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Conserved domains on  [gi|126116585|ref|NP_032499|]
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keratin, type II cytoskeletal 1 [Mus musculus]

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;
187-500 1.09e-125

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 373.87  E-value: 1.09e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585  187 QEREQIKSLNDKFASFIDKVRFLEQQNQVLQTKWELLQQVdTTTRTQNLDPFFENYISILRRKVDSLKSDQSRMDSELKN 266
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQK-KGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585  267 MQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQDIDFFSALYQMEMSQMQTQISETNVVLS 346
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585  347 MDNNRSLDLDGIISEVKAQYDSICQRSKAEAETFYQSKYEELQITAGKHGDSVRNTKMEISELNRMIQRLRSEIDGCKKQ 426
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126116585  427 ISQIQQNINDAEQRGEKALKDAQNKLNEIEDALSQCKEDLARLLRDFQELMNTKLALDMEIATYKKLLEGEEIR 500
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
153-184 4.38e-19

Keratin type II head;


:

Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 84.32  E-value: 4.38e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 126116585  153 PVCPPGGIQEVTINQSLLQPLNVEVDPQIQKV 184
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
187-500 1.09e-125

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 373.87  E-value: 1.09e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585  187 QEREQIKSLNDKFASFIDKVRFLEQQNQVLQTKWELLQQVdTTTRTQNLDPFFENYISILRRKVDSLKSDQSRMDSELKN 266
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQK-KGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585  267 MQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQDIDFFSALYQMEMSQMQTQISETNVVLS 346
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585  347 MDNNRSLDLDGIISEVKAQYDSICQRSKAEAETFYQSKYEELQITAGKHGDSVRNTKMEISELNRMIQRLRSEIDGCKKQ 426
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126116585  427 ISQIQQNINDAEQRGEKALKDAQNKLNEIEDALSQCKEDLARLLRDFQELMNTKLALDMEIATYKKLLEGEEIR 500
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
153-184 4.38e-19

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 84.32  E-value: 4.38e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 126116585  153 PVCPPGGIQEVTINQSLLQPLNVEVDPQIQKV 184
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 247-503 7.91e-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: 7.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   247 RRKVDSLKSDQSRMDSELKNMQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQDIDFFSAL 326
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   327 ---YQMEMSQMQTQISETNVVLSMDNNRSLDLDGIISEVKAQYDSICQRSKAEaetfyQSKYEELQITAGKHGDSVRNTK 403
Cdd:TIGR02168  756 lteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-----RAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   404 MEISELNRMIQRLRSEIDGCKKQISQIQQNINDAEQRGEK---ALKDAQNKLNEIEDALSQCKEDLARLLRDFQELMNTK 480
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEElesELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                          250       260
                   ....*....|....*....|...
gi 126116585   481 LALDMEIATYKKLLEGEEIRMSG 503
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEG 933
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 382-471 1.72e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 382 QSKYEELQITAGKHGDSVRNTKMEISELNRMIQRLRSEIDGCKKQISQIQQNINDAEQRgekaLKDAQNKLNEIEDALSQ 461
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEIAELRAELEA 101

                         90
                 ....*....|
gi 126116585 462 CKEDLARLLR 471
Cdd:COG4942  102 QKEELAELLR 111
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 158-472 2.67e-04

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 44.07  E-value: 2.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 158 GGIQEvtinqsllqplNVEVDPqIQKVKSQEREQIKSLNDKFASFIDKVRfleqqNQVLQTKWELLQQVDTTTR------ 231
Cdd:PLN03229 405 GGFQE-----------GVPVDP-ERKVNMKKREAVKTPVRELEGEVEKLK-----EQILKAKESSSKPSELALNemiekl 467

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 232 TQNLD-PFFENYISI-LRRKVDSLKSDQSRMDSELKNMQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVD-----SAYM 304
Cdd:PLN03229 468 KKEIDlEYTEAVIAMgLQERLENLREEFSKANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlnefSRAK 547

