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Conserved domains on  [gi|1622865983|ref|XP_028689749|]
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angiomotin-like protein 1 isoform X5 [Macaca mulatta]

Protein Classification

Smc and Angiomotin_C domain-containing protein( domain architecture ID 10573751)

Smc and Angiomotin_C domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 556-762 1.86e-112

Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.


:

Pssm-ID: 463503 [Multi-domain]  Cd Length: 200  Bit Score: 342.90  E-value: 1.86e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 556 YVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANVPEYNAPALLELVREKEERILALEADM 635
Cdd:pfam12240   1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 636 TKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYgESSLeahiwqeEEEVVQANRRCQDMEYTIKNLHAKIIE 715
Cdd:pfam12240  81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622865983 716 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 762
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 387-645 4.74e-10

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 4.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 387 AIVERAQQMVEILTEENRVLHQELQgyyDNADKLHKFEKELQRISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 466
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 467 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 546
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 547 EEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpanvpeynapALLELVREKEE 626
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456

                         250
                  ....*....|....*....
gi 1622865983 627 RILALEADMTKWEQKYLEE 645
Cdd:COG1196   457 EEEALLELLAELLEEAALL 475
 
Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 556-762 1.86e-112

Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.


Pssm-ID: 463503 [Multi-domain]  Cd Length: 200  Bit Score: 342.90  E-value: 1.86e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 556 YVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANVPEYNAPALLELVREKEERILALEADM 635
Cdd:pfam12240   1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 636 TKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYgESSLeahiwqeEEEVVQANRRCQDMEYTIKNLHAKIIE 715
Cdd:pfam12240  81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622865983 716 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 762
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 387-645 4.74e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 4.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 387 AIVERAQQMVEILTEENRVLHQELQgyyDNADKLHKFEKELQRISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 466
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 467 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 546
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 547 EEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpanvpeynapALLELVREKEE 626
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456

                         250
                  ....*....|....*....
gi 1622865983 627 RILALEADMTKWEQKYLEE 645
Cdd:COG1196   457 EEEALLELLAELLEEAALL 475
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 384-645 1.08e-09

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: 62.39  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  384 DAFAIVERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRE-SLDKAMRNKLEGEIRRL 462
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  463 HDFNRDLRDRLETANRQLSSREYEGHedkaaeghYASQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILDQALSNAQA 541
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRLTLEKE--------YLEKEIQELQEQrIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  542 RVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKREQMERRLRTWLE---RELDALRTQQKHGNGQPANVPEYna 614
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIEDPKGEDEEIPEEELSL-- 953

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1622865983  615 PALLELVREKEERILALEADMTKWEQKYLEE 645
Cdd:TIGR02169  954 EDVQAELQRVEEEIRALEPVNMLAIQEYEEV 984
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
387-596 1.48e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 387 AIVERAQQMVEILTEE---NRVLHQELQ-GYYDNADK-LHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEG---E 458
Cdd:PRK03918  129 AIYIRQGEIDAILESDesrEKVVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrE 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 459 IRRLHDFNRDLRDRLETANRQLssREYEGHEDKAAEghYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD----- 533
Cdd:PRK03918  209 INEISSELPELREELEKLEKEV--KELEELKEEIEE--LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvke 284

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622865983 534 ----QALSNAQARVIKLEEELREKQAYVEK-VEKLQQALTQLQSACEKREQMERRLRtWLERELDALR 596
Cdd:PRK03918  285 lkelKEKAEEYIKLSEFYEEYLDELREIEKrLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELE 351
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 415-599 2.61e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 48.25  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  415 DNADKLHKFEKELQ-RISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 490
Cdd:pfam01576  145 DQNSKLSKERKLLEeRISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  491 KAaegHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTql 570
Cdd:pfam01576  224 IA---ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG-- 298

                          170       180
                   ....*....|....*....|....*....
gi 1622865983  571 qsacekrEQMErRLRTWLERELDALRTQQ 599
Cdd:pfam01576  299 -------EELE-ALKTELEDTLDTTAAQQ 319
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
534-595 1.58e-04

Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];


Pssm-ID: 442400 [Multi-domain]  Cd Length: 202  Bit Score: 43.78  E-value: 1.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622865983 534 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKREQMERRLRTwlERELDAL 595
Cdd:COG3167    46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 418-590 2.22e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 43.50  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 418 DKLHKFEKELQRISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSsreyeGHEDKAAEGHY 497
Cdd:cd07596    11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLG-----KAAEELSSLSE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 498 ASQNKEFLKEKEKLEMEL---AAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQ----QAL 567
Cdd:cd07596    82 AQANQELVKLLEPLKEYLrycQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPA---KVEELEeeleEAE 158

