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Conserved domains on  [gi|331999954|ref|NP_002263|]
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keratin, type II cytoskeletal 4 [Homo sapiens]

Protein Classification

type II keratin (domain architecture ID 12177255)

type II keratin is an intermediate filament-forming protein that provides mechanical support and fulfills a variety of additional functions in epithelial cells

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
136-449 2.34e-150

Intermediate filament protein;


:

Pssm-ID: 365827 [Multi-domain]  Cd Length: 313  Bit Score: 432.42  E-value: 2.34e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  136 EEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSkNLEPLFETYLSVLRKQLDTLGNDKGRLQSELKT 215
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGAEPS-RLYSLYEREIRDLRRQLDQLTVERARLQLEIDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  216 MQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDTSVVLS 295
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRQSAEADLVGLRKDLDEATLARVDLEMKVESLQEELAFLKKNHEEEVRELQSQVQDTQVNVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  296 MDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQ 375
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 331999954  376 CQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEGEEYR 449
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQDLISELEAELQQIRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
14-133 2.25e-34

Keratin type II head;


:

Pssm-ID: 406589  Cd Length: 160  Bit Score: 127.08  E-value: 2.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   14 GFSCGSAIVGGGKRGAFSSVSMSG----------GAGRCSSGGFGSRSLYNLRGNKSISMSVA--GSRQGACFGGAGGFG 81
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSCSRsggggggggyGAGGGHGGGFGSRSLYNLGGSKSISISVAggGSRPGGFGFGGGGGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   82 TGGFGGGFGGSFSGKGGPGF----------------------------PVCPAGGIQEVTINQSLLTPLHVEIDPEIQKV 133
Cdd:pfam16208  81 GFGFGFGGGGGGGFGGGGGFggggfgggggfggggfggggfggggfggPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 160
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
136-449 2.34e-150

Intermediate filament protein;


Pssm-ID: 365827 [Multi-domain]  Cd Length: 313  Bit Score: 432.42  E-value: 2.34e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  136 EEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSkNLEPLFETYLSVLRKQLDTLGNDKGRLQSELKT 215
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGAEPS-RLYSLYEREIRDLRRQLDQLTVERARLQLEIDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  216 MQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDTSVVLS 295
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRQSAEADLVGLRKDLDEATLARVDLEMKVESLQEELAFLKKNHEEEVRELQSQVQDTQVNVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  296 MDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQ 375
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 331999954  376 CQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEGEEYR 449
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQDLISELEAELQQIRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
14-133 2.25e-34

Keratin type II head;


Pssm-ID: 406589  Cd Length: 160  Bit Score: 127.08  E-value: 2.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   14 GFSCGSAIVGGGKRGAFSSVSMSG----------GAGRCSSGGFGSRSLYNLRGNKSISMSVA--GSRQGACFGGAGGFG 81
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSCSRsggggggggyGAGGGHGGGFGSRSLYNLGGSKSISISVAggGSRPGGFGFGGGGGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   82 TGGFGGGFGGSFSGKGGPGF----------------------------PVCPAGGIQEVTINQSLLTPLHVEIDPEIQKV 133
Cdd:pfam16208  81 GFGFGFGGGGGGGFGGGGGFggggfgggggfggggfggggfggggfggPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 160
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
179-450 2.36e-12

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 69.74  E-value: 2.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  179 TSSKNLEPLFETYLSVLRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVEL 258
Cdd:COG1196   656 SRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQL 735
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  259 EAKVDSLndeinflkvlyDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEAL--YQTKVQQ 336
Cdd:COG1196   736 QSRLEEL-----------EEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELeeLEEELEE 804
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  337 LQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGENA---LKDAHSKRVELEAALQQAKE 413
Cdd:COG1196   805 AERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELkeeLEELEAEKEELEDELKELEE 884
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 331999954  414 ELARMLREYQELMSVKLALDIEIATYRKLLEGEEYRM 450
Cdd:COG1196   885 EKEELEEELRELESELAELKEEIEKLRERLEELEAKL 921
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
165-425 2.65e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 2.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   165 LETKWNLLQQQT-TTTSSKNL-EPLFETYLSVLRKQLDTLGNDKGRLQSELKTMQDSVEDfktkYEEEINKRTAAENDFV 242
Cdd:TIGR02168  198 LERQLKSLERQAeKAERYKELkAELRELELALLVLRLEELREELEELQEELKEAEEELEE----LTAELQELEEKLEELR 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   243 VLKKDVDAAYlnkVELEAKVDSLNDEINFL---KVLYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIA 319
Cdd:TIGR02168  274 LEVSELEEEI---EELQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   320 QRSKAEAEAL--YQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRG------- 390
Cdd:TIGR02168  351 EELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkkl 430
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 331999954   391 -ENALKDAHSKRVELEAALQQAKEELARMLREYQEL 425
Cdd:TIGR02168  431 eEAELKELQAELEELEEELEELQEELERLEEALEEL 466
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
211-415 1.01e-07

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 54.53  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 211 SELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAylnkvelEAKVDSLNDEINFLKvlydAELSQMQTHVSDT 290
Cdd:NF033930 157 EELAETKKKAEEAKAEEPVAKKKVDEAKKKVEEAKKKVEAE-------EAEIEKLQNEEVALE----AKIAELENQVDNL 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 291 SVVLSmDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAeALYQTKVQQLQISVDQHG--DNLKNTKSEIAELNRMIQRLRAE 368
Cdd:NF033930 226 EKELA-EIDESDSEDYIKEGLRAPLESELDAKQAKL-AKKQTELEKLLDSLDPEGktQDELDKEAAEEELSKKIDELDNE 303
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 331999954 369 IENIKKQCQTLQVSVAD-AEQRGENALKDAHSKRVELE---AALQQAKEEL 415
Cdd:NF033930 304 VAKLEKEVSDLENSDNNvADYYKEALEKDLATKKAELEktqKDLDKALNEL 354
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
191-402 4.99e-06

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 49.16  E-value: 4.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 191 YLSVLRKQLDTLGndkgRLQSELKTMQDSVEDFKTKYEEEINKRtaAENDFVVLKKDVDAaYLNKV-ELEAKVDSLNDEI 269
Cdd:PRK05771  51 LLTKLSEALDKLR----SYLPKLNPLREEKKKVSVKSLEELIKD--VEEELEKIEKEIKE-LEEEIsELENEIKELEQEI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 270 NFLKVL--YDAELSQMQTHvSDTSVVLSMDNNRNLDLDSIIAEVRAQYEE----------IAQRSKAEAEALYQTK---V 334
Cdd:PRK05771 124 ERLEPWgnFDLDLSLLLGF-KYVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvyvvVVVLKELSDEVEEELKklgF 202
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 331999954 335 QQLQISVDQH-GDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADA----EQRGENALKDAHSKRV 402
Cdd:PRK05771 203 ERLELEEEGTpSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYleieLERAEALSKFLKTDKT 275
Streccoc_I_II NF033804
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ...
204-432 4.14e-04

antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.