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 305 TKVELQAKADALQQDID--FFSALYQME----MSQMQTQISETNV-------------VLSMDNNRSLDLDGIISEVKAQ 365
Cdd:PLN03229 548 ALSEKKSKAEKLKAEINkkFKEVMDRPEikekMEALKAEVASSGAssgdeldddlkekVEKMKKEIELELAGVLKSMGLE 627

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 366 YDSICQRSKAEAETF----YQSKYEELQITAGKHGDSVrntkMEISELNRMIQRLRSEI--------DGCKKQI----SQ 429
Cdd:PLN03229 628 VIGVTKKNKDTAEQTpppnLQEKIESLNEEINKKIERV----IRSSDLKSKIELLKLEVakasktpdVTEKEKIealeQQ 703

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 126116585 430 IQQNINDAEQRGEkaLKDAQNKLN-EIEDALSQCKEDLARLLRD 472
Cdd:PLN03229 704 IKQKIAEALNSSE--LKEKFEELEaELAAARETAAESNGSLKND 745
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
187-500 1.09e-125

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 373.87  E-value: 1.09e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585  187 QEREQIKSLNDKFASFIDKVRFLEQQNQVLQTKWELLQQVdTTTRTQNLDPFFENYISILRRKVDSLKSDQSRMDSELKN 266
Cdd:pfam00038   1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQK-KGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585  267 MQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQDIDFFSALYQMEMSQMQTQISETNVVLS 346
Cdd:pfam00038  80 LRLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585  347 MDNNRSLDLDGIISEVKAQYDSICQRSKAEAETFYQSKYEELQITAGKHGDSVRNTKMEISELNRMIQRLRSEIDGCKKQ 426
Cdd:pfam00038 160 MDAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQ 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 126116585  427 ISQIQQNINDAEQRGEKALKDAQNKLNEIEDALSQCKEDLARLLRDFQELMNTKLALDMEIATYKKLLEGEEIR 500
Cdd:pfam00038 240 KASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
Keratin_2_head pfam16208
Keratin type II head;
153-184 4.38e-19

Keratin type II head;


Pssm-ID: 465068 [Multi-domain]  Cd Length: 156  Bit Score: 84.32  E-value: 4.38e-19
                          10        20        30
                  ....*....|....*....|....*....|..
gi 126116585  153 PVCPPGGIQEVTINQSLLQPLNVEVDPQIQKV 184
Cdd:pfam16208 125 PPCPPGGIQEVTVNQSLLQPLNLEIDPEIQRV 156
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 247-503 7.91e-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: 7.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   247 RRKVDSLKSDQSRMDSELKNMQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQDIDFFSAL 326
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   327 ---YQMEMSQMQTQISETNVVLSMDNNRSLDLDGIISEVKAQYDSICQRSKAEaetfyQSKYEELQITAGKHGDSVRNTK 403
Cdd:TIGR02168  756 lteLEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-----RAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   404 MEISELNRMIQRLRSEIDGCKKQISQIQQNINDAEQRGEK---ALKDAQNKLNEIEDALSQCKEDLARLLRDFQELMNTK 480
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEElesELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                          250       260
                   ....*....|....*....|...
gi 126116585   481 LALDMEIATYKKLLEGEEIRMSG 503
Cdd:TIGR02168  911 SELRRELEELREKLAQLELRLEG 933
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 187-476 1.65e-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: 51.60  E-value: 1.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   187 QEREQ-IKSLNDKFASFIDKVRFLEQQNQVLQTKWELLQQVDTTTRTQNLDPF-----FENYISILRRKVDSLKSDQSRM 260
Cdd:TIGR02168  673 LERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSrqisaLRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   261 DSELKNMQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQDIDFFSALY---QMEMSQMQTQ 337
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERR 832

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   338 ISETNVVLSMDNNRSLDLDGIISEVKAQYDSiCQRSKAEAETFYQSKYEE---LQITAGKHGDSVRNTKMEISELNRMIQ 414
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEE-LEELIEELESELEALLNErasLEEALALLRSELEELSEELRELESKRS 911

