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Conserved domains on  [gi|568960194|ref|XP_006510729|]
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angiomotin-like protein 1 isoform X2 [Mus musculus]

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 ...
 653-859 5.91e-109

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: 335.97  E-value: 5.91e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   653 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGTGPPVSLPECNAPALMELVREKEERILALEADM 732
Cdd:pfam12240    1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   733 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 812
Cdd:pfam12240   81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 568960194   813 KDAMIKVLQQRSRKDAGKTDSASLRPARSVPSI-AAATGTHSRQTSLT 859
Cdd:pfam12240  153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 484-742 3.52e-09

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: 61.11  E-value: 3.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  484 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRTKLEGEIRRLHDFN 563
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  564 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 643
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  644 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgtgppvslpecnapALMELVREKEE 723
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456

                         250
                  ....*....|....*....
gi 568960194  724 RILALEADMTKWEQKYLEE 742
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 ...
 653-859 5.91e-109

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: 335.97  E-value: 5.91e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   653 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGTGPPVSLPECNAPALMELVREKEERILALEADM 732
Cdd:pfam12240    1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   733 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 812
Cdd:pfam12240   81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 568960194   813 KDAMIKVLQQRSRKDAGKTDSASLRPARSVPSI-AAATGTHSRQTSLT 859
Cdd:pfam12240  153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 484-742 3.52e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 3.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  484 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRTKLEGEIRRLHDFN 563
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  564 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 643
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  644 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgtgppvslpecnapALMELVREKEE 723
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456

                         250
                  ....*....|....*....
gi 568960194  724 RILALEADMTKWEQKYLEE 742
Cdd:COG1196   457 EEEALLELLAELLEEAALL 475
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 481-742 8.31e-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: 59.70  E-value: 8.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   481 DAFAIVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRE-SLDKAMRTKLEGEIRRL 559
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   560 HDFNRDLRDRLETANRQLSSREYdghedkaaESHYVSQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILDQALSNAQA 638
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRLTL--------EKEYLEKEIQELQEQrIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   639 RVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKH-GTGPPVSLPECNAPA 713
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkGEDEEIPEEELSLED 955

                          250       260
                   ....*....|....*....|....*....
gi 568960194   714 LMELVREKEERILALEADMTKWEQKYLEE 742
Cdd:TIGR02169  956 VQAELQRVEEEIRALEPVNMLAIQEYEEV 984
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
505-673 7.05e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 7.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  505 QELQGCYDNADKLHKFEKELQSISEAYESLvksttkRESLDKAmRTKLEGEIRRLhdfnRDLRDRLETANRQLSSREYdg 584
Cdd:PRK03918  595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEY-- 661

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  585 hedkaaeshyvsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 664
Cdd:PRK03918  662 --------------EELREEYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720


                  ....*....
gi 568960194  665 TQLQSACEK 673
Cdd:PRK03918  721 ERVEELREK 729
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 487-669 3.17e-05

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: 47.89  E-value: 3.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   487 ERAQQMVEIlteENRVLHQELQgcydnadkLHKFEKELQSISEAYE---SLVKSTTKRESLDKAMRTKlEGEIRRLHDFN 563
Cdd:pfam10174  182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   564 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKeFLKEK--------EKLEMELAAVRTASE-------DHRRHIEI 628
Cdd:pfam10174  250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK-FMKNKidqlkqelSKKESELLALQTKLEtltnqnsDCKQHIEV 328

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 568960194   629 LDQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQLQS 669
Cdd:pfam10174  329 LKESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEEKS 376
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 515-687 1.11e-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: 44.65  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  515 DKLHKFEKELQSISEAYESLVKsttKRESLDKAMRtKLEGEIRRLHDFNRDLRDRLETANRQLSSReydgHEDKAAESH- 593
Cdd:cd07596    11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSALG-EFGKALIKLAKCEEEVGGELGEALSKLGKA----AEELSSLSEa 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  594 YVSQNKEFLKE--KEKLEMeLAAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEK-LQQALTQL 667
Cdd:cd07596    83 QANQELVKLLEplKEYLRY-CQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEeLEEAESAL 161

                         170       180
                  ....*....|....*....|
gi 568960194  668 QSACEKRGQMERRLRTWLER 687
Cdd:cd07596   162 EEARKRYEEISERLKEELKR 181
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
631-692 1.23e-04

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


Pssm-ID: 442400 [Multi-domain]  Cd Length: 202  Bit Score: 44.17  E-value: 1.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960194  631 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKRGQMERRLRTwlERELDAL 692
Cdd:COG3167    46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 551-813 1.31e-04

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: 46.20  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   551 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD 630
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   631 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQ--KHGTGPPVSLPE 708
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAE---AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerLESLERRIAATE 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   709 CNAPALMELVREKEERILALEADMTKWE----------QKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSL 778
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 568960194   779 EAhiwpEEEEVVQANRRCQDMEYTIKNLHAKIIEK 813
Cdd:TIGR02168  918 EE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
 
Name Accession Description Interval E-value
Angiomotin_C pfam12240
Angiomotin C terminal; This domain family is found in eukaryotes, and is typically between 197 ...
 653-859 5.91e-109

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: 335.97  E-value: 5.91e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   653 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKHGTGPPVSLPECNAPALMELVREKEERILALEADM 732
Cdd:pfam12240    1 YVEKVERLQQALAQLQAACEKREQLELRLRTRLEQELKSLRAQQRQGGSQGSGPSEYSAPALMELLREKEERILALEADM 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   733 TKWEQKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYgESSLeahiwpeEEEVVQANRRCQDMEYTIKNLHAKIIE 812
Cdd:pfam12240   81 TKWEQKYLEESTMRQFAMDAAATAAAQRDTTIINHSPRHSY-DSSF-------NEELLLANRRCQEMENRIKNLHAQILE 152

