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Conserved domains on  [gi|47132620|ref|NP_000414|]
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keratin, type II cytoskeletal 2 epidermal [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;
177-490 2.30e-138

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 406.23  E-value: 2.30e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   177 QEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQMNvGTRPINLEPIFQGYIDSLKRYLDGLTAERTSQNSELNN 256
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKK-GAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   257 MQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDNAYMIKVELQSKVDLLNQEIEFLKVLYDAEISQIHQSVTDTNVILS 336
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   337 MDNSRNLDLDSIIAEVKAQYEEIAQRSKEEAEALYHSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQ 416
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132620   417 CKNVQDAIADAEQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLEGEECR 490
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
150-174 1.51e-10

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 60.05  E-value: 1.51e-10
                          10        20
                  ....*....|....*....|....*
gi 47132620   150 IHEVSVNQSLLQPLNVKVDPEIQNV 174
Cdd:pfam16208 132 IQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
177-490 2.30e-138

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 406.23  E-value: 2.30e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   177 QEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQMNvGTRPINLEPIFQGYIDSLKRYLDGLTAERTSQNSELNN 256
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKK-GAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   257 MQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDNAYMIKVELQSKVDLLNQEIEFLKVLYDAEISQIHQSVTDTNVILS 336
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   337 MDNSRNLDLDSIIAEVKAQYEEIAQRSKEEAEALYHSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQ 416
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132620   417 CKNVQDAIADAEQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLEGEECR 490
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
150-174 1.51e-10

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 60.05  E-value: 1.51e-10
                          10        20
                  ....*....|....*....|....*
gi 47132620   150 IHEVSVNQSLLQPLNVKVDPEIQNV 174
Cdd:pfam16208 132 IQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 179-466 2.46e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.30  E-value: 2.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    179 REQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQMnVGTRPINLEPI------FQGYIDSLKRYLDGLTAERTSQNS 252
Cdd:TIGR02169  680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK-IGEIEKEIEQLeqeeekLKERLEELEEDLSSLEQEIENVKS 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    253 ELnnmqDLVEDYKKKYEDEINKRTAAENDfvtLKKDvdnaymikvELQSKVDLLNQEIEFLKvlydAEISQIHQSVTDTN 332
Cdd:TIGR02169  759 EL----KELEARIEELEEDLHKLEEALND---LEAR---------LSHSRIPEIQAELSKLE----EEVSRIEARLREIE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    333 VILSMDNSRNLDLDSIIAEVKAQYEEIAQRSKEEAEALyhskyEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAH 412
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-----ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 47132620    413 VKKQCKNVQDAIADAEQrgehALKDARNKLNDLEEALQQAKEDLARLLRDYQEL 466
Cdd:TIGR02169  894 LEAQLRELERKIEELEA----QIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 389-469 1.83e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 1.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 389 LKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQR---GEHALKDARNKLNDLEEALQQAKEDLARLLRDYQE 465
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108


                ....
gi 47132620 466 LMNV 469
Cdd:COG4942 109 LLRA 112
46 PHA02562
endonuclease subunit; Provisional
 194-447 1.78e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620  194 DKVRFLEQQNQVLQTKWELLQQMnvgtrpinlepifqgyIDSLKRYLDGLTAERTSQNSELNNMQDLVEDYKKKYEDEIN 273
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ----------------IKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620  274 KRTAAENDFVTLKKDVDNAY----MIKVELQSKVDLLNQEIEFLKvlYDAEISQIHQSVTDTNVILSmdnsrnlDLDSII 349
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYE--KGGVCPTCTQQISEGPDRIT-------KIKDKL 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620  350 AEVKAQYEEIAQRSKEEAEALyhSKYEELQVTvgrhgdsLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQ 429
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIM--DEFNEQSKK-------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379

                        250       260
                 ....*....|....*....|.
gi 47132620  430 RGE---HALKDARNKLNDLEE 447
Cdd:PHA02562 380 ELAklqDELDKIVKTKSELVK 400
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
177-490 2.30e-138

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 406.23  E-value: 2.30e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   177 QEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQMNvGTRPINLEPIFQGYIDSLKRYLDGLTAERTSQNSELNN 256
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKK-GAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   257 MQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDNAYMIKVELQSKVDLLNQEIEFLKVLYDAEISQIHQSVTDTNVILS 336
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   337 MDNSRNLDLDSIIAEVKAQYEEIAQRSKEEAEALYHSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQ 416
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132620   417 CKNVQDAIADAEQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLEGEECR 490
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
150-174 1.51e-10