                         170       180
                  ....*....|....*....|...
gi 1622865983 568 TQLQSACEKREQMERRLRTWLER 590
Cdd:cd07596   159 SALEEARKRYEEISERLKEELKR 181
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 394-733 2.74e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  394 QMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESL-VKSTTKRESLDKAMRNKLEGEIRRlhdfnrDLRDR 472
Cdd:TIGR02169  146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAERYQ------ALLKE 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  473 LetanrqlssREYEGhedkaaeghyasqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELRE 552
Cdd:TIGR02169  220 K---------REYEG--------------YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  553 KQAYVEKV--EKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpaNVPEYNapALLELVREKEERILA 630
Cdd:TIGR02169  277 LNKKIKDLgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-------LEAEID--KLLAEIEELEREIEE 347

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  631 LEADMTKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHS----RNGSYGE--SSLEAHIWQEEEEVVQANRRCQDMEY 704
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyreKLEKLKReiNELKRELDRLQEELQRLSEELADLNA 427

                          330       340
                   ....*....|....*....|....*....
gi 1622865983  705 TIKNLHAKIIEKDAMIKVLQQRSRKDAGK 733
Cdd:TIGR02169  428 AIAGIEAKINELEEEKEDKALEIKKQEWK 456
 
Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 556-762 1.86e-112

Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 and 211 amino acids in length. This family is the C terminal region of angiomotin. Angiomotin regulates the action of angiogenesis inhibitor angiostatin. The C terminal region of angiomotin appears to be involved in directing the protein chemotactically.


Pssm-ID: 463503 [Multi-domain]  Cd Length: 200  Bit Score: 342.90  E-value: 1.86e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 556 YVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANVPEYNAPALLELVREKEERILALEADM 635
Cdd:pfam12240   1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 636 TKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYgESSLeahiwqeEEEVVQANRRCQDMEYTIKNLHAKIIE 715
Cdd:pfam12240  81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622865983 716 KDAMIKVLQQRSRKDAGKTDSSSLRPARSVPSI-AAATGTHSRQTSLT 762
Cdd:pfam12240 153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 387-645 4.74e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 4.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 387 AIVERAQQMVEILTEENRVLHQELQgyyDNADKLHKFEKELQRISEAYESLVKSttkresldkamRNKLEGEIRRLHDFN 466
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 467 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 546
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 547 EEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpanvpeynapALLELVREKEE 626
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456

                         250
                  ....*....|....*....
gi 1622865983 627 RILALEADMTKWEQKYLEE 645
Cdd:COG1196   457 EEEALLELLAELLEEAALL 475
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 384-645 1.08e-09

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: 62.39  E-value: 1.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  384 DAFAIVERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRE-SLDKAMRNKLEGEIRRL 462
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  463 HDFNRDLRDRLETANRQLSSREYEGHedkaaeghYASQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILDQALSNAQA 541
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRLTLEKE--------YLEKEIQELQEQrIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  542 RVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKREQMERRLRTWLE---RELDALRTQQKHGNGQPANVPEYna 614
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIEDPKGEDEEIPEEELSL-- 953

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1622865983  615 PALLELVREKEERILALEADMTKWEQKYLEE 645
Cdd:TIGR02169  954 EDVQAELQRVEEEIRALEPVNMLAIQEYEEV 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 381-726 1.11e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 1.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  381 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGyydnADKLHKFEKE-LQRISEAYESLVKSTTKRESLDKAMrNKL 455
Cdd:TIGR02168  133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQL-KSL 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  456 EGEIRRLHDFnRDLRDRLETANRQLSSREYEghedkaaeghyasqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQA 535
Cdd:TIGR02168  206 ERQAEKAERY-KELKAELRELELALLVLRLE----------------ELREELEELQEELKEAEEELEELTAELQELEEK 268

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  536 LSNAQARVIKLEEELREKQayvekveKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHgNGQPANVPEYNAP 615
Cdd:TIGR02168  269 LEELRLEVSELEEEIEELQ-------KELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE-LESKLDELAEELA 340

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  616 ALLELVREKEERILALEADMTKWEQKYLE-ESTIR----HFAMNAAATAAAERDTTIINH--SRNGSYGEsSLEAHIWQE 688
Cdd:TIGR02168  341 ELEEKLEELKEELESLEAELEELEAELEElESRLEeleeQLETLRSKVAQLELQIASLNNeiERLEARLE-RLEDRRERL 419

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1622865983  689 EEEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 726
Cdd:TIGR02168  420 QQEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 387-633 3.29e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 3.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  387 AIVERAQQMVEILTEENRVLHQELQGYYDN-----------ADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKL 455
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLERQLEELEAQleeleskldelAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  456 EGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYA--SQNKEFLkEKEKLEMELAAVRTASEDHRRHIEILD 533
Cdd:TIGR02168  375 EELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRErlQQEIEEL-LKKLEEAELKELQAELEELEEELEELQ 453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  534 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKREQMERRLRTwlerELDALRTQQKHGNGQPANVpeyn 613
Cdd:TIGR02168  454 EELERLEEALEELREELEEAE---QALDAAERELAQLQARLDSLERLQENLEG----FSEGVKALLKNQSGLSGIL---- 522