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 568960194   813 KDAMIKVLQQRSRKDAGKTDSASLRPARSVPSI-AAATGTHSRQTSLT 859
Cdd:pfam12240  153 KDAMIKVLQQRSRKDPGKTDQQSLRPARSVPSIsAAATGLHSRQTSLS 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 484-742 3.52e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 3.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  484 AIVERAQQMVEILTEENRVLHQELQgcyDNADKLHKFEKELQSISEAYESLVKSttkresldkamRTKLEGEIRRLHDFN 563
Cdd:COG1196   246 AELEELEAELEELEAELAELEAELE---ELRLELEELELELEEAQAEEYELLAE-----------LARLEQDIARLEERR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  564 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKL 643
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  644 EEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgtgppvslpecnapALMELVREKEE 723
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE---------------EAAEEEAELEE 456

                         250
                  ....*....|....*....
gi 568960194  724 RILALEADMTKWEQKYLEE 742
Cdd:COG1196   457 EEEALLELLAELLEEAALL 475
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 481-742 8.31e-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: 59.70  E-value: 8.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   481 DAFAIVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRE-SLDKAMRTKLEGEIRRL 559
Cdd:TIGR02169  724 EIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKL 803

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   560 HDFNRDLRDRLETANRQLSSREYdghedkaaESHYVSQNKEFLKEK-EKLEMELAAVRTASEDHRRHIEILDQALSNAQA 638
Cdd:TIGR02169  804 EEEVSRIEARLREIEQKLNRLTL--------EKEYLEKEIQELQEQrIDLKEQIKSIEKEIENLNGKKEELEEELEELEA 875

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   639 RVIKLEEELREKQAYVEKVEK----LQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKH-GTGPPVSLPECNAPA 713
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEAqlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPkGEDEEIPEEELSLED 955

                          250       260
                   ....*....|....*....|....*....
gi 568960194   714 LMELVREKEERILALEADMTKWEQKYLEE 742
Cdd:TIGR02169  956 VQAELQRVEEEIRALEPVNMLAIQEYEEV 984
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
512-696 2.78e-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: 2.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  512 DNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEgEIRRLHDFNRDLRDRLETAnrqlssREYDGHEDKAAE 591
Cdd:COG4913   607 DNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERRE-ALQRLAEYSWDEIDVASAE------REIAELEAELER 679

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  592 shyVSQNKEFLKEkekLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAltQLQSAC 671
Cdd:COG4913   680 ---LDASSDDLAA---LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL--ELRALL 751

                         170       180       190
                  ....*....|....*....|....*....|.
gi 568960194  672 EKR------GQMERRLRTWLERELDALRTQQ 696
Cdd:COG4913   752 EERfaaalgDAVERELRENLEERIDALRARL 782
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 478-823 7.75e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 7.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   478 LGPDAFAIVEraQQMV-EILT---EENRVLHQELQGcydnADKLHKFEKE-LQSISEAYESLVKSTTKRESLDKAMRtKL 552
Cdd:TIGR02168  133 LGKRSYSIIE--QGKIsEIIEakpEERRAIFEEAAG----ISKYKERRKEtERKLERTRENLDRLEDILNELERQLK-SL 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   553 EGEIRRLHDFnRDLRDRLETANRQLSSREYDGHEDKAAE-----SHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIE 627
Cdd:TIGR02168  206 ERQAEKAERY-KELKAELRELELALLVLRLEELREELEElqeelKEAEEELEELTAELQELEEKLEELRLEVSELEEEIE 284

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   628 ILDQALSNAQARVIKLEEELREKQayvekvEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQQKhgtgppVSLP 707
Cdd:TIGR02168  285 ELQKELYALANEISRLEQQKQILR------ERLANLERQLEELEAQLEELESKLDE-LAEELAELEEKLE------ELKE 351

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   708 ECNapALMELVREKEERILALEADMTKWEQKYLEESTIRHfamsaaaaATAERDTTISNH-SRNGSYGEsSLEAHIWPEE 786
Cdd:TIGR02168  352 ELE--SLEAELEELEAELEELESRLEELEEQLETLRSKVA--------QLELQIASLNNEiERLEARLE-RLEDRRERLQ 420

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 568960194   787 EEVVQANRRCQDMEytIKNLHAKIIEKDAMIKVLQQR 823
Cdd:TIGR02168  421 QEIEELLKKLEEAE--LKELQAELEELEEELEELQEE 455
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 485-730 7.95e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.60  E-value: 7.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   485 IVERAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEGEIRRLHDFNR 564
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   565 DLRDRLETANRQLSSREYDGHEDKAAESH--YVSQNKEFLkEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIK 642
Cdd:TIGR02168  387 KVAQLELQIASLNNEIERLEARLERLEDRreRLQQEIEEL-LKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   643 LEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTwlerELDALRTQQKHGTGPPVSLpecnaPALMELVREKE 722
Cdd:TIGR02168  466 LREELEEAE---QALDAAERELAQLQARLDSLERLQENLEG----FSEGVKALLKNQSGLSGIL-----GVLSELISVDE 533


                   ....*...
gi 568960194   723 ERILALEA 730
Cdd:TIGR02168  534 GYEAAIEA 541
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
481-697 1.75e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  481 DAFAIVERAQQMVEILTEENRvLHQELQGCYDNADKLhkfeKELQSISEAYESlvksTTKRESLDKAMRtKLEGEIRRLH 560
Cdd:COG4913   239 RAHEALEDAREQIELLEPIRE-LAERYAAARERLAEL----EYLRAALRLWFA----QRRLELLEAELE-ELRAELARLE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  561 DFNRDLRDRLETANRQLSS--REYDGHEdkaaeshyvsqnkefLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQA 638
Cdd:COG4913   309 AELERLEARLDALREELDEleAQIRGNG---------------GDRLEQLEREIERLERELEERERRRARLEALLAALGL 373

