREELEELQEELKEAE----EELEELTAELQELEEKLEELRLevsELEEEIEELQKELYALANEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 916 RYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKaqqeqaahqasLRKEQLRV 995
Cdd:TIGR02168 299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE-----------LEELEAEL 367
|
170
....*....|....*..
gi 11119414 996 DALERTLEQKNKEIEEL 1012
Cdd:TIGR02168 368 EELESRLEELEEQLETL 384
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
813-1005 |
1.72e-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: 48.90 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 813 EKPAGLLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMiEDEQREKSVSHQTVQQL 892
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL-ESRLEELEEQLETLRSK 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 893 VLEKEQALADLNS----VEKSLADLFRRYEKMKEVLEGFRKN-EEVLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRAN 967
Cdd:TIGR02168 388 VAQLELQIASLNNeierLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
170 180 190
....*....|....*....|....*....|....*...
gi 11119414 968 AEIAQVRgkaqQEQAAHQASLRKEQLRVDALERTLEQK 1005
Cdd:TIGR02168 468 EELEEAE----QALDAAERELAQLQARLDSLERLQENL 501
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
833-1014 |
2.03e-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: 48.90 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 833 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQM---IEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKS 909
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLrkeLEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 910 LADLfrrYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLR 989
Cdd:TIGR02168 756 LTEL---EAEIEELEERLEEAEEELAEAEAE-IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831
|
170 180
....*....|....*....|....*...
gi 11119414 990 K---EQLRVDALERTLEQKNKEIEELTK 1014
Cdd:TIGR02168 832 RiaaTERRLEDLEEQIEELSEDIESLAA 859
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
832-1021 |
4.78e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.76 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 832 ARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIED-----EQREKSVSHQTVQQ---------LVLEKE 897
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQlerlrREREKAERYQALLKekreyegyeLLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 898 QALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKE-EQRYQALKvhaeEKLDRANAEIAQVRGK 976
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVK----EKIGELEAEIASLERS 309
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 11119414 977 AQQEQAAHQAS---LRKEQLRVDALERTLEQKNKEIEELTKICDELIA 1021
Cdd:TIGR02169 310 IAEKERELEDAeerLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTE 357
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
818-1011 |
6.16e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 47.37 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 818 LLFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQ-------REKSVSHQTVQ 890
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekiGELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 891 QLVLEKEQALADLnsvEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQALKVHAEE---KLDRAN 967
Cdd:TIGR02169 308 RSIAEKERELEDA---EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETR 384
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 11119414 968 AEIAQVRgKAQQEQAAHQASLRKEQLRVDALERTLEQKNKEIEE 1011
Cdd:TIGR02169 385 DELKDYR-EKLEKLKREINELKRELDRLQEELQRLSEELADLNA 427
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
773-1022 |
9.78e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 773 ARQIALASRSHQDAKREAAHPTDVSISKTALYSRigTAEVEKPAGLLFQQPDLDSALQIARAEIITKEREVSewkdKYEE 852
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAK--KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKK----KAEE 1568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 853 SRREvmEMRKIVAEYEKTIAQMIEdEQREKSVSHQTVQQLVLEKEQALADlnSVEKSLADLFRRYEKMKEVLEGFRKNEE 932
Cdd:PTZ00121 1569 AKKA--EEDKNMALRKAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAKKA--EEAKIKAEELKKAEEEKKKVEQLKKKEA 1643
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 933 VLKRCAQEylsrVKKEEQRYqalKVHAEEKLDRANAEiaqvRGKAQQEQAAHQASLRKEQlrvdALERTLEQKNKeIEEL 1012
Cdd:PTZ00121 1644 EEKKKAEE----LKKAEEEN---KIKAAEEAKKAEED----KKKAEEAKKAEEDEKKAAE----ALKKEAEEAKK-AEEL 1707
|
250
....*....|
gi 11119414 1013 TKICDELIAK 1022
Cdd:PTZ00121 1708 KKKEAEEKKK 1717
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
764-1014 |
9.78e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 9.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 764 IMRIEALKLARQIALASRSHQDAKREAAHPTDVSISKTALYSRIgtAEVEKpaglLFQQPDLDSALQIARAEiitKEREV 843
Cdd:PTZ00121 1551 LKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARI--EEVMK----LYEEEKKMKAEEAKKAE---EAKIK 1621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 844 SEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQA--LADLNSVEKSLADLFRRYEKMK 921
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEA 1701
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 922 EVLEGFRKNEEVLKRCAQEYlsRVKKEEQRYQALKVHAEEKLDRANAEIAQVR-------GKAQQEQAAHQASLRKEQLR 994
Cdd:PTZ00121 1702 KKAEELKKKEAEEKKKAEEL--KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDeeekkkiAHLKKEEEKKAEEIRKEKEA 1779
|
250 260
....*....|....*....|..