                          250       260
                   ....*....|....*....|
gi 1622865983  614 aPALLELVREKEERILALEA 633
Cdd:TIGR02168  523 -GVLSELISVDEGYEAAIEA 541
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 390-601 6.44e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 6.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  390 ERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDL 469
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  470 RDRLETANRQLSSREYEGHEDKA----AEGHYASQNKEFLKEKE---KLEMELAAVRTA--------------SEDHRRH 528
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAeieeLEAQIEQLKEELKALREaldELRAELTLLNEEaanlrerleslerrIAATERR 839

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  529 IEILDQALSNAQARVIKLEEELREKQAYVEKVEK--------LQQALTQLQSACEKREQMERRLRTW------LERELDA 594
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESeleallneRASLEEALALLRSELEELSEELRELeskrseLRRELEE 919


                   ....*..
gi 1622865983  595 LRTQQKH 601
Cdd:TIGR02168  920 LREKLAQ 926
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 390-646 8.57e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 8.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 390 ERAQQmveiLTEENRVLHQELQGYydnadKLHKFEKELQRISEAYESLvksTTKRESLDKAMRnKLEGEIRRLHDFNRDL 469
Cdd:COG1196   213 ERYRE----LKEELKELEAELLLL-----KLRELEAELEELEAELEEL---EAELEELEAELA-ELEAELEELRLELEEL 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 470 RDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE 549
Cdd:COG1196   280 ELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 550 LREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpanvpeynapALLELVREKEERIL 629
Cdd:COG1196   360 LAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE---------------ALLERLERLEEELE 424

                         250
                  ....*....|....*..
gi 1622865983 630 ALEADMTKWEQKYLEES 646
Cdd:COG1196   425 ELEEALAELEEEEEEEE 441
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
415-599 1.67e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.77  E-value: 1.67e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  415 DNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEgEIRRLHDFNRDLRDRLETAnrqlssREYEGHEDKAAE 494
Cdd:COG4913    607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIDVASAE------REIAELEAELER 679

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  495 ghyASQNKEFLKEkekLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSAC 574
Cdd:COG4913    680 ---LDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALL 751

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1622865983  575 EKR------EQMERRLRTWLERELDALRTQQ 599
Cdd:COG4913    752 EERfaaalgDAVERELRENLEERIDALRARL 782
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
384-623 2.55e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.00  E-value: 2.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  384 DAFAIVERAQQMVEilteenrvlH-QELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDkAMRNKL-----EG 457
Cdd:COG4913    219 EEPDTFEAADALVE---------HfDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELE-YLRAALrlwfaQR 288

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  458 EIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDK--AAEGHYASQNkefLKEKEKLEMELAAVRTASEDHRRHIEILD 533
Cdd:COG4913    289 RLELLEAELEELRAELARLEAELErlEARLDALREEldELEAQIRGNG---GDRLEQLEREIERLERELEERERRRARLE 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  534 QALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHGNGQPANVPEYN 613
Cdd:COG4913    366 ALLAALGLPLPASAEEFAALRA---EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARL 442

                          250
                   ....*....|
gi 1622865983  614 APALLELVRE 623
Cdd:COG4913    443 LALRDALAEA 452
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
387-596 1.48e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 387 AIVERAQQMVEILTEE---NRVLHQELQ-GYYDNADK-LHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEG---E 458
Cdd:PRK03918  129 AIYIRQGEIDAILESDesrEKVVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrE 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 459 IRRLHDFNRDLRDRLETANRQLssREYEGHEDKAAEghYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD----- 533
Cdd:PRK03918  209 INEISSELPELREELEKLEKEV--KELEELKEEIEE--LEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEekvke 284

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622865983 534 ----QALSNAQARVIKLEEELREKQAYVEK-VEKLQQALTQLQSACEKREQMERRLRtWLERELDALR 596
Cdd:PRK03918  285 lkelKEKAEEYIKLSEFYEEYLDELREIEKrLSRLEEEINGIEERIKELEEKEERLE-ELKKKLKELE 351
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
408-576 1.48e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 55.46  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 408 QELQGYYDNADKLHKFEKELQRISEAYESLvksttkRESLDKAmRNKLEGEIRRLhdfnRDLRDRLETANRQLSSREYEG 487
Cdd:PRK03918  595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEYEE 663

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 488 HEDkaaeghyasqnkeflkEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 567
Cdd:PRK03918  664 LRE----------------EYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720


                  ....*....
gi 1622865983 568 TQLQSACEK 576
Cdd:PRK03918  721 ERVEELREK 729
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 409-590 5.17e-07

