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Conserved domains on  [gi|118442834|ref|NP_056087|]
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protein fantom isoform a [Homo sapiens]

Protein Classification

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List of domain hits

Name Accession Description Interval E-value
C2-C2_1 pfam11618
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ...
597-738 1.52e-77

First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.


:

Pssm-ID: 463310  Cd Length: 143  Bit Score: 252.17  E-value: 1.52e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   597 TIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKN 676
Cdd:pfam11618    1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118442834   677 TITLEVHQAYSTEYETIAACQLKFHEILEK-SGRIFCTASLIGTKGDIPNFGTVEYWFRLRVP 738
Cdd:pfam11618   81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEIQIIGTLEYWIRLRVP 143
RPGR1_C pfam18111
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ...
1145-1308 2.26e-71

Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.


:

Pssm-ID: 465655  Cd Length: 166  Bit Score: 235.39  E-value: 2.26e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  1145 PSEKIRIEIIALSL-NDSQVTMDDTIQRLFVECRFYSLPAE--ETPVSLPKPKSGQWVYYNYSNVIYVDKENNKAKRDIL 1221
Cdd:pfam18111    1 DSDTIRIEIISLQLlNESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  1222 KAILQKQEMPNRSLRFTVVSDPPeDEQDLECEDIGVAHVDLADMFQEGRDLIEQNIDVFDARADGEGIGKLRVTVEALHA 1301
Cdd:pfam18111   81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159

                   ....*..
gi 118442834  1302 LQSVYKQ 1308
Cdd:pfam18111  160 LRAIYSE 166
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
201-543 2.38e-16

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: 84.99  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  201 LEEARGEIRNLENVIQSQRGQIEELEHLAEI------LKTQLRRKEneIELSLLQLREQQATDQRsnirdnvemikLHKQ 274
Cdd:COG1196   181 LEATEENLERLEDILGELERQLEPLERQAEKaeryreLKEELKELE--AELLLLKLRELEAELEE-----------LEAE 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  275 LVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHS----MKFSERRIEELQDRIND 350
Cdd:COG1196   248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleerRRELEERLEELEEELAE 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  351 LEKERELLKENYDKLydsafsAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQ 430
Cdd:COG1196   328 LEEELEELEEELEEL------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  431 YLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEIN------KDLERSMRELQATHAE 504
Cdd:COG1196   402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEallellAELLEEAALLEAALAE 481
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 118442834  505 TVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQD 543
Cdd:COG1196   482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
792-891 3.94e-13

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 66.71  E-value: 3.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  792 LHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMdldrylkSESLSFYVFDDSDT 871
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPE-------SDTLTVEVWDKDRF 73
                          90       100
                  ....*....|....*....|
gi 118442834  872 QENIYIGKVNVPLISLAHDR 891
Cdd:cd00030    74 SKDDFLGEVEIPLSELLDSG 93
 
Name Accession Description Interval E-value
C2-C2_1 pfam11618
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ...
597-738 1.52e-77

First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.


Pssm-ID: 463310  Cd Length: 143  Bit Score: 252.17  E-value: 1.52e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   597 TIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKN 676
Cdd:pfam11618    1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118442834   677 TITLEVHQAYSTEYETIAACQLKFHEILEK-SGRIFCTASLIGTKGDIPNFGTVEYWFRLRVP 738
Cdd:pfam11618   81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEIQIIGTLEYWIRLRVP 143
RPGR1_C pfam18111
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ...
1145-1308 2.26e-71

Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.


Pssm-ID: 465655  Cd Length: 166  Bit Score: 235.39  E-value: 2.26e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  1145 PSEKIRIEIIALSL-NDSQVTMDDTIQRLFVECRFYSLPAE--ETPVSLPKPKSGQWVYYNYSNVIYVDKENNKAKRDIL 1221
Cdd:pfam18111    1 DSDTIRIEIISLQLlNESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  1222 KAILQKQEMPNRSLRFTVVSDPPeDEQDLECEDIGVAHVDLADMFQEGRDLIEQNIDVFDARADGEGIGKLRVTVEALHA 1301
Cdd:pfam18111   81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159

                   ....*..
gi 118442834  1302 LQSVYKQ 1308
Cdd:pfam18111  160 LRAIYSE 166
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
201-543 2.38e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 84.99  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  201 LEEARGEIRNLENVIQSQRGQIEELEHLAEI------LKTQLRRKEneIELSLLQLREQQATDQRsnirdnvemikLHKQ 274
Cdd:COG1196   181 LEATEENLERLEDILGELERQLEPLERQAEKaeryreLKEELKELE--AELLLLKLRELEAELEE-----------LEAE 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  275 LVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHS----MKFSERRIEELQDRIND 350
Cdd:COG1196   248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleerRRELEERLEELEEELAE 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  351 LEKERELLKENYDKLydsafsAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQ 430
Cdd:COG1196   328 LEEELEELEEELEEL------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  431 YLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEIN------KDLERSMRELQATHAE 504
Cdd:COG1196   402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEallellAELLEEAALLEAALAE 481
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 118442834  505 TVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQD 543
Cdd:COG1196   482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
201-445 3.94e-16

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: 84.34  E-value: 3.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSN 280
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   281 ALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKE-------QRLKCCSLEKQLHSmkfSERRIEELQDRINDLEK 353
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLERRIAA---TERRLEDLEEQIEELSE 852
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   354 ERELLKENYDKLydSAFSAAHEEQWKLKEQQLKVQIAQLEtALKSDLTDKTEILDRLKTERDQNEKLVQENRE----LQL 429
Cdd:TIGR02168  853 DIESLAAEIEEL--EELIEELESELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELEELREklaqLEL 929
                          250
                   ....*....|....*.
gi 118442834   430 QYLEQKQQLDELKKRI 445
Cdd:TIGR02168  930 RLEGLEVRIDNLQERL 945
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
792-891 3.94e-13

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 66.71  E-value: 3.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  792 LHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMdldrylkSESLSFYVFDDSDT 871
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPE-------SDTLTVEVWDKDRF 73
                          90       100
                  ....*....|....*....|
gi 118442834  872 QENIYIGKVNVPLISLAHDR 891
Cdd:cd00030    74 SKDDFLGEVEIPLSELLDSG 93
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
107-570 1.79e-11

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 68.99  E-value: 1.79e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGyrqtpyNNVQSRINTGRRKANENAGLQECprkgikfQDADVA 186
Cdd:pfam15921  257 KIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQA------NSIQSQLEIIQEQARNQNSMYMR-------QLSDLE 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   187 ETphpmftkygnslLEEARGEIRNLENVIQSQrgqIEELEHLAEILKTQLRRKENEielsllqlrEQQATDQRSNIRDNV 266
Cdd:pfam15921  324 ST------------VSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTE---------RDQFSQESGNLDDQL 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   267 E--MIKLHKQlvEKSNALSAMEGKfiQLQEKQRTLRISHDALMANGDELNMQ-------LKEQRLKC-CSLEKQLHSMKF 336
Cdd:pfam15921  380 QklLADLHKR--EKELSLEKEQNK--RLWDRDTGNSITIDHLRRELDDRNMEvqrlealLKAMKSECqGQMERQMAAIQG 455
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   337 SERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQW------KLKEQQLKVQIAQLE-TALKSDLTDKTEILDR 409
Cdd:pfam15921  456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdltaSLQEKERAIEATNAEiTKLRSRVDLKLQELQH 535
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   410 LKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINAdELSEALLLIKAQKEQKNGDLSFLVKvDSEINK 489
Cdd:pfam15921  536 LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG-RTAGAMQVEKAQLEKEINDRRLELQ-EFKILK 613
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   490 DLERS-MRELQATHAETvqELEKT--------RNMLIMQHKINKDYQM-EVEAVTRKMENLQQDYELKVEQYVHLLDIRA 559
Cdd:pfam15921  614 DKKDAkIRELEARVSDL--ELEKVklvnagseRLRAVKDIKQERDQLLnEVKTSRNELNSLSEDYEVLKRNFRNKSEEME 691
                          490
                   ....*....|.
gi 118442834   560 ARIHKLEAQLK 570
Cdd:pfam15921  692 TTTNKLKMQLK 702
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
792-887 1.57e-09

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 56.34  E-value: 1.57e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    792 LHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHD--TAIIPSSNDPQFDDHMYFPVPmnmdldrYLKSESLSFYVFDDS 869
Cdd:smart00239    2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEVP-------PPELAELEIEVYDKD 74
                            90
                    ....*....|....*...
gi 118442834    870 DTQENIYIGKVNVPLISL 887
Cdd:smart00239   75 RFGRDDFIGQVTIPLSDL 92
C2 pfam00168
C2 domain;
792-899 6.02e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 54.63  E-value: 6.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   792 LHITIRCCNHLQSRASHLQPHPYV-VYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDldrylksESLSFYVFDDSD 870
Cdd:pfam00168    3 LTVTVIEAKNLPPKDGNGTSDPYVkVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDR 75
                           90       100
                   ....*....|....*....|....*....
gi 118442834   871 TQENIYIGKVNVPLISLAHDRCISGIFEL 899
Cdd:pfam00168   76 FGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
48-569 6.65e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.38  E-value: 6.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   48 EELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRL-GRDVEMEEMIEQLQEKVHELEKQN 126
Cdd:PRK03918  203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLeEKIRELEERIEELKKEIEELEEKV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  127 ETLKN---------RLISAKQQLQTQGYR--------QTPYNNVQSRINTGRRKANENAGLQEcPRKGIKfQDADVAETP 189
Cdd:PRK03918  283 KELKElkekaeeyiKLSEFYEEYLDELREiekrlsrlEEEINGIEERIKELEEKEERLEELKK-KLKELE-KRLEELEER 360
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  190 HpmftkygnSLLEEARGEIRNLENViqSQRGQIEELEHLAEILKTQLRRKEnEIELSLLQLREQQAT--DQRSNIRDNVE 267
Cdd:PRK03918  361 H--------ELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKE-EIEEEISKITARIGElkKEIKELKKAIE 429
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  268 MIKLHK----------------QLVEKSNA-LSAMEGKFIQLQEKQRTLRishdalmANGDELNMQLKEQR--LKCCSLE 328
Cdd:PRK03918  430 ELKKAKgkcpvcgrelteehrkELLEEYTAeLKRIEKELKEIEEKERKLR-------KELRELEKVLKKESelIKLKELA 502
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  329 KQLHSM--KFSERRIEELQDRindlEKERELLKENYDKLyDSAFSAAHEEQWKLKEqqLKVQIAQLETALKSDLTDKTEI 406
Cdd:PRK03918  503 EQLKELeeKLKKYNLEELEKK----AEEYEKLKEKLIKL-KGEIKSLKKELEKLEE--LKKKLAELEKKLDELEEELAEL 575
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  407 LDRLKTE----RDQNEKLVQENRELQLQYLEQK---QQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNgdlSF 479
Cdd:PRK03918  576 LKELEELgfesVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE---EL 652
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  480 LVKVDSEINKDLERSMRELQATHA----------ETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYElKVE 549
Cdd:PRK03918  653 EKKYSEEEYEELREEYLELSRELAglraeleeleKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE-KVK 731
                         570       580
                  ....*....|....*....|.
gi 118442834  550 QYVHLLDIRA-ARIHKLEAQL 569
Cdd:PRK03918  732 KYKALLKERAlSKVGEIASEI 752
HpsJ_fam NF038305
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ...
403-499 1.48e-03

HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.


Pssm-ID: 468465 [Multi-domain]  Cd Length: 230  Bit Score: 41.80  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  403 KTEILDRLKTERDQNEKLVQeNRELQLQYLEQKQQLDELKKRIKLYNQEndINADELSEALL-LIKAQKEQKNGDLSFLV 481
Cdd:NF038305  106 STQALQQINQQAGQQETQLQ-QQLNQLQAQTSPQQLNQLLKSEQKQGQA--LASGQLPEEQKeQLQQFKSNPQALDKFLA 182
                          90
                  ....*....|....*...
gi 118442834  482 KVDSEINKDLERSMRELQ 499
Cdd:NF038305  183 QQLTQIRTQAEEAEKQAR 200
 
Name Accession Description Interval E-value
C2-C2_1 pfam11618
First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 ...
597-738 1.52e-77

First C2 domain of RPGR-interacting protein 1; This domain is the first, more N-terminal, C2 domain on X-linked retinitis pigmentosa GTPase regulator-interacting proteins, or RPGR-interacting proteins.


Pssm-ID: 463310  Cd Length: 143  Bit Score: 252.17  E-value: 1.52e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   597 TIHLERGENLFEIHINKVTFSSEVLQASGDKEPVTFCTYAFYDFELQTTPVVRGLHPEYNFTSQYLVHVNDLFLQYIQKN 676
Cdd:pfam11618    1 TVELERGENLFELHIGGVTFSPEALRALGDKEPSTFCTYDFYDFETQTTPVVRGLNPFYDFTSQYKVTVDDLFLQYLQTN 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118442834   677 TITLEVHQAYSTEYETIAACQLKFHEILEK-SGRIFCTASLIGTKGDIPNFGTVEYWFRLRVP 738
Cdd:pfam11618   81 SLTLELHQALGVDFKTLAAAQLRLHGLLEDrGGRIHGTVTLTGVEGEIQIIGTLEYWIRLRVP 143
RPGR1_C pfam18111
Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain ...
1145-1308 2.26e-71

Retinitis pigmentosa G-protein regulator interacting C-terminal; This is the C-terminal domain of retinitis pigmentosa G-protein regulator (RPGR) interacting protein-1 present in Homo sapiens. A mutation in RPGR interacting protein-1 can be observed in the eye disease Leber congenital amaurosis. The domain is commonly known as the RPGR-interacting domain (RID) and is thought to have a C2-like fold.


Pssm-ID: 465655  Cd Length: 166  Bit Score: 235.39  E-value: 2.26e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  1145 PSEKIRIEIIALSL-NDSQVTMDDTIQRLFVECRFYSLPAE--ETPVSLPKPKSGQWVYYNYSNVIYVDKENNKAKRDIL 1221
Cdd:pfam18111    1 DSDTIRIEIISLQLlNESEVMQDDNIQQLFVEYRFLGRPEEetETPVSLPKPKTGQELYYNFSKVIDVDKEKNSARREIL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  1222 KAILQKQEMPNRSLRFTVVSDPPeDEQDLECEDIGVAHVDLADMFQEGRDLIEQNIDVFDARADGEGIGKLRVTVEALHA 1301
Cdd:pfam18111   81 RSMLLPEDPNQGNLKFTVVSEPL-DTEDGECEEIGYAYVDLKQILQSGRDIIEQDLDVKDARDENEQIGKLKVSVEALAA 159

                   ....*..
gi 118442834  1302 LQSVYKQ 1308
Cdd:pfam18111  160 LRAIYSE 166
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
201-543 2.38e-16

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 84.99  E-value: 2.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  201 LEEARGEIRNLENVIQSQRGQIEELEHLAEI------LKTQLRRKEneIELSLLQLREQQATDQRsnirdnvemikLHKQ 274
Cdd:COG1196   181 LEATEENLERLEDILGELERQLEPLERQAEKaeryreLKEELKELE--AELLLLKLRELEAELEE-----------LEAE 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  275 LVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHS----MKFSERRIEELQDRIND 350
Cdd:COG1196   248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARleerRRELEERLEELEEELAE 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  351 LEKERELLKENYDKLydsafsAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQ 430
Cdd:COG1196   328 LEEELEELEEELEEL------EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  431 YLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEIN------KDLERSMRELQATHAE 504
Cdd:COG1196   402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEallellAELLEEAALLEAALAE 481
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 118442834  505 TVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQD 543
Cdd:COG1196   482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
201-445 3.94e-16

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: 84.34  E-value: 3.94e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSN 280
Cdd:TIGR02168  700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE----QLEERIAQLSKELTELEAEIEELEERLEEAEE 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   281 ALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKE-------QRLKCCSLEKQLHSmkfSERRIEELQDRINDLEK 353
Cdd:TIGR02168  776 ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaanLRERLESLERRIAA---TERRLEDLEEQIEELSE 852
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   354 ERELLKENYDKLydSAFSAAHEEQWKLKEQQLKVQIAQLEtALKSDLTDKTEILDRLKTERDQNEKLVQENRE----LQL 429
Cdd:TIGR02168  853 DIESLAAEIEEL--EELIEELESELEALLNERASLEEALA-LLRSELEELSEELRELESKRSELRRELEELREklaqLEL 929
                          250
                   ....*....|....*.
gi 118442834   430 QYLEQKQQLDELKKRI 445
Cdd:TIGR02168  930 RLEGLEVRIDNLQERL 945
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
198-572 8.59e-16

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: 83.18  E-value: 8.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   198 NSLLEEARgEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllqlreqqatdqrsnirdnvemiKLHKQLVE 277
Cdd:TIGR02168  670 SSILERRR-EIEELEEKIEELEEKIAELEKALAELRKELEELEEELE-------------------------QLRKELEE 723
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   278 KSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSmkfSERRIEELQDRINDLEKEREL 357
Cdd:TIGR02168  724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE---AEAEIEELEAQIEQLKEELKA 800
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   358 LKENYDKLydsafSAAHEEQwKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:TIGR02168  801 LREALDEL-----RAELTLL-NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE 874
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   438 LDELKKRIklynqendinaDELSEALLLIKAQKEQKNGDLsflvKVDSEINKDLERSMRELQATHAETVQELEKTRNMLI 517
Cdd:TIGR02168  875 LEALLNER-----------ASLEEALALLRSELEELSEEL----RELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 118442834   518 -MQHKINKDYQMEVEAVTRKMENLqQDYELKVEQyvhlldiraaRIHKLEAQLKDI 572
Cdd:TIGR02168  940 nLQERLSEEYSLTLEEAEALENKI-EDDEEEARR----------RLKRLENKIKEL 984
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
792-891 3.94e-13

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 66.71  E-value: 3.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  792 LHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMdldrylkSESLSFYVFDDSDT 871
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPE-------SDTLTVEVWDKDRF 73
                          90       100
                  ....*....|....*....|
gi 118442834  872 QENIYIGKVNVPLISLAHDR 891
Cdd:cd00030    74 SKDDFLGEVEIPLSELLDSG 93
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
106-492 4.94e-13