Pssm-ID: 411384 [Multi-domain]  Cd Length: 1552  Bit Score: 43.39  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  204 NDKGRLQSELKTMQDSVEDFKTKYEEEINKRTA------AENDFV-----VLKKDVDAA---YLNKVELEAKVDSLNDEI 269
Cdd:NF033804  227 NKLSAYQTELARVQKANAEAKEAYDKAVKENTAknaalqAENEAIkqrneTAKANYEAAmkqYEADLAAIKKAKEDNDAD 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  270 NFLK-VLYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAevrAQYEEIAQRSkAEAEALYQTKVQQLQI---SVDQ-H 344
Cdd:NF033804  307 YQAKlAAYQTELARVQKANADAKAAYEKAVEENTAKNTAIQ---AENEAIKQRN-AAAKATYEAALKQYEAdlaAVKKaN 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  345 GDNLKNTKSEIAELNRMIQRLRAE-----------IENIKKQCQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKE 413
Cdd:NF033804  383 AANEADYQAKLAAYQTELARVQKAnadakaayekaVEDNKAKNAALQAENEAIKQRNAAAKADYEAKLAKYQADLAKYKK 462
                         250       260
                  ....*....|....*....|...
gi 331999954  414 ELA---RMLREYQ-ELMSVKLAL 432
Cdd:NF033804  463 DLAeypAKLKAYEdEQAKIKAAL 485
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
136-449 2.34e-150

Intermediate filament protein;


Pssm-ID: 365827 [Multi-domain]  Cd Length: 313  Bit Score: 432.42  E-value: 2.34e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  136 EEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSkNLEPLFETYLSVLRKQLDTLGNDKGRLQSELKT 215
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKDLETKISELRQKKGAEPS-RLYSLYEREIRDLRRQLDQLTVERARLQLEIDN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  216 MQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDTSVVLS 295
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRQSAEADLVGLRKDLDEATLARVDLEMKVESLQEELAFLKKNHEEEVRELQSQVQDTQVNVE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  296 MDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQ 375
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRQIQSLEIELQSLKKQ 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 331999954  376 CQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEGEEYR 449
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQDLISELEAELQQIRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
14-133 2.25e-34

Keratin type II head;


Pssm-ID: 406589  Cd Length: 160  Bit Score: 127.08  E-value: 2.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   14 GFSCGSAIVGGGKRGAFSSVSMSG----------GAGRCSSGGFGSRSLYNLRGNKSISMSVA--GSRQGACFGGAGGFG 81
Cdd:pfam16208   1 GFSSCSAVVPSRSRRSYSSVSCSRsggggggggyGAGGGHGGGFGSRSLYNLGGSKSISISVAggGSRPGGFGFGGGGGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   82 TGGFGGGFGGSFSGKGGPGF----------------------------PVCPAGGIQEVTINQSLLTPLHVEIDPEIQKV 133
Cdd:pfam16208  81 GFGFGFGGGGGGGFGGGGGFggggfgggggfggggfggggfggggfggPPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 160
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
179-450 2.36e-12

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 69.74  E-value: 2.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  179 TSSKNLEPLFETYLSVLRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVEL 258
Cdd:COG1196   656 SRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRRQLEELERQLEELKRELAALEEELEQL 735
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  259 EAKVDSLndeinflkvlyDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEAL--YQTKVQQ 336
Cdd:COG1196   736 QSRLEEL-----------EEELEELEEELEELQERLEELEEELESLEEALAKLKEEIEELEEKRQALQEELeeLEEELEE 804
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  337 LQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGENA---LKDAHSKRVELEAALQQAKE 413
Cdd:COG1196   805 AERRLDALERELESLEQRRERLEQEIEELEEEIEELEEKLDELEEELEELEKELEELkeeLEELEAEKEELEDELKELEE 884
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 331999954  414 ELARMLREYQELMSVKLALDIEIATYRKLLEGEEYRM 450
Cdd:COG1196   885 EKEELEEELRELESELAELKEEIEKLRERLEELEAKL 921
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
165-425 2.65e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 2.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   165 LETKWNLLQQQT-TTTSSKNL-EPLFETYLSVLRKQLDTLGNDKGRLQSELKTMQDSVEDfktkYEEEINKRTAAENDFV 242
Cdd:TIGR02168  198 LERQLKSLERQAeKAERYKELkAELRELELALLVLRLEELREELEELQEELKEAEEELEE----LTAELQELEEKLEELR 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   243 VLKKDVDAAYlnkVELEAKVDSLNDEINFL---KVLYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIA 319
Cdd:TIGR02168  274 LEVSELEEEI---EELQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELK 350
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   320 QRSKAEAEAL--YQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRG------- 390
Cdd:TIGR02168  351 EELESLEAELeeLEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIeellkkl 430
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 331999954   391 -ENALKDAHSKRVELEAALQQAKEELARMLREYQEL 425
Cdd:TIGR02168  431 eEAELKELQAELEELEEELEELQEELERLEEALEEL 466
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
195-447 1.17e-08

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.80  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  195 LRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKv 274
Cdd:COG1196   237 LRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELE- 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  275 lydAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEV------------------RAQYEEIAQRSKAEAEALYQTKVQQ 336
Cdd:COG1196   316 ---NELEELEERLEELKEKIEALKEELEERETLLEELeqllaeleeakeeleeklSALLEELEELFEALREELAELEAEL 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  337 LQIS--VDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRG---ENALKDAHSKRVELEAALQQA 411
Cdd:COG1196   393 AEIRneLEELKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELeelEEQLEELRDRLKELERELAEL 472
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 331999954  412 KEELARMLREYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:COG1196   473 QEELQRLEKELSSLEARLDRLEAEQRASQGVRAVLE 508
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
133-425 6.13e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.45  E-value: 6.13e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   133 VRTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTssKNLEPLFETYLSVLRKQLDTLGNDKGRLQSE 212
Cdd:TIGR02168  671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL--RKELEELSRQISALRKDLARLEAEVEQLEER 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   213 LKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKdvdaaylNKVELEAKVDSLNDEINFLKvlydAELSQMQTHVSDTSV 292
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEA-------EIEELEAQIEQLKEELKALR----EALDELRAELTLLNE 817
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   293 VLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEalyqtkvqqlqisvdqhgdNLKNTKSEIAELNRMIQRLRAEIENI 372
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSE-------------------DIESLAAEIEELEELIEELESELEAL 878
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 331999954   373 KKQCQTLQVSVADAEQRGENA---LKDAHSKRVELEAALQQAKEELARMLREYQEL 425
Cdd:TIGR02168  879 LNERASLEEALALLRSELEELseeLRELESKRSELRRELEELREKLAQLELRLEGL 934
pneumo_PspA NF033930
pneumococcal surface protein A; The pneumococcal surface protein proteins, found in ...
211-415 1.01e-07

pneumococcal surface protein A; The pneumococcal surface protein proteins, found in Streptococcus pneumoniae, are repetitive, with patterns of localized high sequence identity across pairs of proteins given different specific names that recombination may be presumed. This protein, PspA, has an N-terminal region that lacks a cross-wall-targeting YSIRK type extended signal peptide, in contrast to the closely related choline-binding protein CbpA which has a similar C-terminus but a YSIRK-containing region at the N-terminus.