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960194  639 RVIKLEEELREKQAyveKVEKLQQALTQLQSACE--------KRGQMERRLRTwLERELDALRTQQK 697
Cdd:COG4913   374 PLPASAEEFAALRA---EAAALLEALEEELEALEealaeaeaALRDLRRELRE-LEAEIASLERRKS 436
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
494-685 5.09e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.62  E-value: 5.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  494 EILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLvksttkresldKAMRTKLEGEIRRLHDF--NRDLRDRLE 571
Cdd:COG4717    67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEEL-----------EAELEELREELEKLEKLlqLLPLYQELE 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  572 TANRQLSS--REYDGHEDKAAESHYVSQNKEFLKEK-EKLEMELA-AVRTASEDHRRHIEILDQALSNAQARVIKLEEEL 647
Cdd:COG4717   136 ALEAELAElpERLEELEERLEELRELEEELEELEAElAELQEELEeLLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 568960194  648 REKQayvEKVEKLQQALTQLQSACEkRGQMERRLRTWL 685
Cdd:COG4717   216 EEAQ---EELEELEEELEQLENELE-AAALEERLKEAR 249
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 506-687 5.72e-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: 5.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  506 ELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEGEIRRLHDFNRDLRDRLETANRQL----SSRE 581
Cdd:COG1579    11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLgnvrNNKE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  582 YDG--HEDKAAEshyvsqnkeflKEKEKLEMELAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQA-YVEKVE 658
Cdd:COG1579    91 YEAlqKEIESLK-----------RRISDLEDEILELMER-------IEELEEELAELEAELAELEAELEEKKAeLDEELA 152

                         170       180       190
                  ....*....|....*....|....*....|
gi 568960194  659 KLQQALTQLQSACEK-RGQMERRLRTWLER 687
Cdd:COG1579   153 ELEAELEELEAEREElAAKIPPELLALYER 182
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
505-673 7.05e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.53  E-value: 7.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  505 QELQGCYDNADKLHKFEKELQSISEAYESLvksttkRESLDKAmRTKLEGEIRRLhdfnRDLRDRLETANRQLSSREYdg 584
Cdd:PRK03918  595 KELEPFYNEYLELKDAEKELEREEKELKKL------EEELDKA-FEELAETEKRL----EELRKELEELEKKYSEEEY-- 661

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  585 hedkaaeshyvsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSnaqarviKLEEELREKQAYVEKVEKLQQAL 664
Cdd:PRK03918  662 --------------EELREEYLELSRELAGLRAELEELEKRREEIKKTLE-------KLKEELEEREKAKKELEKLEKAL 720


                  ....*....
gi 568960194  665 TQLQSACEK 673
Cdd:PRK03918  721 ERVEELREK 729
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 487-697 1.61e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  487 ERAQQmveiLTEENRVLHQELQgcydnADKLHKFEKELQSISEAYESLvksTTKRESLDKAMRtKLEGEIRRLhdfnRDL 566
Cdd:COG1196   213 ERYRE----LKEELKELEAELL-----LLKLRELEAELEELEAELEEL---EAELEELEAELA-ELEAELEEL----RLE 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  567 RDRLETANRQLSSREYdghedkaaeshyvsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE 646
Cdd:COG1196   276 LEELELELEEAQAEEY-----------------ELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568960194  647 LREKQA--------YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQK 697
Cdd:COG1196   339 LEELEEeleeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
515-723 5.11e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 5.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  515 DKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRtKLEGEIRRLHDFNRDLRDRLETANRQLSSREydgheDKAAEShy 594
Cdd:PRK03918  214 SELPELREELEKLEKEVKELEELKEEIEELEKELE-SLEGSKRKLEEKIRELEERIEELKKEIEELE-----EKVKEL-- 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  595 vsqnkEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKR 674
Cdd:PRK03918  286 -----KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER 360

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 568960194  675 GQMERRLRTwLERELDALRTQQKHGTgppvslPECNAPALMELVREKEE 723
Cdd:PRK03918  361 HELYEEAKA-KKEELERLKKRLTGLT------PEKLEKELEELEKAKEE 402
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
536-738 1.98e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  536 KSTTkRESLDKAMRTKLEGEIRRLHDFN----RDLRDRLETANRQLssreydgHEDKAAESHYvsqnKEFLKEKEKLEME 611
Cdd:COG4717    36 KSTL-LAFIRAMLLERLEKEADELFKPQgrkpELNLKELKELEEEL-------KEAEEKEEEY----AELQEELEELEEE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  612 LAAVRTASEDHRRHIEILDQALSNAQ--ARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTwLEREL 689
Cdd:COG4717   104 LEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELP---ERLEELEERLEELRELEEELEELEAELAE-LQEEL 179

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568960194  690 DALRTQqkhgtgppvsLPECNAPALMELVREKEE---RILALEADMTKWEQK 738
Cdd:COG4717   180 EELLEQ----------LSLATEEELQDLAEELEElqqRLAELEEELEEAQEE 221
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
484-743 3.15e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.14  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  484 AIVERAQQMVEILTEE---NRVLHQELQ-GCYDNADK-LHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEG---E 555
Cdd:PRK03918  129 AIYIRQGEIDAILESDesrEKVVRQILGlDDYENAYKnLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEvlrE 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  556 IRRLHDFNRDLRDRLETANRQLssREYDGHEDKAAESHyvsqnkeflKEKEKLEMELAAvrtasedhrrhieiLDQALSN 635
Cdd:PRK03918  209 INEISSELPELREELEKLEKEV--KELEELKEEIEELE---------KELESLEGSKRK--------------LEEKIRE 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  636 AQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQQKhgtgppvslpecNAPALM 715
Cdd:PRK03918  264 LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELRE-IEKRLSRLEEEIN------------GIEERI 330

