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Conserved domains on  [gi|1386876319|ref|NP_001349987|]
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microtubule-associated tumor suppressor 1 isoform 1 [Homo sapiens]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
919-1215 3.43e-15

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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 81.26  E-value: 3.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  919 ILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTAST----TCEKLEKARNELQTVyEAFVQ 994
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQL-EERIA 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  995 QHQAEKTERENRLKEfYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAY---EASLS 1071
Cdd:TIGR02168  751 QLSKELTELEAEIEE-LEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAanlRERLE 827
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1072 EIKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSE--------NDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1137
Cdd:TIGR02168  828 SLERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELEELSEELRELE 907
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876319 1138 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNtalvdklkrFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 1215
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
919-1215 3.43e-15

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: 81.26  E-value: 3.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  919 ILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTAST----TCEKLEKARNELQTVyEAFVQ 994
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQL-EERIA 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  995 QHQAEKTERENRLKEfYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAY---EASLS 1071
Cdd:TIGR02168  751 QLSKELTELEAEIEE-LEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAanlRERLE 827
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1072 EIKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSE--------NDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1137
Cdd:TIGR02168  828 SLERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELEELSEELRELE 907
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876319 1138 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNtalvdklkrFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 1215
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
946-1232 5.59e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.82  E-value: 5.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  946 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFY-----------TRE 1014
Cdd:COG1196    226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelarleqDIA 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1015 YEKLRdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES 1094
Cdd:COG1196    306 RLEER---RRELEERLEELEEELAELEEELEELEEELEEL-EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1095 LEKQINDLKSENDALNEKLKSEE----QKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1170
Cdd:COG1196    382 EELAEELLEALRAAAELAAQLEEleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876319 1171 NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLW 1232
Cdd:COG1196    462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
900-1222 8.70e-11

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: 66.92  E-value: 8.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  900 EKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKT-LSQELVNLRGELVTAsttcEKL 978
Cdd:pfam02463  690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDeEEEEEEKSRLKKEEK----EEE 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  979 EKARNELQTVYEAFVQQHQAEKTERENRLKEfytREYEKLRdTYIEEAEKYKMQLQEQFDNL-NAAHETSKLEIEASHSE 1057
Cdd:pfam02463  766 KSELSLKEKELAEEREKTEKLKVEEEKEEKL---KAQEEEL-RALEEELKEEAELLEEEQLLiEQEEKIKEEELEELALE 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1058 KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQinDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1137
Cdd:pfam02463  842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ--KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI 919
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1138 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKES 1217
Cdd:pfam02463  920 EERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999

                   ....*
gi 1386876319 1218 KVNKR 1222
Cdd:pfam02463 1000 LEEEK 1004
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
865-1187 5.12e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 5.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  865 RKNLFTALNAVEKSRQKNPrsLCIQPQTAPDalppEKTLeLTQYKTKCENQSGFILQLKQLLacgnTKFEALTVVIQHLL 944
Cdd:PRK03918   421 IKELKKAIEELKKAKGKCP--VCGRELTEEH----RKEL-LEEYTAELKRIEKELKEIEEKE----RKLRKELRELEKVL 489
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  945 SEREEALKQHKTLSQeLVNLRGELvtASTTCEKLEKARNELQTVYEAFVQQhQAEKTERENRLKEFytREYEKLRdtyiE 1024
Cdd:PRK03918   490 KKESELIKLKELAEQ-LKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKL-KGEIKSLKKELEKL--EELKKKL----A 559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1025 EAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEA--SLSEIKKGHEIEKKSLEDL---LSEKQESLEKQI 1099
Cdd:PRK03918   560 ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLeeeLDKAFEELAETE 639
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1100 NDLKSENDALNEKLK--SEEQKRRAREKANLKNPQIMYLEQELESLKAVLE--------IKNEK--LHQQDIKLMKMEKL 1167
Cdd:PRK03918   640 KRLEELRKELEELEKkySEEEYEELREEYLELSRELAGLRAELEELEKRREeikktlekLKEELeeREKAKKELEKLEKA 719
                          330       340
                   ....*....|....*....|
gi 1386876319 1168 VDNNTALVDKLKRFQQENEE 1187
Cdd:PRK03918   720 LERVEELREKVKKYKALLKE 739
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
1023-1183 1.36e-06

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 51.60  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1023 IEEAEKYKMQLQEQFDNLNAAHETSKleieaSHSEKLELLKKAYEASLSeiKKGHEIEKKSLEDLLSEKQESLEKQINDL 1102
Cdd:cd22656    127 LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLNEEYAAKL 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1103 KSENDALNEKLKSEEQKRRAREK---------ANLKN------PQIMYLEQ----------ELESLKAVLEIKNEKLHQQ 1157
Cdd:cd22656    200 KAKIDELKALIADDEAKLAAALRliadltaadTDLDNllaligPAIPALEKlqgawqaiatDLDSLKDLLEDDISKIPAA 279
                          170       180
                   ....*....|....*....|....*.
gi 1386876319 1158 DIKLMKMEKLVDNNTALVDKLKRFQQ 1183
Cdd:cd22656    280 ILAKLELEKAIEKWNELAEKADKFRQ 305
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
1012-1150 1.96e-06

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 51.17  E-value: 1.96e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  1012 TREYEKLRDtYIEEAEKYKMQLQEQFDNLNaahetSKLEIEASHSEKLE-----LLKKAYEAsLSEIKKGHEIEKKSLED 1086
Cdd:smart00787  157 KEDYKLLMK-ELELLNSIKPKLRDRKDALE-----EELRQLKQLEDELEdcdptELDRAKEK-LKKLLQEIMIKVKKLEE 229
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876319  1087 LLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpQIMYLEQELESLKAVLEIK 1150
Cdd:smart00787  230 LEEELQE-LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK--EIEKLKEQLKLLQSLTGWK 290
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
919-1215 3.43e-15

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: 81.26  E-value: 3.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  919 ILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTAST----TCEKLEKARNELQTVyEAFVQ 994
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQL-EERIA 750
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  995 QHQAEKTERENRLKEfYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAY---EASLS 1071
Cdd:TIGR02168  751 QLSKELTELEAEIEE-LEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAanlRERLE 827
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1072 EIKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSE--------NDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1137
Cdd:TIGR02168  828 SLERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELEELSEELRELE 907
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876319 1138 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNtalvdklkrFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 1215
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
946-1232 5.59e-13

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 73.82  E-value: 5.59e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  946 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFY-----------TRE 1014
Cdd:COG1196    226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelarleqDIA 305
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1015 YEKLRdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES 1094
Cdd:COG1196    306 RLEER---RRELEERLEELEEELAELEEELEELEEELEEL-EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1095 LEKQINDLKSENDALNEKLKSEE----QKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1170
Cdd:COG1196    382 EELAEELLEALRAAAELAAQLEEleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876319 1171 NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLW 1232
Cdd:COG1196    462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
943-1218 8.76e-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: 73.17  E-value: 8.76e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  943 LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQ---------QHQAEKTERENRLKEFYTR 1013
Cdd:TIGR02168  244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrleqqkQILRERLANLERQLEELEA 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1014 EYEKL---RDTYIEEA---EKYKMQLQEQFDNLNAAHETSKLEIEASHSeKLELLKKAYEASLSEIkkgHEIEKKslEDL 1087
Cdd:TIGR02168  324 QLEELeskLDELAEELaelEEKLEELKEELESLEAELEELEAELEELES-RLEELEEQLETLRSKV---AQLELQ--IAS 397
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1088 LSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKL 1167
Cdd:TIGR02168  398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELREELEEAEQA 476
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386876319 1168 VDnntALVDKLKRFQQENEELKARMDKHMAISR----------QLSTEQAVLQESLEKESK 1218
Cdd:TIGR02168  477 LD---AAERELAQLQARLDSLERLQENLEGFSEgvkallknqsGLSGILGVLSELISVDEG 534
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
940-1230 1.18e-12

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: 72.78  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  940 IQHLLSEREEALKqHKTLSQELVNLRGELVTASTtcEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEfytreyeklr 1019
Cdd:TIGR02168  202 LKSLERQAEKAER-YKELKAELRELELALLVLRL--EELREELEELQEELKEAEEELEELTAELQELEEK---------- 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1020 dtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKlELLKKAYEASLSEIKKGHEI--EKKSLEDLLSEKQESLEK 1097
Cdd:TIGR02168  269 ---LEELRLEVSELEEEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQleELESKLDELAEELAELEE 344
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1098 QINDLKSENDALNEKLKSEEQKRRAREKANLKnpqimyLEQELESLK-AVLEIKNE-KLHQQDIKLMKMEKlvdnnTALV 1175
Cdd:TIGR02168  345 KLEELKEELESLEAELEELEAELEELESRLEE------LEEQLETLRsKVAQLELQiASLNNEIERLEARL-----ERLE 413
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876319 1176 DKLKRFQQENEELKARMDKH--MAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 1230
Cdd:TIGR02168  414 DRRERLQQEIEELLKKLEEAelKELQAELEELEEELEELQEELERLEEALEELREEL 470
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
976-1230 3.11e-12

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: 71.64  E-value: 3.11e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  976 EKLEKARNELQTVYE--AFVQQHQAEKTERENRLKEfytreyEKlrdtyiEEAEKYKMQLQEqfdnlnaahetsKLEIEA 1053
Cdd:TIGR02169  170 RKKEKALEELEEVEEniERLDLIIDEKRQQLERLRR------ER------EKAERYQALLKE------------KREYEG 225
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1054 ShseklELL--KKAYEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLK--SEEQKRRAREKanlk 1129
Cdd:TIGR02169  226 Y-----ELLkeKEALERQKEAIERQLASLEEELEKLTEEISE-LEKRLEEIEQLLEELNKKIKdlGEEEQLRVKEK---- 295
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1130 npqIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQE--------NEELKARMDKHMAISRQ 1201
Cdd:TIGR02169  296 ---IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklTEEYAELKEELEDLRAE 372
                          250       260
                   ....*....|....*....|....*....
gi 1386876319 1202 LSTEQAVLQESLEKESKVNKRLSMENEEL 1230
Cdd:TIGR02169  373 LEEVDKEFAETRDELKDYREKLEKLKREI 401
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
994-1231 5.67e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 67.27  E-value: 5.67e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  994 QQHQAEKTERENRLK----EFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEAS 1069
Cdd:COG1196    216 RELKEELKELEAELLllklRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYEL 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1070 LSEIKkghEIEKKslEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVLEI 1149
Cdd:COG1196    294 LAELA---RLEQD--IARLEERRRELEERLEELEEELAELEEELEELEEELEELEE------ELEEAEEELEEAEAELAE 362
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1150 KNEKLHQQDIKLMKMEKLVDNNT----ALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSM 1225
Cdd:COG1196    363 AEEALLEAEAELAEAEEELEELAeellEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442

                   ....*.
gi 1386876319 1226 ENEELL 1231
Cdd:COG1196    443 ALEEAA 448
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
900-1222 8.70e-11

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: 66.92  E-value: 8.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  900 EKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKT-LSQELVNLRGELVTAsttcEKL 978
Cdd:pfam02463  690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDeEEEEEEKSRLKKEEK----EEE 765
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  979 EKARNELQTVYEAFVQQHQAEKTERENRLKEfytREYEKLRdTYIEEAEKYKMQLQEQFDNL-NAAHETSKLEIEASHSE 1057
Cdd:pfam02463  766 KSELSLKEKELAEEREKTEKLKVEEEKEEKL---KAQEEEL-RALEEELKEEAELLEEEQLLiEQEEKIKEEELEELALE 841
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1058 KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQinDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1137
Cdd:pfam02463  842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ--KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI 919
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1138 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKES 1217
Cdd:pfam02463  920 EERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999

                   ....*
gi 1386876319 1218 KVNKR 1222
Cdd:pfam02463 1000 LEEEK 1004
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
976-1235 1.37e-10