Pssm-ID: 411490 [Multi-domain]  Cd Length: 660  Bit Score: 54.53  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 211 SELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAylnkvelEAKVDSLNDEINFLKvlydAELSQMQTHVSDT 290
Cdd:NF033930 157 EELAETKKKAEEAKAEEPVAKKKVDEAKKKVEEAKKKVEAE-------EAEIEKLQNEEVALE----AKIAELENQVDNL 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 291 SVVLSmDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAeALYQTKVQQLQISVDQHG--DNLKNTKSEIAELNRMIQRLRAE 368
Cdd:NF033930 226 EKELA-EIDESDSEDYIKEGLRAPLESELDAKQAKL-AKKQTELEKLLDSLDPEGktQDELDKEAAEEELSKKIDELDNE 303
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 331999954 369 IENIKKQCQTLQVSVAD-AEQRGENALKDAHSKRVELE---AALQQAKEEL 415
Cdd:NF033930 304 VAKLEKEVSDLENSDNNvADYYKEALEKDLATKKAELEktqKDLDKALNEL 354
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
131-425 1.71e-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: 54.29  E-value: 1.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   131 QKVRTEERE-QIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSKnleplfetyLSVLRKQLDTLGNDKGRL 209
Cdd:TIGR02168  216 KELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK---------LEELRLEVSELEEEIEEL 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   210 QSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQMqthvsd 289
Cdd:TIGR02168  287 QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL------ 360
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   290 tsvvlsmdnnrnldldsiiAEVRAQYEEIAQRSKAEAEAL--YQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRA 367
Cdd:TIGR02168  361 -------------------EELEAELEELESRLEELEEQLetLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQ 421
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 331999954   368 EIENIKKQCQTLQVSVADAEQRGENA-LKDAHSKRVELEAALQQAKEELARMLREYQEL 425
Cdd:TIGR02168  422 EIEELLKKLEEAELKELQAELEELEEeLEELQEELERLEEALEELREELEEAEQALDAA 480
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
304-459 1.55e-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: 1.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   304 LDSIIAEVRAQYEEIAQRSKAEAEALYQTK--VQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQV 381
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRleVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   382 SVADAEQRGENALKDAHSKRV---ELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRK---LLEGEEYRMSGECQ 455
Cdd:TIGR02168  324 QLEELESKLDELAEELAELEEkleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkvaQLELQIASLNNEIE 403

                   ....
gi 331999954   456 SAVS 459
Cdd:TIGR02168  404 RLEA 407
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
208-444 2.23e-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: 50.44  E-value: 2.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   208 RLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINflkvlydaELSQMQTHV 287
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE--------QLEERIAQL 752
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   288 SDTsvvlsmdnnrNLDLDSIIAEVRAQYEEiAQRSKAEAEAlyqtKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRA 367
Cdd:TIGR02168  753 SKE----------LTELEAEIEELEERLEE-AEEELAEAEA----EIEELEAQIEQLKEELKALREALDELRAELTLLNE 817
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   368 EIENIKKQCQTLQVSVADAEQRGENA---LKDAHSKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLE 444
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
129-375 2.91e-06

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 50.02  E-value: 2.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  129 EIQKVRTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKwnlLQQQTTTTSSKNLE-PLFETYLSVLRKQLDTLGNDKG 207
Cdd:TIGR04523 360 EKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESK---IQNQEKLNQQKDEQiKKLQQEKELLEKEIERLKETII 436
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  208 RLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLK---------------------KDVDAAYLNKVELEAKVDSLN 266
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSrsinkikqnleqkqkelkskeKELKKLNEEKKELEEKVKDLT 516
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  267 DEINFLKVLYD---AELSQMQTHVSD-TSVVLSMDNNrnLDLDSIIAEVRAQYEEIAQrSKAEAEALyQTKVQQLQISVD 342
Cdd:TIGR04523 517 KKISSLKEKIEkleSEKKEKESKISDlEDELNKDDFE--LKKENLEKEIDEKNKEIEE-LKQTQKSL-KKKQEEKQELID 592
                         250       260       270
                  ....*....|....*....|....*....|...
gi 331999954  343 QHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQ 375
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKE 625
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
135-410 3.96e-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: 49.66  E-value: 3.96e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   135 TEEREQIKLLNNKFASFIDKVQFLEQQN-----KVLETKWNLL-------QQQTTTTSSKNLEPLFETYLSVlRKQLDTL 202
Cdd:TIGR01612  692 TEDKAKLDDLKSKIDKEYDKIQNMETATvelhlSNIENKKNELldiiveiKKHIHGEINKDLNKILEDFKNK-EKELSNK 770
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   203 GNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDfvvLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQ 282
Cdd:TIGR01612  771 INDYAKEKDELNKYKSKISEIKNHYNDQINIDNIKDED---AKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNK 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   283 MQTHVsdtsvvlSMDNNRNLDLDSiiaeVRAQYEEIAQRSKAEaealyqtkvqqlqISVDQHGD---NLKNTKSEIAELN 359
Cdd:TIGR01612  848 VDKFI-------NFENNCKEKIDS----EHEQFAELTNKIKAE-------------ISDDKLNDyekKFNDSKSLINEIN 903
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 331999954   360 RMIQRLRAEIENIKKQCQTLQVSVADAEqrgenALKDAHSKRVELEAALQQ 410
Cdd:TIGR01612  904 KSIEEEYQNINTLKKVDEYIKICENTKE-----SIEKFHNKQNILKEILNK 949
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
191-402 4.99e-06