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: 74.32  E-value: 4.94e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   106 VEMEEMIEQLQEKVHELEKQNETLKnrlisaKQQLQTQGYR--QTPYNNVQSRINTGRRKANenaglqecpRKGIKFQDA 183
Cdd:TIGR02168  182 ERTRENLDRLEDILNELERQLKSLE------RQAEKAERYKelKAELRELELALLVLRLEEL---------REELEELQE 246
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   184 DVAETphpmftkygNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKT---QLRRKENEIELSLLQLREQQATDQRS 260
Cdd:TIGR02168  247 ELKEA---------EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQKQILRERLANLERQ 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   261 NIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSER- 339
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAs 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   340 ---RIEELQDRINDLEKERELLKENydklydsafsaAHEEQWKLKEQQLKVQIAQLETaLKSDLTDKTEILDRLkteRDQ 416
Cdd:TIGR02168  398 lnnEIERLEARLERLEDRRERLQQE-----------IEELLKKLEEAELKELQAELEE-LEEELEELQEELERL---EEA 462
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   417 NEKLVQENRELQLQYLEQKQQLDELKKRIK-LYNQENdiNADELSEALLLIKAQKEQKNGD---LSFLVKVDSEINKDLE 492
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQARLDsLERLQE--NLEGFSEGVKALLKNQSGLSGIlgvLSELISVDEGYEAAIE 540
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
101-498 6.06e-13

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: 73.94  E-value: 6.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   101 RLGRDVEmeemIEQLQEKVHELEKQNETLKNRLISAKQQLQT---------QGYRQTPYNNVQSRINTGRRKANENAGLQ 171
Cdd:TIGR02168  672 ILERRRE----IEELEEKIEELEEKIAELEKALAELRKELEEleeeleqlrKELEELSRQISALRKDLARLEAEVEQLEE 747
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   172 ECPRKGIKFQDADVAETPHpmftkygNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENeiELSLLQLR 251
Cdd:TIGR02168  748 RIAQLSKELTELEAEIEEL-------EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA--ELTLLNEE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   252 EQQATDQRSNIRDNVEMIK-----LHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRlkccs 326
Cdd:TIGR02168  819 AANLRERLESLERRIAATErrledLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR----- 893
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   327 lekqlhsmkfseRRIEELQDRINDLEKERELLKENYDKLydsafsAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEI 406
Cdd:TIGR02168  894 ------------SELEELSEELRELESKRSELRRELEEL------REKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEE 955
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   407 LDRLkterdqneklvQENRELQLQYLEQKqqLDELKKRIKlynQENDINADELSEAlllikaqkEQKNGDLSFLVKVDSE 486
Cdd:TIGR02168  956 AEAL-----------ENKIEDDEEEARRR--LKRLENKIK---ELGPVNLAAIEEY--------EELKERYDFLTAQKED 1011
                          410
                   ....*....|....*
gi 118442834   487 INK---DLERSMREL 498
Cdd:TIGR02168 1012 LTEakeTLEEAIEEI 1026
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
48-600 1.40e-12

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 72.36  E-value: 1.40e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    48 EELEDrflrlhDENILLKQHARKQE--DKIKRMATKLIRLVNDKKRYErvgggpkrlgrdvemeEMIEQLQEKVHELEKQ 125
Cdd:TIGR04523  169 EELEN------ELNLLEKEKLNIQKniDKIKNKLLKLELLLSNLKKKI----------------QKNKSLESQISELKKQ 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   126 NETLKNRLISAKQQLQTQgyrQTPYNNVQSRINTGRRKANEnaglqecprkgIKFQDADvaetphpmftkyGNSLLEEAR 205
Cdd:TIGR04523  227 NNQLKDNIEKKQQEINEK---TTEISNTQTQLNQLKDEQNK-----------IKKQLSE------------KQKELEQNN 280
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   206 GEIRNLENVIQSQRGQIEEL-----EHLAEILKTQLRRKENEIELSLLQLRE-----QQATDQRSNIRD-----NVEMIK 270
Cdd:TIGR04523  281 KKIKELEKQLNQLKSEISDLnnqkeQDWNKELKSELKNQEKKLEEIQNQISQnnkiiSQLNEQISQLKKeltnsESENSE 360
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   271 LHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDAL---MANGDELNmQLKEQRLKCCSLEKQLhsmkfSERRIEELQDR 347
Cdd:TIGR04523  361 KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLeskIQNQEKLN-QQKDEQIKKLQQEKEL-----LEKEIERLKET 434
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   348 INDLEKE-RELLKENYDK--LYDSAFSAAHEEQWKLKEqqLKVQIAQLETAL---KSDLTDKTEILDRLKTERDQNEKLV 421
Cdd:TIGR04523  435 IIKNNSEiKDLTNQDSVKelIIKNLDNTRESLETQLKV--LSRSINKIKQNLeqkQKELKSKEKELKKLNEEKKELEEKV 512
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   422 QENRELQLQYLEQKQQLDELKKRI--KLYNQENDINADELSEALLLIKAQKEQKNGDLSFLvkvdSEINKDLERSMRELQ 499
Cdd:TIGR04523  513 KDLTKKISSLKEKIEKLESEKKEKesKISDLEDELNKDDFELKKENLEKEIDEKNKEIEEL----KQTQKSLKKKQEEKQ 588
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   500 athaETVQELEKTRNMLIMQHKInkdYQMEVEAVTRKMENLQQDYElKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQY 579
Cdd:TIGR04523  589 ----ELIDQKEKEKKDLIKEIEE---KEKKISSLEKELEKAKKENE-KLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNK 660
                          570       580
                   ....*....|....*....|...
gi 118442834   580 kfKPEIMPD--DSVDEFDETIHL 600
Cdd:TIGR04523  661 --WPEIIKKikESKTKIDDIIEL 681
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
107-570 1.79e-11

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 68.99  E-value: 1.79e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGyrqtpyNNVQSRINTGRRKANENAGLQECprkgikfQDADVA 186
Cdd:pfam15921  257 KIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQA------NSIQSQLEIIQEQARNQNSMYMR-------QLSDLE 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   187 ETphpmftkygnslLEEARGEIRNLENVIQSQrgqIEELEHLAEILKTQLRRKENEielsllqlrEQQATDQRSNIRDNV 266
Cdd:pfam15921  324 ST------------VSQLRSELREAKRMYEDK---IEELEKQLVLANSELTEARTE---------RDQFSQESGNLDDQL 379
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   267 E--MIKLHKQlvEKSNALSAMEGKfiQLQEKQRTLRISHDALMANGDELNMQ-------LKEQRLKC-CSLEKQLHSMKF 336
Cdd:pfam15921  380 QklLADLHKR--EKELSLEKEQNK--RLWDRDTGNSITIDHLRRELDDRNMEvqrlealLKAMKSECqGQMERQMAAIQG 455
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   337 SERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQW------KLKEQQLKVQIAQLE-TALKSDLTDKTEILDR 409
Cdd:pfam15921  456 KNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTvsdltaSLQEKERAIEATNAEiTKLRSRVDLKLQELQH 535
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   410 LKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINAdELSEALLLIKAQKEQKNGDLSFLVKvDSEINK 489
Cdd:pfam15921  536 LKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHG-RTAGAMQVEKAQLEKEINDRRLELQ-EFKILK 613
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   490 DLERS-MRELQATHAETvqELEKT--------RNMLIMQHKINKDYQM-EVEAVTRKMENLQQDYELKVEQYVHLLDIRA 559
Cdd:pfam15921  614 DKKDAkIRELEARVSDL--ELEKVklvnagseRLRAVKDIKQERDQLLnEVKTSRNELNSLSEDYEVLKRNFRNKSEEME 691
                          490
                   ....*....|.
gi 118442834   560 ARIHKLEAQLK 570
Cdd:pfam15921  692 TTTNKLKMQLK 702
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
368-572 9.52e-11

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: 65.17  E-value: 9.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  368 SAFSAAHEEQWKLKEQ--QLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRI 445
Cdd:COG4942    13 LAAAAQADAAAEAEAEleQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  446 KLYNQENDINADELSEalLLIKAQKEQKNGDLSFLVKVDS--------EINKDLERSMRELQATHAETVQELEKTRNMLI 517
Cdd:COG4942    93 AELRAELEAQKEELAE--LLRALYRLGRQPPLALLLSPEDfldavrrlQYLKYLAPARREQAEELRADLAELAALRAELE 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 118442834  518 MQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDI 572
Cdd:COG4942   171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
64-598 3.52e-10

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 64.66  E-value: 3.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    64 LKQHARKQEDKIKRMATKLIRLVND-KKRYERVGGGPKRLGRDvemEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQT 142
Cdd:TIGR04523   24 YKNIANKQDTEEKQLEKKLKTIKNElKNKEKELKNLDKNLNKD---EEKINNSNNKIKILEQQIKDLNDKLKKNKDKINK 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   143 QGYRQTPYNN-VQSRINTGRRKANENAGLQECPRKGIKFQDADVAE-TPHPMFTKYGNSLLEEARGEIRNLENVIQSQRG 220
Cdd:TIGR04523  101 LNSDLSKINSeIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEiKKKEKELEKLNNKYNDLKKQKEELENELNLLEK 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   221 QIEELEHLAEILKTQLRRKE-------------NEIELSLLQLREQQATDQRSNIRDNVEM------------------- 268
Cdd:TIGR04523  181 EKLNIQKNIDKIKNKLLKLElllsnlkkkiqknKSLESQISELKKQNNQLKDNIEKKQQEInektteisntqtqlnqlkd 260
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   269 --IKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGD-----ELNMQLKEQRLKCCSLEKQLHSmkfSERRI 341
Cdd:TIGR04523  261 eqNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEEIQNQISQ---NNKII 337
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   342 EELQDRINDLEKERELLKENYDKLydsafsaahEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDrLKTERDQNEKlv 421
Cdd:TIGR04523  338 SQLNEQISQLKKELTNSESENSEK---------QRELEEKQNEIEKLKKENQSYKQEIKNLESQIND-LESKIQNQEK-- 405
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   422 qENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEaLLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQAT 501
Cdd:TIGR04523  406 -LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKD-LTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQN 483
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   502 HAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQdyelKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKF 581
Cdd:TIGR04523  484 LEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKE----KIEKLESEKKEKESKISDLEDELNKDDFELKKENL 559
                          570
                   ....*....|....*..
gi 118442834   582 KPEImpddsvDEFDETI 598
Cdd:TIGR04523  560 EKEI------DEKNKEI 570
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
39-572 4.45e-10

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 64.37  E-value: 4.45e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    39 RQAVSRVSRE---ELEDRFLRLHDENILLKQHARKQEDKIKRMATKLirlvnDKKRYERVGGGPKRLGRDVEMEEMIEQL 115
Cdd:pfam15921   73 KEHIERVLEEyshQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKL-----QEMQMERDAMADIRRRESQSQEDLRNQL 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   116 QEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGlqecprKGIKFQDAdvaetphpMFTK 195
Cdd:pfam15921  148 QNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEEASG------KKIYEHDS--------MSTM 213
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   196 YGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRK-----------------ENEIELSLLQLREQQATDQ 258
Cdd:pfam15921  214 HFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKSESQNKielllqqhqdrieqlisEHEVEITGLTEKASSARSQ 293
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   259 RSNIRDNVEMIKlhkQLVEKSNA-----LSAMEGKFIQLQEKQRTL-RISHDALmangDELNMQL--KEQRLKCCSLEKQ 330
Cdd:pfam15921  294 ANSIQSQLEIIQ---EQARNQNSmymrqLSDLESTVSQLRSELREAkRMYEDKI----EELEKQLvlANSELTEARTERD 366
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   331 LHSMKfSERRIEELQDRINDL---EKERELLKENYDKLYD----SAFSAAHEEQwKLKEQQLKVQ-IAQLETALKSDLTD 402
Cdd:pfam15921  367 QFSQE-SGNLDDQLQKLLADLhkrEKELSLEKEQNKRLWDrdtgNSITIDHLRR-ELDDRNMEVQrLEALLKAMKSECQG 444
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   403 KTEilDRLKTERDQNEKLvQENRELQLQYLEQKQQL----DELK-KRIKLYNQENDINadELSEALLLIKAQKEQKNGDL 477
Cdd:pfam15921  445 QME--RQMAAIQGKNESL-EKVSSLTAQLESTKEMLrkvvEELTaKKMTLESSERTVS--DLTASLQEKERAIEATNAEI 519
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   478 SFL-VKVDSEIN-----KDLERSMRELQAT-HAETVQELEKTRNMLIMQHKINKDYQ-----------MEVEAVtrKMEN 539
Cdd:pfam15921  520 TKLrSRVDLKLQelqhlKNEGDHLRNVQTEcEALKLQMAEKDKVIEILRQQIENMTQlvgqhgrtagaMQVEKA--QLEK 597
                          570       580       590
                   ....*....|....*....|....*....|...
gi 118442834   540 LQQDYELKVEQYVHLLDIRAARIHKLEAQLKDI 572
Cdd:pfam15921  598 EINDRRLELQEFKILKDKKDAKIRELEARVSDL 630
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
201-512 5.23e-10

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: 64.32  E-value: 5.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLR--EQQATDQRSNIRDNVEMI-----KLHK 273
Cdd:TIGR02169  697 LRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSslEQEIENVKSELKELEARIeeleeDLHK 776
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   274 qLVEKSNALSAMEG--KFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKqlhSMKFSERRIEELQDRINDL 351
Cdd:TIGR02169  777 -LEEALNDLEARLShsRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK---EIQELQEQRIDLKEQIKSI 852
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   352 EKERELLKenydklydsafsaAHEEQWKLKEQQLKVQIAQLETALKSdltdkteildrLKTERDQNEKlvqENRELQLQY 431
Cdd:TIGR02169  853 EKEIENLN-------------GKKEELEEELEELEAALRDLESRLGD-----------LKKERDELEA---QLRELERKI 905
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   432 LEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSfLVKVDSEINKdLERSMRELQATHAETVQELEK 511
Cdd:TIGR02169  906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQR-VEEEIRALEPVNMLAIQEYEE 983

                   .
gi 118442834   512 T 512
Cdd:TIGR02169  984 V 984
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
109-572 5.68e-10

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 63.89  E-value: 5.68e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   109 EEMIEQLQEKVHELEKQNETLKNRLISAKQQLQtqgyrqtpynNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAET 188
Cdd:TIGR04523  151 EKELEKLNNKYNDLKKQKEELENELNLLEKEKL----------NIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQI 220
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   189 PHpmFTKYGNSL---LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELS-----------------LL 248
Cdd:TIGR04523  221 SE--LKKQNNQLkdnIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNnkkikelekqlnqlkseIS 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   249 QLREQQATDQRSNIRDNVEMIKlhKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLE 328
Cdd:TIGR04523  299 DLNNQKEQDWNKELKSELKNQE--KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   329 KQLHSMKFSerrIEELQDRINDLE------KERELLKENYDKLYDSAFSAAHEEQWKLKEQ---------QLKVQIAQLE 393
Cdd:TIGR04523  377 KENQSYKQE---IKNLESQINDLEskiqnqEKLNQQKDEQIKKLQQEKELLEKEIERLKETiiknnseikDLTNQDSVKE 453
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   394 TALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLI------K 467
Cdd:TIGR04523  454 LIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIekleseK 533
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   468 AQKEQKNGDL-SFLVKVDSEINKD-LERSMRELQathaETVQELEKTRNMLIMQHK----INKDYQMEVEAVTRKMENlq 541
Cdd:TIGR04523  534 KEKESKISDLeDELNKDDFELKKEnLEKEIDEKN----KEIEELKQTQKSLKKKQEekqeLIDQKEKEKKDLIKEIEE-- 607
                          490       500       510
                   ....*....|....*....|....*....|.
gi 118442834   542 qdYELKVEQYVHLLDIRAARIHKLEAQLKDI 572
Cdd:TIGR04523  608 --KEKKISSLEKELEKAKKENEKLSSIIKNI 636
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
211-569 5.97e-10

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: 64.04  E-value: 5.97e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   211 LENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQrsnirdnvemiKLHKQLVEKSNALSAMEGKFI 290
Cdd:pfam01576   73 LEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQ-----------KLQLEKVTTEAKIKKLEEDIL 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   291 QLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSmkfSERRIEELQDRINDLEKERELLKENYDKLyDSAF 370
Cdd:pfam01576  142 LLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNK---HEAMISDLEERLKKEEKGRQELEKAKRKL-EGES 217
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   371 SAAHEEQWKLKEQ--QLKVQIAQLETALKSdltdkteILDRLKTERDQNEKLVQENRELQLQYLEQKQQLD-ELKKRIKL 447
Cdd:pfam01576  218 TDLQEQIAELQAQiaELRAQLAKKEEELQA-------ALARLEEETAQKNNALKKIRELEAQISELQEDLEsERAARNKA 290
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   448 YNQENDINAD------ELSEALLLIKAQKE---QKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQE---------- 508
Cdd:pfam01576  291 EKQRRDLGEElealktELEDTLDTTAAQQElrsKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEElteqleqakr 370
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118442834   509 -----------LEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQL 569
Cdd:pfam01576  371 nkanlekakqaLESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
216-572 1.27e-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: 63.16  E-value: 1.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   216 QSQRGQIEELEHLAEILKTQLRRKENEIElsllqlreqQATDQRSNirdnvemikLHKQLVEKSNALSAMEGKFIQLQEK 295
Cdd:TIGR02169  677 QRLRERLEGLKRELSSLQSELRRIENRLD---------ELSQELSD---------ASRKIGEIEKEIEQLEQEEEKLKER 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   296 ----QRTLRISHDALMANGDE---LNMQLKEQRLKCCSLEKQLHSMK--FSERRIEELQDRINDLEKER--------ELL 358
Cdd:TIGR02169  739 leelEEDLSSLEQEIENVKSElkeLEARIEELEEDLHKLEEALNDLEarLSHSRIPEIQAELSKLEEEVsriearlrEIE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   359 KENYDKLYDSAFsaAHEEQWKLKEQQ--LKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQ 436
Cdd:TIGR02169  819 QKLNRLTLEKEY--LEKEIQELQEQRidLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   437 QLDELKKRIklynQENDINADELSEALLLIKAQKEQKNGDLSflvkvdseinkDLERSMRELQATHAETVQElektrnml 516
Cdd:TIGR02169  897 QLRELERKI----EELEAQIEKKRKRLSELKAKLEALEEELS-----------EIEDPKGEDEEIPEEELSL-------- 953
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118442834   517 imqhkinKDYQMEVEAVTRKMENLQ-------QDYELKVEQYVHLLDIRAarihKLEAQLKDI 572
Cdd:TIGR02169  954 -------EDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELKEKRA----KLEEERKAI 1005
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
792-887 1.57e-09

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 56.34  E-value: 1.57e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    792 LHITIRCCNHLQSRASHLQPHPYVVYKFFDFADHD--TAIIPSSNDPQFDDHMYFPVPmnmdldrYLKSESLSFYVFDDS 869
Cdd:smart00239    2 LTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKkkTKVVKNTLNPVWNETFEFEVP-------PPELAELEIEVYDKD 74
                            90
                    ....*....|....*...
gi 118442834    870 DTQENIYIGKVNVPLISL 887
Cdd:smart00239   75 RFGRDDFIGQVTIPLSDL 92
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
107-566 2.31e-09