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: 66.15  E-value: 1.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  976 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHetSKLEIEASH 1055
Cdd:TIGR00618  127 ETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMN--LFPLDQYTQLALMEFAKKKSLH--GKAELLTLR 202
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1056 SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKqindLKSENDALNEKLKSEEQKRRAREKanlknpqimy 1135
Cdd:TIGR00618  203 SQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY----LTQKREAQEEQLKKQQLLKQLRAR---------- 268
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1136 lEQELESLKAVLEIKNEKLHQQdiklMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 1215
Cdd:TIGR00618  269 -IEELRAQEAVLEETQERINRA----RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
                          250       260
                   ....*....|....*....|....*..
gi 1386876319 1216 ESKVNKRLSME-------NEELLWKLH 1235
Cdd:TIGR00618  344 RRLLQTLHSQEihirdahEVATSIREI 370
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
943-1230 1.84e-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: 65.47  E-value: 1.84e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  943 LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKE---FYTREYEKLR 1019
Cdd:TIGR02169  228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigELEAEIASLE 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1020 DTY------IEEAEKYKMQLQEQFDNLNAAHETSKLEIE------ASHSEKLELLKKAYEASLSEIKkghEIEKKSLEdl 1087
Cdd:TIGR02169  308 RSIaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrDKLTEEYAELKEELEDLRAELE---EVDKEFAE-- 382
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1088 LSEKQESLEKQINDLKSENDALNEKL--KSEEQKRRAREKANLKNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKme 1165
Cdd:TIGR02169  383 TRDELKDYREKLEKLKREINELKRELdrLQEELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-- 459
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386876319 1166 klvdnntaLVDKLKRFQQENEELKarmdkhmaisrqlsteqavlqeslEKESKVNKRLSMENEEL 1230
Cdd:TIGR02169  460 --------LAADLSKYEQELYDLK------------------------EEYDRVEKELSKLQREL 492
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
916-1229 7.03e-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: 63.93  E-value: 7.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  916 SGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEK---ARNELQTVYEAF 992
Cdd:TIGR02169  666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeeKLKERLEELEED 745
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  993 VQQHQAEKTERENRLKEFYTReyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSE 1072
Cdd:TIGR02169  746 LSSLEQEIENVKSELKELEAR---------IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1073 IKKghEIEKKSLED--LLSEKQES------LEKQINDLKSENDALN---EKLKSEEQKRRA-------------REKANL 1128
Cdd:TIGR02169  817 IEQ--KLNRLTLEKeyLEKEIQELqeqridLKEQIKSIEKEIENLNgkkEELEEELEELEAalrdlesrlgdlkKERDEL 894
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1129 KNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLmkmEKLVDNNTALVDKLKRFQQENEELkarmdkhmAISRQLSTEQAV 1208
Cdd:TIGR02169  895 EA-QLRELERKIEELEAQIEKKRKRLSELKAKL---EALEEELSEIEDPKGEDEEIPEEE--------LSLEDVQAELQR 962
                          330       340
                   ....*....|....*....|.
gi 1386876319 1209 LQESLEKESKVNKRLSMENEE 1229
Cdd:TIGR02169  963 VEEEIRALEPVNMLAIQEYEE 983
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
900-1236 1.76e-09

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: 62.35  E-value: 1.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  900 EKTLELTQYKTKCENQSGFILQLK-QLLACGNTKFEALTVVIQHLLSEREEALKQHKT-----------LSQELVNLRGE 967
Cdd:TIGR04523  271 EKQKELEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNqisqnnkiisqLNEQISQLKKE 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  968 LVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTEREN--------RLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDN 1039
Cdd:TIGR04523  351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlesqindlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1040 LNAAHETSKLEIEASHSE---------KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSE------KQESLEKQINDLKS 1104
Cdd:TIGR04523  431 LKETIIKNNSEIKDLTNQdsvkeliikNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekELKKLNEEKKELEE 510
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1105 ENDALNEKLKSEEQKRRAREKA-NLKNPQIMYLEQELESLKAVL---EIKNEKLH-QQDIKLMKMEK--LVDNNTALVDK 1177
Cdd:TIGR04523  511 KVKDLTKKISSLKEKIEKLESEkKEKESKISDLEDELNKDDFELkkeNLEKEIDEkNKEIEELKQTQksLKKKQEEKQEL 590
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1386876319 1178 LKRFQQENEELKARMDKHMAISRQLSTEqavlqesLEKESKVNKRLSMENEELLWKLHN 1236
Cdd:TIGR04523  591 IDQKEKEKKDLIKEIEEKEKKISSLEKE-------LEKAKKENEKLSSIIKNIKSKKNK 642
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
934-1159 2.02e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 2.02e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  934 EALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQaektERENRLKEFYTR 1013
Cdd:COG1196    312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA----EAEEELEELAEE 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1014 EYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKkgheiEKKSLEDLLSEKQE 1093
Cdd:COG1196    388 LLEALRA--AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE-----AAEEEAELEEEEEA 460
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876319 1094 SLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDI 1159
Cdd:COG1196    461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
948-1230 3.81e-09

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: 60.91  E-value: 3.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  948 EEALKQHKTLSQELVNLRGELVTASTTC-EKLEKARNELQtvYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtYIEEA 1026
Cdd:pfam05557   44 DRESDRNQELQKRIRLLEKREAEAEEALrEQAELNRLKKK--YLEALNKKLNEKESQLADAREVISCLKNELSE-LRRQI 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1027 EKYKMQLQEQFDNLNAAHEtsKLEIEASHSEKLELLKKAYEASLSEIKKgHEIEKKSLEDLLsEKQESLEKQINDLKSEN 1106
Cdd:pfam05557  121 QRAELELQSTNSELEELQE--RLDLLKAKASEAEQLRQNLEKQQSSLAE-AEQRIKELEFEI-QSQEQDSEIVKNSKSEL 196
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1107 DALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-------------AVLEIKNEKLHQqdiKLMKMEKLVDNNT- 1172
Cdd:pfam05557  197 ARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKrklereekyreeaATLELEKEKLEQ---ELQSWVKLAQDTGl 273
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386876319 1173 ------ALVDKLKRFQQENEELKARMD------KHMAIS-RQLSTEQAVLQESLEKESKVNKRLSMENEEL 1230
Cdd:pfam05557  274 nlrspeDLSRRIEQLQQREIVLKEENSsltssaRQLEKArRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
979-1227 5.11e-09

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 60.80  E-value: 5.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  979 EKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKL-----EIEA 1053
Cdd:COG3206    148 ELAAAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKE-LEEAEAALEEFRQKNGLVDLSEEAKLLlqqlsELES 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1054 SHSEkLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQ-ESLEKQINDLKSENDALNEKLKSeeqkrrarekanlKNPQ 1132
Cdd:COG3206    227 QLAE-ARAELAEAEARLAALRAQLGSGPDALPELLQSPViQQLRAQLAELEAELAELSARYTP-------------NHPD 292
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1133 IMYLEQELESLKAVLEIKNEKLhQQDIKlMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQES 1212
Cdd:COG3206    293 VIALRAQIAALRAQLQQEAQRI-LASLE-AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370
                          250
                   ....*....|....*..
gi 1386876319 1213 LEK--ESKVNKRLSMEN 1227
Cdd:COG3206    371 LQRleEARLAEALTVGN 387
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
865-1187 5.12e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.85  E-value: 5.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  865 RKNLFTALNAVEKSRQKNPrsLCIQPQTAPDalppEKTLeLTQYKTKCENQSGFILQLKQLLacgnTKFEALTVVIQHLL 944
Cdd:PRK03918   421 IKELKKAIEELKKAKGKCP--VCGRELTEEH----RKEL-LEEYTAELKRIEKELKEIEEKE----RKLRKELRELEKVL 489
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  945 SEREEALKQHKTLSQeLVNLRGELvtASTTCEKLEKARNELQTVYEAFVQQhQAEKTERENRLKEFytREYEKLRdtyiE 1024
Cdd:PRK03918   490 KKESELIKLKELAEQ-LKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKL-KGEIKSLKKELEKL--EELKKKL----A 559
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1025 EAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEA--SLSEIKKGHEIEKKSLEDL---LSEKQESLEKQI 1099
Cdd:PRK03918   560 ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLeeeLDKAFEELAETE 639
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1100 NDLKSENDALNEKLK--SEEQKRRAREKANLKNPQIMYLEQELESLKAVLE--------IKNEK--LHQQDIKLMKMEKL 1167
Cdd:PRK03918   640 KRLEELRKELEELEKkySEEEYEELREEYLELSRELAGLRAELEELEKRREeikktlekLKEELeeREKAKKELEKLEKA 719
                          330       340
                   ....*....|....*....|
gi 1386876319 1168 VDNNTALVDKLKRFQQENEE 1187
Cdd:PRK03918   720 LERVEELREKVKKYKALLKE 739
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
939-1259 5.54e-09

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: 60.52  E-value: 5.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  939 VIQH--LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYE---AFVQQHQAEKTERENRL----KE 1009
Cdd:pfam17380  277 IVQHqkAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaAIYAEQERMAMERERELerirQE 356
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1010 FYTREYEKLRD-------TYIEEAEKYKMQLQEQFD----NLNAAHETSKLEIEasHSEKLELLKKAYEASLSEIKKGHE 1078
Cdd:pfam17380  357 ERKRELERIRQeeiameiSRMRELERLQMERQQKNErvrqELEAARKVKILEEE--RQRKIQQQKVEMEQIRAEQEEARQ 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1079 IEKKSLED-----LLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-AVLEIKNE 1152
Cdd:pfam17380  435 REVRRLEEerareMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqAMIEEERK 514
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1153 KlhqqdiKLMKMEkLVDNNTALVDKLKRFQQENEELKAR-MDKHMAISRQL--STEQAVLQESLEKESKVNKRLsMENEE 1229
Cdd:pfam17380  515 R------KLLEKE-MEERQKAIYEEERRREAEEERRKQQeMEERRRIQEQMrkATEERSRLEAMEREREMMRQI-VESEK 586
                          330       340       350
                   ....*....|....*....|....*....|
gi 1386876319 1230 LLWKLhngdlcsPKRSPTSSAIPLQSPRNS 1259
Cdd:pfam17380  587 ARAEY-------EATTPITTIKPIYRPRIS 609
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
931-1236 7.76e-09

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 60.08  E-value: 7.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  931 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELvtasttcEKLEKARNELQTVyeafvqqhQAEKTERENRLKEF 1010
Cdd:PRK03918   317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL-------EELEERHELYEEA--------KAKKEELERLKKRL 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1011 YTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAahETSKLEIEASHseklelLKKAyeasLSEIKK--------GHEIEKK 1082
Cdd:PRK03918   382 TGLTPEKLEKE-LEELEKAKEEIEEEISKITA--RIGELKKEIKE------LKKA----IEELKKakgkcpvcGRELTEE 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1083 SLEDLLSEKQESLEKQINDLKsENDALNEKLKSEEQKrraREKANLKNPQIMYLEQELESLKAVleikNEKLHQQDIKlm 1162
Cdd:PRK03918   449 HRKELLEEYTAELKRIEKELK-EIEEKERKLRKELRE---LEKVLKKESELIKLKELAEQLKEL----EEKLKKYNLE-- 518
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876319 1163 kmeklvdnntalvdKLKRFQQENEELKARMDKhmaisrqLSTEQAVLQESLEKESKVNKRLsmenEELLWKLHN 1236
Cdd:PRK03918   519 --------------ELEKKAEEYEKLKEKLIK-------LKGEIKSLKKELEKLEELKKKL----AELEKKLDE 567
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
976-1229 9.22e-09

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: 58.78  E-value: 9.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  976 EKLEKARNELQTVYEAFVQQH----------QAEKTERENR-LKEFYTREYEKLRDTYIEEAEKyKMQLQEQFDNLNAAH 1044
Cdd:pfam13868   61 EEKEEERKEERKRYRQELEEQieereqkrqeEYEEKLQEREqMDEIVERIQEEDQAEAEEKLEK-QRQLREEIDEFNEEQ 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1045 ETSK-LEIEAshsEKLELLK-KAYEASLSEIKKGHEIEKKSLE---DLLSEKQESLEKQINDLKSENDALNEKLKSEEQK 1119
Cdd:pfam13868  140 AEWKeLEKEE---EREEDERiLEYLKEKAEREEEREAEREEIEeekEREIARLRAQQEKAQDEKAERDELRAKLYQEEQE 216
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1120 RRAREKAnlknpqimyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEElKARMDKHMAIS 1199
Cdd:pfam13868  217 RKERQKE---------REEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE-IEQEEAEKRRM 286
                          250       260       270
                   ....*....|....*....|....*....|
gi 1386876319 1200 RQLSTEQAVLQESLEKESKvnKRLSMENEE 1229
Cdd:pfam13868  287 KRLEHRRELEKQIEEREEQ--RAAEREEEL 314
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
940-1142 1.23e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 1.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAfVQQHQAEKTERENRLKefytREYEKLR 1019
Cdd:COG1196    304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAE----AELAEAE 378
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1020 DTYIEEAEKYKMQLQEQFDNLNA-AHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQ 1098
Cdd:COG1196    379 EELEELAEELLEALRAAAELAAQlEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1386876319 1099 INDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELES 1142
Cdd:COG1196    459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
938-1245 2.80e-08