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 49.16  E-value: 4.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 191 YLSVLRKQLDTLGndkgRLQSELKTMQDSVEDFKTKYEEEINKRtaAENDFVVLKKDVDAaYLNKV-ELEAKVDSLNDEI 269
Cdd:PRK05771  51 LLTKLSEALDKLR----SYLPKLNPLREEKKKVSVKSLEELIKD--VEEELEKIEKEIKE-LEEEIsELENEIKELEQEI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 270 NFLKVL--YDAELSQMQTHvSDTSVVLSMDNNRNLDLDSIIAEVRAQYEE----------IAQRSKAEAEALYQTK---V 334
Cdd:PRK05771 124 ERLEPWgnFDLDLSLLLGF-KYVSVFVGTVPEDKLEELKLESDVENVEYIstdkgyvyvvVVVLKELSDEVEEELKklgF 202
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 331999954 335 QQLQISVDQH-GDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADA----EQRGENALKDAHSKRV 402
Cdd:PRK05771 203 ERLELEEEGTpSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALYEYleieLERAEALSKFLKTDKT 275
PRK01156 PRK01156
chromosome segregation protein; Provisional
125-447 1.28e-05

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 47.97  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 125 EIDPE-IQKVRTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQT------TTTSSKNLEPLFETYlsvlrk 197
Cdd:PRK01156 401 EIDPDaIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSvcpvcgTTLGEEKSNHIINHY------ 474
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 198 qldtlGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAEndfvvlKKDVDA--AYLNKVE-LEAKVDSLNDEINFLK- 273
Cdd:PRK01156 475 -----NEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLE------SEEINKsiNEYNKIEsARADLEDIKIKINELKd 543
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 274 --VLYDAELSQMQT-HVSDTSVVLSMDNNRNLDLDSI-IAEVRAQYEEIAQRSKAEAEALYQTKVQQLQIS--------- 340
Cdd:PRK01156 544 khDKYEEIKNRYKSlKLEDLDSKRTSWLNALAVISLIdIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKsyidksire 623
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 341 VDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQvSVADAEQRGENALKDAHSKRVELEAALQQAKEELARMLR 420
Cdd:PRK01156 624 IENEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEID-SIIPDLKEITSRINDIEDNLKKSRKALDDAKANRARLES 702
                        330       340
                 ....*....|....*....|....*..
gi 331999954 421 EYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:PRK01156 703 TIEILRTRINELSDRINDINETLESMK 729
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
129-413 2.53e-05

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 47.02  E-value: 2.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  129 EIQKVRTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSKnLEPLFETyLSVLRKQLDTLGNDKGR 208
Cdd:COG1196   243 ELEEELSRLEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELKEE-IEELEGE-ISLLRERLEELENELEE 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  209 LQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVD----AAYLNKVELEAKVDSLN---DEINFLKVLYDAELS 281
Cdd:COG1196   321 LEERLEELKEKIEALKEELEERETLLEELEQLLAELEEAKEeleeKLSALLEELEELFEALReelAELEAELAEIRNELE 400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  282 QMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRA-------QYEEIAQRSKAEAEALyqtkvQQLQISVDQHGDNLKNTKSE 354
Cdd:COG1196   401 ELKREIESLEERLERLSERLEDLKEELKELEAeleelqtELEELNEELEELEEQL-----EELRDRLKELERELAELQEE 475
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 331999954  355 IAELNRMIQRLRAEIENIKKQCQTLQV--SVADAEQRGENALKDAHSKRVELEAALQQAKE 413
Cdd:COG1196   476 LQRLEKELSSLEARLDRLEAEQRASQGvrAVLEALESGLPGVYGPVAELIKVKEKYETALE 536
PRK09039 PRK09039
peptidoglycan -binding protein;
277-417 4.58e-05

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 45.34  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 277 DAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEiAQRSKAEAEALY---QTKVQQLQISVDQHGDNLKNTKS 353
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLaelAGAGAAAEGRAGELAQELDSEKQ 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 331999954 354 EIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKEELAR 417
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLGRRLNVALAQRVQELNR 194
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
125-447 4.75e-05

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 46.29  E-value: 4.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 125 EIDPEIQKVRTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSKNLEplFETYLSVLRKQLDTLGN 204
Cdd:COG0419  347 ELAEEKNELAKLLEERLKELEERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEE--IQEELEELEKELEELER 424
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 205 DKGRLQSELKTMQDSVEDFKtKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQ-M 283
Cdd:COG0419  425 ELEELEEEIKKLEEQINQLE-SKELMIAELAGAGEKCPVCGQELPEEHEKELLELYELELEELEEELSREKEEAELREeI 503
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 284 QTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRM-- 361
Cdd:COG0419  504 EELEKELRELEEELIELLELEEALKEELEEKLEKLENLLEELEELKEKLQLQQLKEELRQLEDRLQELKELLEELRLLrt 583
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 362 --------------IQRLRAEIENIKKQCQTL--QVSVADAEQRGENALKDAHSKR------VELEAALQQAKEELARML 419
Cdd:COG0419  584 rkeeleelrerlkeLKKKLKELEERLSQLEELlqSLELSEAENELEEAEEELESELeklnlqAELEELLQAALEELEEKV 663
                        330       340
                 ....*....|....*....|....*...
gi 331999954 420 REYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:COG0419  664 EELEAEIRRELQRIENEEQLEEKLEELE 691
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
129-374 6.22e-05

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 45.86  E-value: 6.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  129 EIQKVRTEEREQIKLLNNKFASFIDKVQFLEQQNKvlETKWNLLQQQTTTTSSKNLEPLFETYLSVLRKQLDTLGNDKGR 208
Cdd:COG1196   748 ELEEELEELQERLEELEEELESLEEALAKLKEEIE--ELEEKRQALQEELEELEEELEEAERRLDALERELESLEQRRER 825
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  209 LQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYD---AELSQMQT 285
Cdd:COG1196   826 LEQEIEELEEEIEELEEKLDELEEELEELEKELEELKEELEELEAEKEELEDELKELEEEKEELEEELReleSELAELKE 905
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  286 HVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIaqrSKAEAEALYQTKVQQLQISVDQHG-------DNLKNTKSEIAEL 358
Cdd:COG1196   906 EIEKLRERLEELEAKLERLEVELPELEEELEEE---YEDTLETELEREIERLEEEIEALGpvnlraiEEYEEVEERYEEL 982
                         250
                  ....*....|....*.
gi 331999954  359 NRMIQRLRAEIENIKK 374
Cdd:COG1196   983 KSQREDLEEAKEKLLE 998
Spc7 pfam08317
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
304-388 1.50e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 400559 [Multi-domain]  Cd Length: 311  Bit Score: 43.76  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  304 LDSIIAEVRAQYEEIA------QRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQ 377
Cdd:pfam08317 166 LDELLPELVEEYAELEeelellQEAAEELENCDKDELEELREELAEQDAEIEEKKRELAELQEQLEELEEKIEELKEQKQ 245
                          90
                  ....*....|.
gi 331999954  378 TLQVSVADAEQ 388
Cdd:pfam08317 246 ELLEEIAEAER 256
COG1579 COG1579
Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function ...
260-429 1.62e-04