gi 11119414 995 V--DALERTLEQKNKEIEELTK 1014
Cdd:PTZ00121 1780 VieEELDEEDEKRRMEVDKKIK 1801
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
828-1012 |
1.18e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 828 ALQIARAEIITKEREVSEWKDKYEESRREVMEMRKI----------------VAEYEKTIAQmIEDEQREKSVSHQTVQQ 891
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALEAELDALQERrealqrlaeyswdeidVASAEREIAE-LEAELERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 892 LVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRcAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEIA 971
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD-RLEAAEDLARLELRALLEERFAAALGDAVERELR 768
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 11119414 972 QvrgkaqqeqaahqaSLRKeqlRVDALERTLEQKNKEIEEL 1012
Cdd:COG4913 769 E--------------NLEE---RIDALRARLNRAEEELERA 792
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
756-974 |
1.59e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 45.83 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 756 LQEELEFAIMRIEALKlaRQIALASRSHQDAKREAAHpTDVSISKT-----ALYSRIGTAEVEKPAgllfqqpdLDSALQ 830
Cdd:TIGR02169 292 VKEKIGELEAEIASLE--RSIAEKERELEDAEERLAK-LEAEIDKLlaeieELEREIEEERKRRDK--------LTEEYA 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 831 IARAEIITKEREVSEWKDKYEESRREVMEMRKivaEYEKTIAQMiEDEQREKSVSHQTVQQLVLEKEQALADLNSVEKSL 910
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREI-NELKRELDRLQEELQRLSEELADLNAAIAGIEAKI 436
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 11119414 911 ADLfrrYEKMKEVLEGFRKNEEVLKRCAQEylsrVKKEEQRYQALKvhaeEKLDRANAEIAQVR 974
Cdd:TIGR02169 437 NEL---EEEKEDKALEIKKQEWKLEQLAAD----LSKYEQELYDLK----EEYDRVEKELSKLQ 489
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
830-994 |
5.47e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 830 QIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQ-TVQQLVLEKEQALADLNSVEK 908
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 909 SLADLFRRYEKMKEVLEGFRKNEEVLKRCAQE--------------YLSRVKKEEQRYQALKVHAEEKLDRANAEIAQVR 974
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEEleelleqlslateeELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180
....*....|....*....|
gi 11119414 975 GKAQQEQAAHQASLRKEQLR 994
Cdd:COG4717 227 EELEQLENELEAAALEERLK 246
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
743-946 |
7.38e-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: 43.52 E-value: 7.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 743 DLAEKNPPLFAQKLQEELEFAIMRIEALKLARQIALASRSHQDAKREAAHPTDvsiSKTALYSRIGTAEvEKPAGLLFQQ 822
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE---ELQRLSEELADLN-AAIAGIEAKI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 823 PDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQM---IEDEQREKSVSHQTVQQLVLEKEQA 899
Cdd:TIGR02169 437 NELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLqreLAEAEAQARASEERVRGGRAVEEVL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 11119414 900 LADLNSVEKSLADLFR---RYEKMKEVLEGFR------KNEEVLKRCAqEYLSRVK 946
Cdd:TIGR02169 517 KASIQGVHGTVAQLGSvgeRYATAIEVAAGNRlnnvvvEDDAVAKEAI-ELLKRRK 571
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
811-1019 |
1.07e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.13 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 811 EVEKPAGLLFQQPdldSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQ 890
Cdd:PRK03918 311 EIEKRLSRLEEEI---NGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 891 QLVLEKEQALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLK----RCA-----------QEYLSRVKKEEQRYQAL 955
Cdd:PRK03918 388 KLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgKCPvcgrelteehrKELLEEYTAELKRIEKE 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 11119414 956 KVHAEEKLDRANAEIAQVRGKAQQEQAAHQASLRKEQLRvdALERTL--------EQKNKEIEELTKICDEL 1019
Cdd:PRK03918 468 LKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLK--ELEEKLkkynleelEKKAEEYEKLKEKLIKL 537
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