                         250       260       270
                  ....*....|....*....|....*....|
gi 568960194  716 ELVREKEERILALEADMTKWEQKY--LEES 743
Cdd:PRK03918  331 KELEEKEERLEELKKKLKELEKRLeeLEER 360
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 487-669 3.17e-05

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: 47.89  E-value: 3.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   487 ERAQQMVEIlteENRVLHQELQgcydnadkLHKFEKELQSISEAYE---SLVKSTTKRESLDKAMRTKlEGEIRRLHDFN 563
Cdd:pfam10174  182 ERTRRIAEA---EMQLGHLEVL--------LDQKEKENIHLREELHrrnQLQPDPAKTKALQTVIEMK-DTKISSLERNI 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   564 RDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKeFLKEK--------EKLEMELAAVRTASE-------DHRRHIEI 628
Cdd:pfam10174  250 RDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSK-FMKNKidqlkqelSKKESELLALQTKLEtltnqnsDCKQHIEV 328

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 568960194   629 LDQALSNAQARVIKLEEE-------LREKQAYVEKVEKLQQALTQLQS 669
Cdd:pfam10174  329 LKESLTAKEQRAAILQTEvdalrlrLEEKESFLNKKTKQLQDLTEEKS 376
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 512-696 4.80e-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: 47.48  E-value: 4.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   512 DNADKLHKFEKELQS-ISEAYESLVKSTTKRESLDKaMRTKLEGEIRRLHDFNR---DLRDRLETANRQLSSREYDGHED 587
Cdd:pfam01576  145 DQNSKLSKERKLLEErISEFTSNLAEEEEKAKSLSK-LKNKHEAMISDLEERLKkeeKGRQELEKAKRKLEGESTDLQEQ 223

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   588 KAAESHYVSQNKEFLKEKEKlemELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQL 667
Cdd:pfam01576  224 IAELQAQIAELRAQLAKKEE---ELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300

                          170       180
                   ....*....|....*....|....*....
gi 568960194   668 QSAcekrgqmerrLRTWLERELDALRTQQ 696
Cdd:pfam01576  301 LEA----------LKTELEDTLDTTAAQQ 319
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
487-695 6.81e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 6.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  487 ERAQQMVEILTEENRVLHQELQgcydnadklhKFEKELQSISEAYeSLVKSTTKRESLDKAMRTkLEGEIRRLHDFNRDL 566
Cdd:COG3206   171 EEARKALEFLEEQLPELRKELE----------EAEAALEEFRQKN-GLVDLSEEAKLLLQQLSE-LESQLAEARAELAEA 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  567 RDRLETANRQLSSREydgheDKAAESHYVSQNKEFLKEKEKLEMELAAVR-TASEDHRRHIEI---LDQALSNAQARVIK 642
Cdd:COG3206   239 EARLAALRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAELAELSaRYTPNHPDVIALraqIAALRAQLQQEAQR 313

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568960194  643 LEEELR-EKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTwLERELDALRTQ 695
Cdd:COG3206   314 ILASLEaELEALQAREASLQAQLAQLEARLAELPELEAELRR-LEREVEVAREL 366
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 502-742 1.06e-04

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: 46.25  E-value: 1.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   502 VLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLeGEIRRLHDFNRdlrdRLETANRQLSSRE 581
Cdd:pfam05483  364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIL-AEDEKLLDEKK----QFEKIAEELKGKE 438

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   582 ydghedkaAESHYVSQNKEflKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEE-----LREKQAYVEK 656
Cdd:pfam05483  439 --------QELIFLLQARE--KEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHcdkllLENKELTQEA 508

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   657 VEKLQQALTQLQSACEKRGQMERRLR---------TWLERELDALR---TQQKHGTGPPVSLPECNAPALMELVREKEER 724
Cdd:pfam05483  509 SDMTLELKKHQEDIINCKKQEERMLKqienleekeMNLRDELESVReefIQKGDEVKCKLDKSEENARSIEYEVLKKEKQ 588

                          250       260
                   ....*....|....*....|....
gi 568960194   725 ILALEADMTKWEQ------KYLEE 742
Cdd:pfam05483  589 MKILENKCNNLKKqienknKNIEE 612
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 515-687 1.11e-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: 44.65  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  515 DKLHKFEKELQSISEAYESLVKsttKRESLDKAMRtKLEGEIRRLHDFNRDLRDRLETANRQLSSReydgHEDKAAESH- 593
Cdd:cd07596    11 DYILKLEEQLKKLSKQAQRLVK---RRRELGSALG-EFGKALIKLAKCEEEVGGELGEALSKLGKA----AEELSSLSEa 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  594 YVSQNKEFLKE--KEKLEMeLAAVRTASEDH---RRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEK-LQQALTQL 667
Cdd:cd07596    83 QANQELVKLLEplKEYLRY-CQAVKETLDDRadaLLTLQSLKKDLASKKAQLEKLKAAPGIKPAKVEELEEeLEEAESAL 161

                         170       180
                  ....*....|....*....|
gi 568960194  668 QSACEKRGQMERRLRTWLER 687
Cdd:cd07596   162 EEARKRYEEISERLKEELKR 181
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
631-692 1.23e-04