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 126116585   415 RLRSEIDGCKKQISQIQQNINDAEQR-----------GEKALKDAQNKLNEIEDALSQCKEDLARLLRDFQEL 476
Cdd:TIGR02168  912 ELRRELEELREKLAQLELRLEGLEVRidnlqerlseeYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 243-467 1.90e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 1.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   243 ISILRRKVDSLKSDQSRMDSELKNMQDLVEEYRTKYEdEINKRTNA--ENEFVTIKKDVDsaymtkvELQAKADALQQDI 320
Cdd:TIGR02169  239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLE-ELNKKIKDlgEEEQLRVKEKIG-------ELEAEIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   321 DFfsalYQMEMSQMQTQISETNVVLSMDNNRSLDLDGIISEVKAQYDSICQRSKAEAETF------YQSKYEELQITAGK 394
Cdd:TIGR02169  311 AE----KERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELedlraeLEEVDKEFAETRDE 386

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 126116585   395 HGDSVR---NTKMEISELNRMIQRLRSEIDGCKKQISQIQQNINDAEQRG---EKALKDAQNKLNEIEDALSQCKEDLA 467
Cdd:TIGR02169  387 LKDYREkleKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKInelEEEKEDKALEIKKQEWKLEQLAADLS 465
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 187-477 5.97e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 49.68  E-value: 5.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   187 QEREQIKSLNDkfaSFIDKVRFLEQQNQVLQTKWELLQQVDTTTRTQNLDpfFENYISILRRKVDSLKSDQSRMDSELKN 266
Cdd:TIGR02169  695 SELRRIENRLD---ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEE--LEEDLSSLEQEIENVKSELKELEARIEE 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   267 MQDLVEEYRTKYEDEinKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQDIDFFSALYQMEMSQMQtqisetnvvls 346
Cdd:TIGR02169  770 LEEDLHKLEEALNDL--EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQ----------- 836

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   347 mdnnrslDLDGIISEVKAQYDSICQRskaeaetfyqskYEELQITAGKHGDSVRNTKMEISELNRMIQRLRSEIDGCKKQ 426
Cdd:TIGR02169  837 -------ELQEQRIDLKEQIKSIEKE------------IENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ 897

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 126116585   427 ISQIQQNINDAE---QRGEKALKDAQNKLNEIEDALSQCKEDLARLLRDFQELM 477
Cdd:TIGR02169  898 LRELERKIEELEaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEEL 951
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-461 1.94e-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: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   170 LQPLNVEVDPQIQKVKSQEREqIKSLNDKFASFIDKVRFLEQQNQVLQTKWELLQQvdtttRTQNLdpffENYISILRRK 249
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAE-LQELEEKLEELRLEVSELEEEIEELQKELYALAN-----EISRL----EQQKQILRER 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   250 VDSLKSDQSRMDSELKNMQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQDIDFFSALY-- 327
Cdd:TIGR02168  311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVaq 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   328 --------QMEMSQMQTQISETNVVLSMDNNRSLDLDGIISEVKAQYDSICQRSKAEAETFYQSKYEELQITAGKHGDSV 399
Cdd:TIGR02168  391 lelqiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 126116585   400 RNTKMEISELNRMIQRLRSEIDGCKkqisQIQQNiNDAEQRGEKALKDAQNKLNEIEDALSQ 461
Cdd:TIGR02168  471 EEAEQALDAAERELAQLQARLDSLE----RLQEN-LEGFSEGVKALLKNQSGLSGILGVLSE 527
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 246-495 5.40e-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: 46.59  E-value: 5.40e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   246 LRRKVDSLKSDQSRMDSELKNMQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVDsaymtkvELQAKADALQQDIDFFSA 325
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY-------ALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   326 lyqmEMSQMQTQISETNVVLSMDNNRSLDLDGIISEVKAQYDSIcqrskaeaetfyQSKYEELQITAGKHGDSVRNTKME 405
Cdd:TIGR02168  310 ----RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL------------KEELESLEAELEELEAELEELESR 373

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   406 ISELNRMIQRLRSEIDGCKKQISQIQQNINDAEQRgekalkdaqnkLNEIEDALSQCKEDLARLLRDFQElmNTKLALDM 485
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEAR-----------LERLEDRRERLQQEIEELLKKLEE--AELKELQA 440