833-1019 |
1.20e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 42.74 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 833 RAEIITKEREVSEWKDKYEESRREVMEMRKIVAE------YEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALADLNSV 906
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKLRKELRELEKVLKKeselikLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKL 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 907 EKSLADLFRRYEKMKE-------VLEGFRKNEE----VLKRCAQEYLSRVKKEEQRYQALKVHAEEKLDRANAEiaqvrg 975
Cdd:PRK03918 538 KGEIKSLKKELEKLEElkkklaeLEKKLDELEEelaeLLKELEELGFESVEELEERLKELEPFYNEYLELKDAE------ 611
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 11119414 976 kaqQEQAAHQASLRKEQLRVDALERTLEQKNKEIEELTKICDEL 1019
Cdd:PRK03918 612 ---KELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEEL 652
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
205-538 |
1.34e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 205 TKKPRPPSLKKKQTTKKPTETPPVKETQQEPDEESLVPsgenlASETKTESAKTEGPSPAlleeTPLEPAVGPKAACPLD 284
Cdd:PHA03247 2680 PQRPRRRAARPTVGSLTSLADPPPPPPTPEPAPHALVS-----ATPLPPGPAAARQASPA----LPAAPAPPAVPAGPAT 2750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 285 SESAEGVVPPASGGGRVQNSPPVGRKTLP---LTTAPEAGEVTPSDSGGQEDSPAKGLSVRLEFDYSEDKSSWDNQQENP 361
Cdd:PHA03247 2751 PGGPARPARPPTTAGPPAPAPPAAPAAGPprrLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPP 2830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 362 PPTKKIGKKPVAKMPL-----------------RRPKMKKTPEKldntPASPPRSPAEPNDIPIAKgtytfdidkwddPN 424
Cdd:PHA03247 2831 PTSAQPTAPPPPPGPPppslplggsvapggdvrRRPPSRSPAAK----PAAPARPPVRRLARPAVS------------RS 2894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 425 FNPFSSTSKMQESPKLPQQSYNFDPDTCDESVDPFKTSSKTPSSPSKSPASFEIPASAMEANGVDGDGLNKPAKKKKTPL 504
Cdd:PHA03247 2895 TESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAV 2974
|
330 340 350
....*....|....*....|....*....|....
gi 11119414 505 KTdtFRVkkspkrsplsdPPSQDPTPAATPETPP 538
Cdd:PHA03247 2975 PR--FRV-----------PQPAPSREAPASSTPP 2995
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
829-970 |
3.86e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 829 LQIARAEIITKEREVSEWKDKYEESRREVMEMRKI--VAEYEKtiaqmIEDEQREKSVSHQTVQQlvlEKEQALADLNSV 906
Cdd:PRK03918 621 LKKLEEELDKAFEELAETEKRLEELRKELEELEKKysEEEYEE-----LREEYLELSRELAGLRA---ELEELEKRREEI 692
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 11119414 907 EKSLADLFRRYEKMKEVlegfRKNEEVLKRcAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEI 970
Cdd:PRK03918 693 KKTLEKLKEELEEREKA----KKELEKLEK-ALERVEELREKVKKYKALlKERALSKVGEIASEI 752
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
889-1013 |
5.27e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 889 VQQLVLEKEQALADLNsvekSLADLFRRYEKMKEVLEGFRKNEEVLKRC---AQEYLS-RVKKEEQRYQALKVH---AEE 961
Cdd:COG4913 213 VREYMLEEPDTFEAAD----ALVEHFDDLERAHEALEDAREQIELLEPIrelAERYAAaRERLAELEYLRAALRlwfAQR 288
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 11119414 962 KLDRANAEIAQVRGKaqqeqaahqasLRKEQLRVDALERTLEQKNKEIEELT 1013
Cdd:COG4913 289 RLELLEAELEELRAE-----------LARLEAELERLEARLDALREELDELE 329
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
766-1022 |
6.66e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 766 RIEALKLARQialASRSHQDAKR--------EAAHPTDVSISKTALYSRIGTAEVEKPAGLLFQQPDLDSALQIARAEII 837
Cdd:PTZ00121 1225 KAEAVKKAEE---AKKDAEEAKKaeeernneEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK 1301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 838 TKEREV---SEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALAD--LNSVEKSLAD 912
Cdd:PTZ00121 1302 KKADEAkkkAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAekKKEEAKKKAD 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 913 LFRRYEKMKEVLEGFRKNEEVLKRCAQEyLSRVKKEEQRYQALKVHAEE--KLDRANAEIAQVRgKAQQEQAAHQASLRK 990
Cdd:PTZ00121 1382 AAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEAK-KADEAKKKAEEAKKA 1459
|
250 260 270
....*....|....*....|....*....|..