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


Pssm-ID: 442400 [Multi-domain]  Cd Length: 202  Bit Score: 44.17  E-value: 1.23e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960194  631 QALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQsacEKRGQMERRLRTwlERELDAL 692
Cdd:COG3167    46 EELEELEAEEAQLKQELEKKQAKAANLPALKAQLEELE---QQLGELLKQLPS--KAEVPAL 102
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 551-813 1.31e-04

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: 46.20  E-value: 1.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   551 KLEGEIRRLHDFNRDLRDRLETANRQLSSREYDGHEDKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILD 630
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE 760

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   631 QALSNAQARVIKLEEELREKQayvEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQ--KHGTGPPVSLPE 708
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAE---AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRerLESLERRIAATE 837

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   709 CNAPALMELVREKEERILALEADMTKWE----------QKYLEESTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSL 778
Cdd:TIGR02168  838 RRLEDLEEQIEELSEDIESLAAEIEELEelieeleselEALLNERASLEEALALLRSELEELSEELRELESKRSELRREL 917

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 568960194   779 EAhiwpEEEEVVQANRRCQDMEYTIKNLHAKIIEK 813
Cdd:TIGR02168  918 EE----LREKLAQLELRLEGLEVRIDNLQERLSEE 948
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 514-697 1.54e-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: 45.14  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  514 ADKLHKFEKELQSISE---AYESLVKSTTKRESLDKAMRTKLEGEIRRLHDFNRDLRDRLETANRQLSS---------RE 581
Cdd:COG4942    19 ADAAAEAEAELEQLQQeiaELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekeiaelrAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  582 YDGHEDKAAE---SHYVSQNKEFLK------EKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQA 652
Cdd:COG4942    99 LEAQKEELAEllrALYRLGRQPPLAlllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568960194  653 YVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQK 697
Cdd:COG4942   179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE 223
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
487-724 1.60e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 45.83  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  487 ERAQQMVEILTEENRVLHQelqgcYDNADKLHKFEKELQSISeaYESLVKSTTKRESLDKAMRtKLEGEIRRLH-DFNR- 564
Cdd:PRK03918  480 KELRELEKVLKKESELIKL-----KELAEQLKELEEKLKKYN--LEELEKKAEEYEKLKEKLI-KLKGEIKSLKkELEKl 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  565 -DLRDRLETANRQLssreyDGHEDKAAESHYVSQNKEFLKEKEkLEMELAAVRTASE------DHRRHIEILDQALSNAQ 637
Cdd:PRK03918  552 eELKKKLAELEKKL-----DELEEELAELLKELEELGFESVEE-LEERLKELEPFYNeylelkDAEKELEREEKELKKLE 625

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  638 ARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRGQMERRLRtwLERELDALRTQQKHGTgppvSLPECNAPALMEL 717
Cdd:PRK03918  626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLE--LSRELAGLRAELEELE----KRREEIKKTLEKL 699


                  ....*..
gi 568960194  718 VREKEER 724
Cdd:PRK03918  700 KEELEER 706
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
521-660 2.24e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 45.23  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  521 EKELQSISEAYESLVKST-TKRESLDKAMRtKLEGEIRRLHDFNRDLRDRLETANRQLSSREYDGHEDKAAEshyvsqNK 599
Cdd:COG2433   387 EKELPEEEPEAEREKEHEeRELTEEEEEIR-RLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEE------RR 459

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960194  600 EFLKEKE--KLEMELAAVRTASEDHRRHIEILdqalsnaQARVIKLEE----ELREKQAYVEKVEKL 660
Cdd:COG2433   460 EIRKDREisRLDREIERLERELEEERERIEEL-------KRKLERLKElwklEHSGELVPVKVVEKF 519
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 478-742 2.33e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 2.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  478 LGPDAFAIVEraQQMV-EILT---EENRVLhqelqgcydnadklhkFEkELQSISEAYEslvkstTKRESLDK--AMRTK 551
Cdd:COG1196   133 LGPESYSIIG--QGMIdRIIEakpEERRAI----------------IE-EAAGISKYKE------RKEEAERKleATEEN 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  552 LEgeirRLHDFNRDLRDRLETANRQlssREydghedkAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQ 631
Cdd:COG1196   188 LE----RLEDILGELERQLEPLERQ---AE-------KAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEA 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  632 ALSNAQARVIKLEEELRE-KQAYVEKVEKLQQALTQLQSACEKRGQMERRLRTWLERELDALRTQQKhgtgppvslpecn 710
Cdd:COG1196   254 ELEELEAELAELEAELEElRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE------------- 320

                         250       260       270
                  ....*....|....*....|....*....|..
gi 568960194  711 apaLMELVREKEERILALEADMTKWEQKYLEE 742
Cdd:COG1196   321 ---LEEELAELEEELEELEEELEELEEELEEA 349
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 486-823 2.81e-04

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: 45.05  E-value: 2.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   486 VERAQQMVEILTEENRVLHQELqgcydnADKLHKFEKELQSISEAYESLVkstTKRESLDKAMRTkLEGEIRRLHDFNRD 565
Cdd:TIGR02168  209 AEKAERYKELKAELRELELALL------VLRLEELREELEELQEELKEAE---EELEELTAELQE-LEEKLEELRLEVSE 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   566 LRDRLETANRQLssreydghedkaaeshyvsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEE 645
Cdd:TIGR02168  279 LEEEIEELQKEL---------------------YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAE 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   646 ELREKQAYVEKVEKLQQALT-QLQSACEKRGQMERRLRTwLERELDALRTQqkhgtgppVSLPECNAPALMELVREKEER 724
Cdd:TIGR02168  338 ELAELEEKLEELKEELESLEaELEELEAELEELESRLEE-LEEQLETLRSK--------VAQLELQIASLNNEIERLEAR 408