                          250
                   ....*....|
gi 126116585   486 EIATYKKLLE 495
Cdd:TIGR02168  441 ELEELEEELE 450
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 382-471 1.72e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.37  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 382 QSKYEELQITAGKHGDSVRNTKMEISELNRMIQRLRSEIDGCKKQISQIQQNINDAEQRgekaLKDAQNKLNEIEDALSQ 461
Cdd:COG4942   26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAE----LAELEKEIAELRAELEA 101

                         90
                 ....*....|
gi 126116585 462 CKEDLARLLR 471
Cdd:COG4942  102 QKEELAELLR 111
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
240-504 2.26e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 240 ENYI-SILRRKVDSLKSDQSRMDSELKNMQDLVEEYRTKYEDeinkrTNAENEFVTIKKDVDSAYMTKVELQAKADALQQ 318
Cdd:COG3206  159 EAYLeQNLELRREEARKALEFLEEQLPELRKELEEAEAALEE-----FRQKNGLVDLSEEAKLLLQQLSELESQLAEARA 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 319 DIDFFSALYQmemsQMQTQISETNVVLSMDNNrsldlDGIISEVKAQYDSIcQRSKAEAETFYQSKYEELQitagkhgds 398
Cdd:COG3206  234 ELAEAEARLA----ALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAEL-EAELAELSARYTPNHPDVI--------- 294

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 399 vrntkmeisELNRMIQRLRSEIdgcKKQISQIQQNIndaeqrgEKALKDAQNKLNEIEDALSQCKEDLARLLRDFQELmn 478
Cdd:COG3206  295 ---------ALRAQIAALRAQL---QQEAQRILASL-------EAELEALQAREASLQAQLAQLEARLAELPELEAEL-- 353

                        250       260
                 ....*....|....*....|....*....
gi 126116585 479 TKLALDMEIA--TYKKLLEG-EEIRMSGE 504
Cdd:COG3206  354 RRLEREVEVAreLYESLLQRlEEARLAEA 382
PLN03229 PLN03229
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
 158-472 2.67e-04

acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional


Pssm-ID: 178768 [Multi-domain]  Cd Length: 762  Bit Score: 44.07  E-value: 2.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 158 GGIQEvtinqsllqplNVEVDPqIQKVKSQEREQIKSLNDKFASFIDKVRfleqqNQVLQTKWELLQQVDTTTR------ 231
Cdd:PLN03229 405 GGFQE-----------GVPVDP-ERKVNMKKREAVKTPVRELEGEVEKLK-----EQILKAKESSSKPSELALNemiekl 467

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 232 TQNLD-PFFENYISI-LRRKVDSLKSDQSRMDSELKNMQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVD-----SAYM 304
Cdd:PLN03229 468 KKEIDlEYTEAVIAMgLQERLENLREEFSKANSQDQLMHPVLMEKIEKLKDEFNKRLSRAPNYLSLKYKLDmlnefSRAK 547

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 305 TKVELQAKADALQQDID--FFSALYQME----MSQMQTQISETNV-------------VLSMDNNRSLDLDGIISEVKAQ 365
Cdd:PLN03229 548 ALSEKKSKAEKLKAEINkkFKEVMDRPEikekMEALKAEVASSGAssgdeldddlkekVEKMKKEIELELAGVLKSMGLE 627

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 366 YDSICQRSKAEAETF----YQSKYEELQITAGKHGDSVrntkMEISELNRMIQRLRSEI--------DGCKKQI----SQ 429
Cdd:PLN03229 628 VIGVTKKNKDTAEQTpppnLQEKIESLNEEINKKIERV----IRSSDLKSKIELLKLEVakasktpdVTEKEKIealeQQ 703

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 126116585 430 IQQNINDAEQRGEkaLKDAQNKLN-EIEDALSQCKEDLARLLRD 472
Cdd:PLN03229 704 IKQKIAEALNSSE--LKEKFEELEaELAAARETAAESNGSLKND 745
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 397-476 6.00e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 6.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 397 DSVRNTKMEISELNRMIQRLRSEIDGCKKQISQIQQNINDAEQR---GEKALKDAQNKLNEIEDALSQCKEDLARLLRDF 473
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaaLARRIRALEQELAALEAELAELEKEIAELRAEL 99