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: 58.44  E-value: 2.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  938 VVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYeafvQQHQAEKTERENRLKEFYTREYEK 1017
Cdd:pfam02463  162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY----QLKEKLELEEEYLLYLDYLKLNEE 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1018 LRDTYIE----EAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQE 1093
Cdd:pfam02463  238 RIDLLQEllrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1094 SLEKQINDLKSENDAL----NEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIK------LMK 1163
Cdd:pfam02463  318 ESEKEKKKAEKELKKEkeeiEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSaaklkeEEL 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1164 MEKLVDNNTALvDKLKRFQQENEELKARMDKhmaisrqLSTEQAVLQESLEKESKVNKRLSmENEELLWKLHNGDLCSPK 1243
Cdd:pfam02463  398 ELKSEEEKEAQ-LLLELARQLEDLLKEEKKE-------ELEILEEEEESIELKQGKLTEEK-EELEKQELKLLKDELELK 468

                   ..
gi 1386876319 1244 RS 1245
Cdd:pfam02463  469 KS 470
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
940-1101 4.28e-08

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: 55.32  E-value: 4.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVY---EAFVQQHQAEKTERENRL------KEF 1010
Cdd:COG1579     12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLgnvrnnKEY 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1011 --YTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAsHSEKLELLKKAYEASLSEIKKghEIEKksledlL 1088
Cdd:COG1579     92 eaLQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAE-LEAELEEKKAELDEELAELEA--ELEE------L 161
                          170
                   ....*....|...
gi 1386876319 1089 SEKQESLEKQIND 1101
Cdd:COG1579    162 EAEREELAAKIPP 174
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
904-1149 6.05e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 57.37  E-value: 6.05e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  904 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 983
Cdd:TIGR02168  783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  984 ELQTVYEAF---VQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1060
Cdd:TIGR02168  863 ELEELIEELeseLEALLNERASLEEALALL-RSELEELSEE-LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1061 LLKKA---YEASLSEIKKgHEIEKKSLEDLLSEKQESLEKQINDLKSEN-DALNEklkSEEQKRRAREKANlknpQIMYL 1136
Cdd:TIGR02168  941 LQERLseeYSLTLEEAEA-LENKIEDDEEEARRRLKRLENKIKELGPVNlAAIEE---YEELKERYDFLTA----QKEDL 1012
                          250
                   ....*....|....
gi 1386876319 1137 EQELESL-KAVLEI 1149
Cdd:TIGR02168 1013 TEAKETLeEAIEEI 1026
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
940-1235 6.54e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.38  E-value: 6.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEkterenrLKEFYTREYEKLR 1019
Cdd:PRK03918   393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKE-------LLEEYTAELKRIE 465
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1020 DTyIEEAEKYKMQLQEqfdnlnaahETSKLEIEASHSEKLELLKKAYEaSLSEIKKghEIEKKSLEDL--LSEKQESLEK 1097
Cdd:PRK03918   466 KE-LKEIEEKERKLRK---------ELRELEKVLKKESELIKLKELAE-QLKELEE--KLKKYNLEELekKAEEYEKLKE 532
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1098 QINDLKSENDALNEKLKSEEQKRRAREKANLKnpqIMYLEQELESLKAVLEIKN-EKLHQQDIKLMKMEKLVDNNTALVD 1176
Cdd:PRK03918   533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKK---LDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKD 609
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1386876319 1177 KLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLH 1235
Cdd:PRK03918   610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
932-1215 8.43e-08

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 57.00  E-value: 8.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  932 KFEALTVVIQHLLSERE----EALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvqQHQAEKTERENRL 1007
Cdd:PRK03918   183 KFIKRTENIEELIKEKEkeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIE--------ELEKELESLEGSK 254
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1008 KefytREYEKLRDT--YIEEAEKYKMQLQEQfdnlnaAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIekksle 1085
Cdd:PRK03918   255 R----KLEEKIRELeeRIEELKKEIEELEEK------VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR------ 318
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1086 dlLSEKQESLEKQINDLKSENDALNEKLKSEEqkrrarekanlknpqimyleqELESLKAVLEIKNEKLHQQDIKLMKME 1165
Cdd:PRK03918   319 --LEEEINGIEERIKELEEKEERLEELKKKLK---------------------ELEKRLEELEERHELYEEAKAKKEELE 375
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1386876319 1166 KLVDNNTA-----LVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 1215
Cdd:PRK03918   376 RLKKRLTGltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
946-1226 8.95e-08

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: 56.44  E-value: 8.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  946 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA---EKTERENRLKEF-----------Y 1011
Cdd:pfam07888   67 DREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAllaQRAAHEARIRELeediktltqrvL 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1012 TREYEKLRDTyiEEAEKYKMQLQEQfdnlNAAHETSKLEIEASHSEKLELLKKAYEAslseikKGHEIEKKSLEDLLSEK 1091
Cdd:pfam07888  147 ERETELERMK--ERAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKEFQEL------RNSLAQRDTQVLQLQDT 214
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1092 QESLEKQINDlKSENDALNEKLKseEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDN 1170
Cdd:pfam07888  215 ITTLTQKLTT-AHRKEAENEALL--EELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTlQLADA 291
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876319 1171 NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSME 1226
Cdd:pfam07888  292 SLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
903-1185 1.15e-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: 56.27  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  903 LELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKA- 981
Cdd:pfam05483  457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQi 536
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  982 ----------RNELQTVYEAFVQQH-----QAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHET 1046
Cdd:pfam05483  537 enleekemnlRDELESVREEFIQKGdevkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE 616
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1047 SKLEIEASHSE------------KLEL----LKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES---------LEKQInD 1101
Cdd:pfam05483  617 NKALKKKGSAEnkqlnayeikvnKLELelasAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavkLQKEI-D 695
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1102 LK-----SENDALNEKLKSEEQK---RRAREKANLKNPqimylEQELESLKAVLEIKNEKLHQQdikLMKMEKLVDNNTA 1173
Cdd:pfam05483  696 KRcqhkiAEMVALMEKHKHQYDKiieERDSELGLYKNK-----EQEQSSAKAALEIELSNIKAE---LLSLKKQLEIEKE 767
                          330
                   ....*....|..
gi 1386876319 1174 LVDKLKRFQQEN 1185
Cdd:pfam05483  768 EKEKLKMEAKEN 779
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
946-1215 1.34e-07

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: 56.34  E-value: 1.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  946 EREEALKQHKTLSQELVNLRG-------ELVTASTTCEKLEKARNELQ-TVYEAfvQQHQAE-----KTERENRLKEfyt 1012
Cdd:pfam01576  216 ESTDLQEQIAELQAQIAELRAqlakkeeELQAALARLEEETAQKNNALkKIREL--EAQISElqedlESERAARNKA--- 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1013 reyEKLRDTYIEEAEKYKMQLQEQFDNLNAAHE-TSKLEIEASHSEK-LELLKKAYEASLSEIKKGH-----------EI 1079
Cdd:pfam01576  291 ---EKQRRDLGEELEALKTELEDTLDTTAAQQElRSKREQEVTELKKaLEEETRSHEAQLQEMRQKHtqaleelteqlEQ 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1080 EKKSLEDLLSEKQeSLEKQINDLKSENDALNE-KLKSEEQKRRA---------------REKANLkNPQIMYLEQELESL 1143
Cdd:pfam01576  368 AKRNKANLEKAKQ-ALESENAELQAELRTLQQaKQDSEHKRKKLegqlqelqarlseseRQRAEL-AEKLSKLQSELESV 445
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1144 KAVL---EIKNEKLHQQ----DIKLMKMEKLVDNNT----ALVDKLKRFQQENEELKARMDKHM----AISRQLSTEQAV 1208
Cdd:pfam01576  446 SSLLneaEGKNIKLSKDvsslESQLQDTQELLQEETrqklNLSTRLRQLEDERNSLQEQLEEEEeakrNVERQLSTLQAQ 525

                   ....*..
gi 1386876319 1209 LQESLEK 1215
Cdd:pfam01576  526 LSDMKKK 532
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
944-1136 1.39e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.93  E-value: 1.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  944 LSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA-----EKTERENRLKEFyTREYEKL 1018
Cdd:COG4717     73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAEL-PERLEEL 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1019 RdtyiEEAEKYKmQLQEQFDNLNAAHETSKLEIEashsEKLELLKKAYEASLSEIKKghEIEKksledlLSEKQESLEKQ 1098
Cdd:COG4717    152 E----ERLEELR-ELEEELEELEAELAELQEELE----ELLEQLSLATEEELQDLAE--ELEE------LQQRLAELEEE 214
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1386876319 1099 INDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYL 1136
Cdd:COG4717    215 LEEAQEELEELEEELEQlENELEAAALEERLKEARLLLL 253
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1023-1265 2.15e-07

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: 54.77  E-value: 2.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1023 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAYEASLSEIKKgheiekksledlLSEKQESLEKQINDL 1102
Cdd:COG4942     22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-LAALERRIAALARRIRA------------LEQELAALEAELAEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1103 KSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE------------QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1170
Cdd:COG4942     89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1171 NTALVDKLKRFQQENEE----LKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLsmenEELLWKLHNGDLCSPKRSP 1246
Cdd:COG4942    169 LEAERAELEALLAELEEeraaLEALKAERQKLLARLEKELAELAAELAELQQEAEEL----EALIARLEAEAAAAAERTP 244
                          250
                   ....*....|....*....
gi 1386876319 1247 TSSAiplqsPRNSGSFPSP 1265
Cdd:COG4942    245 AAGF-----AALKGKLPWP 258
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
921-1126 2.21e-07

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: 54.77  E-value: 2.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  921 QLKQLlacgNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEK 1000
Cdd:COG4942     28 ELEQL----QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1001 TERENRLKEFYT---REYEKL------------RDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLK-- 1063
Cdd:COG4942    104 EELAELLRALYRlgrQPPLALllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAel 183
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876319 1064 KAYEASLSEIKKgheiEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1126
Cdd:COG4942    184 EEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
940-1238 2.39e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 54.52  E-value: 2.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVYEAfVQQHQAEKTERENRLKEFYtREYEKLR 1019
Cdd:COG4372     40 LDKLQEELEQLREELEQAREELEQLEEELEQAR---SELEQLEEELEELNEQ-LQAAQAELAQAQEELESLQ-EEAEELQ 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1020 DTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIeASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQI 1099
Cdd:COG4372    115 EE-LEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1100 ND--LKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNntalVDK 1177
Cdd:COG4372    193 NRnaEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL----AIL 268
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386876319 1178 LKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLHNGD 1238
Cdd:COG4372    269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLE 329
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
990-1224 2.50e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 55.16  E-value: 2.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  990 EAFVQQHQAEKTERENRLKEFYTREYEKLRDTY-------IEEAEKYKMQLQEQFDNLNAAHE-TSKLEIEASHSEKLEL 1061
Cdd:COG4717    296 EKASLGKEAEELQALPALEELEEEELEELLAALglppdlsPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAAL 375
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1062 LKKAYEASLSEIKKGHEIEKKSLEdlLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREkanlknpqimyLEQELE 1141
Cdd:COG4717    376 LAEAGVEDEEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELLEALDEEELEEELEE-----------LEEELE 442
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1142 SLKAVLEIKNEKLHQQDIKLMKMEklvdNNTALVDKLKRFQQENEELKARMDKHMAisrqLSTEQAVLQESL-----EKE 1216
Cdd:COG4717    443 ELEEELEELREELAELEAELEQLE----EDGELAELLQELEELKAELRELAEEWAA----LKLALELLEEAReeyreERL 514