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   725 ILALEADMTKWEQkyleesTIRHFAMSAAAAATAERDTTISNHSRNGSYGESSLEAHIWPEE---EEVVQANRRCQDMEY 801
Cdd:TIGR02168  409 LERLEDRRERLQQ------EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEelrEELEEAEQALDAAER 482

                          330       340
                   ....*....|....*....|..
gi 568960194   802 TIKNLHAKIiekdAMIKVLQQR 823
Cdd:TIGR02168  483 ELAQLQARL----DSLERLQEN 500
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 493-677 4.34e-04

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: 42.82  E-value: 4.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  493 VEILTEENRVLHQELQGCYDNADKLHKFEKEL---------------QSISEAYESLVKSTTKResldkamRTKLEgEIR 557
Cdd:cd00176    35 VEALLKKHEALEAELAAHEERVEALNELGEQLieeghpdaeeiqerlEELNQRWEELRELAEER-------RQRLE-EAL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  558 RLHDFNRDLRD---RLETANRQLSSREYDGHEDKAaeshyvsqnKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALS 634
Cdd:cd00176   107 DLQQFFRDADDleqWLEEKEAALASEDLGKDLESV---------EELLKKHKELEEELEAHEPRLKSLNELAEELLEEGH 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 568960194  635 NAQARVIKleeelrekqayvEKVEKLQQALTQLQSACEKRGQM 677
Cdd:cd00176   178 PDADEEIE------------EKLEELNERWEELLELAEERQKK 208
RecN COG0497
DNA repair ATPase RecN [Replication, recombination and repair];
521-747 4.58e-04

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


Pssm-ID: 440263 [Multi-domain]  Cd Length: 555  Bit Score: 43.91  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  521 EKELQSISEAYESLVKSTTKRESLDKAMRtklegEIRRLHDFNRDLRDRLETANrqLSSREYdghEDKAAEshyvsqnKE 600
Cdd:COG0497   154 EELLEEYREAYRAWRALKKELEELRADEA-----ERARELDLLRFQLEELEAAA--LQPGEE---EELEEE-------RR 216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  601 FLKEKEKLemeLAAVRTAsedhrrhIEILDQALSNAQARVIKLEEELREKQAYVEK----VEKLQQALTQLQSACEK-RG 675
Cdd:COG0497   217 RLSNAEKL---REALQEA-------LEALSGGEGGALDLLGQALRALERLAEYDPSlaelAERLESALIELEEAASElRR 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  676 QMER------RLRTWLEReLDALRT-QQKHGtgppVSLPEcnAPALMELVREK-------EERILALEADMTKWEQKYLE 741
Cdd:COG0497   287 YLDSlefdpeRLEEVEER-LALLRRlARKYG----VTVEE--LLAYAEELRAElaelensDERLEELEAELAEAEAELLE 359

                         250
                  ....*....|
gi 568960194  742 E----STIRH 747
Cdd:COG0497   360 AaeklSAARK 369
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 596-742 5.51e-04

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: 42.60  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  596 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSAcekrg 675
Cdd:COG1579    17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA---RIKKYEEQLGNVRNN----- 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960194  676 qmeRRLRTwLERELDALRTQQkhgtgppvSLPECNAPALMELVREKEERILALEADMTKWEQKYLEE 742
Cdd:COG1579    89 ---KEYEA-LQKEIESLKRRI--------SDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
540-734 1.24e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  540 KRESLDKamrtkLEGEIRRLHDfnRDLRDRLETANRQLSS-----REYDGHEDKAAE-----SHYVSQNKEFLKEKEKLE 609
Cdd:PRK02224  185 QRGSLDQ-----LKAQIEEKEE--KDLHERLNGLESELAEldeeiERYEEQREQAREtrdeaDEVLEEHEERREELETLE 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  610 MELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLQSACEKRgqmerrlRTWLEREL 689
Cdd:PRK02224  258 AEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDR-------DEELRDRL 330

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568960194  690 DALRTQQKHGTGPPVSLPEcNAPALMELVREKEERILALEADMTK 734
Cdd:PRK02224  331 EECRVAAQAHNEEAESLRE-DADDLEERAEELREEAAELESELEE 374
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 486-673 1.75e-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: 42.35  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   486 VERAQQMVEILTEENRVLHQELQGCYDNADKLhkfEKELQSISEAYESLvksTTKRESLDKAMRtKLEGEIRRLHDFNRD 565
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEEL---ESELEALLNERASL---EEALALLRSELE-ELSEELRELESKRSE 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   566 LRDRLETANRQLSS--REYDGHEDKaaeshyVSQNKEFLKEKEKLEMELAAvrtasedhrRHIEILDQALSNAQARVIKL 643
Cdd:TIGR02168  913 LRRELEELREKLAQleLRLEGLEVR------IDNLQERLSEEYSLTLEEAE---------ALENKIEDDEEEARRRLKRL 977

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 568960194   644 E-----------------EELREKQAYVEK-VEKLQQALTQLQSACEK 673
Cdd:TIGR02168  978 EnkikelgpvnlaaieeyEELKERYDFLTAqKEDLTEAKETLEEAIEE 1025
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 505-674 2.25e-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: 42.08  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   505 QELQGCYDN--------ADKLHKFEKELQSISEAYESLVKSTTK---------------RESLDKAMRTKLE--GEIRRL 559
Cdd:pfam01576  415 QELQARLSEserqraelAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesqlqdtQELLQEETRQKLNlsTRLRQL 494

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   560 HDFNRDLRDRLEtanRQLSSReydghedKAAESHYVSQNKEFLKEKEKLEMELAAVRTASEDHRRhieildqalsnAQAR 639
Cdd:pfam01576  495 EDERNSLQEQLE---EEEEAK-------RNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKR-----------LQRE 553