Predicted nucleic acid-binding protein, contains Zn-ribbon domain [General function prediction only];


Pssm-ID: 224495 [Multi-domain]  Cd Length: 239  Bit Score: 43.12  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 260 AKVDSLNDEINFLKVLYDAELSQMQTHVSDTSVVLSmdnNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKV----- 334
Cdd:COG1579   13 QKLDLEKDRLEPRIKEIRKALKKAKAELEALNKALE---ALEIELEDLENQVSQLESEIQEIRERIKRAEEKLSAvkder 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 335 --QQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAK 412
Cdd:COG1579   90 elRALNIEIQIAKERINSLEDELAELMEEIEKLEKEIEDLKERLERLEKNLAEAEARLEEEVAEIREEGQELSSKREELK 169
                        170
                 ....*....|....*...
gi 331999954 413 EEL-ARMLREYQELMSVK 429
Cdd:COG1579  170 EKLdPELLSEYERIRKNK 187
46 PHA02562
endonuclease subunit; Provisional
153-385 1.98e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 43.85  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 153 DKVQFLEQQNKVLETKWNLLQQQTTTtssknleplFETYLSVLRKQLDtlgNDKGRLQSELKTMQDSVEDFKTkyeeEIN 232
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQIKT---------YNKNIEEQRKKNG---ENIARKQNKYDELVEEAKTIKA----EIE 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 233 KRTAAENDFVVLKKDVDAAyLNK-----VELEAKVDSLNDEINFLKvlydaELSQMQTHVSDTSvvlsmdnnrnlDLDSI 307
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAA-LNKlntaaAKIKSKIEQFQKVIKMYE-----KGGVCPTCTQQIS-----------EGPDR 300
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 331999954 308 IAEVRAQYEEIAQRSKAEAEAlyQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVAD 385
Cdd:PHA02562 301 ITKIKDKLKELQHSLEKLDTA--IDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVD 376
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
136-458 2.00e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 318193 [Multi-domain]  Cd Length: 1112  Bit Score: 44.34  E-value: 2.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   136 EEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSKNLEPL-FETYLSVLRKQLDTLGNDKGRLQSELK 214
Cdd:pfam15921  507 EKERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAeKDKVIEILRQQIENMTQLVGQHGRTAG 586
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   215 TMQdsVEdfKTKYEEEINKRTAAENDFVVLKKDVDAAYLnkvELEAKVDSLNDEINFLKVLYDAELSQMQTHVSDTSVVL 294
Cdd:pfam15921  587 AMQ--VE--KAQLEKEINDRRLELQEFKILKDKKDAKIR---ELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLL 659
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   295 SMDNNRNLDLDSIIAEvraqYEEIAQRSKAEAEALYQT------KVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAE 368
Cdd:pfam15921  660 NEVKTSRNELNSLSED----YEVLKRNFRNKSEEMETTtnklkmQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQ 735
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   369 IENIKKQCQTLQVSVADAEQRGENALKDAH---SKRVELEAALQQAKEELARMLREYQELMSVKLALDIEIATYRKLLEG 445
Cdd:pfam15921  736 ITAKRGQIDALQSKIQFLEEAMTNANKEKHflkEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDK 815
                          330
                   ....*....|...
gi 331999954   446 EEYRMSgECQSAV 458
Cdd:pfam15921  816 ASLQFA-ECQDII 827
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
195-450 2.12e-04

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.93  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  195 LRKQLDTLGNDK------GRLQSELKTMQDSVedFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDE 268
Cdd:COG1196   198 LEKQLEKLERQAekaeryQELKAELRELELAL--LLAKLKELRKELEELEEELSRLEEELEELQEELEEAEKEIEELKSE 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  269 INflkvLYDAELSQMQThvsdtsvvlsmdnnRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDqhgdnL 348
Cdd:COG1196   276 LE----ELREELEELQE--------------ELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEK-----I 332
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  349 KNTKSEIAELNRMIQRLRAEIENIKKQCQTLQvsvadaeqrgenalKDAHSKRVELEAALQQAKEELARMLREYQELMSV 428
Cdd:COG1196   333 EALKEELEERETLLEELEQLLAELEEAKEELE--------------EKLSALLEELEELFEALREELAELEAELAEIRNE 398
                         250       260
                  ....*....|....*....|..
gi 331999954  429 KLALDIEIATYRKLLEGEEYRM 450
Cdd:COG1196   399 LEELKREIESLEERLERLSERL 420
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
195-434 2.26e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 44.01  E-value: 2.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   195 LRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKv 274
Cdd:pfam01576  501 LQEQLEEEEEAKRNVERQLSTLQAQLSEMKKKLEEDAGAVEALEEAKKRLQRELEALTQRLEEKAAAYDKLEKTKNRLQ- 579
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   275 lydAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAE---VRAQYEEiaQRSKAEAEAL-YQTKVqqlqISVDQHGDNLKN 350
Cdd:pfam01576  580 ---QELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEekaISARYAE--ERDRAEAEAReKETRA----LSLSRALEEALE 650
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   351 TKSEIAELNRMiqrLRAEIENIkkqcqtlqVSVADAEqrGENALKDAHSKRVeLEAALQQAKEELARMLREYQELMSVKL 430
Cdd:pfam01576  651 AKEELERQNKQ---LRAEMEDL--------VSSKDDV--GKNVHELERSKRA-LEQQVEEMKTQLEELEDELQATEDAKL 716

                   ....
gi 331999954   431 ALDI 434
Cdd:pfam01576  717 RLEV 720
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
188-447 3.24e-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: 3.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   188 FETYLSVLRKQLDTLGNDKGRLQsELKTMQDSVEDFKtkYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLND 267
Cdd:TIGR02169  189 LDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYE--GYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEK 265
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   268 EINFLKVLydaeLSQMQTHVSDtsvvlsMDNNRNLDLDSIIAEVRAqyeEIAQRSKAEAEalYQTKVQQLQisvdqhgDN 347
Cdd:TIGR02169  266 RLEEIEQL----LEELNKKIKD------LGEEEQLRVKEKIGELEA---EIASLERSIAE--KERELEDAE-------ER 323
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   348 LKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGE-------------NALKDAHSKRVEleaALQQAKEE 414
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEdlraeleevdkefAETRDELKDYRE---KLEKLKRE 400
                          250       260       270
                   ....*....|....*....|....*....|...
gi 331999954   415 LARMLREYQELMSVKLALDIEIATYRKLLEGEE 447
Cdd:TIGR02169  401 INELKRELDRLQEELQRLSEELADLNAAIAGIE 433
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
125-373 3.93e-04