                 ...
gi 126116585 474 QEL 476
Cdd:COG4942  100 EAQ 102
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 397-475 6.35e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 6.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 397 DSVRNTKMEISELNRMIQRLRSEIDGCKKQISQIQQNINDAEQR---GEKALKDAQNKLNEIEDALSQCKEDLARLLRDF 473
Cdd:COG3883   16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEleaLQAEIDKLQAEIAEAEAEIEERREELGERARAL 95


                 ..
gi 126116585 474 QE 475
Cdd:COG3883   96 YR 97
PRK01156 PRK01156
chromosome segregation protein; Provisional
 176-479 1.47e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.81  E-value: 1.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 176 EVDPQIQKVKSQE-REQIKSLNDKFASFIDKVRFLEQQNQVLQTKWELLQQ------VDTTTRTQNLDPFFENY---ISI 245
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGqsvcpvCGTTLGEEKSNHIINHYnekKSR 480

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 246 LRRKVDSLKSDQSRMDSELKNMQDLVEEYRTKyedEINKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQDIDFFSA 325
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKIVDLKKRKEYLESE---EINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRYKS 557

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 326 LYQMEMSQMQTQISETNVVLSmdnnrSLDLDGIIS---EVKAQYDSICQRSK------AEAETFYQSKYEELQITAgkhg 396
Cdd:PRK01156 558 LKLEDLDSKRTSWLNALAVIS-----LIDIETNRSrsnEIKKQLNDLESRLQeieigfPDDKSYIDKSIREIENEA---- 628

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 397 DSVRNTKMEISELNRMIQRLRSEIDGCKKQISQIQQNINDaeqrgekaLKDAQNKLNEIEDALSQCKEDLARLLRDFQEL 476
Cdd:PRK01156 629 NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPD--------LKEITSRINDIEDNLKKSRKALDDAKANRARL 700


                 ...
gi 126116585 477 MNT 479
Cdd:PRK01156 701 EST 703
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 247-492 1.58e-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: 1.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   247 RRKVDSLKSDQSRMDseLKNMQDLVEEYRTKYEdeiNKRTNAE--NEFVTIKKDVDSA-----YMTKVELQAKADALQQD 319
Cdd:TIGR02168  173 RRKETERKLERTREN--LDRLEDILNELERQLK---SLERQAEkaERYKELKAELRELelallVLRLEELREELEELQEE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   320 IdffsALYQMEMSQMQTQISETNVVLSmdnnrslDLDGIISEVKAQYDSIcqrskaeaetfyQSKYEELQItagkhgdsv 399
Cdd:TIGR02168  248 L----KEAEEELEELTAELQELEEKLE-------ELRLEVSELEEEIEEL------------QKELYALAN--------- 295

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   400 rntkmEISELNRMIQRLRSEIDGCKKQISQIQQNINDAEQRGEKA---LKDAQNKLNEIEDALSQCKEDLARLLRDFQEL 476
Cdd:TIGR02168  296 -----EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELaeeLAELEEKLEELKEELESLEAELEELEAELEEL 370

                          250
                   ....*....|....*.
gi 126116585   477 MNTKLALDMEIATYKK 492
Cdd:TIGR02168  371 ESRLEELEEQLETLRS 386
46 PHA02562
endonuclease subunit; Provisional
 332-498 2.13e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 332 SQM----QTQISETNvvlsmDNNRSLD--LDGIISEVKAQYDSICQRSKAEAE--TFYQSKYEELQITAGKHGDSVRNTK 403
Cdd:PHA02562 166 SEMdklnKDKIRELN-----QQIQTLDmkIDHIQQQIKTYNKNIEEQRKKNGEniARKQNKYDELVEEAKTIKAEIEELT 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 404 MEISELNR-------MIQRLRSEIDGCKKQISQIQ----------------QNINDAEQRGEKA---LKDAQNKLNEIED 457
Cdd:PHA02562 241 DELLNLVMdiedpsaALNKLNTAAAKIKSKIEQFQkvikmyekggvcptctQQISEGPDRITKIkdkLKELQHSLEKLDT 320