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 51.85  E-value: 5.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 409 ELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQL----SSRE 484
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 485 YEG--HEDKAAEghyasqnkeflKEKEKLEMELAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQA-YVEKVE 561
Cdd:COG1579    91 YEAlqKEIESLK-----------RRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAeLDEELA 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 1622865983 562 KLQQALTQLQSACEK-REQMERRLRTWLER 590
Cdd:COG1579   153 ELEAELEELEAEREElAAKIPPELLALYER 182
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
427-603 3.23e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.92  E-value: 3.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 427 LQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRL---HDFNRDLRDRLETANRQLSS--REYEGHEDKAAEGHYASQN 501
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAeekEEEYAELQEELEELEEELEEleAELEELREELEKLEKLLQL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 502 KEFLKEKEKLEMELAAVRTASEDHRRHIEI---LDQALSNAQARVIKLEEELREKQAY------------VEKVEKLQQA 566
Cdd:COG4717   128 LPLYQELEALEAELAELPERLEELEERLEElreLEEELEELEAELAELQEELEELLEQlslateeelqdlAEELEELQQR 207

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622865983 567 LTQLQsacEKREQMERRLRTwLERELDALRTQQKHGN 603
Cdd:COG4717   208 LAELE---EELEEAQEELEE-LEEELEQLENELEAAA 240
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
418-626 5.90e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.06  E-value: 5.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 418 DKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETanrqlSSREYEGHEDKAAEghy 497
Cdd:PRK03918  214 SELPELREELEKLEKEVKELEELKEEIEELEKELE-SLEGSKRKLEEKIRELEERIEE-----LKKEIEELEEKVKE--- 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 498 asqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKR 577
Cdd:PRK03918  285 ----LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622865983 578 EQMERRLRTwLERELDALRTQQKhgngqpANVPEYNAPALLELVREKEE 626
Cdd:PRK03918  361 HELYEEAKA-KKEELERLKKRLT------GLTPEKLEKELEELEKAKEE 402
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 415-599 2.61e-05

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 48.25  E-value: 2.61e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  415 DNADKLHKFEKELQ-RISEAYESLVKSTTKRESLDKaMRNKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYEGHED 490
Cdd:pfam01576  145 DQNSKLSKERKLLEeRISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  491 KAaegHYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTql 570
Cdd:pfam01576  224 IA---ELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLG-- 298

                          170       180
                   ....*....|....*....|....*....
gi 1622865983  571 qsacekrEQMErRLRTWLERELDALRTQQ 599
Cdd:pfam01576  299 -------EELE-ALKTELEDTLDTTAAQQ 319
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
424-650 3.63e-05

DNA repair ATPase RecN [Replication, recombination and repair];


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 47.38  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 424 EKELQRISEAYESLVKSTTKRESLDKAMRnklegEIRRLHDFNRDLRDRLETANrqLSSREYEgheDKAAEghyasqnKE 503
Cdd:COG0497   154 EELLEEYREAYRAWRALKKELEELRADEA-----ERARELDLLRFQLEELEAAA--LQPGEEE---ELEEE-------RR 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 504 FLKEKEKLemeLAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQAYVEK----VEKLQQALTQLQSACEK--- 576
Cdd:COG0497   217 RLSNAEKL---REALQEA-------LEALSGGEGGALDLLGQALRALERLAEYDPSlaelAERLESALIELEEAASElrr 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 577 -REQME---RRLRTWLEReLDALRT-QQKHGnGQPANVPEY--NAPALLELVREKEERILALEADMTKWEQKYLEE---- 645
Cdd:COG0497   287 yLDSLEfdpERLEEVEER-LALLRRlARKYG-VTVEELLAYaeELRAELAELENSDERLEELEAELAEAEAELLEAaekl 364


                  ....*
gi 1622865983 646 STIRH 650
Cdd:COG0497   365 SAARK 369
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
424-563 7.72e-05

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 46.39  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 424 EKELQRISEAYESLVKST-TKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEghyasqNK 502
Cdd:COG2433   387 EKELPEEEPEAEREKEHEeRELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE------RR 459

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622865983 503 EFLKEKE--KLEMELAAVRTASEDHRRHIEILdqalsnaQARVIKLEE----ELREKQAYVEKVEKL 563
Cdd:COG2433   460 EIRKDREisRLDREIERLERELEEERERIEEL-------KRKLERLKElwklEHSGELVPVKVVEKF 519
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
534-595 1.58e-04

Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];


Pssm-ID: 442400 [Multi-domain]  Cd Length: 202  Bit Score: 43.78  E-value: 1.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622865983 534 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKREQMERRLRTwlERELDAL 595
Cdd:COG3167    46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 417-600 1.75e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 44.75  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 417 ADKLHKFEKELQRISE---AYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLSS---------RE 484
Cdd:COG4942    19 ADAAAEAEAELEQLQQeiaELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelrAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 485 YEGHEDKAAE---GHYASQNKEFLK------EKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQA 555
Cdd:COG4942    99 LEAQKEELAEllrALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1622865983 556 YVEKVEKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQK 600
Cdd:COG4942   179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 390-646 2.21e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 45.20  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 390 ERAQQMVEIlteENRVLHQELQgyydnadkLHKFEKELQRISEAYE---SLVKSTTKRESLDKAMRNKlEGEIRRLHDFN 466
Cdd:pfam10174 182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 467 RDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKeFLKEK--------EKLEMELAAVRTASE-------DHRRHIEI 531
Cdd:pfam10174 250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK-FMKNKidqlkqelSKKESELLALQTKLEtltnqnsDCKQHIEV 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 532 LDQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQ----LQSACEKREQM----ERRLRTwLERELDALR 596
Cdd:pfam10174 329 LKESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEekstLAGEIRDLKDMldvkERKINV-LQKKIENLQ 407