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 43.16  E-value: 3.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  125 EIDPEIQKVRTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSKnLEPLfETYLSVLRKQLDTLGN 204
Cdd:COG1196   786 EKRQALQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEK-LDEL-EEELEELEKELEELKE 863
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  205 DKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQMQ 284
Cdd:COG1196   864 ELEELEAEKEELEDELKELEEEKEELEEELRELESELAELKEEIEKLRERLEELEAKLERLEVELPELEEELEEEYEDTL 943
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  285 THVSDTSV---VLSMDNNRNLDLDSI--IAEVRAQYEEI-AQRSKAEAEAlyqTKVQQLQISVDQHGDN-LKNTKSEI-A 356
Cdd:COG1196   944 ETELEREIerlEEEIEALGPVNLRAIeeYEEVEERYEELkSQREDLEEAK---EKLLEVIEELDKEKRErFKETFDKInE 1020
                         250       260
                  ....*....|....*....|.
gi 331999954  357 ELNRMIQRL----RAEIENIK 373
Cdd:COG1196  1021 NFSEIFKELfgggTAELELTE 1041
Streccoc_I_II NF033804
antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins ...
204-432 4.14e-04

antigen I/II family LPXTG-anchored adhesin; Members of the antigen I/II family are adhesins with a glucan-binding domain, two types of repetitive regions, an isopeptide bond-forming domain associated with shear resistance, and a C-terminal LPXTG motif for anchoring to the cell wall. They occur in oral Streptococci, and tend to be major cell surface adhesins. Members of this family include SspA and SspB from Streptococcus gordonii, antigen I/II from S. mutans, etc.


Pssm-ID: 411384 [Multi-domain]  Cd Length: 1552  Bit Score: 43.39  E-value: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  204 NDKGRLQSELKTMQDSVEDFKTKYEEEINKRTA------AENDFV-----VLKKDVDAA---YLNKVELEAKVDSLNDEI 269
Cdd:NF033804  227 NKLSAYQTELARVQKANAEAKEAYDKAVKENTAknaalqAENEAIkqrneTAKANYEAAmkqYEADLAAIKKAKEDNDAD 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  270 NFLK-VLYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAevrAQYEEIAQRSkAEAEALYQTKVQQLQI---SVDQ-H 344
Cdd:NF033804  307 YQAKlAAYQTELARVQKANADAKAAYEKAVEENTAKNTAIQ---AENEAIKQRN-AAAKATYEAALKQYEAdlaAVKKaN 382
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  345 GDNLKNTKSEIAELNRMIQRLRAE-----------IENIKKQCQTLQVSVADAEQRGENALKDAHSKRVELEAALQQAKE 413
Cdd:NF033804  383 AANEADYQAKLAAYQTELARVQKAnadakaayekaVEDNKAKNAALQAENEAIKQRNAAAKADYEAKLAKYQADLAKYKK 462
                         250       260
                  ....*....|....*....|...
gi 331999954  414 ELA---RMLREYQ-ELMSVKLAL 432
Cdd:NF033804  463 DLAeypAKLKAYEdEQAKIKAAL 485
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
349-424 4.15e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 42.85  E-value: 4.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 349 KNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQR-GENALKDAhSKRVELEAALQQ----------------- 410
Cdd:PRK10636 545 KDQKRREAELRTQTQPLRKEIARLEKEMEKLNAQLAQAEEKlGDSELYDQ-SRKAELTACLQQqasaksgleecemawle 623
                         90
                 ....*....|....
gi 331999954 411 AKEELARMLREYQE 424
Cdd:PRK10636 624 AQEQLEQMLLEGQS 637
PRK11281 PRK11281
mechanosensitive channel MscK;
309-416 7.05e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.59  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  309 AEVRAQYEEIAQRSKAEAEAlyQTKVQQLQISVDQHgDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQ-VSVADAE 387
Cdd:PRK11281   39 ADVQAQLDALNKQKLLEAED--KLVQQDLEQTLALL-DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKdDNDEETR 115
                          90       100       110
                  ....*....|....*....|....*....|
gi 331999954  388 QRGENA-LKDAHSKRVELEAALQQAKEELA 416
Cdd:PRK11281  116 ETLSTLsLRQLESRLAQTLDQLQNAQNDLA 145
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
303-451 7.79e-04

Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 42.39  E-value: 7.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  303 DLDSIIAEVRAQYEEIAQRSKAEAEAL--YQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQ 380
Cdd:COG1196   243 ELEEELSRLEEELEELQEELEEAEKEIeeLKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELE 322
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 331999954  381 VSVADAEQRGENALKDAhSKRVELEAALQQAKEELARMLREYQELMSVKL-ALDIEIATYRKLLEGEEYRMS 451
Cdd:COG1196   323 ERLEELKEKIEALKEEL-EERETLLEELEQLLAELEEAKEELEEKLSALLeELEELFEALREELAELEAELA 393
46 PHA02562
endonuclease subunit; Provisional
187-429 7.81e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.92  E-value: 7.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 187 LFETYLSVLRKQLDTLGNDKGRLQSELKTMQdsvedfktKYEEEINKRTAAENDfvvlkkdvdaaylnkvELEAKVDSLN 266
Cdd:PHA02562 171 LNKDKIRELNQQIQTLDMKIDHIQQQIKTYN--------KNIEEQRKKNGENIA----------------RKQNKYDELV 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 267 DEINFLKvlydAELSQMQTHVSDtsVVLSMDNNRNL--DLDSIIAEVRAQYEEIAQRSK---------------AEAEAL 329
Cdd:PHA02562 227 EEAKTIK----AEIEELTDELLN--LVMDIEDPSAAlnKLNTAAAKIKSKIEQFQKVIKmyekggvcptctqqiSEGPDR 300
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 330 Y---QTKVQQLQISVDQ---HGDNLKNTKSEIAELNRMIQRLRAEIENIKkqcQTLQVSVADAeqrgenalKDAHSKRVE 403
Cdd:PHA02562 301 ItkiKDKLKELQHSLEKldtAIDELEEIMDEFNEQSKKLLELKNKISTNK---QSLITLVDKA--------KKVKAAIEE 369
                        250       260
                 ....*....|....*....|....*.
gi 331999954 404 LEAALQQAKEELARMLREYQELMSVK 429
Cdd:PHA02562 370 LQAEFVDNAEELAKLQDELDKIVKTK 395
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
130-433 8.60e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 318193 [Multi-domain]  Cd Length: 1112  Bit Score: 42.03  E-value: 8.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   130 IQKVRTEEREQIKLLNNKFASFIDKVQFL--EQQNKVletkwNLLQQQttttSSKNLEPLF---ETYLSVLRKQLDTLGN 204
Cdd:pfam15921  222 ISKILRELDTEISYLKGRIFPVEDQLEALksESQNKI-----ELLLQQ----HQDRIEQLIsehEVEITGLTEKASSARS 292
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   205 DKGRLQSELKTMQDSVEDFKTKYEEEINKrtaAENDFVVLKKDVDAAylnKVELEAKVDSLNDEInflkVLYDAELSQMQ 284
Cdd:pfam15921  293 QANSIQSQLEIIQEQARNQNSMYMRQLSD---LESTVSQLRSELREA---KRMYEDKIEELEKQL----VLANSELTEAR 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   285 THVSDTSvvlsmDNNRNLD--LDSIIAEVRAQYEEIAQRsKAEAEALYQTKVQQlQISVDqhgdnlkNTKSEIAELNRMI 362
Cdd:pfam15921  363 TERDQFS-----QESGNLDdqLQKLLADLHKREKELSLE-KEQNKRLWDRDTGN-SITID-------HLRRELDDRNMEV 428
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 331999954   363 QRLRAEIENIKKQCQTlQVSVADAEQRGENalkDAHSKRVELEAALQQAKEELARMLreyQELMSVKLALD 433
Cdd:pfam15921  429 QRLEALLKAMKSECQG-QMERQMAAIQGKN---ESLEKVSSLTAQLESTKEMLRKVV---EELTAKKMTLE 492
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
195-423 1.06e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 41.98  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   195 LRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEInflkv 274
Cdd:TIGR02169  679 LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI----- 753
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   275 lydAELSQMQTHVsdtsvvlsmdNNRNLDLDSIIAEVRAQYEEIAQRskaeaeaLYQTKVQQLQISVDQHGDNLKNTKSE 354
Cdd:TIGR02169  754 ---ENVKSELKEL----------EARIEELEEDLHKLEEALNDLEAR-------LSHSRIPEIQAELSKLEEEVSRIEAR 813
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 331999954   355 IAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRgenalKDAHSKRVELeaaLQQAKEELARMLREYQ 423
Cdd:TIGR02169  814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ-----IKSIEKEIEN---LNGKKEELEEELEELE 874
PRK12704 PRK12704
phosphodiesterase; Provisional
309-424 1.18e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 1.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 309 AEVRAQYEEIAQRSKAEAE--------ALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQ 380
Cdd:PRK12704  58 ALLEAKEEIHKLRNEFEKElrerrnelQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELI 137
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 331999954 381 vsvADAEQRGEN--ALKDAHSKRVELEAALQQAKEELARMLREYQE 424
Cdd:PRK12704 138 ---EEQLQELERisGLTAEEAKEILLEKVEEEARHEAAVLIKEIEE 180
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
350-447 1.23e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   350 NTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVADAEQRGENALKDAHSKR---VELEAALQQAKEELARMLREYQELM 426
Cdd:TIGR02168  674 ERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqiSALRKDLARLEAEVEQLEERIAQLS 753
                           90       100
                   ....*....|....*....|.
gi 331999954   427 SVKLALDIEIATYRKLLEGEE 447
Cdd:TIGR02168  754 KELTELEAEIEELEERLEEAE 774
Spc7 pfam08317
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
187-345 2.00e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 400559 [Multi-domain]  Cd Length: 311  Bit Score: 40.30  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  187 LFETYLSVLRKQLDTLGNDKGRLQSELKTMQDSVEDFKTKYeEEINKRTAAENDFVVLKKDVDAAYLNkvELEAKVDSLN 266
Cdd:pfam08317 137 LLEGLKEGLEENLEGLEEDKAVLEKQEELLDELLPELVEEY-AELEEELELLQEAAEELENCDKDELE--ELREELAEQD 213
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 331999954  267 DEINFLKvlydAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALyQTKVQQLQisvDQHG 345
Cdd:pfam08317 214 AEIEEKK----RELAELQEQLEELEEKIEELKEQKQELLEEIAEAERVLEECRGWTESEVSRL-KARVDALE---NLTG 284
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
195-436 2.17e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   195 LRKQLDTLgndkgRLQSELktmqdsVEDFKTKYEEEINKrtaaendfvvlkkDVDAAYLNKVELEAKVDSLNDEINFLKV 274
Cdd:TIGR02168  198 LERQLKSL-----ERQAEK------AERYKELKAELREL-------------ELALLVLRLEELREELEELQEELKEAEE 253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   275 LYDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIA------QRSKAEAEALyQTKVQQLQISVDQHGDNL 348
Cdd:TIGR02168  254 ELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISrleqqkQILRERLANL-ERQLEELEAQLEELESKL 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   349 KNTKSEIAELNRMIQRLRAEIENIKKQCQTLqvsvadaeqrgENALKDAHSKRVELEAALQQAKEELARMLREYQELMSV 428
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEEL-----------EAELEELESRLEELEEQLETLRSKVAQLELQIASLNNE 401

                   ....*...
gi 331999954   429 KLALDIEI 436
Cdd:TIGR02168  402 IERLEARL 409
OEP pfam02321
Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric ...
302-419 2.27e-03

Outer membrane efflux protein; The OEP family (Outer membrane efflux protein) form trimeric channels that allow export of a variety of substrates in Gram negative bacteria. Each member of this family is composed of two repeats. The trimeric channel is composed of a 12 stranded all beta sheet barrel that spans the outer membrane, and a long all helical barrel that spans the periplasm.


Pssm-ID: 396757 [Multi-domain]  Cd Length: 181  Bit Score: 39.04  E-value: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  302 LDLDSIIAEVRAqyeeiAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQV 381
Cdd:pfam02321  69 FDGGKRRARVKA-----AKAQVEAAEAQLEQARQQLRLEVAQAYLQLLAAKEQLELAEQALELAEEALELAEARYEAGLI 143
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 331999954  382 SVADAEQrGENALKDAHSKRVELEAALQQAKEELARML 419
Cdd:pfam02321 144 SLLDVLQ-AEVELLEARLELLNAEADLELALAQLEQLL 180
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
134-372 3.06e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.43  E-value: 3.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   134 RTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETKWNLLQQQTTTTSSKnleplfetyLSVLRKQLDTLGNDKGRLQSEL 213
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE---------LKALREALDELRAELTLLNEEA 819
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   214 KTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDEINFLKVLYDAELSQMQTHVSD---T 290
Cdd:TIGR02168  820 ANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEleeL 899
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954   291 SVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRsKAEAEALYQTKVQQL----QISVDQHGDNLKNTKSEIAELNRMIQRLR 366
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELR-LEGLEVRIDNLQERLseeySLTLEEAEALENKIEDDEEEARRRLKRLE 978

                   ....*.
gi 331999954   367 AEIENI 372
Cdd:TIGR02168  979 NKIKEL 984
EzrA COG4477
Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome ...
208-426 4.29e-03