                   ....*...
gi 1386876319 1217 SKVNKRLS 1224
Cdd:COG4717    515 PPVLERAS 522
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
941-1214 2.50e-07

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: 55.57  E-value: 2.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  941 QHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvqqhqAEKTERENRLKEFYTREYEKLRD 1020
Cdd:pfam01576   22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLA-----------ARKQELEEILHELESRLEEEEER 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1021 TYIEEAEKYKMQ-----LQEQFDNLNAAHEtsKLEIEASHSE----KLELLKKAYEASLSEIKKgheiEKKSLEDLLSE- 1090
Cdd:pfam01576   91 SQQLQNEKKKMQqhiqdLEEQLDEEEAARQ--KLQLEKVTTEakikKLEEDILLLEDQNSKLSK----ERKLLEERISEf 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1091 -----KQESLEKQINDLKSENDA----LNEKLKSEEQKRRAREKANLK--------NPQIMYLEQELESLKAVLEIKNEK 1153
Cdd:pfam01576  165 tsnlaEEEEKAKSLSKLKNKHEAmisdLEERLKKEEKGRQELEKAKRKlegestdlQEQIAELQAQIAELRAQLAKKEEE 244
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386876319 1154 LHQqdiKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLE 1214
Cdd:pfam01576  245 LQA---ALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELE 302
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1019-1230 2.73e-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: 2.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1019 RDTYIEEA---EKYKMQLQEQFDNLNAA-----------HETSK----LEIEASHSEKLellkKAYEASLSEIKKG-HEI 1079
Cdd:TIGR02168  157 RRAIFEEAagiSKYKERRKETERKLERTrenldrledilNELERqlksLERQAEKAERY----KELKAELRELELAlLVL 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1080 EKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpqimyLEQELESL-KAVLEIKNEklhQQD 1158
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----------LEEEIEELqKELYALANE---ISR 299
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876319 1159 IKLMKMEkLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 1230
Cdd:TIGR02168  300 LEQQKQI-LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
941-1231 3.20e-07

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: 55.03  E-value: 3.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  941 QHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEklrd 1020
Cdd:TIGR04523  200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---- 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1021 tyIEEAEKYKMQLQEQFDNLNAahetsklEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLE------DLLSEKQES 1094
Cdd:TIGR04523  276 --LEQNNKKIKELEKQLNQLKS-------EISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISqnnkiiSQLNEQISQ 346
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1095 LEKQINDLKSENDALN----------EKLKSEEQKRRaREKANLKNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM 1164
Cdd:TIGR04523  347 LKKELTNSESENSEKQreleekqneiEKLKKENQSYK-QEIKNLES-QINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386876319 1165 EKLVDN----NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKE----SKVNKRLSMENEELL 1231
Cdd:TIGR04523  425 EKEIERlketIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIkqnlEQKQKELKSKEKELK 499
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
997-1231 3.55e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 3.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  997 QAEKTERenrlkefytreYEKLRdtyiEEAEKYKMQLQ-EQFDNLNAAHETSKLEIEAshsekLELLKKAYEASLSEIKK 1075
Cdd:COG1196    208 QAEKAER-----------YRELK----EELKELEAELLlLKLRELEAELEELEAELEE-----LEAELEELEAELAELEA 267
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1076 GHEIEKKSLEDLlsekqeslEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVL-------- 1147
Cdd:COG1196    268 ELEELRLELEEL--------ELELEEAQAEEYELLAELARLEQDIARLEE------RRRELEERLEELEEELaeleeele 333
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1148 -------EIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVN 1220
Cdd:COG1196    334 eleeeleELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
                          250
                   ....*....|.
gi 1386876319 1221 KRLSMENEELL 1231
Cdd:COG1196    414 ERLERLEEELE 424
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
902-1231 4.66e-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: 4.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  902 TLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREE--ALKQHKTLS-QELVNLRGELVTASTTCEKL 978
Cdd:pfam05483  348 SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVElEELKKILAEDEKLLDEKKQF 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  979 EKARNELQTVYEAFV---QQHQAEKTERENRL------KEFYTREYEKLRdtyiEEAEKYKMQLQE--------QFDNLN 1041
Cdd:pfam05483  428 EKIAEELKGKEQELIfllQAREKEIHDLEIQLtaiktsEEHYLKEVEDLK----TELEKEKLKNIEltahcdklLLENKE 503
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1042 AAHETSKLEIE-ASHSEKLELLKKAYEASLSEIKKGHEIEKKsLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKR 1120
Cdd:pfam05483  504 LTQEASDMTLElKKHQEDIINCKKQEERMLKQIENLEEKEMN-LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEV 582
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1121 RAREKA---------NL------KNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDNNTALVDKLKRFQQE 1184
Cdd:pfam05483  583 LKKEKQmkilenkcnNLkkqienKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKE 662
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1386876319 1185 NEELKARMDKHMAisrQLSTEQAVLQESLEKESKVNKRLSMENEELL 1231
Cdd:pfam05483  663 IEDKKISEEKLLE---EVEKAKAIADEAVKLQKEIDKRCQHKIAEMV 706
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
940-1224 5.19e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 54.30  E-value: 5.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  940 IQHLLSEREEALKQHKTLSQELVNLRGELVTAS------TTCEKLEKARNELQtvyeafvqQHQAEKTEREnrlkefyTR 1013
Cdd:PRK03918   461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkELAEQLKELEEKLK--------KYNLEELEKK-------AE 525
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1014 EYEKLRdtyiEEAEKYKmqlqeqfdnlnaahetSKLEIEASHSEKLELLKKAYEASLSEIKKGHEiEKKSLEDLLSEK-- 1091
Cdd:PRK03918   526 EYEKLK----EKLIKLK----------------GEIKSLKKELEKLEELKKKLAELEKKLDELEE-ELAELLKELEELgf 584
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1092 --QESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLM--KMEKL 1167
Cdd:PRK03918   585 esVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeEYEEL 664
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876319 1168 VDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLS 1224
Cdd:PRK03918   665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
1091-1216 7.59e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.91  E-value: 7.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1091 KQESLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMK------ 1163
Cdd:COG3883     17 QIQAKQKELSELQAELEAAQAELDAlQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1164 ---------------------------MEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKE 1216
Cdd:COG3883     97 rsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
900-1215 8.17e-07

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: 53.67  E-value: 8.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  900 EKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLE 979
Cdd:pfam10174  363 KKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE 442
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  980 KARNELQTVYEAFvqQHQAEKTERENRlkefytreyeklrdtyiEEAEKYKMQLQEQFDNLNAAHeTSKLEIEAShseKL 1059
Cdd:pfam10174  443 EALSEKERIIERL--KEQREREDRERL-----------------EELESLKKENKDLKEKVSALQ-PELTEKESS---LI 499
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1060 ELLKKAYEASLSEIKKGHEIekKSLEDLLSEKQESLEKQINDL-KSENDALNEKLKSE--EQKRRAREKANLKNPQIMYL 1136
Cdd:pfam10174  500 DLKEHASSLASSGLKKDSKL--KSLEIAVEQKKEECSKLENQLkKAHNAEEAVRTNPEinDRIRLLEQEVARYKEESGKA 577
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1137 EQELESLKAVL-EIKNEKlHQQDIKLMKMEKL----VDNNTALVDKLKRFQQEN--------EELKARMDKHMAISRQLS 1203
Cdd:pfam10174  578 QAEVERLLGILrEVENEK-NDKDKKIAELESLtlrqMKEQNKKVANIKHGQQEMkkkgaqllEEARRREDNLADNSQQLQ 656
                          330
                   ....*....|..
gi 1386876319 1204 TEQavLQESLEK 1215
Cdd:pfam10174  657 LEE--LMGALEK 666
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
944-1229 9.31e-07

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 52.22  E-value: 9.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  944 LSEREEALKQHKT-LSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFytREYEKLRDTY 1022
Cdd:COG1340      6 LSSSLEELEEKIEeLREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV--KELKEERDEL 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1023 IEEAEKYKMQLqEQFDNLNAAHETSKLEIEAshseklelLKKAYEaslseikkghEIEKKSL-EDLLSEKQESLEKQIND 1101
Cdd:COG1340     84 NEKLNELREEL-DELRKELAELNKAGGSIDK--------LRKEIE----------RLEWRQQtEVLSPEEEKELVEKIKE 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1102 LKSEndaLNEKLKSEEQKRRAREkanlknpqimyLEQELESLKavleIKNEKLHQQDIKLM--------KMEKLVDNNTA 1173
Cdd:COG1340    145 LEKE---LEKAKKALEKNEKLKE-----------LRAELKELR----KEAEEIHKKIKELAeeaqelheEMIELYKEADE 206
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876319 1174 LVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEE 1229
Cdd:COG1340    207 LRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
939-1188 1.07e-06

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: 53.43  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  939 VIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARnelqtvyeaFVQQHQAEKTERENRLKEF-YTREYEK 1017
Cdd:TIGR00618  630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE---------LLASRQLALQKMQSEKEQLtYWKEMLA 700
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1018 LRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQ--ESL 1095
Cdd:TIGR00618  701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgAEL 780
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1096 EKQINDLKSENDALNE-----KLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1170
Cdd:TIGR00618  781 SHLAAEIQFFNRLREEdthllKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
                          250
                   ....*....|....*...
gi 1386876319 1171 NTALVDKLKRFQQENEEL 1188
Cdd:TIGR00618  861 LAQLTQEQAKIIQLSDKL 878
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
976-1162 1.22e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.85  E-value: 1.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  976 EKLEKARNELQTVYEAFvqqhqAEKTERENRLKEfytrEYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIE-AS 1054
Cdd:COG4717     74 KELEEELKEAEEKEEEY-----AELQEELEELEE----ELEELEAE-LEELREELEKLEKLLQLLPLYQELEALEAElAE 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1055 HSEKLELLKKAYEA------SLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanl 1128
Cdd:COG4717    144 LPERLEELEERLEElreleeELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE--- 220
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1386876319 1129 knpQIMYLEQELESLKAVLEI--KNEKLHQQDIKLM 1162
Cdd:COG4717    221 ---ELEELEEELEQLENELEAaaLEERLKEARLLLL 253
PRK09039 PRK09039
peptidoglycan -binding protein;
1034-1184 1.23e-06

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 52.28  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1034 QEQFDNLNA--AHETSKLEIEASHSEKLELLKKAYEASLSEIkkghEIEKKSLEDLLSEkqesLEKQINDLKSENDALNE 1111
Cdd:PRK09039    52 DSALDRLNSqiAELADLLSLERQGNQDLQDSVANLRASLSAA----EAERSRLQALLAE----LAGAGAAAEGRAGELAQ 123
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876319 1112 KLKSEEQ-KRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM-EKLvdnNTALVDK---LKRFQQE 1184
Cdd:PRK09039   124 ELDSEKQvSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgRRL---NVALAQRvqeLNRYRSE 198
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
1023-1183 1.36e-06

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 51.60  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1023 IEEAEKYKMQLQEQFDNLNAAHETSKleieaSHSEKLELLKKAYEASLSeiKKGHEIEKKSLEDLLSEKQESLEKQINDL 1102
Cdd:cd22656    127 LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLNEEYAAKL 199
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1103 KSENDALNEKLKSEEQKRRAREK---------ANLKN------PQIMYLEQ----------ELESLKAVLEIKNEKLHQQ 1157
Cdd:cd22656    200 KAKIDELKALIADDEAKLAAALRliadltaadTDLDNllaligPAIPALEKlqgawqaiatDLDSLKDLLEDDISKIPAA 279
                          170       180
                   ....*....|....*....|....*.
gi 1386876319 1158 DIKLMKMEKLVDNNTALVDKLKRFQQ 1183
Cdd:cd22656    280 ILAKLELEKAIEKWNELAEKADKFRQ 305
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1006-1230 1.61e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1006 RLKEFYTREYEKLRDTYIEEAEKykMQLqeqFDNLNAAHETSKLE-IEAshsekleLLKKAYEASLSEIKKG----HEIE 1080
Cdd:COG4717      2 KIKELEIYGFGKFRDRTIEFSPG--LNV---IYGPNEAGKSTLLAfIRA-------MLLERLEKEADELFKPqgrkPELN 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1081 KKSLEDLLSEKQE--SLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLE--QELESLKAVLEIKNEKLH 1155
Cdd:COG4717     70 LKELKELEEELKEaeEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386876319 1156 QQDIKLMKMEklvdnntALVDKLKRFQQENEELKARMDKHMAiSRQLSTEQAvLQESLEKESKVNKRLSMENEEL 1230
Cdd:COG4717    150 ELEERLEELR-------ELEEELEELEAELAELQEELEELLE-QLSLATEEE-LQDLAEELEELQQRLAELEEEL 215
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
982-1145 1.69e-06