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: 61.91  E-value: 2.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   107 EMEEMIEQLQEKVHELEKQNETL--KNRLISAKQQLQTQGYRQTP----YNNVQSRINTGRRKAN---ENAGLQECpRKG 177
Cdd:TIGR00618  230 HLREALQQTQQSHAYLTQKREAQeeQLKKQQLLKQLRARIEELRAqeavLEETQERINRARKAAPlaaHIKAVTQI-EQQ 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   178 IKFQDADVAETphpmftkygnsllEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQ--LRRKENEIELSLLQLREQQA 255
Cdd:TIGR00618  309 AQRIHTELQSK-------------MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQeiHIRDAHEVATSIREISCQQH 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   256 TDqRSNIRDNVEMIKLhkqLVEKSNALSAMEGKFIQLQEKQRTLRISHDAL----MANGDELNMQLKEQRLKCCSLEKQL 331
Cdd:TIGR00618  376 TL-TQHIHTLQQQKTT---LTQKLQSLCKELDILQREQATIDTRTSAFRDLqgqlAHAKKQQELQQRYAELCAAAITCTA 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   332 HSMKFSERRIEELQDRInDLEKERELLKENYDKLYdsafsaahEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLK 411
Cdd:TIGR00618  452 QCEKLEKIHLQESAQSL-KEREQQLQTKEQIHLQE--------TRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN 522
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   412 TERDQNEKLVQENRELQLQYLEQK--QQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINK 489
Cdd:TIGR00618  523 PGPLTRRMQRGEQTYAQLETSEEDvyHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK 602
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118442834   490 DLERSMRELQATHAETVQELEKTRNMLIMQH--KINKDYQMEVEAVTRKMENLQQDyelkvEQYVHLLDIRAARIHKLE 566
Cdd:TIGR00618  603 LSEAEDMLACEQHALLRKLQPEQDLQDVRLHlqQCSQELALKLTALHALQLTLTQE-----RVREHALSIRVLPKELLA 676
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
201-446 3.08e-09

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: 60.55  E-value: 3.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIelsllQLREQQATDQRSNIRDN-VEMIKLHKQLVEKS 279
Cdd:COG4942    29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRI-----RALEQELAALEAELAELeKEIAELRAELEAQK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  280 NALSAMegkfiqLQEKQRTLRISHDALMANGDELNMQLKEQRlkccsLEKQLhsMKFSERRIEELQDRINDLEKERELLK 359
Cdd:COG4942   104 EELAEL------LRALYRLGRQPPLALLLSPEDFLDAVRRLQ-----YLKYL--APARREQAEELRADLAELAALRAELE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  360 ENYDKLydsafsaaheeqwklkeQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEklvQENRELQLQYLEQKQQLD 439
Cdd:COG4942   171 AERAEL-----------------EALLAELEEERAALEALKAERQKLLARLEKELAELA---AELAELQQEAEELEALIA 230

                  ....*..
gi 118442834  440 ELKKRIK 446
Cdd:COG4942   231 RLEAEAA 237
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
341-573 4.15e-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: 4.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  341 IEELQDRINDLEKEREL------LKENYdKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTER 414
Cdd:COG1196   195 LGELERQLEPLERQAEKaeryreLKEEL-KELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  415 DQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEInKDLERS 494
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-EEAEEE 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  495 MRELQATHAETVQEL-EKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIA 573
Cdd:COG1196   353 LEEAEAELAEAEEALlEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
C2 pfam00168
C2 domain;
792-899 6.02e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 54.63  E-value: 6.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   792 LHITIRCCNHLQSRASHLQPHPYV-VYKFFDFADHDTAIIPSSNDPQFDDHMYFPVPMNMDldrylksESLSFYVFDDSD 870
Cdd:pfam00168    3 LTVTVIEAKNLPPKDGNGTSDPYVkVYLLDGKQKKKTKVVKNTLNPVWNETFTFSVPDPEN-------AVLEIEVYDYDR 75
                           90       100
                   ....*....|....*....|....*....
gi 118442834   871 TQENIYIGKVNVPLISLAHDRCISGIFEL 899
Cdd:pfam00168   76 FGRDDFIGEVRIPLSELDSGEGLDGWYPL 104
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
273-473 6.57e-09

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: 59.39  E-value: 6.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  273 KQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLhsmKFSERRIEELQDRINDLE 352
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAELR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  353 KERELLKENYDKLYDSAFSAAHEEQWKLK---------------EQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQN 417
Cdd:COG4942    97 AELEAQKEELAELLRALYRLGRQPPLALLlspedfldavrrlqyLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118442834  418 EKLVQEN----RELQLQYLEQKQQLDELKKRIKLYNQENDI---NADELSEALLLIKAQKEQK 473
Cdd:COG4942   177 EALLAELeeerAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAA 239
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
229-572 3.14e-08

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: 58.26  E-value: 3.14e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   229 AEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNV-----------EM-IKLHKQLVEKSNALSAMEGKFIQLQEKQ 296
Cdd:pfam01576   12 EELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLqaetelcaeaeEMrARLAARKQELEEILHELESRLEEEEERS 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   297 RTLRISHDALMANGDELNMQLKE-----QRLKccsLEKQL--HSMKFSERRIEELQDRINDLEKERELLKEnydKLYDSA 369
Cdd:pfam01576   92 QQLQNEKKKMQQHIQDLEEQLDEeeaarQKLQ---LEKVTteAKIKKLEEDILLLEDQNSKLSKERKLLEE---RISEFT 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   370 FSAAHEEQWKLKEQQLKVQiaqlETALKSDLTDkteildRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYN 449
Cdd:pfam01576  166 SNLAEEEEKAKSLSKLKNK----HEAMISDLEE------RLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELR 235
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   450 QENDINADELSEALLLIKAQKEQKNgdlsflvkvdseinkDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQME 529
Cdd:pfam01576  236 AQLAKKEEELQAALARLEEETAQKN---------------NALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEE 300
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 118442834   530 VEAVTRKME------NLQQDYELKVEQYVHLLDiRA----ARIHklEAQLKDI 572
Cdd:pfam01576  301 LEALKTELEdtldttAAQQELRSKREQEVTELK-KAleeeTRSH--EAQLQEM 350
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
49-558 3.17e-08

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 58.21  E-value: 3.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    49 ELEDRFLRLHDEnilLKQHARKQEDKIKRMATKLIrLVNDK---KRYERVGGGPKRLGRDVEMEEMIEQLQEKVHEL--- 122
Cdd:pfam15921  321 DLESTVSQLRSE---LREAKRMYEDKIEELEKQLV-LANSElteARTERDQFSQESGNLDDQLQKLLADLHKREKELsle 396
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   123 EKQNETLKNR----------------------------LISAKQQLQTQGYRQTPynNVQSRINTGRRKANENAGLQ--- 171
Cdd:pfam15921  397 KEQNKRLWDRdtgnsitidhlrrelddrnmevqrlealLKAMKSECQGQMERQMA--AIQGKNESLEKVSSLTAQLEstk 474
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   172 ECPRKGIKFQDAD--VAETPHPMFTKYGNSLLEEARG-EIRNLEnvIQSQRGQI----EELEHLAEiLKTQLRRKENEIE 244
Cdd:pfam15921  475 EMLRKVVEELTAKkmTLESSERTVSDLTASLQEKERAiEATNAE--ITKLRSRVdlklQELQHLKN-EGDHLRNVQTECE 551
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   245 LSLLQLREQQATDQ--RSNIRDNVEMIKLHKQ-----LVEKSNALSAMEGKFIQLQEkqrtLRISHDALMANGDELNMQL 317
Cdd:pfam15921  552 ALKLQMAEKDKVIEilRQQIENMTQLVGQHGRtagamQVEKAQLEKEINDRRLELQE----FKILKDKKDAKIRELEARV 627
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   318 KEQRLKCCSL----EKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLydsafsaahEEQWKLKEQQLKVQIAQLE 393
Cdd:pfam15921  628 SDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVL---------KRNFRNKSEEMETTTNKLK 698
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   394 TALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKlYNQENDINADELSEALllikaqKEQK 473
Cdd:pfam15921  699 MQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQ-FLEEAMTNANKEKHFL------KEEK 771
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   474 NGDLSFLVKVDSEINKdlerSMRELQATHAETVQELEKTRNMLIMQHKINKDYQmEVEAVTRKMEnlQQDYELKVEqyvH 553
Cdd:pfam15921  772 NKLSQELSTVATEKNK----MAGELEVLRSQERRLKEKVANMEVALDKASLQFA-ECQDIIQRQE--QESVRLKLQ---H 841

                   ....*
gi 118442834   554 LLDIR 558
Cdd:pfam15921  842 TLDVK 846
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
48-569 6.65e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.38  E-value: 6.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   48 EELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRL-GRDVEMEEMIEQLQEKVHELEKQN 126
Cdd:PRK03918  203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLeEKIRELEERIEELKKEIEELEEKV 282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  127 ETLKN---------RLISAKQQLQTQGYR--------QTPYNNVQSRINTGRRKANENAGLQEcPRKGIKfQDADVAETP 189
Cdd:PRK03918  283 KELKElkekaeeyiKLSEFYEEYLDELREiekrlsrlEEEINGIEERIKELEEKEERLEELKK-KLKELE-KRLEELEER 360
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  190 HpmftkygnSLLEEARGEIRNLENViqSQRGQIEELEHLAEILKTQLRRKEnEIELSLLQLREQQAT--DQRSNIRDNVE 267
Cdd:PRK03918  361 H--------ELYEEAKAKKEELERL--KKRLTGLTPEKLEKELEELEKAKE-EIEEEISKITARIGElkKEIKELKKAIE 429
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  268 MIKLHK----------------QLVEKSNA-LSAMEGKFIQLQEKQRTLRishdalmANGDELNMQLKEQR--LKCCSLE 328
Cdd:PRK03918  430 ELKKAKgkcpvcgrelteehrkELLEEYTAeLKRIEKELKEIEEKERKLR-------KELRELEKVLKKESelIKLKELA 502
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  329 KQLHSM--KFSERRIEELQDRindlEKERELLKENYDKLyDSAFSAAHEEQWKLKEqqLKVQIAQLETALKSDLTDKTEI 406
Cdd:PRK03918  503 EQLKELeeKLKKYNLEELEKK----AEEYEKLKEKLIKL-KGEIKSLKKELEKLEE--LKKKLAELEKKLDELEEELAEL 575
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  407 LDRLKTE----RDQNEKLVQENRELQLQYLEQK---QQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNgdlSF 479
Cdd:PRK03918  576 LKELEELgfesVEELEERLKELEPFYNEYLELKdaeKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELE---EL 652
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  480 LVKVDSEINKDLERSMRELQATHA----------ETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYElKVE 549
Cdd:PRK03918  653 EKKYSEEEYEELREEYLELSRELAglraeleeleKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELRE-KVK 731
                         570       580
                  ....*....|....*....|.
gi 118442834  550 QYVHLLDIRA-ARIHKLEAQL 569
Cdd:PRK03918  732 KYKALLKERAlSKVGEIASEI 752
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
201-573 8.37e-08

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 56.70  E-value: 8.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLH-KQLVEKS 279
Cdd:COG4717    83 AEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERlEELRELE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  280 NALSAMEGKFIQLQEKQRTLRISHDAlmangdelnmqLKEQRLKccSLEKQLHSMkfsERRIEELQDRINDLEKERELLK 359
Cdd:COG4717   163 EELEELEAELAELQEELEELLEQLSL-----------ATEEELQ--DLAEELEEL---QQRLAELEEELEEAQEELEELE 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  360 ENYDKLYDSAFSAAHEEQWKLKEQQLKV--QIAQLETALKSDLTDKTEILDRLKT---------ERDQNEKLVQENRELQ 428
Cdd:COG4717   227 EELEQLENELEAAALEERLKEARLLLLIaaALLALLGLGGSLLSLILTIAGVLFLvlgllallfLLLAREKASLGKEAEE 306
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  429 LQYLEQKQQLD--ELKKRIKLYNQENDINADELSEALLLIKAQKEQkngdLSFLVKVDSEInkDLERSMRELQATHAETV 506
Cdd:COG4717   307 LQALPALEELEeeELEELLAALGLPPDLSPEELLELLDRIEELQEL----LREAEELEEEL--QLEELEQEIAALLAEAG 380
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118442834  507 QELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLqqDYELKVEQYVHLLDIRAARIHKLEAQLKDIA 573
Cdd:COG4717   381 VEDEEELRAALEQAEEYQELKEELEELEEQLEEL--LGELEELLEALDEEELEEELEELEEELEELE 445
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
66-594 1.10e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 56.46  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   66 QHARKQEDKIKRMATKLiRLVNDKKRYERVGggpKRLgrdVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGY 145
Cdd:COG4913   265 AAARERLAELEYLRAAL-RLWFAQRRLELLE---AEL---EELRAELARLEAELERLEARLDALREELDELEAQIRGNGG 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  146 RQTpyNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETPhpmftkygnSLLEEARGEIRNLENVIQSQRGQIEEL 225
Cdd:COG4913   338 DRL--EQLEREIERLERELEERERRRARLEALLAALGLPLPASA---------EEFAALRAEAAALLEALEEELEALEEA 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  226 EHLAEILKTQLRRKENEIELSLLQLREqqatdQRSNIRDnvEMIKLHKQLVEksnALSAME------GKFIQLQEKQ--- 296
Cdd:COG4913   407 LAEAEAALRDLRRELRELEAEIASLER-----RKSNIPA--RLLALRDALAE---ALGLDEaelpfvGELIEVRPEEerw 476
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  297 --------RTLRIS---------------------------------HDALMANGDE-----------------LNMQLK 318
Cdd:COG4913   477 rgaiervlGGFALTllvppehyaaalrwvnrlhlrgrlvyervrtglPDPERPRLDPdslagkldfkphpfrawLEAELG 556
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  319 EQR-LKCCSLEKQLHSMKFS---------------------------------------ERRIEELQDRINDLEKERELL 358
Cdd:COG4913   557 RRFdYVCVDSPEELRRHPRAitragqvkgngtrhekddrrrirsryvlgfdnraklaalEAELAELEEELAEAEERLEAL 636
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  359 KENYDKL--YDSAFSAAHEEQWKLKE-QQLKVQIAQLETALKsDLTDKTEILDRLKTERDQNEK----LVQENRELQLQY 431
Cdd:COG4913   637 EAELDALqeRREALQRLAEYSWDEIDvASAEREIAELEAELE-RLDASSDDLAALEEQLEELEAeleeLEEELDELKGEI 715
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  432 LEQKQQLDELKKRIK-LYNQENDINADELSEALLLIKAQKEQKNGDlsflvKVDSEINKDLERSMRELQATHAETVQELE 510
Cdd:COG4913   716 GRLEKELEQAEEELDeLQDRLEAAEDLARLELRALLEERFAAALGD-----AVERELRENLEERIDALRARLNRAEEELE 790
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  511 KTRnmlimqHKINKDYQMEVEAVT----------RKMENLQQD----YELK------------VEQYVHLLD--IRAA-- 560
Cdd:COG4913   791 RAM------RAFNREWPAETADLDadleslpeylALLDRLEEDglpeYEERfkellnensiefVADLLSKLRraIREIke 864
                         650       660       670
                  ....*....|....*....|....*....|....*
gi 118442834  561 RIHKLEAQLKDIAYGT-KQYKFKPEIMPDDSVDEF 594
Cdd:COG4913   865 RIDPLNDSLKRIPFGPgRYLRLEARPRPDPEVREF 899
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
219-580 1.55e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 1.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  219 RGQIEELehlAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEmiKLHKQlveKSNALsamegKFIQLQEKQRT 298
Cdd:COG1196   158 RAIIEEA---AGISKYKERKEEAERKLEATEENLERLEDILGELERQLE--PLERQ---AEKAE-----RYRELKEELKE 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  299 LRISHDALmangdelnmQLKEQRLKccsLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLyDSAFSAAHEEqw 378
Cdd:COG1196   225 LEAELLLL---------KLRELEAE---LEELEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAE-- 289
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  379 klkEQQLKVQIAQLETALKSDLTDKTEILDRLkterdqnEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQEndinADE 458
Cdd:COG1196   290 ---EYELLAELARLEQDIARLEERRRELEERL-------EELEEELAELEEELEELEEELEELEEELEEAEEE----LEE 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  459 LSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAEtVQELEKTRNMLIMQHKINKDYQMEVEAVTRKME 538
Cdd:COG1196   356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEALAELE 434
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 118442834  539 NLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYK 580
Cdd:COG1196   435 EEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
PTZ00121 PTZ00121
MAEBL; Provisional
65-549 2.70e-07