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622865983 597 TQQKHGNGQPANVPEY------------NAPALLE-LVREKEERILALEADMTKWEQKYLEES 646
Cdd:pfam10174 408 EQLRDKDKQLAGLKERvkslqtdssntdTALTTLEeALSEKERIIERLKEQREREDRERLEEL 470
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 418-590 2.22e-04

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 43.50  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 418 DKLHKFEKELQRISEAYESLVKsttKRESLDKAMrNKLEGEIRRLHDFNRDLRDRLETANRQLSsreyeGHEDKAAEGHY 497
Cdd:cd07596    11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSAL-GEFGKALIKLAKCEEEVGGELGEALSKLG-----KAAEELSSLSE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 498 ASQNKEFLKEKEKLEMEL---AAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQ----QAL 567
Cdd:cd07596    82 AQANQELVKLLEPLKEYLrycQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPA---KVEELEeeleEAE 158

                         170       180
                  ....*....|....*....|...
gi 1622865983 568 TQLQSACEKREQMERRLRTWLER 590
Cdd:cd07596   159 SALEEARKRYEEISERLKEELKR 181
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 394-733 2.74e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.06  E-value: 2.74e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  394 QMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESL-VKSTTKRESLDKAMRNKLEGEIRRlhdfnrDLRDR 472
Cdd:TIGR02169  146 DFISMSPVERRKIIDEIAGVAEFDRKKEKALEELEEVEENIERLdLIIDEKRQQLERLRREREKAERYQ------ALLKE 219

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  473 LetanrqlssREYEGhedkaaeghyasqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELRE 552
Cdd:TIGR02169  220 K---------REYEG--------------YELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEE 276

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  553 KQAYVEKV--EKLQQALTQLQSACEKREQMERRLRTWLERELDALRTQQKhgngqpaNVPEYNapALLELVREKEERILA 630
Cdd:TIGR02169  277 LNKKIKDLgeEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAK-------LEAEID--KLLAEIEELEREIEE 347

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  631 LEADMTKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHS----RNGSYGE--SSLEAHIWQEEEEVVQANRRCQDMEY 704
Cdd:TIGR02169  348 ERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKdyreKLEKLKReiNELKRELDRLQEELQRLSEELADLNA 427

                          330       340
                   ....*....|....*....|....*....
gi 1622865983  705 TIKNLHAKIIEKDAMIKVLQQRSRKDAGK 733
Cdd:TIGR02169  428 AIAGIEAKINELEEEKEDKALEIKKQEWK 456
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 498-743 3.11e-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: 43.98  E-value: 3.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 498 ASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQsacEKR 577
Cdd:COG4942    19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQ---ELAALEAELAELE---KEI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 578 EQMERRLRTWLERELDALRTQQKHG---------NGQPANVPEYNAPALLELVREKEERILALEADMTKWEQKYLEESTI 648
Cdd:COG4942    93 AELRAELEAQKEELAELLRALYRLGrqpplalllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 649 RHFAMNAAATAAAERDttiinhsrngsygesSLEAHIWQEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSR 728
Cdd:COG4942   173 RAELEALLAELEEERA---------------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237

                         250
                  ....*....|....*
gi 1622865983 729 KDAGKTDSSSLRPAR 743
Cdd:COG4942   238 AAAERTPAAGFAALK 252
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
443-637 4.18e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.26  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 443 KRESLDKamrnkLEGEIRRLHDfnRDLRDRLETANRQLSS-----REYEGHEDKAAEGHYASQN-----KEFLKEKEKLE 512
Cdd:PRK02224  185 QRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREQARETRDEADEvleehEERREELETLE 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 513 MELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREqmerrlrTWLEREL 592
Cdd:PRK02224  258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRD-------EELRDRL 330

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1622865983 593 DALRTQQKHGNGQPANVPEyNAPALLELVREKEERILALEADMTK 637
Cdd:PRK02224  331 EECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
399-584 5.13e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 5.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 399 LTEENRvlhQELQGYYdnADKLHKFEKELQRISEAYESLVKSTTKresLDKAMRNklEGEIRRLH---DFNRDLRDRLET 475
Cdd:PRK03918  445 LTEEHR---KELLEEY--TAELKRIEKELKEIEEKERKLRKELRE---LEKVLKK--ESELIKLKelaEQLKELEEKLKK 514