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 60.05  E-value: 1.51e-10
                          10        20
                  ....*....|....*....|....*
gi 47132620   150 IHEVSVNQSLLQPLNVKVDPEIQNV 174
Cdd:pfam16208 132 IQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 179-466 2.46e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.30  E-value: 2.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    179 REQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQMnVGTRPINLEPI------FQGYIDSLKRYLDGLTAERTSQNS 252
Cdd:TIGR02169  680 RERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK-IGEIEKEIEQLeqeeekLKERLEELEEDLSSLEQEIENVKS 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    253 ELnnmqDLVEDYKKKYEDEINKRTAAENDfvtLKKDvdnaymikvELQSKVDLLNQEIEFLKvlydAEISQIHQSVTDTN 332
Cdd:TIGR02169  759 EL----KELEARIEELEEDLHKLEEALND---LEAR---------LSHSRIPEIQAELSKLE----EEVSRIEARLREIE 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    333 VILSMDNSRNLDLDSIIAEVKAQYEEIAQRSKEEAEALyhskyEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAH 412
Cdd:TIGR02169  819 QKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI-----ENLNGKKEELEEELEELEAALRDLESRLGDLKKERDE 893

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 47132620    413 VKKQCKNVQDAIADAEQrgehALKDARNKLNDLEEALQQAKEDLARLLRDYQEL 466
Cdd:TIGR02169  894 LEAQLRELERKIEELEA----QIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 243-466 2.80e-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: 53.91  E-value: 2.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    243 LTAERTSQNSELNNMQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDNAYMIKVELQSKVDLLNQEIEFL---KVLYDA 319
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    320 EISQIHQSVTDTNVILSMDNSRNLDLDSIIAEVKAQYEEIAQRSKEEAEAL---------YHSKYEELQVTVGRHGDSLK 390
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELeeleaeleeLESRLEELEEQLETLRSKVA 389

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 47132620    391 EIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQR-GEHALKDARNKLNDLEEALQQAKEDLARLLRDYQEL 466
Cdd:TIGR02168  390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKlEEAELKELQAELEELEEELEELQEELERLEEALEEL 466
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 230-466 6.46e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 52.76  E-value: 6.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    230 QGYIDSLKRYLDGLTAERTSQNSELNNMQDLVEDYKKKYEDEinkrtaAENDFVTLKKDVDNAYMIKVELQSKVDLLNQE 309
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL------GEEEQLRVKEKIGELEAEIASLERSIAEKERE 316

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    310 IEFLK---VLYDAEISQIHQSVTDTNVILSMDNSRNLDLDSIIAEVKAQYEEIAQRSKEEAEALYHSKYEELQVTVgrhg 386
Cdd:TIGR02169  317 LEDAEerlAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---- 392

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    387 dSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQRG---EHALKDARNKLNDLEEALQQAKEDLARLLRDY 463
Cdd:TIGR02169  393 -KLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADLSKYEQEL 471


                   ...
gi 47132620    464 QEL 466
Cdd:TIGR02169  472 YDL 474
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 247-485 9.83e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.37  E-value: 9.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    247 RTSQNSELNNMQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDNAYMIKVELQSKVDLLNQEIEFLKvlydAEISQIHQ 326
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLE----AEVEQLEE 747

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    327 SVTDTNVilsmdnsRNLDLDSIIAEVKAQYEEIAQRSKEEAEalyhsKYEELQVTVGRHGDSLKEIKIEISELNRVIQRL 406
Cdd:TIGR02168  748 RIAQLSK-------ELTELEAEIEELEERLEEAEEELAEAEA-----EIEELEAQIEQLKEELKALREALDELRAELTLL 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    407 QGEIAHVKKQCKNVQDAIADAEQRGEHA---LKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKL 483
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLeeqIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895