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 55.53  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   65 KQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNEtLKNRLISAKqqlqtqg 144
Cdd:PTZ00121 1373 KEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADE-AKKKAEEAK------- 1444
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  145 yrqtpynnvqsRINTGRRKANENAGLQECPRKGIKFQDADVAETPHPMFTKygnslLEEARGEIRNLENVIQSQRGQIEE 224
Cdd:PTZ00121 1445 -----------KADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADEAKKAAEA 1508
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  225 LEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHK-QLVEKSNALSAMEGKFIQLQEKQRTLRISh 303
Cdd:PTZ00121 1509 KKKADEAKKAEEAKKADEAK----KAEEAKKADEAKKAEEKKKADELKKaEELKKAEEKKKAEEAKKAEEDKNMALRKA- 1583
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  304 dalmangdELNMQLKEQRL-KCCSLEKQLHSMKFSE-RRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLK 381
Cdd:PTZ00121 1584 --------EEAKKAEEARIeEVMKLYEEEKKMKAEEaKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  382 EQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKK--RIKLYNQENDINADEL 459
Cdd:PTZ00121 1656 EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeELKKAEEENKIKAEEA 1735
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  460 SEallliKAQKEQKNGDlsfLVKVDSEINKDLERSMRELQATHAETVQELEKtrnmlIMQHKINKDYQMEVEAVTRKMEN 539
Cdd:PTZ00121 1736 KK-----EAEEDKKKAE---EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA-----VIEEELDEEDEKRRMEVDKKIKD 1802
                         490
                  ....*....|
gi 118442834  540 LQQDYELKVE 549
Cdd:PTZ00121 1803 IFDNFANIIE 1812
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
206-446 2.74e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 55.46  E-value: 2.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   206 GEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElSLLQLREQQA---------------------TDQRSNIRD 264
Cdd:TIGR02169  230 KEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLE-EIEQLLEELNkkikdlgeeeqlrvkekigelEAEIASLER 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   265 NV-----EMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKqlhsmKFSER 339
Cdd:TIGR02169  309 SIaekerELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK-----EFAET 383
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   340 RIE--ELQDRINDLEKERELLKENYDKLYDSAfsaaheEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQN 417
Cdd:TIGR02169  384 RDElkDYREKLEKLKREINELKRELDRLQEEL------QRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
                          250       260
                   ....*....|....*....|....*....
gi 118442834   418 EKLVQENRELQLQYLEQKQQLDELKKRIK 446
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLKEEYDRVEKELS 486
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
47-571 2.89e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.45  E-value: 2.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDV-EMEEMIEQLQEKVHELEKQ 125
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEIsRLEQQKQILRERLANLERQ 317
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   126 NETLKNRLISAKQQLQTQGYR----QTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDAdvaetphpmftkygnsLL 201
Cdd:TIGR02168  318 LEELEAQLEELESKLDELAEElaelEEKLEELKEELESLEAELEELEAELEELESRLEELEE----------------QL 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   202 EEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMI------------ 269
Cdd:TIGR02168  382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELeelqeelerlee 461
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   270 ---KLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFS---ERRIEE 343
Cdd:TIGR02168  462 aleELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDegyEAAIEA 541
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   344 -LQDRINDLEKER--------ELLKEN---------YDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALK-----SDL 400
Cdd:TIGR02168  542 aLGGRLQAVVVENlnaakkaiAFLKQNelgrvtflpLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkalSYL 621
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   401 TDKTEILDRLKTERDQNEKLVQENR--------------------ELQLQYLEQKQQLDELKKRIKLynQENDINA---- 456
Cdd:TIGR02168  622 LGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggvitggsaKTNSSILERRREIEELEEKIEE--LEEKIAEleka 699
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   457 -DELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQaTHAETVQELEKTRNMLIMQHKINKDY----QMEVE 531
Cdd:TIGR02168  700 lAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE-QLEERIAQLSKELTELEAEIEELEERleeaEEELA 778
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|
gi 118442834   532 AVTRKMENLQQDyelkVEQYVHLLDIRAARIHKLEAQLKD 571
Cdd:TIGR02168  779 EAEAEIEELEAQ----IEQLKEELKALREALDELRAELTL 814
PLN02939 PLN02939
transferase, transferring glycosyl groups
148-511 3.19e-07

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 54.91  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  148 TPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAetphpmftkygnslLEEARGEIRNLE-NVIQSQRGQIEELE 226
Cdd:PLN02939   91 TSSDDDHNRASMQRDEAIAAIDNEQQTNSKDGEQLSDFQ--------------LEDLVGMIQNAEkNILLLNQARLQALE 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  227 HLAEIL--KTQLRRKENEIELSLLQLREQQATDQRSNIrdNVEMikLHKQLVEKSNALSAmegkfiqlqekqrTLRISHD 304
Cdd:PLN02939  157 DLEKILteKEALQGKINILEMRLSETDARIKLAAQEKI--HVEI--LEEQLEKLRNELLI-------------RGATEGL 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  305 ALMANGDELNMqLKEQRLkccSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLyDSAFSAAHEEQWKLKEQQ 384
Cdd:PLN02939  220 CVHSLSKELDV-LKEENM---LLKDDIQFLKAELIEVAETEERVFKLEKERSLLDASLREL-ESKFIVAQEDVSKLSPLQ 294
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  385 LKVQIAQLETalksdLTDkteILDRLKTERDQNEKLVQENRELqlqyleqKQQLDELKKRIKLYN--QENDINADELSEA 462
Cdd:PLN02939  295 YDCWWEKVEN-----LQD---LLDRATNQVEKAALVLDQNQDL-------RDKVDKLEASLKEANvsKFSSYKVELLQQK 359
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 118442834  463 LLLIKAQKEQKNGDLSFLVKVdseinkdLERSMRELQATHAETVQELEK 511
Cdd:PLN02939  360 LKLLEERLQASDHEIHSYIQL-------YQESIKEFQDTLSKLKEESKK 401
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
341-578 5.00e-07

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.30  E-value: 5.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   341 IEELQDRINDLEKERELlKENYDKLydsafsaaheeQWKLKEQQLKVQIAQLETALKSdltdKTEILDRLKTERDQNEKL 420
Cdd:TIGR02169  193 IDEKRQQLERLRREREK-AERYQAL-----------LKEKREYEGYELLKEKEALERQ----KEAIERQLASLEEELEKL 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   421 VQENRELQLQYLEQKQQLDELKKRIKlynQENDINADELSEALLLIKAQKEQKNGDLSF-----------LVKVDSEINK 489
Cdd:TIGR02169  257 TEEISELEKRLEEIEQLLEELNKKIK---DLGEEEQLRVKEKIGELEAEIASLERSIAEkereledaeerLAKLEAEIDK 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   490 ------DLERSMRELQATHA---ETVQELEKTRNMLIMQ-------HKI----NKDYQMEVEAVTRKMENLQQDY----E 545
Cdd:TIGR02169  334 llaeieELEREIEEERKRRDkltEEYAELKEELEDLRAEleevdkeFAEtrdeLKDYREKLEKLKREINELKRELdrlqE 413
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 118442834   546 LKVEQYVHLLDIRA------ARIHKLEAQLKDIAYGTKQ 578
Cdd:TIGR02169  414 ELQRLSEELADLNAaiagieAKINELEEEKEDKALEIKK 452
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
200-569 5.25e-07

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: 54.34  E-value: 5.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   200 LLEEARGEIRNLENVIQSQ----RGQIEELEHLA---EILKTQLRR-----KENEIELSLLQLREQQATDQRSnirdnVE 267
Cdd:pfam05483  262 LLEESRDKANQLEEKTKLQdenlKELIEKKDHLTkelEDIKMSLQRsmstqKALEEDLQIATKTICQLTEEKE-----AQ 336
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   268 MIKLHKQLVEKSNALSAMEGKFIQLQEkqrTLRISHDALMANGDELNMQLKEQRLKCCSLEKQlhsMKFSERRIEELQDR 347
Cdd:pfam05483  337 MEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEKNEDQLKIITMELQKKSSELEEM---TKFKNNKEVELEEL 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   348 INDLEKERELLKEN--YDKLYDSAFSAAHEEQWKLKEQQ-----LKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKL 420
Cdd:pfam05483  411 KKILAEDEKLLDEKkqFEKIAEELKGKEQELIFLLQAREkeihdLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIEL 490
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   421 VQENRELQLQYLEQKQQLDELKkrIKLYNQENDINADELSEALLL-----IKAQKEQKNGDLSF----LVKVDSEINKDL 491
Cdd:pfam05483  491 TAHCDKLLLENKELTQEASDMT--LELKKHQEDIINCKKQEERMLkqienLEEKEMNLRDELESvreeFIQKGDEVKCKL 568
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   492 ERSMRELQATHAETvqeLEKTRNMLIMQHKINkDYQMEVEAVTRKMENLQQD---YELKVEQYVHLLDIRAARIHKLEAQ 568
Cdd:pfam05483  569 DKSEENARSIEYEV---LKKEKQMKILENKCN-NLKKQIENKNKNIEELHQEnkaLKKKGSAENKQLNAYEIKVNKLELE 644

                   .
gi 118442834   569 L 569
Cdd:pfam05483  645 L 645
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
201-463 7.68e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 7.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  201 LEEARGEIRNLEnviqsqrgqiEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRdnvemIKLHKQLVEKSN 280
Cdd:COG4913   237 LERAHEALEDAR----------EQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRR-----LELLEAELEELR 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  281 ALSAmegkfiQLQEKQRTLRISHDALMANGDELNMQLKEQRLkccslekqlhsmkfseRRIEELQDRINDLEKERELLKE 360
Cdd:COG4913   302 AELA------RLEAELERLEARLDALREELDELEAQIRGNGG----------------DRLEQLEREIERLERELEERER 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  361 NYDKlYDSAFSAAHEEqWKLKEQQLKVQIAQLETALksdlTDKTEILDRLKTERDQnekLVQENRELQLQYLEQKQQLDE 440
Cdd:COG4913   360 RRAR-LEALLAALGLP-LPASAEEFAALRAEAAALL----EALEEELEALEEALAE---AEAALRDLRRELRELEAEIAS 430
                         250       260
                  ....*....|....*....|...
gi 118442834  441 LKKRIKLYNQENDINADELSEAL 463
Cdd:COG4913   431 LERRKSNIPARLLALRDALAEAL 453
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
47-365 9.54e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 9.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    47 REELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVN-DKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQ 125
Cdd:TIGR02168  718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTElEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEE 797
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   126 NETLKNRLISAKQQLQTQgyrqtpynnvqsrintgrrkaNENAGLQECPRKGIKFQDADVAETphpmftkygnslLEEAR 205
Cdd:TIGR02168  798 LKALREALDELRAELTLL---------------------NEEAANLRERLESLERRIAATERR------------LEDLE 844
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   206 GEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIE-----LSLLQLREQQATDQRSNIRDNV-----EMIKLHKQL 275
Cdd:TIGR02168  845 EQIEELSEDIESLAAEIEELEELIEELESELEALLNERAsleeaLALLRSELEELSEELRELESKRselrrELEELREKL 924
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   276 VEKSNALSAMEGKFIQLQEKQRTL-RISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMK----FSERRIEELQDRIND 350
Cdd:TIGR02168  925 AQLELRLEGLEVRIDNLQERLSEEySLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGpvnlAAIEEYEELKERYDF 1004
                          330
                   ....*....|....*
gi 118442834   351 LEKERELLKENYDKL 365
Cdd:TIGR02168 1005 LTAQKEDLTEAKETL 1019
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
225-586 1.43e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 1.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   225 LEHLAEILKTQLRRKEneielSLLQLREQQA-----TDQRSNIRDNVEmiKLHKQlVEKSNalsamegKFIQLQEKQRTL 299
Cdd:TIGR02168  161 FEEAAGISKYKERRKE-----TERKLERTREnldrlEDILNELERQLK--SLERQ-AEKAE-------RYKELKAELREL 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   300 RIS-----HDALMANGDELNMQLKEQRLKCCSLEKQLHSmkfSERRIEELQDRINDLEKERELLKENYDKLydsafsaah 374
Cdd:TIGR02168  226 ELAllvlrLEELREELEELQEELKEAEEELEELTAELQE---LEEKLEELRLEVSELEEEIEELQKELYAL--------- 293
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   375 eeqwklkeqqlkvqiaqleTALKSDLTDKTEILDrlktERDQNekLVQENRELQLQYLEQKQQLDELKKRI-----KLYN 449
Cdd:TIGR02168  294 -------------------ANEISRLEQQKQILR----ERLAN--LERQLEELEAQLEELESKLDELAEELaeleeKLEE 348
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   450 QENDINA--DELSEALLLIKAQK----------EQKNGDLSFLVKVDSEINKDLER---SMRELQATHAETVQELEKTRN 514
Cdd:TIGR02168  349 LKEELESleAELEELEAELEELEsrleeleeqlETLRSKVAQLELQIASLNNEIERleaRLERLEDRRERLQQEIEELLK 428
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118442834   515 MLIMQHKinKDYQMEVEAVTRKMENLQQDYELKVEQyvhlLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIM 586
Cdd:TIGR02168  429 KLEEAEL--KELQAELEELEEELEELQEELERLEEA----LEELREELEEAEQALDAAERELAQLQARLDSL 494
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
63-474 1.59e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   63 LLKQHARKQEDKI--KRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQL 140
Cdd:COG4717    46 MLLERLEKEADELfkPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  141 QTQGYRQTP------YNNVQSRINTGRRKANENAGLQEcprkGIKFQDADVAETpHPMFTKYGNSLLEEARGEIRNLENV 214
Cdd:COG4717   126 QLLPLYQELealeaeLAELPERLEELEERLEELRELEE----ELEELEAELAEL-QEELEELLEQLSLATEEELQDLAEE 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  215 IQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQrsnIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQE 294
Cdd:COG4717   201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER---LKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  295 KQRT-----------LRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSE--------------RRIEELQDRIN 349
Cdd:COG4717   278 VLFLvlgllallfllLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPdlspeellelldriEELQELLREAE 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  350 DLEKEREL--LKENYDKLYDSAFSAAHEE-----QWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTE--RDQNEKL 420
Cdd:COG4717   358 ELEEELQLeeLEQEIAALLAEAGVEDEEElraalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEelEEELEEL 437
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 118442834  421 VQENRELQLQYLEQKQQLDELKKRIKlyNQENDinaDELSEALLLIKAQKEQKN 474
Cdd:COG4717   438 EEELEELEEELEELREELAELEAELE--QLEED---GELAELLQELEELKAELR 486
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
339-514 1.81e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  339 RRIEELQDRINDLEKERELLkenydklyDSAFSAAHEEQWKLKEQQLKVQIAQLETA---LKSDLTDKTEILDRLKTERD 415
Cdd:COG4913   262 ERYAAARERLAELEYLRAAL--------RLWFAQRRLELLEAELEELRAELARLEAElerLEARLDALREELDELEAQIR 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  416 QN-----EKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKD 490
Cdd:COG4913   334 GNggdrlEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAA 413
                         170       180
                  ....*....|....*....|....
gi 118442834  491 LERSMRELQATHAEtVQELEKTRN 514
Cdd:COG4913   414 LRDLRRELRELEAE-IASLERRKS 436
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
107-572 1.93e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 52.35  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTqgyrqtpynnvqsrINTGRRKANENAGLQECPRKGIKFQDADVA 186
Cdd:PRK02224  255 TLEAEIEDLRETIAETEREREELAEEVRDLRERLEE--------------LEEERDDLLAEAGLDDADAEAVEARREELE 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  187 ETphpmftkygnslLEEARGEIRNLENVIQSQRGQIE-------ELEHLAEILKTQLRRKENEIELSLLQLREQQA--TD 257
Cdd:PRK02224  321 DR------------DEELRDRLEECRVAAQAHNEEAEslredadDLEERAEELREEAAELESELEEAREAVEDRREeiEE 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  258 QRSNIRDN--------VEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRIS---HDALMANG---------------- 310
Cdd:PRK02224  389 LEEEIEELrerfgdapVDLGNAEDFLEELREERDELREREAELEATLRTARERveeAEALLEAGkcpecgqpvegsphve 468
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  311 ---------DELNMQLKEQRLKCCSLEK---QLHSMKFSERRIEELQDRINDLEK----ERELLKENYDKL--------- 365
Cdd:PRK02224  469 tieedrervEELEAELEDLEEEVEEVEErleRAEDLVEAEDRIERLEERREDLEEliaeRRETIEEKRERAeelreraae 548
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  366 YDSAFSAAHEEQWKLKEQQLKVQ--IAQLETALkSDLTDKTEILDRLKT---ERDQNEKLVQENRE----LQLQYLEQKQ 436
Cdd:PRK02224  549 LEAEAEEKREAAAEAEEEAEEAReeVAELNSKL-AELKERIESLERIRTllaAIADAEDEIERLREkreaLAELNDERRE 627
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  437 QLDELKKRIKlyNQENDINADELSEAllliKAQKEQKNgdlSFLVKVDSEInKDLERSMRELQATHAETVQELEKTRNmL 516
Cdd:PRK02224  628 RLAEKRERKR--ELEAEFDEARIEEA----REDKERAE---EYLEQVEEKL-DELREERDDLQAEIGAVENELEELEE-L 696
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 118442834  517 IMQHKINKDYQMEVEAVTRKMENLQQDY-ELKVEqyvhlldIRAARIHKLEAQLKDI 572
Cdd:PRK02224  697 RERREALENRVEALEALYDEAEELESMYgDLRAE-------LRQRNVETLERMLNET 746
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
223-588 2.90e-06

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: 51.65  E-value: 2.90e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   223 EELEHLAEILKTQLRRKENEIELSLLQLREQQAT---------DQRSNIRDNVEMIKLH----KQLVEKSNAL-SAMEGK 288
Cdd:pfam05483  222 EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKmkdltflleESRDKANQLEEKTKLQdenlKELIEKKDHLtKELEDI 301
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   289 FIQLQEKQRTLR-ISHDALMANGDELNM-QLKEQRLKCCSLEKQLHSMKfserrIEELQDRINDLEkerELLKENYDKLY 366
Cdd:pfam05483  302 KMSLQRSMSTQKaLEEDLQIATKTICQLtEEKEAQMEELNKAKAAHSFV-----VTEFEATTCSLE---ELLRTEQQRLE 373
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   367 DsafsaaHEEQWKLKEQQLKVQIAQLETALKsdLTDKTEI-LDRLKTERDQNEKLVQENREL-----QLQYLEQKQQLDE 440
Cdd:pfam05483  374 K------NEDQLKIITMELQKKSSELEEMTK--FKNNKEVeLEELKKILAEDEKLLDEKKQFekiaeELKGKEQELIFLL 445
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   441 LKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKD-LERSMRELQATHAETVQELEKTRNMLIMQ 519
Cdd:pfam05483  446 QAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDkLLLENKELTQEASDMTLELKKHQEDIINC 525
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118442834   520 HKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPD 588
Cdd:pfam05483  526 KKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILEN 594
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
221-499 4.40e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 51.22  E-value: 4.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  221 QIEELEHLAEILKTQLRRKENEIElsllqlREQQATDQRSNIRDNVEMIKlhKQLVEKSNALSAMEGKFIQLQEKQRTLR 300
Cdd:PRK03918  156 GLDDYENAYKNLGEVIKEIKRRIE------RLEKFIKRTENIEELIKEKE--KELEEVLREINEISSELPELREELEKLE 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  301 ISHDALmangDELNMQLKEQRLKCCSLEKqlhSMKFSERRIEELQDRINDLEKERELLKENYDKL-----YDSAFSAAHE 375
Cdd:PRK03918  228 KEVKEL----EELKEEIEELEKELESLEG---SKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkeKAEEYIKLSE 300
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  376 --EQWKLKEQQLKVQIAQLETALK------SDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQ---QLDELKKR 444
Cdd:PRK03918  301 fyEEYLDELREIEKRLSRLEEEINgieeriKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAkkeELERLKKR 380
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 118442834  445 IKLYNQEndinadELSEALLLIKAQKEQKNGDLSFLVKVDSEIN---KDLERSMRELQ 499
Cdd:PRK03918  381 LTGLTPE------KLEKELEELEKAKEEIEEEISKITARIGELKkeiKELKKAIEELK 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
37-572 6.23e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 6.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   37 KSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERvgggpkrlgRDVEMEEMIEQLQ 116
Cdd:COG1196   252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE---------RRRELEERLEELE 322
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  117 EKVHELEKQNETLKNRLISAKQQLQTQGYRQTpyNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAETphpmftky 196
Cdd:COG1196   323 EELAELEEELEELEEELEELEEELEEAEEELE--EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL-------- 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  197 gnSLLEEARGEIRNLENVIQSQRGQIEELEHLAEilktQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLV 276
Cdd:COG1196   393 --RAAAELAAQLEELEEAEEALLERLERLEEELE----ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  277 EKSNALSAMEGKFIQLQEKQRTLRISHDALMA--------NGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEE----- 343
Cdd:COG1196   467 ELLEEAALLEAALAELLEELAEAAARLLLLLEaeadyegfLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEaalaa 546
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  344 -LQDRIN----DLEKERELLKEN---------YDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDR 409
Cdd:COG1196   547 aLQNIVVeddeVAAAAIEYLKAAkagratflpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  410 LKTERDQNEKLVQenRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQkngdlsflvkVDSEINK 489
Cdd:COG1196   627 LVAARLEAALRRA--VTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAER----------LAEEELE 694
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  490 DLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRA--ARIHKLEA 567
Cdd:COG1196   695 LEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEleRELERLER 774