gi 11119414 991 EQLRVDALERTLEQKNKEIEELTKICDELIAK 1022
Cdd:PTZ00121 1460 EEAKKKAEEAKKADEAKKKAEEAKKADEAKKK 1491
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
747-939 |
7.58e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.14 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 747 KNPPLFAQKLqEELEfaimriEALKLARQIALASRSHQDAKREA-AHPTDVSISKTALYSRIGTAEVEKPAGLLFQQpdl 825
Cdd:COG4717 64 RKPELNLKEL-KELE------EELKEAEEKEEEYAELQEELEELeEELEELEAELEELREELEKLEKLLQLLPLYQE--- 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 826 dsaLQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALADLNS 905
Cdd:COG4717 134 ---LEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190
....*....|....*....|....*....|....
gi 11119414 906 VEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQ 939
Cdd:COG4717 211 LEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
825-1019 |
8.47e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 8.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 825 LDSALQIARAEIitkeREVSEW-KDKYEESRREVMEMRKIVAEYEKtiAQMIEDEQREKSVSHQTVQQLVLEKEQALADL 903
Cdd:COG3206 162 LEQNLELRREEA----RKALEFlEEQLPELRKELEEAEAALEEFRQ--KNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 904 NSVEKSLADLFRRYEKMKEVLEGFRKNEEVlkrcaQEYLSRVKKEEQRYQALKVHAEEK---LDRANAEIAQVRGKAQQE 980
Cdd:COG3206 236 AEAEARLAALRAQLGSGPDALPELLQSPVI-----QQLRAQLAELEAELAELSARYTPNhpdVIALRAQIAALRAQLQQE 310
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 11119414 981 QAAHQASLRKE----QLRVDALERTLEQKNKEIEELTKICDEL 1019
Cdd:COG3206 311 AQRILASLEAElealQAREASLQAQLAQLEARLAELPELEAEL 353
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
836-1021 |
9.33e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 836 IITKEREVSEWKDKYE-----ESRREVMEMRKIVA---EYEKTIAQMIEDEQREKSVSHQTVQQLVLEKEQALAD--LNS 905
Cdd:PRK03918 488 VLKKESELIKLKELAEqlkelEEKLKKYNLEELEKkaeEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEkkLDE 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 906 VEKSLADLFRRYEKmkevlEGFRKNEEV------LKRCAQEYL------SRVKKEEQRYQALK---VHAEEKLDRANAEI 970
Cdd:PRK03918 568 LEEELAELLKELEE-----LGFESVEELeerlkeLEPFYNEYLelkdaeKELEREEKELKKLEeelDKAFEELAETEKRL 642
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 11119414 971 AQVRGK----AQQEQAAHQASLRKEQLRvdaLERTLEQKNKEIEELTKICDELIA 1021
Cdd:PRK03918 643 EELRKEleelEKKYSEEEYEELREEYLE---LSRELAGLRAELEELEKRREEIKK 694
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
819-974 |
9.54e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 9.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 11119414 819 LFQQPDLDSALQIARAEIITKEREVSEWKDKYEESRREVMEMRKIVAEyektIAQMIEDEQREKSVSHQTVQQLVLEKEQ 898
Cdd:COG4372 37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEE----LNEQLQAAQAELAQAQEELESLQEEAEE 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 11119414 899 ALADLNSVEKSLADLFRRYEKMKEVLEGFRKNEEVLKRCAQEYLSRVKKEEQRYQAL-KVHAEEKLDRANAEIAQVR 974
Cdd:COG4372 113 LQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALeQELQALSEAEAEQALDELL 189
|
|
| |