                   ..
gi 47132620    484 LE 485
Cdd:TIGR02168  896 LE 897
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 341-482 1.66e-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: 48.13  E-value: 1.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    341 RNLDLDSIIAEVKAQYEEIAQRSKEEAEA------------LYHSKYEELQVTVGRHGDS-------LKEIKIEISELNR 401
Cdd:TIGR02168  223 RELELALLVLRLEELREELEELQEELKEAeeeleeltaelqELEEKLEELRLEVSELEEEieelqkeLYALANEISRLEQ 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    402 VIQRLQGEIAHVKKQCKNVQDAIADAEQRGEHA---LKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIA 478
Cdd:TIGR02168  303 QKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE 382


                   ....
gi 47132620    479 TYRK 482
Cdd:TIGR02168  383 TLRS 386
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 389-469 1.83e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 47.45  E-value: 1.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 389 LKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQR---GEHALKDARNKLNDLEEALQQAKEDLARLLRDYQE 465
Cdd:COG4942  29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAE 108


                ....
gi 47132620 466 LMNV 469
Cdd:COG4942 109 LLRA 112
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 176-472 4.10e-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: 46.97  E-value: 4.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    176 AQEREQ-IKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQMNVGTRPINLEPIFQ-----GYIDSLKRYLDGLTAERTS 249
Cdd:TIGR02168  672 ILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQisalrKDLARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    250 QNSELNNMQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDNA--------YMIKvELQSKVDLLNQEI----------E 311
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLkeelkalrEALD-ELRAELTLLNEEAanlrerleslE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    312 FLKVLYDAEISQIHQSVTDTNVILSMDNSRNLDLDSIIAEVKAQYEEI--AQRSKEEAEALYHSKYEELQVTVGRHGDSL 389
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALlnERASLEEALALLRSELEELSEELRELESKR 910

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    390 KEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQRgehALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNV 469
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL---TLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV 987


                   ...
gi 47132620    470 KLA 472
Cdd:TIGR02168  988 NLA 990
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 240-474 5.74e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 5.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 240 LDGLTAERTSQNSELNNMQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDNAYMIKVELQSKVDLLNQEIEFLKvlydA 319
Cdd:COG1196 262 LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE----E 337

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 320 EISQIHQSVTDTNVILSmdnsrnlDLDSIIAEVKAQYEEIAQRSKEEAEALyhskyEELQVTVGRHGDSLKEIKIEISEL 399
Cdd:COG1196 338 ELEELEEELEEAEEELE-------EAEAELAEAEEALLEAEAELAEAEEEL-----EELAEELLEALRAAAELAAQLEEL 405

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47132620 400 NRVIQRLQGEIAHVKKQCKNVQDAIADAEQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALD 474
Cdd:COG1196 406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALA 480
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 350-488 1.28e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 350 AEVKAQYEEIAQRSKE-EAEALYHsKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADA- 427
Cdd:COG1196 209 AEKAERYRELKEELKElEAELLLL-KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAq 287

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47132620 428 --EQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLEGEE 488
Cdd:COG1196 288 aeEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 349-488 2.09e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 349 IAEVKAQYEEIAQRSKEEAEAL--YHSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIAD 426
Cdd:COG1196 262 LAELEAELEELRLELEELELELeeAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEE 341

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 47132620 427 AEQRGEHA---LKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLEGEE 488
Cdd:COG1196 342 LEEELEEAeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
344-466 4.35e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 4.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620  344 DLDSIIAEVKAQYEEIAQRsKEEAEAlyhsKYEELQVTVGRH-GDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNV-- 420
Cdd:COG4913  299 ELRAELARLEAELERLEAR-LDALRE----ELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAALgl 373

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 47132620  421 -----QDAIADAEQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQEL 466
Cdd:COG4913  374 plpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL 424
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 344-466 7.07e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 7.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 344 DLDSIIAEVKAQYEEIAQRSKEEAEAL--YHSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQ 421
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELaeLEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 47132620 422 DAIADAEQRgehaLKDARNKLNDLEEALQQAKEDLARLLRDYQEL 466
Cdd:COG1196 316 ERLEELEEE----LAELEEELEELEEELEELEEELEEAEEELEEA 356
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 344-485 1.16e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 344 DLDSIIAEVKAQYEEIAQR--SKEEAEALYHSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVK--KQCKN 419
Cdd:COG1579  14 ELDSELDRLEHRLKELPAElaELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnKEYEA 93