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 568960194   640 VIKLEEELREKQAYVEKVEK----LQQALT----------QLQSACEKR 674
Cdd:pfam01576  554 LEALTQQLEEKAAAYDKLEKtknrLQQELDdllvdldhqrQLVSNLEKK 602
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 491-738 2.73e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.96  E-value: 2.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   491 QMVEILTEENrvlhqelQGCYDNADKLHKFEKELQSISEAYESLVKST-TKRESLDKAMRTK-------------LEGEI 556
Cdd:TIGR00606  667 QFITQLTDEN-------QSCCPVCQRVFQTEAELQEFISDLQSKLRLApDKLKSTESELKKKekrrdemlglapgRQSII 739

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   557 RRLHDFNRDLRDRLETANRQLSSREYD-----------GHEDKAAES-----HYVSQNKEFLKEKEKLEMELAAvRTASE 620
Cdd:TIGR00606  740 DLKEKEIPELRNKLQKVNRDIQRLKNDieeqetllgtiMPEEESAKVcltdvTIMERFQMELKDVERKIAQQAA-KLQGS 818

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   621 DHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQAL-----------TQLQSACEKRGQMERRLRTwLEREL 689
Cdd:TIGR00606  819 DLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLksktnelksekLQIGTNLQRRQQFEEQLVE-LSTEV 897

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 568960194   690 DALRTQQKHGTGPPVSLpecnAPALMELVREKEERILALEADMTKWEQK 738
Cdd:TIGR00606  898 QSLIREIKDAKEQDSPL----ETFLEKDQQEKEELISSKETSNKKAQDK 942
Val_tRNA-synt_C pfam10458
Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA ...
 603-668 2.85e-03

Valyl tRNA synthetase tRNA binding arm; This domain is found at the C-terminus of Valyl tRNA synthetases.


Pssm-ID: 431296 [Multi-domain]  Cd Length: 66  Bit Score: 37.25  E-value: 2.85e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568960194   603 KEKEKLEMELAAVRTasedhrrHIEILDQALSN------AQARVIklEEELREKQAYVEKVEKLQQALTQLQ 668
Cdd:pfam10458    4 KERARLEKELAKLQK-------EIERVQGKLANpgfvakAPAEVV--EEEKAKLAELEEQAEKLRERLSKLG 66
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 488-739 3.70e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 41.57  E-value: 3.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   488 RAQQMVEILTEENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLD----------------KAMRTK 551
Cdd:TIGR00606  323 DCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDgfergpfserqiknfhTLVIER 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   552 LEGEIRRLHDFNRDLRDRLETANRQLssreyDGHEDKAAESHYVSQNKEFLKEKEKLEMelaavrtasedhrRHIEILDQ 631
Cdd:TIGR00606  403 QEDEAKTAAQLCADLQSKERLKQEQA-----DEIRDEKKGLGRTIELKKEILEKKQEEL-------------KFVIKELQ 464

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   632 ALSNAQARVIKLEEELREKQAYVEKVEKlqQALTQLQSACEKRGQMERrlrtwlereLDALRTQQKhgtgppvsLPECNA 711
Cdd:TIGR00606  465 QLEGSSDRILELDQELRKAERELSKAEK--NSLTETLKKEVKSLQNEK---------ADLDRKLRK--------LDQEME 525

                          250       260       270
                   ....*....|....*....|....*....|.
gi 568960194   712 palmELVREKEER--ILALEAD-MTKWEQKY 739
Cdd:TIGR00606  526 ----QLNHHTTTRtqMEMLTKDkMDKDEQIR 552
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
564-687 4.03e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  564 RDLRDRLETANRQLSS--------REYDGHEDKAAESHYvsqnkefLKEK---EKLEMELAAVRTASEDHRRHIEILDQA 632
Cdd:COG4913   238 ERAHEALEDAREQIELlepirelaERYAAARERLAELEY-------LRAAlrlWFAQRRLELLEAELEELRAELARLEAE 310

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  633 LSNAQARVIKLEEELRE-KQAY----VEKVEKLQQALTQLQSACEKRGQMERRLRTWLER 687
Cdd:COG4913   311 LERLEARLDALREELDElEAQIrgngGDRLEQLEREIERLERELEERERRRARLEALLAA 370
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 505-730 4.72e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.83  E-value: 4.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   505 QELQGCYDN-ADKLHKFEKELQSISEAYESLVKsttKRESLDK---AMRTKLEgEIRRLHdfnrdLRDRLETANRQLSSR 580
Cdd:pfam05622  193 QELHGKLSEeSKKADKLEFEYKKLEEKLEALQK---EKERLIIerdTLRETNE-ELRCAQ-----LQQAELSQADALLSP 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   581 EYDGHEDKAAESHYVSqnkefLKEK-EKLEMELAAVRTASE-DHRRHIEILDQALSNAQARVIKLEEELREKQAYV---- 654
Cdd:pfam05622  264 SSDPGDNLAAEIMPAE-----IREKlIRLQHENKMLRLGQEgSYRERLTELQQLLEDANRRKNELETQNRLANQRIlelq 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   655 EKVEKLQQALTQLQSACEKRGQMERRLRTWLE--RELDALR---TQQKHGTGPPVSL-PECNAPALMELVREKEERILAL 728
Cdd:pfam05622  339 QQVEELQKALQEQGSKAEDSSLLKQKLEEHLEklHEAQSELqkkKEQIEELEPKQDSnLAQKIDELQEALRKKDEDMKAM 418