                  ....*
gi 118442834  568 QLKDI 572
Cdd:COG1196   775 EIEAL 779
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
201-443 6.95e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.45  E-value: 6.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILK------TQLRRKENEIELSLLQLREqqatdQRSNIRDNVEMIKLH-K 273
Cdd:PRK03918  202 LEEVLREINEISSELPELREELEKLEKEVKELEelkeeiEELEKELESLEGSKRKLEE-----KIRELEERIEELKKEiE 276
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  274 QLVEKSNALSAMEGKfiqlQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEK 353
Cdd:PRK03918  277 ELEEKVKELKELKEK----AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK 352
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  354 ERELLKEnYDKLYDSAfSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKterdqneKLVQENRELQLQYLE 433
Cdd:PRK03918  353 RLEELEE-RHELYEEA-KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEIS-------KITARIGELKKEIKE 423
                         250
                  ....*....|
gi 118442834  434 QKQQLDELKK 443
Cdd:PRK03918  424 LKKAIEELKK 433
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
39-375 9.18e-06

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 9.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    39 RQAVSRVSRE--ELEDRFLRLHDE----NILLKQHARKQ---EDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEME 109
Cdd:TIGR02169  708 SQELSDASRKigEIEKEIEQLEQEeeklKERLEELEEDLsslEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEAR 787
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   110 EMIEQLQEKVHELEKQNETLKN---RLISAKQQLQTQGYR----QTPYNNVQSRINTGRRKANENaglqecpRKGIKFQD 182
Cdd:TIGR02169  788 LSHSRIPEIQAELSKLEEEVSRieaRLREIEQKLNRLTLEkeylEKEIQELQEQRIDLKEQIKSI-------EKEIENLN 860
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   183 ADVAETphpmftkygNSLLEEARGEIRNLENVIQSQRGQIEELEhlAEIlkTQLRRKENEIELSLLQLREQQA--TDQRS 260
Cdd:TIGR02169  861 GKKEEL---------EEELEELEAALRDLESRLGDLKKERDELE--AQL--RELERKIEELEAQIEKKRKRLSelKAKLE 927
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   261 NIRDNVEMI-KLHKQLVEKSNALSAMEGKFIQLQEKQRtlrishdALMANGDeLNMQLKEQrlkccslekqlhsMKFSER 339
Cdd:TIGR02169  928 ALEEELSEIeDPKGEDEEIPEEELSLEDVQAELQRVEE-------EIRALEP-VNMLAIQE-------------YEEVLK 986
                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 118442834   340 RIEELQDRINDLEKERELLK---ENYDKLYDSAFSAAHE 375
Cdd:TIGR02169  987 RLDELKEKRAKLEEERKAILeriEEYEKKKREVFMEAFE 1025
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
201-365 1.61e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.24  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  201 LEEARGEIR---------NLENVIQSQRGQIEELEhlAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKL 271
Cdd:COG3206   191 LEEAEAALEefrqknglvDLSEEAKLLLQQLSELE--SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQL 268
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  272 HKQLVEKSNALSAMEGKF-------IQLQEKQRTLRISHDALMANG-DELNMQLKEQRLKCCSLEKQLHSMKFSERRIEE 343
Cdd:COG3206   269 RAQLAELEAELAELSARYtpnhpdvIALRAQIAALRAQLQQEAQRIlASLEAELEALQAREASLQAQLAQLEARLAELPE 348
                         170       180
                  ....*....|....*....|..
gi 118442834  344 LQDRINDLEKERELLKENYDKL 365
Cdd:COG3206   349 LEAELRRLEREVEVARELYESL 370
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
208-460 1.88e-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: 49.05  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   208 IRNLENVIQSQRGQIEELEHLAEILKTQ--------------LRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHK 273
Cdd:pfam10174  403 IENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttleeaLSEKERIIE----RLKEQREREDRERLEELESLKKENK 478
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   274 QLVEKSNAL----SAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQL---HSMKFSERRIEELQD 346
Cdd:pfam10174  479 DLKEKVSALqpelTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkaHNAEEAVRTNPEIND 558
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   347 RINDLEKERELLKE-------NYDKLYDSAFSAAHEEQWKLKeqqlkvQIAQLETALKSDLTDKTEILDRLKT----ERD 415
Cdd:pfam10174  559 RIRLLEQEVARYKEesgkaqaEVERLLGILREVENEKNDKDK------KIAELESLTLRQMKEQNKKVANIKHgqqeMKK 632
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 118442834   416 QNEKLVQENRELQLQYLE--QKQQLDELKKRIKLYNQENDINADELS 460
Cdd:pfam10174  633 KGAQLLEEARRREDNLADnsQQLQLEELMGALEKTRQELDATKARLS 679
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
201-477 1.96e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.36  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  201 LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQAtdqrsnirdnvEMIKLHKQLVEKSN 280
Cdd:COG4372    40 LDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQA-----------ELAQAQEELESLQE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  281 ALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELlke 360
Cdd:COG4372   109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL--- 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  361 nyDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDE 440
Cdd:COG4372   186 --DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEEL 263
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 118442834  441 LKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDL 477
Cdd:COG4372   264 ELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
191-533 2.01e-05

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: 49.20  E-value: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   191 PMFTKYGNSLLEEARGEIRNLENVIQSQR-----GQIEELEHLAEILKTQLRRK--ENEIELSLLQLREQQATDQRSNIR 263
Cdd:TIGR00618  601 EKLSEAEDMLACEQHALLRKLQPEQDLQDvrlhlQQCSQELALKLTALHALQLTltQERVREHALSIRVLPKELLASRQL 680
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   264 DNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLR--------ISHDA---LMANGDELNMQLKE----QRLKCCSLE 328
Cdd:TIGR00618  681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDrefneienASSSLgsdLAAREDALNQSLKElmhqARTVLKART 760
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   329 KQlHSMKFSERRIE-----ELQDRINDLEKERELLKENYdklydsafsaaheeqwklkeQQLKVQIAQLETALKSDLTDK 403
Cdd:TIGR00618  761 EA-HFNNNEEVTAAlqtgaELSHLAAEIQFFNRLREEDT--------------------HLLKTLEAEIGQEIPSDEDIL 819
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   404 TEILDRLKTERDQNEKLVQEN-------RELQLQYLEQKQQLDELKKRIKLYNQendinadeLSEALLLIKAQKEQKNGD 476
Cdd:TIGR00618  820 NLQCETLVQEEEQFLSRLEEKsatlgeiTHQLLKYEECSKQLAQLTQEQAKIIQ--------LSDKLNGINQIKIQFDGD 891
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 118442834   477 LsfLVKVDSEINKDLERSMRELQATHAETVQELektrnmlimQHKINKDYQMEVEAV 533
Cdd:TIGR00618  892 A--LIKFLHEITLYANVRLANQSEGRFHGRYAD---------SHVNARKYQGLALLV 937
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
109-464 2.44e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  109 EEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVAet 188
Cdd:COG4717    87 EEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE-- 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  189 phpmftkygnslLEEARGEIRNLENVIQSQRGQ--IEELEHLAEILKT----QLRRKENEIELSLLQLREQQATDQRSNI 262
Cdd:COG4717   165 ------------LEELEAELAELQEELEELLEQlsLATEEELQDLAEEleelQQRLAELEEELEEAQEELEELEEELEQL 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  263 RDNVEMIKLHKQLVEKSN------ALSAMEGKFIQLQEKQRT------------------LRISHDALMANGDELNMQLK 318
Cdd:COG4717   233 ENELEAAALEERLKEARLllliaaALLALLGLGGSLLSLILTiagvlflvlgllallfllLAREKASLGKEAEELQALPA 312
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  319 EQRLKCCSLEKQLHSMKFSE--------------RRIEELQDRINDLEKEREL--LKENYDKLYDSAFSAAHEE-----Q 377
Cdd:COG4717   313 LEELEEEELEELLAALGLPPdlspeellelldriEELQELLREAEELEEELQLeeLEQEIAALLAEAGVEDEEElraalE 392
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  378 WKLKEQQLKVQIAQLETALKS---------DLTDKTEI---LDRLKTERDQNEKLVQENRE------LQLQYLEQKQQLD 439
Cdd:COG4717   393 QAEEYQELKEELEELEEQLEEllgeleellEALDEEELeeeLEELEEELEELEEELEELREelaeleAELEQLEEDGELA 472
                         410       420       430
                  ....*....|....*....|....*....|
gi 118442834  440 ELKKRI-----KLYNQENDINADELSEALL 464
Cdd:COG4717   473 ELLQELeelkaELRELAEEWAALKLALELL 502
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
316-517 2.77e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 48.61  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  316 QLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLydsafsaaheeqwkLKEQQLKVQIAQLEtA 395
Cdd:COG4717    72 ELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL--------------EKLLQLLPLYQELE-A 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  396 LKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQEndiNADELSEALLLIKAQKEQKNG 475
Cdd:COG4717   137 LEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEE---ELQDLAEELEELQQRLAELEE 213
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 118442834  476 DLSFLVKVDSEINKDLERsmRELQATHAETVQELEKTRNMLI 517
Cdd:COG4717   214 ELEEAQEELEELEEELEQ--LENELEAAALEERLKEARLLLL 253
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
244-562 2.84e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 2.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  244 ELSLLQLREQQATDQ------RSNIRDNVEMIKLHKQLVEKSNALSAMEGKF---IQLQEKQRT--LRISH--------- 303
Cdd:COG3206    72 GLSSLSASDSPLETQieilksRPVLERVVDKLNLDEDPLGEEASREAAIERLrknLTVEPVKGSnvIEISYtspdpelaa 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  304 ---DALMANGDELNMQLKEQRLKccslekqlHSMKFSERRIEELQDRINDLEKERELLKENYDkLYDSafsaahEEQWKL 380
Cdd:COG3206   152 avaNALAEAYLEQNLELRREEAR--------KALEFLEEQLPELRKELEEAEAALEEFRQKNG-LVDL------SEEAKL 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  381 KEQQLkVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQEN------RELQLQYLEQKQQLDELKKRiklYNQENDI 454
Cdd:COG3206   217 LLQQL-SELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqspviQQLRAQLAELEAELAELSAR---YTPNHPD 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  455 nadelsealllIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLimqhkinkdyqMEVEAVT 534
Cdd:COG3206   293 -----------VIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARL-----------AELPELE 350
                         330       340
                  ....*....|....*....|....*....
gi 118442834  535 RKMENLQQDYELKVEQYVHLLD-IRAARI 562
Cdd:COG3206   351 AELRRLEREVEVARELYESLLQrLEEARL 379
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
221-504 2.92e-05

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 47.60  E-value: 2.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  221 QIEELEHLAEILKT---QLRRKENEIELSLLQLREQqatdqrsniRDnvemiKLHKQLVEKSNALSAMEGKFIQLQEKQR 297
Cdd:COG1340     9 SLEELEEKIEELREeieELKEKRDELNEELKELAEK---------RD-----ELNAQVKELREEAQELREKRDELNEKVK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  298 TLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRIN----DLEKERELLKE--NYDKLYDSAfs 371
Cdd:COG1340    75 ELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQQtevlSPEEEKELVEKikELEKELEKA-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  372 aaheeqwkLKEQQLKVQIAQLETALKsdltdktEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQE 451
Cdd:COG1340   153 --------KKALEKNEKLKELRAELK-------ELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKE 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 118442834  452 ND---INADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAE 504
Cdd:COG1340   218 IVeaqEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIF 273
PTZ00121 PTZ00121
MAEBL; Provisional
69-552 3.24e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   69 RKQEDKIKRMATKL---IRLVNDKKRYERvgggpkrlGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGY 145
Cdd:PTZ00121 1194 RKAEDARKAEAARKaeeERKAEEARKAED--------AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHF 1265
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  146 --RQTPYNNVQSRINTGRRKANENAGLQECpRKGIKFQDADVAETPHPMFTKygnslLEEARGEIRNLENVIQSQRGQIE 223
Cdd:PTZ00121 1266 arRQAAIKAEEARKADELKKAEEKKKADEA-KKAEEKKKADEAKKKAEEAKK-----ADEAKKKAEEAKKKADAAKKKAE 1339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  224 ELEHLAEILKTQLRRKENEIELSllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALsamEGKFIQLQEKQRTLRISH 303
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAA--EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEA---KKKAEEDKKKADELKKAA 1414
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  304 DAlMANGDELNMQLKEQRlKCCSLEKQLHSmkfsERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQ 383
Cdd:PTZ00121 1415 AA-KKKADEAKKKAEEKK-KADEAKKKAEE----AKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  384 QLKVQiaqlETALKSDLTDKTEildRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKriklynQENDINADELSEAL 463
Cdd:PTZ00121 1489 KKKAE----EAKKKADEAKKAA---EAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKK------AEEKKKADELKKAE 1555
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  464 LLIKAQKEQKNgdlsflvkvdSEINKDLERsmRELQATHAETVQELEKTRNMLIMQhKINKDYQMEVEAVTRKMENLQQD 543
Cdd:PTZ00121 1556 ELKKAEEKKKA----------EEAKKAEED--KNMALRKAEEAKKAEEARIEEVMK-LYEEEKKMKAEEAKKAEEAKIKA 1622

                  ....*....
gi 118442834  544 YELKVEQYV 552
Cdd:PTZ00121 1623 EELKKAEEE 1631
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
47-492 3.29e-05

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: 48.53  E-value: 3.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    47 REELEDRFLRLhDENILLKQHARKQEDKIKRMATKLIR---LVNDKKRYErvggGPKRLGRDVEMEEMIEQLQEKVHELE 123
Cdd:TIGR02169  176 LEELEEVEENI-ERLDLIIDEKRQQLERLRREREKAERyqaLLKEKREYE----GYELLKEKEALERQKEAIERQLASLE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   124 KQNETLKnrlisakQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQecprkgIKFQdadvaetphpmftkygnslLEE 203
Cdd:TIGR02169  251 EELEKLT-------EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR------VKEK-------------------IGE 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   204 ARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHKQlveksnals 283
Cdd:TIGR02169  299 LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLTEEYAELKEE--------- 365
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   284 aMEGKFIQLQEKQRTLRISHDALMAngdelnmqlkeqrlkccslekqlhsmkfSERRIEELQDRINDLEKERELLKENYD 363
Cdd:TIGR02169  366 -LEDLRAELEEVDKEFAETRDELKD----------------------------YREKLEKLKREINELKRELDRLQEELQ 416
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   364 KLydSAFSAAHEEQWKLKEQQLKVQIAQLETA---LKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDE 440
Cdd:TIGR02169  417 RL--SEELADLNAAIAGIEAKINELEEEKEDKaleIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|..
gi 118442834   441 LKKRIKLYNQENDINADelseALLLIKAQKEQKNGDLSFLVKVDSEINKDLE 492
Cdd:TIGR02169  495 AEAQARASEERVRGGRA----VEEVLKASIQGVHGTVAQLGSVGERYATAIE 542
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
311-512 3.56e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.90  E-value: 3.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  311 DELNMQLKEQRLKCCSLEKQLHSMkfsERRIEELQDRINDLEKERELLKENYDKLYDSAfsAAHEEQWKLKEQQLKVQIA 390
Cdd:COG3883    19 QAKQKELSELQAELEAAQAELDAL---QAELEELNEEYNELQAELEALQAEIDKLQAEI--AEAEAEIEERREELGERAR 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  391 Q----------LETALKS-DLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLynqendiNADEL 459
Cdd:COG3883    94 AlyrsggsvsyLDVLLGSeSFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA-------LKAEL 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118442834  460 SEALLLIKAQKEQKNGDLSFLvkvdSEINKDLERSMRELQATHAETVQELEKT 512
Cdd:COG3883   167 EAAKAELEAQQAEQEALLAQL----SAEEAAAEAQLAELEAELAAAEAAAAAA 215
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
209-446 3.58e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 3.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  209 RNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIE-------LSLLQLREQQATDQRSNIRDnvemiklhkQLVEKSNA 281
Cdd:COG3206   164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEefrqkngLVDLSEEAKLLLQQLSELES---------QLAEARAE 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  282 LSAMEGKFIQLQEKQRTLRISHDALMAngDELNMQLKEQRLKccsLEKQLHSM--KFSER--RIEELQDRINDLekeREL 357
Cdd:COG3206   235 LAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAE---LEAELAELsaRYTPNhpDVIALRAQIAAL---RAQ 306
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  358 LKENYDKLYDSAFSAAheeqwklkeQQLKVQIAQLETALksdltdkteilDRLKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:COG3206   307 LQQEAQRILASLEAEL---------EALQAREASLQAQL-----------AQLEARLAELPELEAELRRLEREVEVAREL 366

                  ....*....
gi 118442834  438 LDELKKRIK 446
Cdd:COG3206   367 YESLLQRLE 375
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
372-513 4.03e-05

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: 46.46  E-value: 4.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  372 AAHEEQWKLKE-QQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQ 450
Cdd:COG1579     1 AMPEDLRALLDlQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  451 -------ENDINA------------DELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEK 511
Cdd:COG1579    81 qlgnvrnNKEYEAlqkeieslkrriSDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160