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 47132620 420 VQDAIADAEQR---GEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELmnvKLALDVEIATYRKLLE 485
Cdd:COG1579  94 LQKEIESLKRRisdLEDEILELMERIEELEEELAELEAELAELEAELEEK---KAELDEELAELEAELE 159
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
345-482 1.18e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.06  E-value: 1.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 345 LDSIIAEVKAQYEEIAQRSKEEAEALyhSKYEELQVTVGRHGDSLKEI--KIEISELNRVIQRLQGEIAHVKKQCKNVQD 422
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQELK--EELEELEEQLEELLGELEELleALDEEELEEELEELEEELEELEEELEELRE 453

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 423 AIADAEQRGEHALKDARnkLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRK 482
Cdd:COG4717 454 ELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 349-488 1.67e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 349 IAEVKAQYEEIAQRSKEEAEALyhskyEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAE 428
Cdd:COG1196 234 LRELEAELEELEAELEELEAEL-----EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47132620 429 QRGEHA---LKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLEGEE 488
Cdd:COG1196 309 ERRRELeerLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
46 PHA02562
endonuclease subunit; Provisional
 194-447 1.78e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620  194 DKVRFLEQQNQVLQTKWELLQQMnvgtrpinlepifqgyIDSLKRYLDGLTAERTSQNSELNNMQDLVEDYKKKYEDEIN 273
Cdd:PHA02562 174 DKIRELNQQIQTLDMKIDHIQQQ----------------IKTYNKNIEEQRKKNGENIARKQNKYDELVEEAKTIKAEIE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620  274 KRTAAENDFVTLKKDVDNAY----MIKVELQSKVDLLNQEIEFLKvlYDAEISQIHQSVTDTNVILSmdnsrnlDLDSII 349
Cdd:PHA02562 238 ELTDELLNLVMDIEDPSAALnklnTAAAKIKSKIEQFQKVIKMYE--KGGVCPTCTQQISEGPDRIT-------KIKDKL 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620  350 AEVKAQYEEIAQRSKEEAEALyhSKYEELQVTvgrhgdsLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQ 429
Cdd:PHA02562 309 KELQHSLEKLDTAIDELEEIM--DEFNEQSKK-------LLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAE 379

                        250       260
                 ....*....|....*....|.
gi 47132620  430 RGE---HALKDARNKLNDLEE 447
Cdd:PHA02562 380 ELAklqDELDKIVKTKSELVK 400
PRK09039 PRK09039
peptidoglycan -binding protein;
318-458 2.43e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 40.72  E-value: 2.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620  318 DAEISQIHQSVTDTNVILSMDNSRNLDLDSIIAEVKAQYEEiAQRSKEEAEALYHSKYEELQVTVGRHGD---SLKEIKI 394
Cdd:PRK09039  52 DSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQ 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 47132620  395 EISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQRGehalKDARNKLNDLEE----ALQQAKEDLAR 458
Cdd:PRK09039 131 VSARALAQVELLNQQIAALRRQLAALEAALDASEKRD----RESQAKIADLGRrlnvALAQRVQELNR 194
ElaB COG4575
Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD ...
 395-463 4.18e-03

Membrane-anchored ribosome-binding protein ElaB, inhibits growth in stationary phase, YqjD/DUF883 family [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443632 [Multi-domain]  Cd Length: 108  Bit Score: 37.23  E-value: 4.18e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 395 EISELNRVIQRLQGEIAHVKKQCKN-VQDAIADAEQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDY 463
Cdd:COG4575  13 SKEDLEADLKALVDDLEELLKSTADdAGEKAAELREKAEAALDEARERLSEAEDAAVERAREAADAADDY 82
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 233-458 4.33e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 4.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 233 IDSLKRYLDGLTAERTSQNSELNNMQDLVEDYKKKYEDEINKRTAAENDFVTLKKDVDnaymikvELQSKVDLLNQEI-E 311
Cdd:COG3883  18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIA-------EAEAEIEERREELgE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 312 FLKVLYDAEisqihQSVTDTNVILSMDN-----SRNLDLDSIIAEVKAQYEEI--AQRSKEEAEALYHSKYEELQVTVGR 384
Cdd:COG3883  91 RARALYRSG-----GSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELkaDKAELEAKKAELEAKLAELEALKAE 165