                   ..
gi 568960194   729 EA 730
Cdd:pfam05622  419 EE 420
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
521-745 4.91e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  521 EKELQSISEAYESLVKSTTKRESLDKAMrTKLEGEIRRLHDFNRDLRDRLETANRQLSSREYDgHEDKAAESHYVSQNKE 600
Cdd:COG4372    34 RKALFELDKLQEELEQLREELEQAREEL-EQLEEELEQARSELEQLEEELEELNEQLQAAQAE-LAQAQEELESLQEEAE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  601 FLKEK-EKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAYVEKVEKLQQALTQLqsacEKRGQMER 679
Cdd:COG4372   112 ELQEElEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA----EAEQALDE 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568960194  680 RLRTWLERELDAlrTQQKHGTGPPVSLPECNAPALMELVREKEERILALEADMTKWEQKYLEESTI 745
Cdd:COG4372   188 LLKEANRNAEKE--EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 608-730 6.13e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 40.51  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194   608 LEMELAAVRTASEDHRRHI----EILDQALSNAQARVI----KLEEELREKQAYVEKVEKLQQALTQLQ-----SACEKR 674
Cdd:pfam07111  504 IQQEVGRAREQGEAERQQLsevaQQLEQELQRAQESLAsvgqQLEVARQGQQESTEEAASLRQELTQQQeiygqALQEKV 583

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 568960194   675 GQMERRLRTWL---ERELDALRTQQKHGTgppVSLPECNAPALMELVREKEERILALEA 730
Cdd:pfam07111  584 AEVETRLREQLsdtKRRLNEARREQAKAV---VSLRQIQHRATQEKERNQELRRLQDEA 639
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
487-696 6.71e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  487 ERAQQMVEILTEENRVLHQELQGCY----DNADKLHKFEKELQSISEAYESLVKSTtkreSLDKAMRTKLEGEIRRLHDF 562
Cdd:PRK02224  247 EERREELETLEAEIEDLRETIAETErereELAEEVRDLRERLEELEEERDDLLAEA----GLDDADAEAVEARREELEDR 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  563 NRDLRDRLETANRQLS--SREYDGHEDKAAESHyvSQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQAL------- 633
Cdd:PRK02224  323 DEELRDRLEECRVAAQahNEEAESLREDADDLE--ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIeelrerf 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  634 ---------------------SNAQARVIKLEEELREKQAYVEKVEKLQ---------QALTQLQSAC---EKRGQMERr 680
Cdd:PRK02224  401 gdapvdlgnaedfleelreerDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGSPHVEtieEDRERVEE- 479

                         250
                  ....*....|....*.
gi 568960194  681 lrtwLERELDALRTQQ 696
Cdd:PRK02224  480 ----LEAELEDLEEEV 491
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 596-840 8.27e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 8.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  596 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEILDQALSNAQARVIKLEEELREKQAyveKVEKLQQALTQLQSACEKRG 675
Cdd:COG4942    27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---ELAELEKEIAELRAELEAQK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  676 QMERRLrtwlereldaLRTQQKHGTGPPVSL---PECNAPALM------ELVREKEERILALEADMTKWEQKYLEESTIR 746
Cdd:COG4942   104 EELAEL----------LRALYRLGRQPPLALllsPEDFLDAVRrlqylkYLAPARREQAEELRADLAELAALRAELEAER 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  747 HFAMSAAAAATAERDttisnhsrngsygesSLEAHIWPEEEEVVQANRRCQDMEYTIKNLHAKIIEKDAMIKVLQQRSRK 826
Cdd:COG4942   174 AELEALLAELEEERA---------------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238

                         250
                  ....*....|....
gi 568960194  827 DAGKTDSASLRPAR 840
Cdd:COG4942   239 AAERTPAAGFAALK 252
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 519-683 9.12e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 39.91  E-value: 9.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  519 KFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEGEIRRL---HDFNRDLRDRLETANrqLSSREYDGHEDKAAESHYV 595
Cdd:PRK05771   86 ELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERLepwGNFDLDLSLLLGFKY--VSVFVGTVPEDKLEELKLE 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  596 SQNKEFLKEKEKLEMELAAVRTASEDHRRHIEIL----------------DQALSNAQARVIKLE---EELREK-QAYVE 655
Cdd:PRK05771  164 SDVENVEYISTDKGYVYVVVVVLKELSDEVEEELkklgferleleeegtpSELIREIKEELEEIEkerESLLEElKELAK 243

                         170       180
                  ....*....|....*....|....*...
gi 568960194  656 KVEKLQQALTQLQSACEKRGQMERRLRT 683
Cdd:PRK05771  244 KYLEELLALYEYLEIELERAEALSKFLK 271
PTZ00121 PTZ00121
MAEBL; Provisional
 498-742 9.84e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 9.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  498 EENRVLHQELQGCYDNADKLHKFEKELQSISEAYESLVKSTTKRESLDKAMRTKLEGEIRRLHDFNRDLRDRLETANRQL 577
Cdd:PTZ00121 1401 EEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  578 SSREYDGHEDKAAEShyvSQNKEFLKEKEKLEMELAAVRTASEdhRRHIEILDQALSNAQARVIKLEEELReKQAYVEKV 657
Cdd:PTZ00121 1481 EAKKADEAKKKAEEA---KKKADEAKKAAEAKKKADEAKKAEE--AKKADEAKKAEEAKKADEAKKAEEKK-KADELKKA 1554

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960194  658 EKLQQAlTQLQSACEKRGQMERRlRTWLERELDALRTQQKHGTGPPVSLPECNAPALMELVREKEERILALEADMTKWEQ 737
Cdd:PTZ00121 1555 EELKKA-EEKKKAEEAKKAEEDK-NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEK 1632


                  ....*
gi 568960194  738 KYLEE 742
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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