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 476 ANRQ---LSSREYEGHEDKAA--EGHYASQNKEfLKEKEKLEMELAAVRTASED-HRRHIEILDQALSNAQARVIKLEEE 549
Cdd:PRK03918  515 YNLEeleKKAEEYEKLKEKLIklKGEIKSLKKE-LEKLEELKKKLAELEKKLDElEEELAELLKELEELGFESVEELEER 593

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1622865983 550 LREKQAYVEKVEKLQQALTQLQSACEKREQMERRL 584
Cdd:PRK03918  594 LKELEPFYNEYLELKDAEKELEREEKELKKLEEEL 628
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 387-580 5.44e-04

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 44.06  E-value: 5.44e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  387 AIVERAQQMVEILTEENRVLHQE-LQGYYDNADKLHKFEKELQRISEAYESLVKS----TTKRESLDKAMRNKLEGEIRR 461
Cdd:pfam12128  315 AAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERLKALTGKhqdvTAKYNRRRSKIKEQNNRDIAG 394

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  462 LHDfnrDLRDRLETANRQLSSRE--YEGHEDKAAEGHYAsQNKEFLKEKEKLEMELAAVR------TASEDHRRHIEILD 533
Cdd:pfam12128  395 IKD---KLAKIREARDRQLAVAEddLQALESELREQLEA-GKLEFNEEEYRLKSRLGELKlrlnqaTATPELLLQLENFD 470

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622865983  534 QALSNAQ-------ARVIKLEEELRE-KQAYVEKVEKLQQA---LTQLQSACEKREQM 580
Cdd:pfam12128  471 ERIERAReeqeaanAEVERLQSELRQaRKRRDQASEALRQAsrrLEERQSALDELELQ 528
PRK10361 PRK10361
DNA recombination protein RmuC; Provisional
 492-602 6.24e-04

DNA recombination protein RmuC; Provisional


Pssm-ID: 182409 [Multi-domain]  Cd Length: 475  Bit Score: 43.43  E-value: 6.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 492 AAEGHYASQNKEFLKEKEKLEMELAAVR---TASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKV-----EKL 563
Cdd:PRK10361   22 FASYQHAQQKAEQLAEREEMVAELSAAKqqiTQSEHWRAECELLNNEVRSLQSINTSLEADLREVTTRMEAAqqhadDKI 101

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1622865983 564 QQALTQLQSACEKREQMERRLRTWLERELDALRTQQKHG 602
Cdd:PRK10361  102 RQMINSEQRLSEQFENLANRIFEHSNRRVDEQNRQSLNS 140
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
390-565 6.58e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 6.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 390 ERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLvksttkresldKAMRNKLEGEIRRLHDFNR-- 467
Cdd:COG4717    67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-----------REELEKLEKLLQLLPLYQEle 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 468 DLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELA--------AVRTASEDHRRH---IEILDQAL 536
Cdd:COG4717   136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEqlslateeELQDLAEELEELqqrLAELEEEL 215

                         170       180
                  ....*....|....*....|....*....
gi 1622865983 537 SNAQARVIKLEEELREKQAYVEKVEKLQQ 565
Cdd:COG4717   216 EEAQEELEELEEELEQLENELEAAALEER 244
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
504-642 7.05e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 7.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 504 FLKEKEKLEMELAAVRTASEDHRRHIEILDQAlsnaQARVIKLEEELREKQAYVEKVEKLQQALT----------QLQSA 573
Cdd:COG4717    69 NLKELKELEEELKEAEEKEEEYAELQEELEEL----EEELEELEAELEELREELEKLEKLLQLLPlyqelealeaELAEL 144

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622865983 574 CEKREQMERRLRTW--LERELDALRTQQKHGNGQPANVPEYNAPALLELVREKEERILALEADMTKWEQKY 642
Cdd:COG4717   145 PERLEELEERLEELreLEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
390-650 1.24e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 390 ERAQQMVEILTEENRVLHQELQGYydnadKLHKFEKELQRISEAYESLvkstTKRESLDKAMRNKLEGEIRRLhdfnRDL 469
Cdd:PRK03918  361 HELYEEAKAKKEELERLKKRLTGL-----TPEKLEKELEELEKAKEEI----EEEISKITARIGELKKEIKEL----KKA 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 470 RDRLETANRQ--LSSREYEGHEDKAAEGHY-------ASQNKEFLKEKEKLEMELAAVRTASEDHRRHI---EILDQaLS 537
Cdd:PRK03918  428 IEELKKAKGKcpVCGRELTEEHRKELLEEYtaelkriEKELKEIEEKERKLRKELRELEKVLKKESELIklkELAEQ-LK 506

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 538 NAQAR-----VIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTwLERELDALRTQQKHGNGQPANVPey 612
Cdd:PRK03918  507 ELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE-LEKKLDELEEELAELLKELEELG-- 583