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 47132620 385 HGDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQRGEHALKDARNKLNDLEEALQQAKEDLAR 458
Cdd:COG3883 166 LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 239
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 273-486 4.83e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 4.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 273 NKRTAAENDFVTLKKDVDNAYMIKVELQSKVDLLNQEIEFLkvlyDAEISQIHQSVTDTNVILSMDNSRNLDLDSIIAEV 352
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 353 KAQYEEIAQRSKEEAEALY-HSKYEELQVTVGRHG--DSLKEIKIeISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQ 429
Cdd:COG4942  96 RAELEAQKEELAELLRALYrLGRQPPLALLLSPEDflDAVRRLQY-LKYLAPARREQAEELRADLAELAALRAELEAERA 174

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 47132620 430 RGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLEG 486
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 387-485 5.23e-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: 40.05  E-value: 5.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620    387 DSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQRgehaLKDARNKLNDLEEALQQAKEDLARLLRDYQEL 466
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRK----IGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749

                           90
                   ....*....|....*....
gi 47132620    467 MNVKLALDVEIATYRKLLE 485
Cdd:TIGR02169  750 EQEIENVKSELKELEARIE 768
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 154-456 5.56e-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: 40.00  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   154 SVNQSLLQPLNVKVDP--EIQNVKAQEREQIKTLNNKFASFIDKVRFLEQQNQVLQTKWELLQQmnvgtrpiNLEPIFQG 231
Cdd:TIGR04523 356 SENSEKQRELEEKQNEieKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ--------EKELLEKE 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   232 Y------IDSLKRYLDGLTAERTSQNSELNNMQDLVEDYKKK---YEDEINK-RTAAENDFVTLKKDVDNAYMI---KVE 298
Cdd:TIGR04523 428 IerlketIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQlkvLSRSINKiKQNLEQKQKELKSKEKELKKLneeKKE 507

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   299 LQSKVDLLNQEIEFLKVLYD---AEISQIHQSVTDTNVILSMDNSrNLDLDSIIAEVKAQYEEIAQrSKEEAEALyHSKY 375
Cdd:TIGR04523 508 LEEKVKDLTKKISSLKEKIEkleSEKKEKESKISDLEDELNKDDF-ELKKENLEKEIDEKNKEIEE-LKQTQKSL-KKKQ 584

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620   376 EELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIadaeqrgehalKDARNKLNDLEEALQQAKED 455
Cdd:TIGR04523 585 EEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSII-----------KNIKSKKNKLKQEVKQIKET 653


                  .
gi 47132620   456 L 456
Cdd:TIGR04523 654 I 654
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 389-488 7.63e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 7.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 389 LKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQDAIADAEQrgehALKDARNKLNDLEEALQQAKedlARLLRDYQELMN 468
Cdd:COG1579  12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKT----ELEDLEKEIKRLELEIEEVE---ARIKKYEEQLGN 84

                        90       100
                ....*....|....*....|....*
gi 47132620 469 VK-----LALDVEIATYRKLLEGEE 488
Cdd:COG1579  85 VRnnkeyEALQKEIESLKRRISDLE 109
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 345-485 7.98e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 7.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620 345 LDSIIAEVKAQYEEI--AQRSKEEAEALYHSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAHVKKQCKNVQD 422
Cdd:COG1196 244 LEAELEELEAELEELeaELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 47132620 423 AIADAEQRGEHALKDARNKLNDLEEALQQAKEDLARLLRDYQELMNVKLALDVEIATYRKLLE 485
Cdd:COG1196 324 ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
298-468 8.23e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620  298 ELQSKVDLLNQEIEFLKVLYDA--EISQIHQSVTDTNvilsmdnSRNLDLDSI---IAEVKAQYEEI---------AQRS 363
Cdd:COG4913  621 ELEEELAEAEERLEALEAELDAlqERREALQRLAEYS-------WDEIDVASAereIAELEAELERLdassddlaaLEEQ 693

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 47132620  364 KEEAEALY---HSKYEELQVTVGRHGDSLKEIKIEISELNRVIQRLQGEIAhvkkqcknvQDAIADAEQRGEHALKDA-- 438
Cdd:COG4913  694 LEELEAELeelEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR---------LELRALLEERFAAALGDAve 764

                        170       180       190
                 ....*....|....*....|....*....|
gi 47132620  439 RNKLNDLEEALQQAKEDLARLLRDYQELMN 468
Cdd:COG4913  765 RELRENLEERIDALRARLNRAEEELERAMR 794
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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