Septation ring formation regulator EzrA [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 226883 [Multi-domain]  Cd Length: 570  Bit Score: 39.67  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 208 RLQSELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLND-----EINFLKVL-YDAELS 281
Cdd:COG4477  278 EAEEELGLIQEKIESLYDLLEREVEAKNVVEENLPILPDYLEKAKENNEHLKEEIERVKEsyrlaETELGSVRkFEKELK 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 282 QMQTHVSDTSVVLSMDNNRNLDLDSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISvdqhgDNLKNTKSEIAELNRM 361
Cdd:COG4477  358 ELESVLDEILENIEAQEVAYSELQDNLEEIEKALTDIEDEQEKVQEHLTSLRKDELEAR-----ENLERLKSKLHEIKRY 432
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 331999954 362 IQRlraeiENIKKQCQTLQVSVADAEQRGENALKDAHSKRVELEAA---LQQAKEELARMLREYQELM 426
Cdd:COG4477  433 MEK-----SNLPGLPETFLSLFFTAGHEIQDLMKELSEVPINMEAVsalVDIATEDMNTLEDETEEVV 495
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
125-444 5.15e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 39.74  E-value: 5.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 125 EIDPEIQKVRTEEREQIKLLNNKFASFIDKVQFLEQQNKVLETkwnLLQQQTTTTSSKNLEPLFETYLSVLRKQLDT--- 201
Cdd:COG0419  386 QLEEAIQELKEELAELSAALEEIQEELEELEKELEELERELEE---LEEEIKKLEEQINQLESKELMIAELAGAGEKcpv 462
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 202 ----LGNDKGRLQSELKTMQD-------SVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAY-LNKVELEAKVDSLNDEI 269
Cdd:COG0419  463 cgqeLPEEHEKELLELYELELeeleeelSREKEEAELREEIEELEKELRELEEELIELLELEeALKEELEEKLEKLENLL 542
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 270 NFLKVLY--------DAELSQMQTHVSDTSVVLSmDNNRNLDLDSIIAEVRAQYEEIAQRSK--AEAEALYQTKVQQLQI 339
Cdd:COG0419  543 EELEELKeklqlqqlKEELRQLEDRLQELKELLE-ELRLLRTRKEELEELRERLKELKKKLKelEERLSQLEELLQSLEL 621
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 340 SVD--QHGDNLKNTKSEIAELN---RMIQRLRAEIENIKKQCQTLQVSVADAEQRGENALKDAHSKR--VELEAALQQAK 412
Cdd:COG0419  622 SEAenELEEAEEELESELEKLNlqaELEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEelEQLEEELEQLR 701
                        330       340       350
                 ....*....|....*....|....*....|..
gi 331999954 413 EELARMLREYQELMSVKLALDIEIATYRKLLE 444
Cdd:COG0419  702 EELEELLKKLGEIEQLIEELESRKAELEELKK 733
COG4372 COG4372
Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];
212-423 5.42e-03

Uncharacterized conserved protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 226809 [Multi-domain]  Cd Length: 499  Bit Score: 39.24  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 212 ELKTMQDSVEDFKTKYEEEINKRTAAENDFVVLKKDVDAAYLNKVELEAKVDSLNDeiNFLKVLydAELSQMQTHVSDTS 291
Cdd:COG4372   75 QLDDIRPQLRALRTELGTAQGEKRAAETEREAARSELQKARQEREAVRQELAAARQ--NLAKAQ--QELARLTKQAQDLQ 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 292 VVLSMdnnrnldldsiIAEVRAQYEEIAQRSKAEAEALY----QTKVQQLQIS-----VDQHGDNLKNTKSEIAELNRMI 362
Cdd:COG4372  151 TRLKT-----------LAEQRRQLEAQAQSLQASQKQLQasatQLKSQVLDLKlrsaqIEQEAQNLATRANAAQARTEEL 219
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 331999954 363 QRLRAEIENIKKQCQTLQVSVADAEQRG---ENALKDAHSKRVELEAALQQAKEELARMLREYQ 423
Cdd:COG4372  220 ARRAAAAQQTAQAIQQRDAQISQKAQQIaarAEQIRERERQLQRLETAQARLEQEVAQLEAYYQ 283
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
305-447 5.75e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 225288  Cd Length: 652  Bit Score: 39.30  E-value: 5.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954 305 DSIIAEVRAQYEEIAQRSKAEAEALYQTKVQQLQISVDQHGDNLKNTKSEIAELNRMIQRLRAEIENIKKQCQTLQVSVA 384
Cdd:COG2433  388 YPLAEALSKVKEEERPREKEGTEEEERREITVYEKRIKKLEETVERLEEENSELKRELEELKREIEKLESELERFRREVR 467
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 331999954 385 DAEQRG-------------ENALKDAHSKRVELEAALQQAKEelARMLREYQELMSVKLaldIEIATYRKLLEGEE 447
Cdd:COG2433  468 DKVRKDreirardrrierlEKELEEKKKRVEELERKLAELRK--MRKLELSGKGTPVKV---VEKLTLEAIEEAEE 538
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
125-444 8.01e-03

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: 38.85  E-value: 8.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  125 EIDPEIQKVRTEEREQIKLLNNKFASFIDKvqflEQQNKVLETKWNLLQQQTTTTSSKnleplfetyLSVLRKQLDTLGN 204
Cdd:TIGR04523  37 QLEKKLKTIKNELKNKEKELKNLDKNLNKD----EEKINNSNNKIKILEQQIKDLNDK---------LKKNKDKINKLNS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  205 DKGRLQSELKTMQDSVEDFKTKY---EEEINKRTAAENDFV--VLKKDVDAAYLN---------KVELEAKVDSLNDEI- 269
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELnklEKQKKENKKNIDKFLteIKKKEKELEKLNnkyndlkkqKEELENELNLLEKEKl 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  270 NFLKVLYDA--ELSQMQTHVSdtsvVLSMDNNRNLDLDSIIAEVRAQYEEIA------QRSKAEAEALYQTKVQQLQISV 341
Cdd:TIGR04523 184 NIQKNIDKIknKLLKLELLLS----NLKKKIQKNKSLESQISELKKQNNQLKdniekkQQEINEKTTEISNTQTQLNQLK 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 331999954  342 DQHGDN----------LKNTKSEIAELNRMIQRLRAEIENIKKQ-CQTLQVSVADAEQRGENALKDAHSKRVELEAALQQ 410
Cdd:TIGR04523 260 DEQNKIkkqlsekqkeLEQNNKKIKELEKQLNQLKSEISDLNNQkEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQ 339
                         330       340       350
                  ....*....|....*....|....*....|....
gi 331999954  411 AKEELARMLREYQELMSVKLALDIEIATYRKLLE 444
Cdd:TIGR04523 340 LNEQISQLKKELTNSESENSEKQRELEEKQNEIE 373
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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