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: 50.69  E-value: 1.69e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  982 RNELQTVYEafVQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAshsekLEL 1061
Cdd:COG1579      3 PEDLRALLD--LQELDSELDRLEHRLKEL-PAELAELEDE-LAALEARLEAAKTELEDLEKEIKRLELEIEE-----VEA 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1062 LKKAYEASLSEIKK-------GHEIE-----KKSLEDLLSE---KQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1126
Cdd:COG1579     74 RIKKYEEQLGNVRNnkeyealQKEIEslkrrISDLEDEILElmeRIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
                          170
                   ....*....|....*....
gi 1386876319 1127 nlknpqimyLEQELESLKA 1145
Cdd:COG1579    154 ---------LEAELEELEA 163
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
1012-1150 1.96e-06

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 51.17  E-value: 1.96e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  1012 TREYEKLRDtYIEEAEKYKMQLQEQFDNLNaahetSKLEIEASHSEKLE-----LLKKAYEAsLSEIKKGHEIEKKSLED 1086
Cdd:smart00787  157 KEDYKLLMK-ELELLNSIKPKLRDRKDALE-----EELRQLKQLEDELEdcdptELDRAKEK-LKKLLQEIMIKVKKLEE 229
                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876319  1087 LLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpQIMYLEQELESLKAVLEIK 1150
Cdd:smart00787  230 LEEELQE-LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK--EIEKLKEQLKLLQSLTGWK 290
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
940-1181 2.00e-06

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: 52.33  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  940 IQHLLSEREEALKQHKTLSQELV-------NLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYT 1012
Cdd:TIGR04523  414 IKKLQQEKELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1013 REYEklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE-----------LLKKAYEASLSEIKK-----G 1076
Cdd:TIGR04523  494 KEKE------LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkeskisdledeLNKDDFELKKENLEKeidekN 567
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1077 HEIEK-----KSLEDLLSEKQE---SLEKQINDLKSEndaLNEKLKSEEQKRRAREKANLKNpqimyleQELESLKAVLE 1148
Cdd:TIGR04523  568 KEIEElkqtqKSLKKKQEEKQElidQKEKEKKDLIKE---IEEKEKKISSLEKELEKAKKEN-------EKLSSIIKNIK 637
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1386876319 1149 IKNEKLHQQdIKLMKME---------KLVDNNTALVDKLKRF 1181
Cdd:TIGR04523  638 SKKNKLKQE-VKQIKETikeirnkwpEIIKKIKESKTKIDDI 678
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
976-1234 2.33e-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: 52.38  E-value: 2.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  976 EKLEKARNELQTVyeafvqqhQAEKTERENRLKEfYTREyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASh 1055
Cdd:TIGR02169  681 ERLEGLKRELSSL--------QSELRRIENRLDE-LSQE--------LSDASRKIGEIEKEIEQLEQEEEKLKERLEEL- 742
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1056 seklellkkayEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLkSEEQKRRAREKANLKNPQIMY 1135
Cdd:TIGR02169  743 -----------EEDLSSLEQEIENVKSELKELEARIEE-LEEDLHKLEEALNDLEARL-SHSRIPEIQAELSKLEEEVSR 809
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1136 LEQELESLKAVLeikNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR-------MDKHMAISRQLSTEQAV 1208
Cdd:TIGR02169  810 IEARLREIEQKL---NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGD 886
                          250       260
                   ....*....|....*....|....*.
gi 1386876319 1209 LQESLEKESKVNKRLSMENEELLWKL 1234
Cdd:TIGR02169  887 LKKERDELEAQLRELERKIEELEAQI 912
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
913-1222 2.55e-06

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: 51.88  E-value: 2.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  913 ENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEkarnELQTVYEAF 992
Cdd:COG5185    160 IIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAK----EIINIEEAL 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  993 VQQhqaEKTERENRLKEFYTREYEKLrdtyIEEAEKYKM----QLQEQFDNLNAAHETSKLEIEaSHSEKLELLKKAYEA 1068
Cdd:COG5185    236 KGF---QDPESELEDLAQTSDKLEKL----VEQNTDLRLeklgENAESSKRLNENANNLIKQFE-NTKEKIAEYTKSIDI 307
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1069 SLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLE 1148
Cdd:COG5185    308 KKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIE 387
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876319 1149 IKNEKLHQQDIKLMKMEKlvDNNTALVDKLKRFQQENEELKARMDKhmaISRQLSTEQAVLQESLEKESKVNKR 1222
Cdd:COG5185    388 STKESLDEIPQNQRGYAQ--EILATLEDTLKAADRQIEELQRQIEQ---ATSSNEEVSKLLNELISELNKVMRE 456
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
1057-1223 2.59e-06

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: 49.92  E-value: 2.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1057 EKLELLKK--AYEASLSEIK---KGHEIEKKSLEDLLSEKQESLEK---QINDLKSENDALNEKLKSEEQKR-RAREK-A 1126
Cdd:COG1579      4 EDLRALLDlqELDSELDRLEhrlKELPAELAELEDELAALEARLEAaktELEDLEKEIKRLELEIEEVEARIkKYEEQlG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1127 NLKNP-QIMYLEQELESLKAVLEIKNEKLhqqdIKLM-KMEKLVDNNTALVDKLKRFQQENEELKARMDKhmAISRQLST 1204
Cdd:COG1579     84 NVRNNkEYEALQKEIESLKRRISDLEDEI----LELMeRIEELEEELAELEAELAELEAELEEKKAELDE--ELAELEAE 157
                          170
                   ....*....|....*....
gi 1386876319 1205 EQAVLQESLEKESKVNKRL 1223
Cdd:COG1579    158 LEELEAEREELAAKIPPEL 176
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
939-1230 3.00e-06

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: 51.56  E-value: 3.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  939 VIQHLLSEREEALK----QHKTLSQELVNLRGELVTASTTCEKLEKARNELQTvyEAFVQQHQAEKTERE-NRLKEfYTR 1013
Cdd:TIGR04523   58 NLDKNLNKDEEKINnsnnKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS--EIKNDKEQKNKLEVElNKLEK-QKK 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1014 EYEKLRDTYIEEAEKykmqLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAY--EASLSEIKKGHEIEKKSLEDL--LS 1089
Cdd:TIGR04523  135 ENKKNIDKFLTEIKK----KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLniQKNIDKIKNKLLKLELLLSNLkkKI 210
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1090 EKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA-NLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLV 1168
Cdd:TIGR04523  211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386876319 1169 DNNTALVDKLKRFQQEN------EELKARMDKHMAISRQLS-TEQAV--LQESLEKESKVNKRLSMENEEL 1230
Cdd:TIGR04523  291 NQLKSEISDLNNQKEQDwnkelkSELKNQEKKLEEIQNQISqNNKIIsqLNEQISQLKKELTNSESENSEK 361
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
955-1237 4.53e-06

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: 51.33  E-value: 4.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  955 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFV--QQHQ------------------AE-------------KT 1001
Cdd:pfam01576  548 KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdLDHQrqlvsnlekkqkkfdqmlAEekaisaryaeerdRA 627
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1002 ERENRLKEF----YTREYEKLRDTyIEEAEKYKMQLQEQFDNL--------NAAH--ETSKLEIEASHSE---KLELL-- 1062
Cdd:pfam01576  628 EAEAREKETralsLARALEEALEA-KEELERTNKQLRAEMEDLvsskddvgKNVHelERSKRALEQQVEEmktQLEELed 706
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1063 --------KKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDalneklksEEQKRRAREKANLKNpqim 1134
Cdd:pfam01576  707 elqatedaKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELE--------DERKQRAQAVAAKKK---- 774
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1135 yLEQELESLKAVLEIKNeKLHQQDIKLMKmeklvdnntALVDKLKRFQQENEELKARMDKHMAISRQ-------LSTEQA 1207
Cdd:pfam01576  775 -LELDLKELEAQIDAAN-KGREEAVKQLK---------KLQAQMKDLQRELEEARASRDEILAQSKEsekklknLEAELL 843
                          330       340       350
                   ....*....|....*....|....*....|
gi 1386876319 1208 VLQESLEKESKVNKRLSMENEELLWKLHNG 1237
Cdd:pfam01576  844 QLQEDLAASERARRQAQQERDELADEIASG 873
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
940-1161 5.13e-06

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 49.91  E-value: 5.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  940 IQHLLSEREEALKQHKTLSQELVNLR---GELVTASTTCEKLEKARNELQtvyeaFVQQHQAEKTERENRLKEfYTREYE 1016
Cdd:COG1340     73 VKELKEERDELNEKLNELREELDELRkelAELNKAGGSIDKLRKEIERLE-----WRQQTEVLSPEEEKELVE-KIKELE 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1017 KLrdtyIEEAEKyKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLS---------EIKK-----GHEIEKK 1082
Cdd:COG1340    147 KE----LEKAKK-ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEmielykeadELRKeadelHKEIVEA 221
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1083 SLE-DLLSEKQESLEKQINDLKSENDALNEKLKsEEQKRRAREKANLKNPQIMyleqelESLKavleiKNEKLHQQDIKL 1161
Cdd:COG1340    222 QEKaDELHEEIIELQKELRELRKELKKLRKKQR-ALKREKEKEELEEKAEEIF------EKLK-----KGEKLTTEELKL 289
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
976-1156 6.57e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.54  E-value: 6.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  976 EKLEKARNELQTVY--EAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLnaAHETSKLEIEA 1053
Cdd:COG4717     49 ERLEKEADELFKPQgrKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEEL--REELEKLEKLL 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1054 SHSEKLELLKKAyEASLSEIKKGHEIEKKSLEDL--LSEKQESLEKQINDLKSENDALNEK--LKSEEQKRRAREKANLK 1129
Cdd:COG4717    126 QLLPLYQELEAL-EAELAELPERLEELEERLEELreLEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEELEEL 204
                          170       180
                   ....*....|....*....|....*..
gi 1386876319 1130 NPQIMYLEQELESLKAVLEIKNEKLHQ 1156
Cdd:COG4717    205 QQRLAELEEELEEAQEELEELEEELEQ 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
955-1193 6.83e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.68  E-value: 6.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  955 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFvqQHQAEKTERENRLKEfYTREYEKLRDTY--IEEAEKYKMQ 1032
Cdd:COG4913    613 AALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVAS-AEREIAELEAELerLDASSDDLAA 689
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1033 LQEQFDNLNAAHETSKLEIEASHSEK---------LELLKKAYEASLSEIKKGHEIEKKSL--EDLLSEKQESLEKQI-N 1100
Cdd:COG4913    690 LEEQLEELEAELEELEEELDELKGEIgrlekeleqAEEELDELQDRLEAAEDLARLELRALleERFAAALGDAVERELrE 769
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1101 DLKSENDALNEKLKSEEQK-RRAREKANLKNPQIMY-LEQELESLKAVLE----IKNEKL--HQQDIKLMKMEKLVDNNT 1172
Cdd:COG4913    770 NLEERIDALRARLNRAEEElERAMRAFNREWPAETAdLDADLESLPEYLAlldrLEEDGLpeYEERFKELLNENSIEFVA 849
                          250       260
                   ....*....|....*....|.
gi 1386876319 1173 ALVDKLKRfqqENEELKARMD 1193
Cdd:COG4913    850 DLLSKLRR---AIREIKERID 867
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
946-1231 9.14e-06