                  ..
gi 118442834  512 TR 513
Cdd:COG1579   161 LE 162
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
208-561 5.39e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 5.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  208 IRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEG 287
Cdd:COG4372    26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELE----QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  288 KFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLhsmKFSERRIEELQDRINDLEKERELLKENYDKLYD 367
Cdd:COG4372   102 ELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI---AEREEELKELEEQLESLQEELAALEQELQALSE 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  368 safSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKL 447
Cdd:COG4372   179 ---AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  448 YNQENDINADELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNMLIMQHKINKDYQ 527
Cdd:COG4372   256 ILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
                         330       340       350
                  ....*....|....*....|....*....|....
gi 118442834  528 MEVEAVTRKMENLQQDYELKVEQYVHLLDIRAAR 561
Cdd:COG4372   336 LAELADLLQLLLVGLLDNDVLELLSKGAEAGVAD 369
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
388-569 5.69e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 5.69e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  388 QIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEAlllik 467
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER----- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  468 AQKEQKNGD----LSFLVKVDSeINKDLERS--MRELQATHAETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENLQ 541
Cdd:COG3883    92 ARALYRSGGsvsyLDVLLGSES-FSDFLDRLsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK 170
                         170       180
                  ....*....|....*....|....*...
gi 118442834  542 QDYELKVEQYVHLLDIRAARIHKLEAQL 569
Cdd:COG3883   171 AELEAQQAEQEALLAQLSAEEAAAEAQL 198
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
202-462 6.17e-05

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 47.20  E-value: 6.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   202 EEARGEIRNLENVIQSQRGQIEELEhlaeilkTQLRRKENEIELSLLQLREQQATDQRSNIR---DNVEMIKLHKQLVEK 278
Cdd:pfam07888  125 AAHEARIRELEEDIKTLTQRVLERE-------TELERMKERAKKAGAQRKEEEAERKQLQAKlqqTEEELRSLSKEFQEL 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   279 SNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRlkccSLEKQLHSmkfSERRIEELQDRINDLEKERell 358
Cdd:pfam07888  198 RNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR----SLQERLNA---SERKVEGLGEELSSMAAQR--- 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   359 kenydklyDSAFSAAHeeQWKLKEQQLKVQIAQLETALKSDLT----DKTEILDRLKTERDQNEKLvqeNRELQ-LQYLE 433
Cdd:pfam07888  268 --------DRTQAELH--QARLQAAQLTLQLADASLALREGRArwaqERETLQQSAEADKDRIEKL---SAELQrLEERL 334
                          250       260
                   ....*....|....*....|....*....
gi 118442834   434 QKQQLDELKKRIKLyNQENDINADELSEA 462
Cdd:pfam07888  335 QEERMEREKLEVEL-GREKDCNRVQLSES 362
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
43-442 7.03e-05

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: 47.53  E-value: 7.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    43 SRVSREELEdRFLRLHD-----ENIllKQHARKQEDKIKRMATKLIRLVNDKKRYervgggpkrlgrdVEMEEMIEQLQE 117
Cdd:pfam12128  216 SRLNRQQVE-HWIRDIQaiagiMKI--RPEFTKLQQEFNTLESAELRLSHLHFGY-------------KSDETLIASRQE 279
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   118 KVHELEKQnetLKNRLISAKQQLQtqgyrqtpynnvQSRINTGRRKANENAGLQECPrkgikfQDADVAETPHPMFTKYG 197
Cdd:pfam12128  280 ERQETSAE---LNQLLRTLDDQWK------------EKRDELNGELSAADAAVAKDR------SELEALEDQHGAFLDAD 338
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   198 nslLEEARGEIRNLENViqsqRGQIEELEHLAEILKTQLRRKENEIElSLLQLREQQATDQRSNIRDNVEMIK--LHKQL 275
Cdd:pfam12128  339 ---IETAAADQEQLPSW----QSELENLEERLKALTGKHQDVTAKYN-RRRSKIKEQNNRDIAGIKDKLAKIReaRDRQL 410
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   276 VEKSNALSAMEGKfiqlqekqrtLRISHDALMANGDELNMQLKEqrlkccslekqlhsmkfserRIEELQDRINDLEKER 355
Cdd:pfam12128  411 AVAEDDLQALESE----------LREQLEAGKLEFNEEEYRLKS--------------------RLGELKLRLNQATATP 460
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   356 ELLKENydKLYDSAFSAAHEEQWKLKEQQLkvqiaqletALKSDLTdkteildRLKTERDQ-NEKLVQENRELQlqylEQ 434
Cdd:pfam12128  461 ELLLQL--ENFDERIERAREEQEAANAEVE---------RLQSELR-------QARKRRDQaSEALRQASRRLE----ER 518

                   ....*...
gi 118442834   435 KQQLDELK 442
Cdd:pfam12128  519 QSALDELE 526
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
109-321 8.60e-05

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 46.30  E-value: 8.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  109 EEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQ----GYRQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDAD 184
Cdd:COG4942    26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALerriAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  185 VAE----------TPHPMFTKYGNSLLEEARGeIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElSLLQLREQQ 254
Cdd:COG4942   106 LAEllralyrlgrQPPLALLLSPEDFLDAVRR-LQYLKYLAPARREQAEELRADLAELAALRAELEAERA-ELEALLAEL 183
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118442834  255 ATDQRsnirdnvemiKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQR 321
Cdd:COG4942   184 EEERA----------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
46 PHA02562
endonuclease subunit; Provisional
232-598 9.26e-05

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 46.55  E-value: 9.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  232 LKTQLRRK--ENEIELSLL---------QLRE--QQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEgkfiqLQEKQRT 298
Cdd:PHA02562  147 LSAPARRKlvEDLLDISVLsemdklnkdKIRElnQQIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGEN-----IARKQNK 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  299 LrishdalmangDELnmqLKEqrlkccslEKQLHSmkfserRIEELQDRINDLEKERELLKENYDKLYDSAFsaaheeqw 378
Cdd:PHA02562  222 Y-----------DEL---VEE--------AKTIKA------EIEELTDELLNLVMDIEDPSAALNKLNTAAA-------- 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  379 klkeqQLKVQIAQLETALKSdLTDKTEI---LDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNqendin 455
Cdd:PHA02562  266 -----KIKSKIEQFQKVIKM-YEKGGVCptcTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFN------ 333
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  456 adELSEALLLIKAQKEQKNGDLSFLVKVdseiNKDLERSMRELQATHAETVQELEKTRNMLImqhKINKDYQmevEAVTR 535
Cdd:PHA02562  334 --EQSKKLLELKNKISTNKQSLITLVDK----AKKVKAAIEELQAEFVDNAEELAKLQDELD---KIVKTKS---ELVKE 401
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118442834  536 KME-----NLQQDYELKveqyvhlldiraARIHKleaqlKDIAYGTKQYKFKPEIMPDDSV----DEFDETI 598
Cdd:PHA02562  402 KYHrgivtDLLKDSGIK------------ASIIK-----KYIPYFNKQINHYLQIMEADYNftldEEFNETI 456
mukB PRK04863
chromosome partition protein MukB;
264-552 1.83e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 46.10  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  264 DNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKE---QRLKccSLEKQLHSMKFSERR 340
Cdd:PRK04863  835 PEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADEtlaDRVE--EIREQLDEAEEAKRF 912
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  341 IEELQDRINDLEKERELLK---ENYDKLYDSAFSAahEEQWKLKEQQLK--VQIAQLETALK-----SDLTDKTEILDRL 410
Cdd:PRK04863  913 VQQHGNALAQLEPIVSVLQsdpEQFEQLKQDYQQA--QQTQRDAKQQAFalTEVVQRRAHFSyedaaEMLAKNSDLNEKL 990
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  411 KTERDQNEklvQENRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEAlllikaqkEQKNGDLSflVKVDSEINKD 490
Cdd:PRK04863  991 RQRLEQAE---QERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQEL--------KQELQDLG--VPADSGAEER 1057
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118442834  491 LERSMRELQA---THAETVQELEKTRNMLimqhkinkdyQMEVEAVTRKMENLQQDYELKVEQYV 552
Cdd:PRK04863 1058 ARARRDELHArlsANRSRRNQLEKQLTFC----------EAEMDNLTKKLRKLERDYHEMREQVV 1112
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
207-323 1.83e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.90  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  207 EIRNLENVIQSQRGQIEELEHLAEILK--TQLRRKENEIELSLLQLRE--QQATDQRSNIRDNVEMIK-----LHKQLVE 277
Cdd:COG1340   141 KIKELEKELEKAKKALEKNEKLKELRAelKELRKEAEEIHKKIKELAEeaQELHEEMIELYKEADELRkeadeLHKEIVE 220
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 118442834  278 KSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLK 323
Cdd:COG1340   221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELE 266
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
198-367 2.56e-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: 44.15  E-value: 2.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  198 NSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllQLREQQATDQR--SNIRDNVEMIKLHKQL 275
Cdd:COG1579    23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE----EVEARIKKYEEqlGNVRNNKEYEALQKEI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  276 VEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEqrlkccsLEKQLhsmkfsERRIEELQDRINDLEKER 355
Cdd:COG1579    99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE-------KKAEL------DEELAELEAELEELEAER 165
                         170
                  ....*....|....*.
gi 118442834  356 ELLKENYD----KLYD 367
Cdd:COG1579   166 EELAAKIPpellALYE 181
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
341-454 2.82e-04

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 45.46  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  341 IEELQDRINDLEKERELLKENYDKLydsafSAAHEEQWKLKEQQLKVQIAQLETALKSDltdkTEILDRLKTERDQNEKL 420
Cdd:COG0542   413 LDELERRLEQLEIEKEALKKEQDEA-----SFERLAELRDELAELEEELEALKARWEAE----KELIEEIQELKEELEQR 483
                          90       100       110
                  ....*....|....*....|....*....|....
gi 118442834  421 VQENRELQLQYLEQKQQLDELKKRIKLYNQENDI 454
Cdd:COG0542   484 YGKIPELEKELAELEEELAELAPLLREEVTEEDI 517
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
207-410 3.85e-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: 43.37  E-value: 3.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  207 EIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElsllqlreqqatDQRSNIRDNVEMIKLHKQLVEKSnalsame 286
Cdd:COG1579    18 ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE------------DLEKEIKRLELEIEEVEARIKKY------- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  287 gkfiqlQEKQRTLRishdalmaNGDELNmqlkeqrlkccSLEKQLHSMKfseRRIEELQDRINDLEKERELLKENYDKLy 366
Cdd:COG1579    79 ------EEQLGNVR--------NNKEYE-----------ALQKEIESLK---RRISDLEDEILELMERIEELEEELAEL- 129
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 118442834  367 dSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRL 410
Cdd:COG1579   130 -EAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
312-601 4.02e-04

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 45.04  E-value: 4.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   312 ELNMQLKEQRLKCCSLEKQLHSMKFSERRIE-----------ELQDRINDLEKERELLKENYD--KLYDSAfSAAHEEQW 378
Cdd:TIGR01612  562 EIKKELEEENEDSIHLEKEIKDLFDKYLEIDdeiiyinklklELKEKIKNISDKNEYIKKAIDlkKIIENN-NAYIDELA 640
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   379 KLKEQQLKVQIAQLET---ALKSDLTDKTE-ILDRLKTERdqnEKLVQENrelQLQYLEQKQQLDELKKRI-KLYNQEND 453
Cdd:TIGR01612  641 KISPYQVPEHLKNKDKiysTIKSELSKIYEdDIDALYNEL---SSIVKEN---AIDNTEDKAKLDDLKSKIdKEYDKIQN 714
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   454 INADELSEALLLIkaqKEQKNGDLSFLVKVD----SEINKDLERSMRELQATHAE---TVQELEKTRNML-IMQHKINK- 524
Cdd:TIGR01612  715 METATVELHLSNI---ENKKNELLDIIVEIKkhihGEINKDLNKILEDFKNKEKElsnKINDYAKEKDELnKYKSKISEi 791
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118442834   525 --DYQMEVEAVTRKMENLQQDYElKVEQYVHLLDIRAARIHKLEAQLKDiaygtkqykfkpeiMPDDSVDEFDETIHLE 601
Cdd:TIGR01612  792 knHYNDQINIDNIKDEDAKQNYD-KSKEYIKTISIKEDEIFKIINEMKF--------------MKDDFLNKVDKFINFE 855
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
64-511 5.20e-04

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: 44.65  E-value: 5.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    64 LKQHARKQEDKIKRMATKLIRLvnDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQ 143
Cdd:TIGR00606  700 LQSKLRLAPDKLKSTESELKKK--EKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTI 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   144 GYRQTPYNNVQSRINTGRRKANEnagLQECPRKgIKFQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIE 223
Cdd:TIGR00606  778 MPEEESAKVCLTDVTIMERFQME---LKDVERK-IAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQ 853
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   224 ELEHLAEILKTQLRR-KENEIELSLLQLREQQATDQRSNIRDNV-EMIKLHKQLVEKSNALSAMEGKFiqLQEKQRTLRI 301
Cdd:TIGR00606  854 DQQEQIQHLKSKTNElKSEKLQIGTNLQRRQQFEEQLVELSTEVqSLIREIKDAKEQDSPLETFLEKD--QQEKEELISS 931
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   302 SHDALMANGDELNMQLKEqrlkccsLEKQLHSMKFSERRIEELQDRiNDLEKERELLKENYDKLYDSAFSAAHEEQWKLK 381
Cdd:TIGR00606  932 KETSNKKAQDKVNDIKEK-------VKNIHGYMKDIENKIQDGKDD-YLKQKETELNTVNAQLEECEKHQEKINEDMRLM 1003
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   382 EQQLKVQIAQlETALKSDLT--DKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQ--LDELKK-------RIKLYNQ 450
Cdd:TIGR00606 1004 RQDIDTQKIQ-ERWLQDNLTlrKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEenIDLIKRnhvlalgRQKGYEK 1082
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118442834   451 ENDINADELSEALLlikAQKEQKNGDLSFLVKVDSEINKDLERSMRELQAT----HAETVQELEK 511
Cdd:TIGR00606 1083 EIKHFKKELREPQF---RDAEEKYREMMIVMRTTELVNKDLDIYYKTLDQAimkfHSMKMEEINK 1144
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
193-539 5.95e-04

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: 44.27  E-value: 5.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   193 FTKYGNSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQR--SNIRDNVEMIK 270
Cdd:TIGR00606  696 FISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRlkNDIEEQETLLG 775
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   271 LHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQlHSMKFSERRIEELQDRIND 350
Cdd:TIGR00606  776 TIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ-HELDTVVSKIELNRKLIQD 854
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   351 LEKERELLKENYDKLYDSAFS--------AAHEEQW--KLKE--------QQLKVQIAQLETALKSDLTDKTEILDRLKT 412
Cdd:TIGR00606  855 QQEQIQHLKSKTNELKSEKLQigtnlqrrQQFEEQLveLSTEvqslireiKDAKEQDSPLETFLEKDQQEKEELISSKET 934
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   413 ERDQNEKLVQE-NRELQLQYLEQKQQLDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNGDLSfLVKVDSEINKDL 491
Cdd:TIGR00606  935 SNKKAQDKVNDiKEKVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMR-LMRQDIDTQKIQ 1013
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 118442834   492 ERSMRE--LQATHAETVQELEKTRNMLIMQhkINKDYQMEVEAVTRKMEN 539
Cdd:TIGR00606 1014 ERWLQDnlTLRKRENELKEVEEELKQHLKE--MGQMQVLQMKQEHQKLEE 1061
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
209-564 5.97e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 44.40  E-value: 5.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   209 RNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQAtdQRSNIRDNVEmiKLHKQLVEKSNALSAMEGK 288
Cdd:pfam01576  211 RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA--QKNNALKKIR--ELEAQISELQEDLESERAA 286
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   289 FIQLQEKQRTLrishdalmanGDELNMQLKEqrlkccsLEKQLHSMKFSerriEELQDRindLEKERELLKEnydklyds 368
Cdd:pfam01576  287 RNKAEKQRRDL----------GEELEALKTE-------LEDTLDTTAAQ----QELRSK---REQEVTELKK-------- 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   369 afsaAHEEQWKLKEQQLKvQIAQLETALKSDLTDKTEILDRLKTERDQNEK-LVQENRELQ--LQYLEQKQQLDELKKRi 445
Cdd:pfam01576  335 ----ALEEETRSHEAQLQ-EMRQKHTQALEELTEQLEQAKRNKANLEKAKQaLESENAELQaeLRTLQQAKQDSEHKRK- 408
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   446 KLYNQENDINA---------DELSEALLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQAThaetvQEL--EKTRN 514
Cdd:pfam01576  409 KLEGQLQELQArlseserqrAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDT-----QELlqEETRQ 483
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|..
gi 118442834   515 MLIMQHKINkdyQMEVEAvTRKMENLQQDYELK--VEQYVHLLDIRAARIHK 564
Cdd:pfam01576  484 KLNLSTRLR---QLEDER-NSLQEQLEEEEEAKrnVERQLSTLQAQLSDMKK 531
C2A_Tricalbin-like cd04044
C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are ...
792-916 6.45e-04