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1622865983 613 napalLELVREKEERILALEadmtKWEQKYLEESTIRH 650
Cdd:PRK03918  584 -----FESVEELEERLKELE----PFYNEYLELKDAEK 612
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 405-645 1.37e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.40  E-value: 1.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 405 VLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRnKLEGEIRRLHDFNRDLRDRLEtanrqlssrE 484
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK-KILAEDEKLLDEKKQFEKIAE---------E 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 485 YEGHEDkaaEGHYASQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE-----LREKQAYVEK 559
Cdd:pfam05483 434 LKGKEQ---ELIFLLQARE--KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkllLENKELTQEA 508

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 560 VEKLQQALTQLQSACEKREQMERRLR---------TWLERELDALRTQQKHGNGQ---PANVPEYNAPALLELVREKEER 627
Cdd:pfam05483 509 SDMTLELKKHQEDIINCKKQEERMLKqienleekeMNLRDELESVREEFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQ 588

                         250       260
                  ....*....|....*....|....
gi 1622865983 628 ILALEADMTKWEQ------KYLEE 645
Cdd:pfam05483 589 MKILENKCNNLKKqienknKNIEE 612
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 396-580 1.40e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.89  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 396 VEILTEENRVLHQELQGYYDNADKLHKFEKEL---------------QRISEAYESLVKSTTKResldkamRNKLEgEIR 460
Cdd:cd00176    35 VEALLKKHEALEAELAAHEERVEALNELGEQLieeghpdaeeiqerlEELNQRWEELRELAEER-------RQRLE-EAL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 461 RLHDFNRDLRD---RLETANRQLSSREYEGHEDKAaeghyasqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALS 537
Cdd:cd00176   107 DLQQFFRDADDleqWLEEKEAALASEDLGKDLESV---------EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622865983 538 NAQARVIKleeelrekqayvEKVEKLQQALTQLQSACEKREQM 580
Cdd:cd00176   178 PDADEEIE------------EKLEELNERWEELLELAEERQKK 208
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 499-645 1.59e-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: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 499 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAcekRE 578
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNVRNN---KE 90

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622865983 579 QMErrlrtwLERELDALRTQQKhgngqpanVPEYNAPALLELVREKEERILALEADMTKWEQKYLEE 645
Cdd:COG1579    91 YEA------LQKEIESLKRRIS--------DLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
499-762 2.65e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 499 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEEL----REKQAYVEKVEKLQQALTQLQSAC 574
Cdd:COG4372    52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELeslqEEAEELQEELEELQKERQDLEQQR 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 575 EKREQMERRLRTWL---ERELDALRTQQKHGNGQPANVPEYNAPALLELVREK-------EERILALEADMTKWEQKYLE 644
Cdd:COG4372   132 KQLEAQIAELQSEIaerEEELKELEEQLESLQEELAALEQELQALSEAEAEQAldellkeANRNAEKEEELAEAEKLIES 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 645 ESTIRHFAMNAAATAAAER----DTTIINHSRNGSYGESSLEAHIWQEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMI 720
Cdd:COG4372   212 LPRELAEELLEAKDSLEAKlglaLSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEA 291

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1622865983 721 KVLQQRSRKDAGKTDSSSLRPARSVPSIAAATGTHSRQTSLT 762
Cdd:COG4372   292 ALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 389-576 3.62e-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: 41.20  E-value: 3.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  389 VERAQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQR-ISEAYESLVKSTTKRESLDKAMRNkLEGEIRRLHDFNR 467
Cdd:TIGR02168  833 IAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESeLEALLNERASLEEALALLRSELEE-LSEELRELESKRS 911

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  468 DLRDRLETANRQLSS--REYEGHEDKAAeghyasQNKEFLKEKEKLEMELAAvrtasedhrRHIEILDQALSNAQARVIK 545
Cdd:TIGR02168  912 ELRRELEELREKLAQleLRLEGLEVRID------NLQERLSEEYSLTLEEAE---------ALENKIEDDEEEARRRLKR 976

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1622865983  546 LE-----------------EELREKQAYVEK-VEKLQQALTQLQSACEK 576
Cdd:TIGR02168  977 LEnkikelgpvnlaaieeyEELKERYDFLTAqKEDLTEAKETLEEAIEE 1025
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 392-590 4.03e-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: 40.52  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 392 AQQMVEILTEENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESLDKAMRNKLEGEIRRLHDFNRDLRD 471
Cdd:COG4942    18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 472 RLETANRQLSSREY-----------------EGHEDKAAEGHYASQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILD 533
Cdd:COG4942    98 ELEAQKEELAELLRalyrlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELE 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622865983 534 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKREQMERRLRTWLER 590
Cdd:COG4942   178 ALLAELEEERAALEALKAERQ---KLLARLEKELAELAAELAELQQEAEELEALIAR 231
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
417-599 4.08e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 417 ADKLHKFEKELQRISEAYESLVKSTtkreSLDKAMRNKLEGEIRRLHDFNRDLRDRLETANRQLS--SREYEGHEDKAAE 494
Cdd:PRK02224  278 AEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQahNEEAESLREDADD 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 495 ghYASQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQAL----------------------------SNAQARVIKL 546
Cdd:PRK02224  354 --LEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerfgdapvdlgnaedfleelreerDELREREAEL 431