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: 49.68  E-value: 9.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  946 EREEALKQHKTL-SQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQ---------HQAEKTERENRLKEFYTREY 1015
Cdd:pfam15742   41 GKNLDLKQHNSLlQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKirelelevlKQAQSIKSQNSLQEKLAQEK 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1016 EKLRDtyieeAEKYKMQLQEQfdnLNAAHETSKLEIEASHSEKLEllKKAYEASLSEIK-KGHEIEKKSLEDLLSEKQES 1094
Cdd:pfam15742  121 SRVAD-----AEEKILELQQK---LEHAHKVCLTDTCILEKKQLE--ERIKEASENEAKlKQQYQEEQQKRKLLDQNVNE 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1095 LEKQINDLKSENDAL----------------------NEKLKSEEQKRRAREKANlknpQIMYLEQELESLKAVLEI--- 1149
Cdd:pfam15742  191 LQQQVRSLQDKEAQLemtnsqqqlriqqqeaqlkqleNEKRKSDEHLKSNQELSE----KLSSLQQEKEALQEELQQvlk 266
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1150 --------KNEKLHQQDIKLMKMEKlvdnntalvdklkRFQQENEELKARMdkhmaisRQLSTEQAVLQESLEKESKVNK 1221
Cdd:pfam15742  267 qldvhvrkYNEKHHHHKAKLRRAKD-------------RLVHEVEQRDERI-------KQLENEIGILQQQSEKEKAFQK 326
                          330
                   ....*....|
gi 1386876319 1222 RLSMENEELL 1231
Cdd:pfam15742  327 QVTAQNEILL 336
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
927-1210 1.05e-05

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: 50.12  E-value: 1.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  927 ACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVYEAFVQQHQaektereNR 1006
Cdd:pfam15921  199 ASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVE---DQLEALKSESQNKIELLLQQHQ-------DR 268
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1007 LKEFYTrEYEKLRDTYIEEAEKYKMQ----------LQEQFDNLNAAHETSKLEIEASHSE---KLELLKKAYEASLSEI 1073
Cdd:pfam15921  269 IEQLIS-EHEVEITGLTEKASSARSQansiqsqleiIQEQARNQNSMYMRQLSDLESTVSQlrsELREAKRMYEDKIEEL 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1074 KK-----GHEI------------EKKSLEDLLS---------EKQESLEKQ---------------INDLKSEND----- 1107
Cdd:pfam15921  348 EKqlvlaNSELtearterdqfsqESGNLDDQLQklladlhkrEKELSLEKEqnkrlwdrdtgnsitIDHLRRELDdrnme 427
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1108 -----ALNEKLKSEEQKRRAREKANLKNP-----QIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLV-DNNTALVD 1176
Cdd:pfam15921  428 vqrleALLKAMKSECQGQMERQMAAIQGKnesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVsDLTASLQE 507
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1386876319 1177 KLKRFQQENEE---LKARMDKHMAISRQLSTEQAVLQ 1210
Cdd:pfam15921  508 KERAIEATNAEitkLRSRVDLKLQELQHLKNEGDHLR 544
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
949-1229 1.08e-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: 49.97  E-value: 1.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  949 EALKQHKTLSQELVNL--RGELVTASTTC------EKLEKARNELQTVYEAFVQQHQAEkterenrlkEFYTREYEKLrd 1020
Cdd:TIGR00618  184 MEFAKKKSLHGKAELLtlRSQLLTLCTPCmpdtyhERKQVLEKELKHLREALQQTQQSH---------AYLTQKREAQ-- 252
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1021 tyiEEAEKYKMQLQEQ------FDNLNAAHETSKLEIE--------ASHSEKLELLKKAYEASLSEIKKgheiEKKSLED 1086
Cdd:TIGR00618  253 ---EEQLKKQQLLKQLrarieeLRAQEAVLEETQERINrarkaaplAAHIKAVTQIEQQAQRIHTELQS----KMRSRAK 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1087 LLSEKQeSLEKQINDLKSENDALNEKLKSEEQKRRAREKANLK-----------------NPQIMYLEQELESLKAVLEI 1149
Cdd:TIGR00618  326 LLMKRA-AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIreiscqqhtltqhihtlQQQKTTLTQKLQSLCKELDI 404
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1150 KNEKLHQQDIKLMKME----KLVDNNTALVDKLKRFQQ--------------ENEELKARMDKHMAISRQLSTEQAVLQE 1211
Cdd:TIGR00618  405 LQREQATIDTRTSAFRdlqgQLAHAKKQQELQQRYAELcaaaitctaqceklEKIHLQESAQSLKEREQQLQTKEQIHLQ 484
                          330
                   ....*....|....*...
gi 1386876319 1212 SLEKESKVNKRLSMENEE 1229
Cdd:TIGR00618  485 ETRKKAVVLARLLELQEE 502
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
1005-1156 1.30e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 47.59  E-value: 1.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1005 NRLKEFY---TREYEKLRDTYieEAEKYKMQLQEQfDNLNAAHETSKlEIEaSHSEKLE-LLKKAYEasLSEIKKGHEIE 1080
Cdd:pfam13851   11 NEIKNYYndiTRNNLELIKSL--KEEIAELKKKEE-RNEKLMSEIQQ-ENK-RLTEPLQkAQEEVEE--LRKQLENYEKD 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1081 KKSLEDLlSEKQESLEKQINDLKSENDALNEKLKSEEQKRRA------------REKANLKNpqiMYLEQELESLKAVLE 1148
Cdd:pfam13851   84 KQSLKNL-KARLKVLEKELKDLKWEHEVLEQRFEKVERERDElydkfeaaiqdvQQKTGLKN---LLLEKKLQALGETLE 159

                   ....*...
gi 1386876319 1149 IKNEKLHQ 1156
Cdd:pfam13851  160 KKEAQLNE 167
Filament pfam00038
Intermediate filament protein;
978-1202 1.35e-05

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 48.76  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  978 LEKARNELQTVYEAFVQQHQAEkterENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHET----------- 1046
Cdd:pfam00038   23 LEQQNKLLETKISELRQKKGAE----PSRLYSLYEKEIEDLRRQ-LDTLTVERARLQLELDNLRLAAEDfrqkyedelnl 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1047 --------------------SKLEIEA---SHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLK 1103
Cdd:pfam00038   98 rtsaendlvglrkdldeatlARVDLEAkieSLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLD-LTSALAEIR 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1104 SENDALNEKLKSE--------------------EQKRRAREKANLKNPQIMYLEQELESL---KAVLEIKNEKLHQQDIK 1160
Cdd:pfam00038  177 AQYEEIAAKNREEaeewyqskleelqqaaarngDALRSAKEEITELRRTIQSLEIELQSLkkqKASLERQLAETEERYEL 256
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1161 LMKM--EKLVDNNTALV---DKLKRFQQENEEL---KARMDKHMAISRQL 1202
Cdd:pfam00038  257 QLADyqELISELEAELQetrQEMARQLREYQELlnvKLALDIEIATYRKL 306
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
1019-1231 1.43e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 1.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1019 RDTYIEEAEKYKMQLQEQFDNLNAAHEtsklEIEASHSEKLELLKKAyEASLSEIKKGHEIEKKSLEDLlSEKQESLEKQ 1098
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALA----ELRKELEELEEELEQL-RKELEELSRQISALRKDLARL-EAEVEQLEER 748
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1099 INDLKSENDALNEKLKSEEQKRrarEKANlknPQIMYLEQELESLKAV--------------LEIKNEKLHQQDIKLMKM 1164
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERL---EEAE---EELAEAEAEIEELEAQieqlkeelkalreaLDELRAELTLLNEEAANL 822
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876319 1165 EKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELL 1231
Cdd:TIGR02168  823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
PRK12704 PRK12704
phosphodiesterase; Provisional
1013-1207 1.46e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.39  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1013 REYEKLRDTYIEEAEKykmqlqeqfdnlNAAHETSKLEIEAShsEKLELLKKAYEASLSEIKKghEIEKksLEDLLSEKQ 1092
Cdd:PRK12704    34 KEAEEEAKRILEEAKK------------EAEAIKKEALLEAK--EEIHKLRNEFEKELRERRN--ELQK--LEKRLLQKE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1093 ESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpqimyLEQELESLKAVLEIKNEK---LHQQDIKLMKMEKLVD 1169
Cdd:PRK12704    96 ENLDRKLELLEKREEELEKKEKELEQKQQELEK----------KEEELEELIEEQLQELERisgLTAEEAKEILLEKVEE 165
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1386876319 1170 NNTAlvDKLKRFQQENEELKARMDKH------MAISRqLSTEQA 1207
Cdd:PRK12704   166 EARH--EAAVLIKEIEEEAKEEADKKakeilaQAIQR-CAADHV 206
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
932-1194 1.72e-05

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 48.37  E-value: 1.72e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  932 KFEALTVVIQHLLSEREEALKQHKTLSQELVNLRG---ELVtasttcEKLEKARNELQTVYEAfVQQHQAEKTERENRLK 1008
Cdd:COG1340     16 KIEELREEIEELKEKRDELNEELKELAEKRDELNAqvkELR------EEAQELREKRDELNEK-VKELKEERDELNEKLN 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1009 EFYT--REYEKLRDTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEAshsEKlELLKK--AYEASLSEIKKGHEIEKKSL 1084
Cdd:COG1340     89 ELREelDELRKELAELNKAGGSID-KLRKEIERLEWRQQTEVLSPEE---EK-ELVEKikELEKELEKAKKALEKNEKLK 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1085 EDL-----LSEKQESLEKQINDLKSENDALNEKLKSEEQKR-RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQD 1158
Cdd:COG1340    164 ELRaelkeLRKEAEEIHKKIKELAEEAQELHEEMIELYKEAdELRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1386876319 1159 IKLMKMEKlVDNNTALVDKLKRFQQENEELKARMDK 1194
Cdd:COG1340    244 KELKKLRK-KQRALKREKEKEELEEKAEEIFEKLKK 278
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1059-1234 1.80e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1059 LELLKKAYEaSLSEIKKGHEIEKKSLEDLLS----------EKQESLE---KQINDLKSENDALNEKL-KSEEQKRR--- 1121
Cdd:PRK03918   157 LDDYENAYK-NLGEVIKEIKRRIERLEKFIKrtenieelikEKEKELEevlREINEISSELPELREELeKLEKEVKElee 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1122 AREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNntalVDKLKRFQQENEELKARMDKHMAISRQ 1201
Cdd:PRK03918   236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE----LKELKEKAEEYIKLSEFYEEYLDELRE 311
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1386876319 1202 LSTE-----------QAVLQESLEKESKVNKrLSMENEELLWKL 1234
Cdd:PRK03918   312 IEKRlsrleeeingiEERIKELEEKEERLEE-LKKKLKELEKRL 354
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
871-1102 1.88e-05

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 49.18  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  871 ALNAVEKSRQknprsLCIQPQTAPDALPPEktleLTQYKTKCENQSGFILQLKQLLACGN---TKFEALTVVIQHLLSE- 946
Cdd:COG3096    418 AVQALEKARA-----LCGLPDLTPENAEDY----LAAFRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVCKIAGEv 488
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  947 -REEA-------LKQH---KTLSQELVNLRGELVTAsttcEKLEKARNELQTVYEAFVQQHQAEKTERENrLKEFYTREY 1015
Cdd:COG3096    489 eRSQAwqtarelLRRYrsqQALAQRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELE 563
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1016 EKLRD--TYIEEAEKYKMQLQEQFDNLNAAHEtsKLEIEASH----SEKLELLKKAYEASL---SEIKKG------HEIE 1080
Cdd:COG3096    564 AQLEEleEQAAEAVEQRSELRQQLEQLRARIK--ELAARAPAwlaaQDALERLREQSGEALadsQEVTAAmqqlleRERE 641
                          250       260
                   ....*....|....*....|..
gi 1386876319 1081 KKSLEDLLSEKQESLEKQINDL 1102
Cdd:COG3096    642 ATVERDELAARKQALESQIERL 663
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
904-1195 2.20e-05