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 126116585 458 ALsqckEDLARLLRDFQELMNTKLALDMEIATYKKLLEGEE 498
Cdd:PHA02562 321 AI----DELEEIMDEFNEQSKKLLELKNKISTNKQSLITLV 357
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 240-495 2.70e-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: 40.77  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585  240 ENYISILRRKVDSLKSDQSRMDSELKNMQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQD 319
Cdd:TIGR04523 123 EVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585  320 IDFFSALYQ------MEMSQMQTQISETNVVLSMDNNRSLDLDGIISEVKAQYDSICQrSKAEAETFYQSKYEELQitag 393
Cdd:TIGR04523 203 LSNLKKKIQknksleSQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKD-EQNKIKKQLSEKQKELE---- 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585  394 khgdsvrNTKMEISELNRMIQRLRSEIDGCKKQISQ-IQQNINDAEQRGEKALKDAQNKLNEIEDALSQCKEDLARLLRD 472
Cdd:TIGR04523 278 -------QNNKKIKELEKQLNQLKSEISDLNNQKEQdWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKE 350

                         250       260
                  ....*....|....*....|...
gi 126116585  473 FQELMNTKLALDMEIATYKKLLE 495
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIE 373
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 209-495 4.31e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.49  E-value: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   209 LEQQNQVLQTKWELLQQVDTTTRTqnldpfFENYISILRRKVDSLKSDQSRMDSELKNMQDLVEEYRTKyeDEINKRTNA 288
Cdd:pfam15921  446 MERQMAAIQGKNESLEKVSSLTAQ------LESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK--ERAIEATNA 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   289 enEFVTIKKDVDSAYMTKVELQAKADALQQdidffsalYQMEMSQMQTQISETNVVLSMDNNRSLDLDGIISEvKAQYDS 368
Cdd:pfam15921  518 --EITKLRSRVDLKLQELQHLKNEGDHLRN--------VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ-HGRTAG 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   369 ICQRSKAEAETFYQSKYEELQ---ITAGKHGDSVRNTKMEISELNrmIQRLRSEIDGckkqiSQIQQNINDAEQRGEKAL 445
Cdd:pfam15921  587 AMQVEKAQLEKEINDRRLELQefkILKDKKDAKIRELEARVSDLE--LEKVKLVNAG-----SERLRAVKDIKQERDQLL 659

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 126116585   446 KDAQNKLNEIeDALSQCKEDLARLLRDFQELMNTKL-ALDMEIATYKKLLE 495
Cdd:pfam15921  660 NEVKTSRNEL-NSLSEDYEVLKRNFRNKSEEMETTTnKLKMQLKSAQSELE 709
PRK09039 PRK09039
peptidoglycan -binding protein;
330-473 4.50e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.56  E-value: 4.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 330 EMSQMQTQISETNVVLSMDNNRSLDLDGIISEVKAQYDSiCQRSKAEAETFYQSKYEELQITAGKHGD---SVRNTKMEI 406
Cdd:PRK09039  54 ALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSA-AEAERSRLQALLAELAGAGAAAEGRAGElaqELDSEKQVS 132

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585 407 SELNRMIQRLRSEIDGCKKQISQIQQNINDAEQRGEKA---LKDAQNKLNEiedALSQCKEDLARLLRDF 473
Cdd:PRK09039 133 ARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESqakIADLGRRLNV---ALAQRVQELNRYRSEF 199
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 405-495 6.45e-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: 39.67  E-value: 6.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 126116585   405 EISELNRMIQRLRSEIDGCKKQISQIQQNINDAEQRgekaLKDAQNKLNEIEDALSQCKEDLARLLRDFQELMNTKLALD 484
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRK----IGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVK 757

                           90
                   ....*....|.
gi 126116585   485 MEIATYKKLLE 495
Cdd:TIGR02169  758 SELKELEARIE 768
 
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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