C2 domain first repeat present in Tricalbin-like proteins; 5 to 6 copies of the C2 domain are present in Tricalbin, a yeast homolog of Synaptotagmin, which is involved in membrane trafficking and sorting. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 176009 [Multi-domain]  Cd Length: 124  Bit Score: 41.00  E-value: 6.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  792 LHITIRCCNHLQSRASHLQ-PHPYVVYKFFDFADHD-TAIIPSSNDPQFDDHMYFPVpmNMDldrylkSESLSFYVFDDS 869
Cdd:cd04044     4 LAVTIKSARGLKGSDIIGGtVDPYVTFSISNRRELArTKVKKDTSNPVWNETKYILV--NSL------TEPLNLTVYDFN 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 118442834  870 DTQENIYIGKVNVPLISLAHDRCISGI-FELTDHQKhPAGTIHVILKW 916
Cdd:cd04044    76 DKRKDKLIGTAEFDLSSLLQNPEQENLtKNLLRNGK-PVGELNYDLRF 122
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
112-462 9.38e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 9.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  112 IEQLQEKVHELEKQNETLKNRLISAKQQLQTQgyrqtpynnvqsrintgRRKANENAGLQEcprkgIKFQDADVAetphp 191
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDAL-----------------QERREALQRLAE-----YSWDEIDVA----- 664
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  192 mftkygnslleEARGEIRNLENVIQSQR---GQIEELEHLAEILKTQLRRKENEI-----ELSLLQLREQQATDQRSNIR 263
Cdd:COG4913   665 -----------SAEREIAELEAELERLDassDDLAALEEQLEELEAELEELEEELdelkgEIGRLEKELEQAEEELDELQ 733
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  264 DNVEMIKLHKQLVEKSNAlsamEGKFIQLQEKQRTLRIShDALMANGDELNMQLKEQRLKccsLEKQLHsmKFSERRIEE 343
Cdd:COG4913   734 DRLEAAEDLARLELRALL----EERFAAALGDAVERELR-ENLEERIDALRARLNRAEEE---LERAMR--AFNREWPAE 803
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  344 LQDRINDLEKERELLKEnYDKLYDSAFsAAHEEQWK-LKEQQLKVQIAQLETALKSDLTDKTEILDRLkterdqNEKLVQ 422
Cdd:COG4913   804 TADLDADLESLPEYLAL-LDRLEEDGL-PEYEERFKeLLNENSIEFVADLLSKLRRAIREIKERIDPL------NDSLKR 875
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 118442834  423 ----ENRELQLQYLE-QKQQLDELKKRIKLYNQENDINADELSEA 462
Cdd:COG4913   876 ipfgPGRYLRLEARPrPDPEVREFRQELRAVTSGASLFDEELSEA 920
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
198-569 1.16e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 43.19  E-value: 1.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   198 NSLLEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRdNVEMIKLHKQLVE 277
Cdd:pfam05557   89 NKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQL-RQNLEKQQSSLAE 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   278 KSNALSAMEGKfIQLQE---------KQRTLRISH-DALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDR 347
Cdd:pfam05557  168 AEQRIKELEFE-IQSQEqdseivknsKSELARIPElEKELERLREHNKHLNENIENKLLLKEEVEDLKRKLEREEKYREE 246
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   348 INDLEKERELLKEnydKLydsafsaaheEQWKLKEQQLKVQI-------AQLETALKSDLT---DKTEILDRLKTERDQN 417
Cdd:pfam05557  247 AATLELEKEKLEQ---EL----------QSWVKLAQDTGLNLrspedlsRRIEQLQQREIVlkeENSSLTSSARQLEKAR 313
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   418 EKLVQENRELQLQYLE-------QKQQLDELKKRIKLYNQE------------NDINADELSEALLLIKAQKEQ------ 472
Cdd:pfam05557  314 RELEQELAQYLKKIEDlnkklkrHKALVRRLQRRVLLLTKErdgyrailesydKELTMSNYSPQLLERIEEAEDmtqkmq 393
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   473 -KNGDLSFLVKVDSE-------INKDLERSMREL--QATHA------ETVQELEKTRNMLIMQHKINKDYQMEVEAVTRK 536
Cdd:pfam05557  394 aHNEEMEAQLSVAEEelggykqQAQTLERELQALrqQESLAdpsyskEEVDSLRRKLETLELERQRLREQKNELEMELER 473
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 118442834   537 mENLQQDYELKVEQYVHLLD--------IRAARIHKLEAQL 569
Cdd:pfam05557  474 -RCLQGDYDPKKTKVLHLSMnpaaeayqQRKNQLEKLQAEI 513
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
39-517 1.27e-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: 43.20  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    39 RQAVSRVSREELEDrFLRLHDENIL-LKQHARKQEDKIKRMATKLIRLVNDKKRyeRVGGGPKRLGRDVEMEEMIE-QLQ 116
Cdd:pfam07111  131 RKNLEEGSQRELEE-IQRLHQEQLSsLTQAHEEALSSLTSKAEGLEKSLNSLET--KRAGEAKQLAEAQKEAELLRkQLS 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   117 EKVHELEKQNETLKNRLISAKQQLQTQGYRQTPYNNVQSRINTGRRKANENAGLQ----------------------ECP 174
Cdd:pfam07111  208 KTQEELEAQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQatvellqvrvqslthmlalqeeELT 287
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   175 RKgikFQDADVAEtphPMFTKYGNSLLEEARGEIRNLENVIQSQrgqieELEHLAEIlkTQLRRKENEIELSLLQLREQQ 254
Cdd:pfam07111  288 RK---IQPSDSLE---PEFPKKCRSLLNRWREKVFALMVQLKAQ-----DLEHRDSV--KQLRGQVAELQEQVTSQSQEQ 354
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   255 ATDQRSnIRDN-----VEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELN---MQLKEQRLKCCS 326
Cdd:pfam07111  355 AILQRA-LQDKaaeveVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLEttmTRVEQAVARIPS 433
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   327 LEKQL-------HSMK-FSERRIEELQDRIN-------------DLEKERELLKENYDKLYDSAFSAAH---------EE 376
Cdd:pfam07111  434 LSNRLsyavrkvHTIKgLMARKVALAQLRQEscpppppappvdaDLSLELEQLREERNRLDAELQLSAHliqqevgraRE 513
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   377 QWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQlQYLEQKQQLDELKKRIKLYNQENDINA 456
Cdd:pfam07111  514 QGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLR-QELTQQQEIYGQALQEKVAEVETRLRE 592
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118442834   457 DELSEALLLIKAQKEQKNGDLSfLVKVDSEINKDLERS--MRELQATH--------AETVQELEKTRNMLI 517
Cdd:pfam07111  593 QLSDTKRRLNEARREQAKAVVS-LRQIQHRATQEKERNqeLRRLQDEArkeegqrlARRVQELERDKNLML 662
HpsJ_fam NF038305
HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the ...
403-499 1.48e-03

HpsJ family protein; HpsJ (hormogornium polysaccharide J) is thought to be involved in the biosynthesis or secretion of an extracellular polysaccharide shared by many Cyanobacteria.


Pssm-ID: 468465 [Multi-domain]  Cd Length: 230  Bit Score: 41.80  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  403 KTEILDRLKTERDQNEKLVQeNRELQLQYLEQKQQLDELKKRIKLYNQEndINADELSEALL-LIKAQKEQKNGDLSFLV 481
Cdd:NF038305  106 STQALQQINQQAGQQETQLQ-QQLNQLQAQTSPQQLNQLLKSEQKQGQA--LASGQLPEEQKeQLQQFKSNPQALDKFLA 182
                          90
                  ....*....|....*...
gi 118442834  482 KVDSEINKDLERSMRELQ 499
Cdd:NF038305  183 QQLTQIRTQAEEAEKQAR 200
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
27-513 1.52e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   27 LQETSTTRTMKSRQAVSRVSREELEDRFLRLHDENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERvgggpkrlgRDV 106
Cdd:COG1196   389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE---------EEE 459
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  107 EMEEMIEQLQEKVHELEKQNETLKNRLISAKQQLQTQgyrQTPYNNVQSRINTGRRKANENAGLQECPRKGIKFQDADVA 186
Cdd:COG1196   460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLL---LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAY 536
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  187 ETphpmftkygnsLLEEARGEIRNLENVIQSQRGQieeleHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDnv 266
Cdd:COG1196   537 EA-----------ALEAALAAALQNIVVEDDEVAA-----AAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIG-- 598
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  267 EMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMA--NGDELNMQLKEQRLkccSLEKQLHSMKFSERRIEEL 344
Cdd:COG1196   599 AAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVtlAGRLREVTLEGEGG---SAGGSLTGGSRRELLAALL 675
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  345 QDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQEN 424
Cdd:COG1196   676 EAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  425 RELQLQYLEQKQQLDELKKRIK-LynqeNDIN------ADELSEALLLIKAQKEqkngdlsflvkvdseinkDLERSMRE 497
Cdd:COG1196   756 LPEPPDLEELERELERLEREIEaL----GPVNllaieeYEELEERYDFLSEQRE------------------DLEEARET 813
                         490
                  ....*....|....*.
gi 118442834  498 LQathaETVQELEKTR 513
Cdd:COG1196   814 LE----EAIEEIDRET 825
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
202-534 1.81e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 1.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   202 EEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRK-ENEIELSLLQLREQQATDQRsnIRDN---VEMIKLHkqlve 277
Cdd:pfam17380  306 EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAmERERELERIRQEERKRELER--IRQEeiaMEISRMR----- 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   278 ksnalsamEGKFIQLQEKQRTLRISHDALMANgdELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKEREL 357
Cdd:pfam17380  379 --------ELERLQMERQQKNERVRQELEAAR--KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREM 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   358 lkenydklydsafsaaheEQWKLKEQQLKVQIAQLEtalKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:pfam17380  449 ------------------ERVRLEEQERQQQVERLR---QQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   438 LDELKKRIKLYNQENDINADELSEALLLIKAQKEQKNgdlsflvKVDSEINKDLERSMRELQATHAEtVQELEKTRNMLi 517
Cdd:pfam17380  508 MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK-------QQEMEERRRIQEQMRKATEERSR-LEAMEREREMM- 578
                          330
                   ....*....|....*..
gi 118442834   518 MQHKINKDYQMEVEAVT 534
Cdd:pfam17380  579 RQIVESEKARAEYEATT 595
COG5022 COG5022
Myosin heavy chain [General function prediction only];
206-437 1.86e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 42.76  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  206 GEIRNLENVIQSQRG----QIEELEHLAEILKTQLRRKEN-------------------EIELSLLQLREQQATDQRSNI 262
Cdd:COG5022   817 ACIIKLQKTIKREKKlretEEVEFSLKAEVLIQKFGRSLKakkrfsllkketiylqsaqRVELAERQLQELKIDVKSISS 896
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  263 RDNVEmIKLHKQLVEKSNALSamegKFIQLQEKQRTLRISHDALMANgdelNMQLKEQRLKCCSLEKQLHSMKFSERRIE 342
Cdd:COG5022   897 LKLVN-LELESEIIELKKSLS----SDLIENLEFKTELIARLKKLLN----NIDLEEGPSIEYVKLPELNKLHEVESKLK 967
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  343 ELQDRINDL-----EKERELLK--ENYDKLYDSAFS------AAHEEQWKLKEqqLKVQIAQLETALKSDLTDKTEiLDR 409
Cdd:COG5022   968 ETSEEYEDLlkkstILVREGNKanSELKNFKKELAElskqygALQESTKQLKE--LPVEVAELQSASKIISSESTE-LSI 1044
                         250       260
                  ....*....|....*....|....*...
gi 118442834  410 LKTERDQNEKLVQENRELQLQYLEQKQQ 437
Cdd:COG5022  1045 LKPLQKLKGLLLLENNQLQARYKALKLR 1072
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
208-452 2.27e-03

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 464838 [Multi-domain]  Cd Length: 384  Bit Score: 41.97  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   208 IRNLENVIQSQRGQIEELEHLAEILkTQLRRKENEIELSLLQLreQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEG 287
Cdd:pfam15742   92 IRELELEVLKQAQSIKSQNSLQEKL-AQEKSRVADAEEKILEL--QQKLEHAHKVCLTDTCILEKKQLEERIKEASENEA 168
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   288 KF-IQLQEKQRTLRIshdaLMANGDELNMQLKEQRLKCCSLE----KQLHSMKFSERRIEELQDRIND------------ 350
Cdd:pfam15742  169 KLkQQYQEEQQKRKL----LDQNVNELQQQVRSLQDKEAQLEmtnsQQQLRIQQQEAQLKQLENEKRKsdehlksnqels 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   351 -----LEKERELLKENYDKLYDSAfsAAHEEQWKLKEQQLKVQIAQL------ETALKS----DLTDKTEILDRL----- 410
Cdd:pfam15742  245 eklssLQQEKEALQEELQQVLKQL--DVHVRKYNEKHHHHKAKLRRAkdrlvhEVEQRDerikQLENEIGILQQQsekek 322
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 118442834   411 ---KTERDQNEKLVQENRELQLQYLEQ-------KQQLDELKKRIKLYNQEN 452
Cdd:pfam15742  323 afqKQVTAQNEILLLEKRKLLEQLTEQeeliknnKRTISSVQNRVNFLDEEN 374
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
180-573 2.36e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 42.25  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  180 FQDADVAETPHPMFTKYGNSLLEEARGEIRNLENVI-----------QSQRGQIEELEHLAEILKTQLRRKENEIELSLL 248
Cdd:COG5185   113 EWSADILISLLYLYKSEIVALKDELIKVEKLDEIADieasygevetgIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGI 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  249 QLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQlKEQRLKCCSLE 328
Cdd:COG5185   193 SELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQDPESELEDLAQTSDKLEKLVE-QNTDLRLEKLG 271
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  329 KQLHSMKfserRIEELqdrINDLEKERELLKENYDKLYDSAFSAAHEEQWK--LKEQQLKVQIAQLETALKSDLTDKTEI 406
Cdd:COG5185   272 ENAESSK----RLNEN---ANNLIKQFENTKEKIAEYTKSIDIKKATESLEeqLAAAEAEQELEESKRETETGIQNLTAE 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  407 LDRLKTERDQNEKLVQENRElqlqYLEQKQQLDELKKRIKLYNQENDINADELSEALlliKAQKEQKNgdlsflvkvdsE 486
Cdd:COG5185   345 IEQGQESLTENLEAIKEEIE----NIVGEVELSKSSEELDSFKDTIESTKESLDEIP---QNQRGYAQ-----------E 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  487 INKDLERSMRELQATHAETVQELEK-TRNMLIMQHKINKDYQMEVEAVTRKMENLQQDYElkvEQYVHLLDIRAARIHKL 565
Cdd:COG5185   407 ILATLEDTLKAADRQIEELQRQIEQaTSSNEEVSKLLNELISELNKVMREADEESQSRLE---EAYDEINRSVRSKKEDL 483

                  ....*...
gi 118442834  566 EAQLKDIA 573
Cdd:COG5185   484 NEELTQIE 491
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
221-416 2.43e-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: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  221 QIEELEHLAEILK--TQLRRKENEIELSLLQLREQ--QATDQRSNIRDNVEmiKLHKQLVEKSNALSAMEGKFIQLQEKQ 296
Cdd:COG1579     5 DLRALLDLQELDSelDRLEHRLKELPAELAELEDElaALEARLEAAKTELE--DLEKEIKRLELEIEEVEARIKKYEEQL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  297 RTLRishdalmaNGDELNmqlkeqrlkccSLEKQLHSMKfseRRIEELQDRINDLEKEREllkenydklydsafsaAHEE 376
Cdd:COG1579    83 GNVR--------NNKEYE-----------ALQKEIESLK---RRISDLEDEILELMERIE----------------ELEE 124
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 118442834  377 QWKLKEQQL---KVQIAQLETALKSDLTDKTEILDRLKTERDQ 416
Cdd:COG1579   125 ELAELEAELaelEAELEEKKAELDEELAELEAELEELEAEREE 167
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
333-574 2.98e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 41.43  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  333 SMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAfsaaheEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKT 412
Cdd:COG1340     2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEEL------KELAEKRDELNAQVKELREEAQELREKRDELNEKVKE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  413 ERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLYNQ---------------------ENDI--NADELSEALLLIKAQ 469
Cdd:COG1340    76 LKEERDELNEKLNELREELDELRKELAELNKAGGSIDKlrkeierlewrqqtevlspeeEKELveKIKELEKELEKAKKA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  470 KEQKN------GDLSFLVKVDSEINKDLERSMRELQATHA---ETVQELEKTRNMLIMQHKINKDYQMEVEAVTRKMENL 540
Cdd:COG1340   156 LEKNEklkelrAELKELRKEAEEIHKKIKELAEEAQELHEemiELYKEADELRKEADELHKEIVEAQEKADELHEEIIEL 235
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 118442834  541 QQDYELKVEQYVHLLDI-RAARIHKLEAQLKDIAY 574
Cdd:COG1340   236 QKELRELRKELKKLRKKqRALKREKEKEELEEKAE 270
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
49-516 3.00e-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: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    49 ELEDRFLRLHDENILLKQHARKQEDKIKRMATKL--------------------IRLVNDK-KRYERVGGGPKRLGRDVE 107
Cdd:pfam01576  135 KLEEDILLLEDQNSKLSKERKLLEERISEFTSNLaeeeekakslsklknkheamISDLEERlKKEEKGRQELEKAKRKLE 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   108 MEemIEQLQEKVHELEKQNETLKNRLISAKQQLQTQGYR----QTPYNNVQSRIntgRRKANENAGLQEcprkgikfqDA 183
Cdd:pfam01576  215 GE--STDLQEQIAELQAQIAELRAQLAKKEEELQAALARleeeTAQKNNALKKI---RELEAQISELQE---------DL 280
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   184 DVAETPHPMFTKYGNSLLEEARGEIRNLENVIQSQRGQIE-------ELEHLAEILKTQLRRKENEIElsllQLReQQAT 256
Cdd:pfam01576  281 ESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQElrskreqEVTELKKALEEETRSHEAQLQ----EMR-QKHT 355
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   257 DQRSNIRDNVEMIKLHKQLVEKSNAlsAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSlekqlhsmkf 336
Cdd:pfam01576  356 QALEELTEQLEQAKRNKANLEKAKQ--ALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE---------- 423
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   337 SERRIEELQDRINDLEKERELLKENYDKLyDSAFSAAHEEQWKLKEQQLKVQ-IAQLETALKSDLTDKTEILDRLKTE-R 414
Cdd:pfam01576  424 SERQRAELAEKLSKLQSELESVSSLLNEA-EGKNIKLSKDVSSLESQLQDTQeLLQEETRQKLNLSTRLRQLEDERNSlQ 502
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   415 DQNEKLVQENRELQLQYLEQKQQLDELKKRIklynqendinadelsealllikaqkEQKNGDLSFLVKVDSEINKDLERS 494
Cdd:pfam01576  503 EQLEEEEEAKRNVERQLSTLQAQLSDMKKKL-------------------------EEDAGTLEALEEGKKRLQRELEAL 557
                          490       500
                   ....*....|....*....|..
gi 118442834   495 MRELQaTHAETVQELEKTRNML 516
Cdd:pfam01576  558 TQQLE-EKAAAYDKLEKTKNRL 578
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
327-455 3.00e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 41.76  E-value: 3.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   327 LEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQwklKEQQLKVQIAQLETALKSD---LTDK 403
Cdd:pfam06160  279 LEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEELERVQQSYTLNENELE---RVRGLEKQLEELEKRYDEIverLEEK 355
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 118442834   404 ----TEILDRLKTERDQNEKLvqenRELQLQYLEQKQQL--DELKKRIKLYNQENDIN 455
Cdd:pfam06160  356 evaySELQEELEEILEQLEEI----EEEQEEFKESLQSLrkDELEAREKLDEFKLELR 409
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
107-550 3.54e-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: 3.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   107 EMEEMIEQLQEKVHELEKQNETLKNR-LISAKQQLQTQGYRQTPYNNVQSRIN--------TGRRKANEnagLQECPRKG 177
Cdd:TIGR00606  252 NRLKEIEHNLSKIMKLDNEIKALKSRkKQMEKDNSELELKMEKVFQGTDEQLNdlyhnhqrTVREKERE---LVDCQREL 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   178 IKFQDAdvaetphpmftkygNSLLEEARGEIRNLENVIQSQRGQIEElehlaEILKTQLRRKENEIELSLLQLREQQATD 257
Cdd:TIGR00606  329 EKLNKE--------------RRLLNQEKTELLVEQGRLQLQADRHQE-----HIRARDSLIQSLATRLELDGFERGPFSE 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   258 qrsnirdnVEMIKLHKQLVEKSNALSAMEGKFiqLQEKQRTLRISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFS 337
Cdd:TIGR00606  390 --------RQIKNFHTLVIERQEDEAKTAAQL--CADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFV 459
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   338 ERRIEELQDRIND-LEKERELLKenydklydsafsaaheeqwKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQ 416
Cdd:TIGR00606  460 IKELQQLEGSSDRiLELDQELRK-------------------AERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKL 520
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   417 NEKLVQENRELQlqylEQKQQLDELKKRIKLYNQENDIN---ADELSEALLLIKAQKEQKNgdlsFLVKVDSEINKDLER 493
Cdd:TIGR00606  521 DQEMEQLNHHTT----TRTQMEMLTKDKMDKDEQIRKIKsrhSDELTSLLGYFPNKKQLED----WLHSKSKEINQTRDR 592
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118442834   494 sMRELQathaETVQELEKtrnmliMQHKINKDYQMEVEAVTRKMENL-----QQDYELKVEQ 550
Cdd:TIGR00606  593 -LAKLN----KELASLEQ------NKNHINNELESKEEQLSSYEDKLfdvcgSQDEESDLER 643
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
59-426 3.85e-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: 41.63  E-value: 3.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    59 DENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKrlGRDVEMEEMIEQLQEKVHELEKQ------------- 125
Cdd:pfam05483  394 EEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK--GKEQELIFLLQAREKEIHDLEIQltaiktseehylk 471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   126 ----------NETLKNRLISA---------KQQLQTQGYRQTPYNNVQSRINTGRrKANENAGLQECPRKGIKFQDADVA 186
Cdd:pfam05483  472 evedlkteleKEKLKNIELTAhcdklllenKELTQEASDMTLELKKHQEDIINCK-KQEERMLKQIENLEEKEMNLRDEL 550
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   187 ETPHPMFTKYGNSL---LEEARGEIRNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIElSLLQlrEQQATDQRSNIR 263
Cdd:pfam05483  551 ESVREEFIQKGDEVkckLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIE-ELHQ--ENKALKKKGSAE 627
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   264 D---NVEMIKLHKQLVEKSNALSAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKEqrlkccslekqlhSMKFSERR 340
Cdd:pfam05483  628 NkqlNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE-------------AVKLQKEI 694
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   341 IEELQDRINDLEKERELLKENYDKLYDSAFSAAHeeQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKL 420
Cdd:pfam05483  695 DKRCQHKIAEMVALMEKHKHQYDKIIEERDSELG--LYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL 772