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: 48.70  E-value: 2.20e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  904 ELTQYKTKCENQSGFILQL--------KQLLAcGNTKFEALTVVIQHLLSEREEALKQHKTLSQElvnlrGELVTASTTC 975
Cdd:pfam06160  108 ELDELLESEEKNREEVEELkdkyrelrKTLLA-NRFSYGPAIDELEKQLAEIEEEFSQFEELTES-----GDYLEAREVL 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  976 EKLEKARNELQTVYEAFVQQHQaekterenRLKEFYTREYEKLRDTYIE-EAEKYK---MQLQEQFDNLNAAHETS---- 1047
Cdd:pfam06160  182 EKLEEETDALEELMEDIPPLYE--------ELKTELPDQLEELKEGYREmEEEGYAlehLNVDKEIQQLEEQLEENlall 253
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1048 -KLEIEAShSEKLELLKKA----YEASLSEIKKGHEIEKKS--LEDLLS---------------------------EKQE 1093
Cdd:pfam06160  254 eNLELDEA-EEALEEIEERidqlYDLLEKEVDAKKYVEKNLpeIEDYLEhaeeqnkelkeelervqqsytlnenelERVR 332
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1094 SLEKQINDLKSENDALNEKLKSEEQkrrarekanlknPQIMYLEQELESLKAVLEIKNEklhQQDIK--LMKMEKlvDNN 1171
Cdd:pfam06160  333 GLEKQLEELEKRYDEIVERLEEKEV------------AYSELQEELEEILEQLEEIEEE---QEEFKesLQSLRK--DEL 395
                          330       340
                   ....*....|....*....|....
gi 1386876319 1172 TALvDKLKRFQQENEELKARMDKH 1195
Cdd:pfam06160  396 EAR-EKLDEFKLELREIKRLVEKS 418
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
976-1212 2.69e-05

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 48.11  E-value: 2.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  976 EKLEKARnelqtvyeafvQQHQAEKTERENRLKEF-----YTREYEKLRDTYIEEAEKYKMQLQEqfdnlnaaHETSKLE 1050
Cdd:pfam15558  109 EKLERAR-----------QEAEQRKQCQEQRLKEKeeelqALREQNSLQLQERLEEACHKRQLKE--------REEQKKV 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1051 IEASHSEKL--ELLKKAYEaslSEIKKGHEIEKKSLEDLLSEKQESLEKQIndlKSENDALNEK-LKSEEQKRRAREKAN 1127
Cdd:pfam15558  170 QENNLSELLnhQARKVLVD---CQAKAEELLRRLSLEQSLQRSQENYEQLV---EERHRELREKaQKEEEQFQRAKWRAE 243
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1128 LKNpqimylEQELESLKAVLEIKNEKL-----HQQDIKLMKMEKLVDNNTA-----LVDKLKRFQQEN---EELKARMDK 1194
Cdd:pfam15558  244 EKE------EERQEHKEALAELADRKIqqarqVAHKTVQDKAQRARELNLEreknhHILKLKVEKEEKchrEGIKEAIKK 317
                          250
                   ....*....|....*....
gi 1386876319 1195 HMAISRQLSTE-QAVLQES 1212
Cdd:pfam15558  318 KEQRSEQISREkEATLEEA 336
PKK pfam12474
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ...
1055-1206 3.26e-05

Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.


Pssm-ID: 463600 [Multi-domain]  Cd Length: 139  Bit Score: 44.86  E-value: 3.26e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1055 HSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEK-QINDLKsendALNEKLKSEEQKRRAREKANLKNpQI 1133
Cdd:pfam12474    1 HQLQKEQQKDRFEQERQQLKKRYEKELEQLERQQKQQIEKLEQrQTQELR----RLPKRIRAEQKKRLKMFRESLKQ-EK 75
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876319 1134 MYLEQELESLKavleikneKLHQQDIKLMKMEKLvdnntalvdKLKRFQQENEELKARMDKHMAISRQLSTEQ 1206
Cdd:pfam12474   76 KELKQEVEKLP--------KFQRKEAKRQRKEEL---------ELEQKHEELEFLQAQSEALERELQQLQNEK 131
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
944-1230 4.31e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 47.91  E-value: 4.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  944 LSEREEALKQhKTLSQELV-----NLRGElvtASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKL 1018
Cdd:PRK04778    34 LEERKQELEN-LPVNDELEkvkklNLTGQ---SEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEELNDKFRFRKAKHEINE 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1019 RDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAshseklelLKKAYEaslsEIKKghEIEKKSleDLLSEKQESLEKQ 1098
Cdd:PRK04778   110 IESLLDLIEEDIEQILEELQELLESEEKNREEVEQ--------LKDLYR----ELRK--SLLANR--FSFGPALDELEKQ 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1099 INDLKSE---NDALNEK---LKSEEQKRRAREK-ANLKN-----PQIMY-----LEQELESLKAVL-EIKNEKLHQQDIK 1160
Cdd:PRK04778   174 LENLEEEfsqFVELTESgdyVEAREILDQLEEElAALEQimeeiPELLKelqteLPDQLQELKAGYrELVEEGYHLDHLD 253
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1161 LMKM-----EKLVDNNTALVD-KLKRFQQENEELKARMDK------HMAISRQ-LSTEQAVLQESLEKESKVNKRLSMEN 1227
Cdd:PRK04778   254 IEKEiqdlkEQIDENLALLEElDLDEAEEKNEEIQERIDQlydileREVKARKyVEKNSDTLPDFLEHAKEQNKELKEEI 333

                   ...
gi 1386876319 1228 EEL 1230
Cdd:PRK04778   334 DRV 336
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
948-1120 4.32e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  948 EEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKefytREyeklrdtyIEEAE 1027
Cdd:COG4913    284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE----RE--------IERLE 351
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1028 KYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEikkgheiekKSLEDLLSEKQESLEKQINDLKSEND 1107
Cdd:COG4913    352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL---------EEELEALEEALAEAEAALRDLRRELR 422
                          170
                   ....*....|...
gi 1386876319 1108 ALNEKLKSEEQKR 1120
Cdd:COG4913    423 ELEAEIASLERRK 435
PTZ00121 PTZ00121
MAEBL; Provisional
976-1207 4.43e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 4.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  976 EKLEKARNELQTVYEAFVQQHQAE--KTERENRLKEFYTREYEKLRDTY-----IEEAEKYK---MQLQEQFDNLNAAHE 1045
Cdd:PTZ00121  1587 KKAEEARIEEVMKLYEEEKKMKAEeaKKAEEAKIKAEELKKAEEEKKKVeqlkkKEAEEKKKaeeLKKAEEENKIKAAEE 1666
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1046 TSKLEIEASHSEKL------------ELLKKAYEA-SLSEIKKGHEIEKKSLEDLLSEKQESLEKqINDLKSENDalNEK 1112
Cdd:PTZ00121  1667 AKKAEEDKKKAEEAkkaeedekkaaeALKKEAEEAkKAEELKKKEAEEKKKAEELKKAEEENKIK-AEEAKKEAE--EDK 1743
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1113 LKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIK-LMKMEKLV----DNNTALVDKLKR---FQQE 1184
Cdd:PTZ00121  1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKrRMEVDKKIkdifDNFANIIEGGKEgnlVIND 1823
                          250       260
                   ....*....|....*....|...
gi 1386876319 1185 NEELKARMDKHMAISRQLSTEQA 1207
Cdd:PTZ00121  1824 SKEMEDSAIKEVADSKNMQLEEA 1846
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
904-1191 4.75e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.20  E-value: 4.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  904 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 983
Cdd:COG4372     46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  984 ELQT---VYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1060
Cdd:COG4372    126 DLEQqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEE--LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1061 LLKKAYEASLSEIKKGHEIEKKSLE---DLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1137
Cdd:COG4372    204 EAEKLIESLPRELAEELLEAKDSLEaklGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1386876319 1138 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR 1191
Cdd:COG4372    284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
921-1224 5.12e-05

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 46.87  E-value: 5.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  921 QLKQLLACGNT---KFEALTVVIQHLLSEREEALKQHK-------TLSQELVNLRGELVTASTTCEKLEKARNELQTVYE 990
Cdd:pfam09728    5 ELMQLLNKLDSpeeKLAALCKKYAELLEEMKRLQKDLKklkkkqdQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  991 AFVQQHQAEKTERENRLKEFYTREYEKLRD--TYIEEAEKYKMQLQEQFDNLnaahetskleieashSEKLELLKKAYEa 1068
Cdd:pfam09728   85 KLKEESKKLAKEEEEKRKELSEKFQSTLKDiqDKMEEKSEKNNKLREENEEL---------------REKLKSLIEQYE- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1069 sLSEikkgheiekKSLEDLLseKQESLEKQINDLK-SENDALNEKLKSEEQKRRAREkanlKNPQIMYLEQELESLKAVL 1147
Cdd:pfam09728  149 -LRE---------LHFEKLL--KTKELEVQLAEAKlQQATEEEEKKAQEKEVAKARE----LKAQVQTLSETEKELREQL 212
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1148 EIKNEKLHQ-QDIkLMKMEKLVDNNTA----LVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKR 1222
Cdd:pfam09728  213 NLYVEKFEEfQDT-LNKSNEVFTTFKKemekMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEK 291

                   ..
gi 1386876319 1223 LS 1224
Cdd:pfam09728  292 LE 293
Jnk-SapK_ap_N pfam09744
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ...
1013-1179 5.13e-05

JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.


Pssm-ID: 462875 [Multi-domain]  Cd Length: 150  Bit Score: 44.91  E-value: 5.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1013 REYEKLRDTYIEEAEKYKM----QLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASlSEIKKGHEIEKKSLEDLL 1088
Cdd:pfam09744   10 KEFERLIDRYGEDVVKGLMpkvvNVLELLESLASRNQEHNVELEEL-REDNEQLETQYERE-KALRKRAEEELEEIEDQW 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1089 SEKQESLEKQINDLKSENDALneklkseEQKRRARekanlknpqimyleqeLESLKAVLEIKNEKLHQQDIKLMKmeKLV 1168
Cdd:pfam09744   88 EQETKDLLSQVESLEEENRRL-------EADHVSR----------------LEEKEAELKKEYSKLHERETEVLR--KLK 142
                          170
                   ....*....|.
gi 1386876319 1169 DnntaLVDKLK 1179
Cdd:pfam09744  143 E----VVDRQR 149
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
1048-1193 7.92e-05

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 43.83  E-value: 7.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1048 KLEIEASHSEKLELLKKAYEASLSEIKKGHEIEkksledllsekqeSLEKQINDLKSENDALNEKLKseEQKRRAREKAN 1127
Cdd:pfam12718    6 KLEAENAQERAEELEEKVKELEQENLEKEQEIK-------------SLTHKNQQLEEEVEKLEEQLK--EAKEKAEESEK 70
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876319 1128 LK------NPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKlvdnntalvdKLKRFQQENEELKARMD 1193
Cdd:pfam12718   71 LKtnnenlTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLER----------KVQALEQERDEWEKKYE 132
PTZ00121 PTZ00121
MAEBL; Provisional
979-1222 8.34e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 8.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  979 EKARNELQTVYEAFVQQHQAEKTEREnRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEiEASHSEK 1058
Cdd:PTZ00121  1223 AKKAEAVKKAEEAKKDAEEAKKAEEE-RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEE 1300
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1059 L----ELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRARE-KANLKNPQI 1133
Cdd:PTZ00121  1301 KkkadEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKA 1380
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1134 MYLEQELESLKAVLEIKneKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQEN---EELKARM-DKHMAISRQLSTEQAVL 1209
Cdd:PTZ00121  1381 DAAKKKAEEKKKADEAK--KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkaDEAKKKAeEAKKADEAKKKAEEAKK 1458
                          250
                   ....*....|...
gi 1386876319 1210 QESLEKESKVNKR 1222
Cdd:PTZ00121  1459 AEEAKKKAEEAKK 1471
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
1062-1215 9.27e-05

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 44.90  E-value: 9.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1062 LKKAYEASLSEIKKGH-EIEKKSLEDL---------LSEKQESLEKQINDLKSENDALNEKLKsEEQKRRAREKANLKNP 1131
Cdd:pfam13851    2 LMKNHEKAFNEIKNYYnDITRNNLELIkslkeeiaeLKKKEERNEKLMSEIQQENKRLTEPLQ-KAQEEVEELRKQLENY 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1132 QimYLEQELESLKAVLEIKNEKL----HQQDIKLMKMEKLVDNNTALvdkLKRFQQENEELKARMD-KHMAISRQLSTeq 1206
Cdd:pfam13851   81 E--KDKQSLKNLKARLKVLEKELkdlkWEHEVLEQRFEKVERERDEL---YDKFEAAIQDVQQKTGlKNLLLEKKLQA-- 153