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622865983 547 EEELREKQAYVEKVEKLQ---------QALTQLQSAC---EKREQMERrlrtwLERELDALRTQQ 599
Cdd:PRK02224  432 EATLRTARERVEEAEALLeagkcpecgQPVEGSPHVEtieEDRERVEE-----LEAELEDLEEEV 491
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 385-645 5.36e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 40.72  E-value: 5.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  385 AFAIVERAQQMVEILTEENRVLHQELQGYYDNA-DKLHKFEKELQRISEAY----ESLVKSTTKRESLDKAMR------- 452
Cdd:TIGR00618  185 EFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYhERKQVLEKELKHLREALqqtqQSHAYLTQKREAQEEQLKkqqllkq 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  453 -----NKLEGEIRRLHDFNRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASED--- 524
Cdd:TIGR00618  265 lrariEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEeqr 344

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  525 ------HRRHIEILDQalsNAQARVIKleEELREKQAYVEKVEKLQQALT----QLQSACEKREQMERRLRTWLERELD- 593
Cdd:TIGR00618  345 rllqtlHSQEIHIRDA---HEVATSIR--EISCQQHTLTQHIHTLQQQKTtltqKLQSLCKELDILQREQATIDTRTSAf 419

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622865983  594 -ALRTQQKHGNGQpaNVPEYNAPALLELVREKEERILALE-ADMTKWEQKYLEE 645
Cdd:TIGR00618  420 rDLQGQLAHAKKQ--QELQQRYAELCAAAITCTAQCEKLEkIHLQESAQSLKER 471
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
527-703 5.91e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 5.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 527 RHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKREQMERRLRTWLEREldALRTQQKHGngqp 606
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE--ALEAELAEL---- 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 607 anvpeynaPALLELVREKEERILALEADMTKWEQKYLEESTIRHFAMNAAATAAAERDTTIINHSRNGSYGESSLEAHIW 686
Cdd:COG4717   145 --------PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELE 216

                         170
                  ....*....|....*..
gi 1622865983 687 QEEEEVVQANRRCQDME 703
Cdd:COG4717   217 EAQEELEELEEELEQLE 233
PRK09039 PRK09039
peptidoglycan -binding protein;
448-588 6.23e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.95  E-value: 6.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 448 DKAMrNKLEGEIRRLHDF-------NRDLRDRLETANRQLSSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRT 520
Cdd:PRK09039   52 DSAL-DRLNSQIAELADLlslerqgNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKQ 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983 521 ASEDHRRHIEILDQALSNAQARVIKLEEEL-------REKQAyvekveKLQQALTQLQSACEKR-EQMER-------RLR 585
Cdd:PRK09039  131 VSARALAQVELLNQQIAALRRQLAALEAALdasekrdRESQA------KIADLGRRLNVALAQRvQELNRyrseffgRLR 204


                  ...
gi 1622865983 586 TWL 588
Cdd:PRK09039  205 EIL 207
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 408-579 8.65e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.77  E-value: 8.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  408 QELQGYYDN--------ADKLHKFEKELQRISEAYESLVKSTTK---------------RESLDKAMRNKLE--GEIRRL 462
Cdd:pfam01576  415 QELQARLSEserqraelAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesqlqdtQELLQEETRQKLNlsTRLRQL 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  463 HDFNRDLRDRLETanrqlssreyEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEDHRRhieildqalsnAQAR 542
Cdd:pfam01576  495 EDERNSLQEQLEE----------EEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKR-----------LQRE 553

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1622865983  543 VIKLEEELREKQAYVEKVEK----LQQALT----------QLQSACEKREQ 579
Cdd:pfam01576  554 LEALTQQLEEKAAAYDKLEKtknrLQQELDdllvdldhqrQLVSNLEKKQK 604
PTZ00121 PTZ00121
MAEBL; Provisional
 401-645 8.86e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 8.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  401 EENRVLHQELQGYYDNADKLHKFEKELQRISEAYESLVKSTTKRESldKAMRNKLEgEIRRLHDFNRDLRDRLETANRQL 480
Cdd:PTZ00121  1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKA--DEAKKKAE-EAKKAEEAKKKAEEAKKADEAKK 1477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  481 SSREYEGHEDKAAEGHYASQNKEFLKEKEKLEMELAAVRTASEdhRRHIEILDQALSNAQARVIKLEEELReKQAYVEKV 560
Cdd:PTZ00121  1478 KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKK-KADELKKA 1554

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622865983  561 EKLQQAlTQLQSACEKREQMERRlRTWLERELDALRTQQKHGNGQPANVPEYNAPALLELVREKEERILALEADMTKWEQ 640
Cdd:PTZ00121  1555 EELKKA-EEKKKAEEAKKAEEDK-NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632


                   ....*
gi 1622865983  641 KYLEE 645
Cdd:PTZ00121  1633 KKVEQ 1637
 
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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