                   ....*.
gi 118442834   421 VQENRE 426
Cdd:pfam05483  773 KMEAKE 778
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
342-633 3.88e-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: 41.63  E-value: 3.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   342 EELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQiaQLETALKSDLTDKTEILDRL---KTERDQNE 418
Cdd:pfam05483  179 EETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQ--HLEEEYKKEINDKEKQVSLLliqITEKENKM 256
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   419 K----LVQENRElQLQYLEQKQQLDElkKRIKLYNQENDINADELSE-ALLLIKAQKEQK--NGDLSFLVKVDSEINKDL 491
Cdd:pfam05483  257 KdltfLLEESRD-KANQLEEKTKLQD--ENLKELIEKKDHLTKELEDiKMSLQRSMSTQKalEEDLQIATKTICQLTEEK 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   492 ERSMREL---QATHAETVQELEKTR---------------------NMLIMQ-----------HKINKDYQMEVEAV--- 533
Cdd:pfam05483  334 EAQMEELnkaKAAHSFVVTEFEATTcsleellrteqqrleknedqlKIITMElqkksseleemTKFKNNKEVELEELkki 413
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   534 ----------TRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERG 603
Cdd:pfam05483  414 laedeklldeKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAH 493
                          330       340       350
                   ....*....|....*....|....*....|..
gi 118442834   604 ENLFEIHINKVT--FSSEVLQASGDKEPVTFC 633
Cdd:pfam05483  494 CDKLLLENKELTqeASDMTLELKKHQEDIINC 525
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
27-571 4.04e-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: 41.70  E-value: 4.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    27 LQETSTTRTMKSRQAVSRVSR-EELEDrflrlhDENILLKQHARKQEDKI---KRMATKLIRLVNDKKRYERVGG----- 97
Cdd:pfam01576  470 LQDTQELLQEETRQKLNLSTRlRQLED------ERNSLQEQLEEEEEAKRnveRQLSTLQAQLSDMKKKLEEDAGtleal 543
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    98 --GPKRLGRDVEmeEMIEQLQEKVHELEKQNETlKNRLisaKQQLQTQGYRQTPYNNVQSRINTGRRKANEnaGLQECPR 175
Cdd:pfam01576  544 eeGKKRLQRELE--ALTQQLEEKAAAYDKLEKT-KNRL---QQELDDLLVDLDHQRQLVSNLEKKQKKFDQ--MLAEEKA 615
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   176 KGIKFQDA-DVAETPHPMFTKYGNSL---LEEARGEIRNLENVIQSQRGQIEEL---------------------EHLAE 230
Cdd:pfam01576  616 ISARYAEErDRAEAEAREKETRALSLaraLEEALEAKEELERTNKQLRAEMEDLvsskddvgknvhelerskralEQQVE 695
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   231 ILKTQLRRKENEIE------LSL--------------LQLREQQATDQRsnirdnvemiklhKQLVEKSNALSAMegkfI 290
Cdd:pfam01576  696 EMKTQLEELEDELQatedakLRLevnmqalkaqferdLQARDEQGEEKR-------------RQLVKQVRELEAE----L 758
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   291 QLQEKQRTLrishdaLMANGDELNMQLKEqrlkccsLEKQLHSMKFSE----RRIEELQDRINDLEKERELLKENYDKLy 366
Cdd:pfam01576  759 EDERKQRAQ------AVAAKKKLELDLKE-------LEAQIDAANKGReeavKQLKKLQAQMKDLQRELEEARASRDEI- 824
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   367 dsaFSAAHEEQWKLKEQ-----QLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDEL 441
Cdd:pfam01576  825 ---LAQSKESEKKLKNLeaellQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEE 901
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   442 KKRIKLYNqendinaDELSEALLLIKAQKEQKNGDLSFLVKVDSEiNKDLERSMRELQATHAETVQELEKTRNMLI--MQ 519
Cdd:pfam01576  902 QSNTELLN-------DRLRKSTLQVEQLTTELAAERSTSQKSESA-RQQLERQNKELKAKLQEMEGTVKSKFKSSIaaLE 973
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118442834   520 HKINK-DYQMEVEAVTRKMEN--------------LQQDYELKV-EQYVHLLDIRAARIHKLEAQLKD 571
Cdd:pfam01576  974 AKIAQlEEQLEQESRERQAANklvrrtekklkevlLQVEDERRHaDQYKDQAEKGNSRMKQLKRQLEE 1041
mukB PRK04863
chromosome partition protein MukB;
199-354 4.08e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  199 SLLEEARGEIRNLENVIQ---------SQRGQIEELEhLAEILKTQLRRKENEIELSLLQLREQQAtdqrsnirdnvEMI 269
Cdd:PRK04863  949 QTQRDAKQQAFALTEVVQrrahfsyedAAEMLAKNSD-LNEKLRQRLEQAEQERTRAREQLRQAQA-----------QLA 1016
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  270 KLHKQLvekSNALSAMEGKFIQLQEKQR-----TLRISHDA---LMANGDELNMQLKEQRLKCCSLEKQLhsmKFSERRI 341
Cdd:PRK04863 1017 QYNQVL---ASLKSSYDAKRQMLQELKQelqdlGVPADSGAeerARARRDELHARLSANRSRRNQLEKQL---TFCEAEM 1090
                         170
                  ....*....|...
gi 118442834  342 EELQDRINDLEKE 354
Cdd:PRK04863 1091 DNLTKKLRKLERD 1103
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
59-598 4.32e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.58  E-value: 4.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    59 DENILLKQHARKQEDKIKRMATKLIRLVND----KKRYERVGGgpkrlgrdvEMEEMIEQLqEKVHELEKQNETLKNrlI 134
Cdd:TIGR01612 1104 EENIKYADEINKIKDDIKNLDQKIDHHIKAleeiKKKSENYID---------EIKAQINDL-EDVADKAISNDDPEE--I 1171
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   135 SAKQQ--LQTQGYRQTPYNNVQSRINTGRRKANENAGLQECprKGIKFQdadvaetphpmftkYGNSL----LEEARGEI 208
Cdd:TIGR01612 1172 EKKIEniVTKIDKKKNIYDEIKKLLNEIAEIEKDKTSLEEV--KGINLS--------------YGKNLgklfLEKIDEEK 1235
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   209 RNLENVIQSQRGQIEELEHLAEilKTQLRRKENEI------ELSLLQLREQQATDQRSNIRDNVEMIklhKQLVEKSNAL 282
Cdd:TIGR01612 1236 KKSEHMIKAMEAYIEDLDEIKE--KSPEIENEMGIemdikaEMETFNISHDDDKDHHIISKKHDENI---SDIREKSLKI 1310
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   283 SAMEGKFIQLQEKQRTLRISHDALMANGDELNMQLKE-----QRLKCCSLEKQLHSMKFSERRIEELQDRIND-LEKERE 356
Cdd:TIGR01612 1311 IEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEianiyNILKLNKIKKIIDEVKEYTKEIEENNKNIKDeLDKSEK 1390
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   357 LLKENYDKLYDSAFSAAHEEQWKLKEQQLKVQ-IAQLETALKSDLTDKTEILDRLKtERDQNEKLVQENREL---QLQYL 432
Cdd:TIGR01612 1391 LIKKIKDDINLEECKSKIESTLDDKDIDECIKkIKELKNHILSEESNIDTYFKNAD-ENNENVLLLFKNIEMadnKSQHI 1469
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   433 EQKQQ----------LDELKKRI---KLYNQENDINADELSEALLLIKAQKEQ------KNGDLSFLVKVDsEINKDLER 493
Cdd:TIGR01612 1470 LKIKKdnatndhdfnINELKEHIdksKGCKDEADKNAKAIEKNKELFEQYKKDvtellnKYSALAIKNKFA-KTKKDSEI 1548
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   494 SMRELQATHAETVQELEKTRNMliMQHKINKDYQMEVEAVTRKMEN-----LQQDYELKVEQYVHLLDIRA------ARI 562
Cdd:TIGR01612 1549 IIKEIKDAHKKFILEAEKSEQK--IKEIKKEKFRIEDDAAKNDKSNkaaidIQLSLENFENKFLKISDIKKkindclKET 1626
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 118442834   563 HKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETI 598
Cdd:TIGR01612 1627 ESIEKKISSFSIDSQDTELKENGDNLNSLQEFLESL 1662
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
244-510 5.48e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.07  E-value: 5.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  244 ELSLLQLREQQATDQRSNIRDNVE-MIKLhKQLVEKSNALSAMEGKFIQLQEKQRTLRIshdalmangDELnmqLKEQRL 322
Cdd:PRK05771   27 ELGVVHIEDLKEELSNERLRKLRSlLTKL-SEALDKLRSYLPKLNPLREEKKKVSVKSL---------EEL---IKDVEE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  323 KCCSLEKQLHSMkfsERRIEELQDRINDLEKERELLK--ENYD----KLYDSAFSAA-----HEEQWKLKEQQLKVQIAQ 391
Cdd:PRK05771   94 ELEKIEKEIKEL---EEEISELENEIKELEQEIERLEpwGNFDldlsLLLGFKYVSVfvgtvPEDKLEELKLESDVENVE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  392 LET-----------ALKSDLTDKTEILDRLKTERDQ--NEKLVQEN-RELQLQYLEQKQQLDELKKRIKLYNQENDINAD 457
Cdd:PRK05771  171 YIStdkgyvyvvvvVLKELSDEVEEELKKLGFERLEleEEGTPSELiREIKEELEEIEKERESLLEELKELAKKYLEELL 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 118442834  458 ELSEALLLIKAQKEQKNGDLS----FLVK--VDSEINKDLERSMRELQATHAEtVQELE 510
Cdd:PRK05771  251 ALYEYLEIELERAEALSKFLKtdktFAIEgwVPEDRVKKLKELIDKATGGSAY-VEFVE 308
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
369-612 5.55e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 5.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  369 AFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKTERDQNEKLVQENRELQLQYLEQKQQLDELKKRIKLY 448
Cdd:COG4372    27 AALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  449 NQENDINADELSEA---LLLIKAQKEQKNGDLSFLVKVDSEINKDLERSMRELQATHAEtVQELEKTRNMLIMQHKINKD 525
Cdd:COG4372   107 QEEAEELQEELEELqkeRQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE-LAALEQELQALSEAEAEQAL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  526 YQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFDETIHLERGEN 605
Cdd:COG4372   186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265

                  ....*..
gi 118442834  606 LFEIHIN 612
Cdd:COG4372   266 AILVEKD 272
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
239-460 5.99e-03

Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.


Pssm-ID: 464893 [Multi-domain]  Cd Length: 1048  Bit Score: 41.08  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   239 KENEIE-----LSLLQLREQQATDQRSNIRDNVEMIKL-----HKQLVEKSNALSAMEGKFIQLQEkqrtlriSHDALMA 308
Cdd:pfam15818   90 KEKEIEglketLKALQVSKYSLQKKVSEMEQKLQLHLLakedhHKQLNEIEKYYATITGQFGLVKE-------NHGKLEQ 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   309 NGDE---LNMQL----KEQRLKCCSLEKQL---------------HSMK-------FSERRIEELQDRIN-DLEKERELL 358
Cdd:pfam15818  163 NVQEaiqLNKRLsalnKKQESEICSLKKELkkvtsdlikskvtcqYKMGeeninltIKEQKFQELQERLNmELELNKKIN 242
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   359 KEN---YDKLYDSAFSAAHEeqwklkeQQLKVQIAQLETALKSDLTDKTEilDRLKTERD---QNEKlVQENRE--LQLQ 430
Cdd:pfam15818  243 EEIthiQEEKQDIIISFQHM-------QQLLQQQTQANTEMEAELKALKE--NNQTLERDnelQREK-VKENEEkfLNLQ 312
                          250       260       270
                   ....*....|....*....|....*....|
gi 118442834   431 YlEQKQQLDELKKRIKLYNQENDINADELS 460
Cdd:pfam15818  313 N-EHEKALGTWKKHVEELNGEINEIKNELS 341
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
198-399 7.23e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.20  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  198 NSLLEEARGEIRNLENVIQSQRGQIEELEhlAEILKTQLRRKENEIELSLLQLREQQATDQRSN-IRDN---------VE 267
Cdd:COG3883    29 QAELEAAQAELDALQAELEELNEEYNELQ--AELEALQAEIDKLQAEIAEAEAEIEERREELGErARALyrsggsvsyLD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834  268 MIKLHK---QLVEKSNALSAMEGKFIQLQEKQRTLRishDALMANGDELNMQLKEQRLKCCSLEKQLHSMkfsERRIEEL 344
Cdd:COG3883   107 VLLGSEsfsDFLDRLSALSKIADADADLLEELKADK---AELEAKKAELEAKLAELEALKAELEAAKAEL---EAQQAEQ 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 118442834  345 QDRINDLEKERELLKENYDKLydSAFSAAHEEQWKLKEQQLKVQIAQLETALKSD 399
Cdd:COG3883   181 EALLAQLSAEEAAAEAQLAEL--EAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
209-447 8.30e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.90  E-value: 8.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   209 RNLENVIQSQRGQIEELEHLAEILKTQLRRKENEIELSLLQLREQQATDQRSNIRDNVEMIKLHKQLVEKSNALSAMEGK 288
Cdd:pfam13868   55 RALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDE 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   289 FIQLQEKQRTLRIshdalmangdeLNMQLKEQRLKCCSLEKQLHSMKFSERRI------EELQDRINDLEKERELLKENY 362
Cdd:pfam13868  135 FNEEQAEWKELEK-----------EEEREEDERILEYLKEKAEREEEREAEREeieeekEREIARLRAQQEKAQDEKAER 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   363 DKLYDSAFSAAHEEQWKLKEQQLKVQIAQLETALKSDLTDKTEILDRLKT-ERDQNEKLVQENRELQLQYLEQKQQLDEL 441
Cdd:pfam13868  204 DELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAeEAEREEEEFERMLRKQAEDEEIEQEEAEK 283

                   ....*.
gi 118442834   442 KKRIKL 447
Cdd:pfam13868  284 RRMKRL 289
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
60-621 8.31e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.73  E-value: 8.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834    60 ENILLKQHARKQEDKIKRMATKLIRLVNDKKRYERVGGGPKRLGRDVEMEEMIEQLQEKVHELEKQNETLKNRLISAKQQ 139
Cdd:pfam02463  187 ELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEK 266
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   140 LQTQGYRQTPYNNVQSRINTGRRKANENAGLQEcprkgIKFQDADVAEtphpmftKYGNSLLEEARGEIRNLENVIQSQR 219
Cdd:pfam02463  267 LAQVLKENKEEEKEKKLQEEELKLLAKEEEELK-----SELLKLERRK-------VDDEEKLKESEKEKKKAEKELKKEK 334
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   220 GQIEELEHLAEILKTQLRRKENEIElSLLQLREQQATDQRSNIRdnvemiklhKQLVEKSNALSAMEGKFIQLQEKQRTL 299
Cdd:pfam02463  335 EEIEELEKELKELEIKREAEEEEEE-ELEKLQEKLEQLEEELLA---------KKKLESERLSSAAKLKEEELELKSEEE 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   300 RISHDALMANGDELNMQLKEQRLKCCSLEKQLHSMKFSERRIEELQDRINDLEKERELLKENYDKLYDSAFSAAHEEQWK 379
Cdd:pfam02463  405 KEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE 484
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   380 LKEQQLKVQIAQLETALKSDLTDKTEILDRL--------------KTERDQNEKLVQENRELQLQYLEQKQQLDELKKRI 445
Cdd:pfam02463  485 QLELLLSRQKLEERSQKESKARSGLKVLLALikdgvggriisahgRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ 564
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   446 KLYNQENDINADELSEALLLIKAQKEQKNGD----------LSFLVKVDSEINKDLERSMRELQATHAETVQELEKTRNM 515
Cdd:pfam02463  565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAvleidpilnlAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118442834   516 LIMQHKINKDYQMEVEAVTRKMENLQQDYELKVEQYVHLLDIRAARIHKLEAQLKDIAYGTKQYKFKPEIMPDDSVDEFD 595
Cdd:pfam02463  645 ESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLA 724
                          570       580
                   ....*....|....*....|....*.
gi 118442834   596 ETIHLERGENLFEIHINKVTFSSEVL 621
Cdd:pfam02463  725 DRVQEAQDKINEELKLLKQKIDEEEE 750
 
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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