                   ....*....
gi 1386876319 1207 avLQESLEK 1215
Cdd:pfam13851  154 --LGETLEK 160
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
992-1157 1.04e-04

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 45.12  E-value: 1.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  992 FVQQHQAEKTERENrLKEFYTREYEKLRDTyieeaEKYKMQLQEQFDNLNAAHETSKLE------IEASHSEKLELLKKA 1065
Cdd:pfam17078   43 FLENLASLKHENDN-LSSMLNRKERRLKDL-----EDQLSELKNSYEELTESNKQLKKRlenssaSETTLEAELERLQIQ 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1066 YEASLSEIK--KGH---EIE--KKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREkaNLKNPQIMYLEQ 1138
Cdd:pfam17078  117 YDALVDSQNeyKDHyqqEINtlQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFKNLD--NIYVNKNNKLLT 194
                          170       180
                   ....*....|....*....|
gi 1386876319 1139 ELESLKAVLEIKN-EKLHQQ 1157
Cdd:pfam17078  195 KLDSLAQLLDLPSwLNLYPE 214
PRK12704 PRK12704
phosphodiesterase; Provisional
1079-1218 1.18e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.31  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1079 IEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE------EQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNE 1152
Cdd:PRK12704    24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEakeeihKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876319 1153 KLHQQDIKLMKMEKLVDNNTALVDKLkrfQQENEELKARMDKHMAISRQLSTEQA--VLQESLEKESK 1218
Cdd:PRK12704   104 LLEKREEELEKKEKELEQKQQELEKK---EEELEELIEEQLQELERISGLTAEEAkeILLEKVEEEAR 168
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
1084-1234 1.25e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 1.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1084 LEDLLSEkqesLEKQINDLKSE-NDALN-EKLKSEEQKRRAREKANlknpQIMYLEQELESLKAVLEIKNEKLHQQDIKL 1161
Cdd:COG1196    191 LEDILGE----LERQLEPLERQaEKAERyRELKEELKELEAELLLL----KLRELEAELEELEAELEELEAELEELEAEL 262
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876319 1162 MKMEKLVDNNTAlvdKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKL 1234
Cdd:COG1196    263 AELEAELEELRL---ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
1082-1239 1.80e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.90  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1082 KSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRArekanlknpqimyleqeleslkavleiKNEKLHQQDIKL 1161
Cdd:COG1340      7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDE---------------------------LNAQVKELREEA 59
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876319 1162 MKMEKLVDnntALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLsmenEELLWKLHNGDL 1239
Cdd:COG1340     60 QELREKRD---ELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEI----ERLEWRQQTEVL 130
Snf7 pfam03357
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ...
1085-1234 1.81e-04

Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.


Pssm-ID: 460896 [Multi-domain]  Cd Length: 168  Bit Score: 43.38  E-value: 1.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1085 EDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNpQIMYLEQELESLKAVLE-IKNEKLHQQDIKLMK 1163
Cdd:pfam03357   10 IRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEK-QLDQLDGQLSNLEQQRMaIENAKSNQEVLNAMK 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1164 --------MEKLVDnntalVDKLKRFQQENEELKARMD-KHMAISRQLSTEQAVLQESLEKEskVNKRLSMENEELLWKL 1234
Cdd:pfam03357   89 qgakamkaMNKLMD-----IDKIDKLMDEIEDQMEKADeISEMLSDPLDDADEEDEEELDAE--LDALLDEIGDEESVEL 161
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
1023-1236 1.86e-04

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: 46.12  E-value: 1.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1023 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEASH--SEKLELLKKAYEASLSEIK-KGHEIEKKSLEDLLSEKQESLEKQI 1099
Cdd:pfam02463  159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDleELKLQELKLKEQAKKALEYyQLKEKLELEEEYLLYLDYLKLNEER 238
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1100 NDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLK 1179
Cdd:pfam02463  239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKE-NKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876319 1180 RFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLHN 1236
Cdd:pfam02463  318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
910-1161 1.89e-04

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 45.98  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  910 TKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQhktLSQELVNLRGELVtasttcEKLEKARNELQTVY 989
Cdd:pfam12128  244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE---LNQLLRTLDDQWK------EKRDELNGELSAAD 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  990 EAfVQQHQAEKTERENRLKEFYTREYEKLR---------DTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1060
Cdd:pfam12128  315 AA-VAKDRSELEALEDQHGAFLDADIETAAadqeqlpswQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIA 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1061 LLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE--------------EQKR------ 1120
Cdd:pfam12128  394 GIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatpellLQLEnfderi 473
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1386876319 1121 -RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKL 1161
Cdd:pfam12128  474 eRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRL 515
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
1032-1230 1.95e-04

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: 45.89  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1032 QLQEQFDNLNAAHETSKLEIEaSHSEKLELLKKAYEASLS---EIKKGHEIEK--KSLEDLLSEKQESLEKQIN---DLK 1103
Cdd:pfam05557    4 LIESKARLSQLQNEKKQMELE-HKRARIELEKKASALKRQldrESDRNQELQKriRLLEKREAEAEEALREQAElnrLKK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1104 SENDALNEKLKSEEQKR-RARE-KANLKNP------QIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALV 1175
Cdd:pfam05557   83 KYLEALNKKLNEKESQLaDAREvISCLKNElselrrQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1386876319 1176 DKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVnKRLSMENEEL 1230
Cdd:pfam05557  163 SSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKEL-ERLREHNKHL 216
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
947-1241 2.20e-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: 45.55  E-value: 2.20e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  947 REEALKQHKTLSQELVNLRGELV-TASTTcekleKARNELQTVYEAFVQQHQaEKTERENRLKEFYTREYEKLRDTYIEE 1025
Cdd:pfam01576  287 RNKAEKQRRDLGEELEALKTELEdTLDTT-----AAQQELRSKREQEVTELK-KALEEETRSHEAQLQEMRQKHTQALEE 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1026 aekykmqLQEQFDNLN---AAHETSKLEIEASHSEKLELLKkayeaSLSEIKKGHEIEKKSLEDLLSE-----------K 1091
Cdd:pfam01576  361 -------LTEQLEQAKrnkANLEKAKQALESENAELQAELR-----TLQQAKQDSEHKRKKLEGQLQElqarlseserqR 428
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1092 QESLEKqINDLKSENDALNEKLKSEEQK-----------------------RRAREKANLKNpQIMYLEQELESLKAVLE 1148
Cdd:pfam01576  429 AELAEK-LSKLQSELESVSSLLNEAEGKniklskdvsslesqlqdtqellqEETRQKLNLST-RLRQLEDERNSLQEQLE 506
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1149 IKNEK-------LHQQDIKLMKMEKLVDNNTALVDKL----KRFQQENEELKARMDkhmaisrqlstEQAVLQESLEKEs 1217
Cdd:pfam01576  507 EEEEAkrnverqLSTLQAQLSDMKKKLEEDAGTLEALeegkKRLQRELEALTQQLE-----------EKAAAYDKLEKT- 574
                          330       340
                   ....*....|....*....|....*
gi 1386876319 1218 kvNKRLSMENEELLWKL-HNGDLCS 1241
Cdd:pfam01576  575 --KNRLQQELDDLLVDLdHQRQLVS 597
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
1033-1230 2.27e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 45.30  E-value: 2.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1033 LQE----QFDNLNAAHETSKLEIEASH----SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESL---EKQIND 1101
Cdd:PRK05771    25 LHElgvvHIEDLKEELSNERLRKLRSLltklSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELekiEKEIKE 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1102 LKSENDALNEKLKSEEQKRRAREK-ANLKNPQImyLEQELESLKAVL------EIKNEKLHQQDIKLMKMEKLVDNNTAL 1174
Cdd:PRK05771   105 LEEEISELENEIKELEQEIERLEPwGNFDLDLS--LLLGFKYVSVFVgtvpedKLEELKLESDVENVEYISTDKGYVYVV 182
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1175 VDKLKRFQQE-NEELKarmdKHMAISRQLSTE---QAVLQESLEKESKVNKRLSMENEEL 1230
Cdd:PRK05771   183 VVVLKELSDEvEEELK----KLGFERLELEEEgtpSELIREIKEELEEIEKERESLLEEL 238
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
945-1224 2.33e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 2.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  945 SEREEALKQHKTLSQELVN----LRGELVTASTTCEKLEKARNELqtvyEAFVQQHQAEKTERENRLKEFyTREYEKLRD 1020
Cdd:PRK02224   324 EELRDRLEECRVAAQAHNEeaesLREDADDLEERAEELREEAAEL----ESELEEAREAVEDRREEIEEL-EEEIEELRE 398
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1021 TY------IEEAEKYKMQLQEqfdNLNAAHETSKlEIEASHSEKLELLKKAyEASLSEIKK---GHEIEKKSLEDLLSEK 1091
Cdd:PRK02224   399 RFgdapvdLGNAEDFLEELRE---ERDELREREA-ELEATLRTARERVEEA-EALLEAGKCpecGQPVEGSPHVETIEED 473
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1092 QE---SLEKQINDLKSENDALNEKLKSEEQ-----KRRAREKANLKNpqimyLEQELESLKAVLEIKNEKLhqqdiklmk 1163
Cdd:PRK02224   474 RErveELEAELEDLEEEVEEVEERLERAEDlveaeDRIERLEERRED-----LEELIAERRETIEEKRERA--------- 539
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386876319 1164 mEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLS 1224
Cdd:PRK02224   540 -EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA 599
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
999-1119 2.53e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 45.59  E-value: 2.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  999 EKTERENRLKEFYTREYEKLRdtyiEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEI----- 1073
Cdd:PRK00409   523 ASLEELERELEQKAEEAEALL----KEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELrqlqk 598
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1386876319 1074 KKGHEIEKKSLED---LLSEKQESLEKQINDLKSENDALNE----KLKSEEQK 1119
Cdd:PRK00409   599 GGYASVKAHELIEarkRLNKANEKKEKKKKKQKEKQEELKVgdevKYLSLGQK 651
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
993-1197 2.75e-04

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 43.86  E-value: 2.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  993 VQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKlEIEASHSEKLELLKKAYEASlSE 1072
Cdd:pfam00261    3 MQQIKEELDEAEERLKEA-MKKLEEAEKR-AEKAEAEVAALNRRIQLLEEELERTE-ERLAEALEKLEEAEKAADES-ER 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1073 IKKGheIEKKSLEDllSEKQESLEKQINDLKSENDALNEKLKSEEQK--------RRAREKANLKNPQIMYLEQEL---- 1140
Cdd:pfam00261   79 GRKV--LENRALKD--EEKMEILEAQLKEAKEIAEEADRKYEEVARKlvvvegdlERAEERAELAESKIVELEEELkvvg 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1141 ESLKAvLEIKNEKLHQQDIK-------------------------LMKMEKLVDnntALVDKLKRFQQENEELKARMDKH 1195
Cdd:pfam00261  155 NNLKS-LEASEEKASEREDKyeeqirflteklkeaetraefaersVQKLEKEVD---RLEDELEAEKEKYKAISEELDQT 230

                   ..
gi 1386876319 1196 MA 1197
Cdd:pfam00261  231 LA 232
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
980-1229 2.86e-04

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: 44.52  E-value: 2.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  980 KARNELQTVYEAfvQQHQAEKTERENRLKEfytreYEKLRDTYIEEAEKYKMQLQEQfdnlnaahetskleIEASHSEKL 1059
Cdd:pfam13868   32 KRIKAEEKEEER--RLDEMMEEERERALEE-----EEEKEEERKEERKRYRQELEEQ--------------IEEREQKRQ 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1060 EllkkAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINdLKSENDALNEKLKSEEQKRRAREK-ANLKNpqimyleq 1138
Cdd:pfam13868   91 E----EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQ-LREEIDEFNEEQAEWKELEKEEEReEDERI-------- 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1139 eLESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR--MDKHMAISRQLSTEQAvlqeslEKE 1216
Cdd:pfam13868  158 -LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKlyQEEQERKERQKEREEA------EKK 230
                          250
                   ....*....|...
gi 1386876319 1217 SKVNKRLSMENEE 1229
Cdd:pfam13868  231 ARQRQELQQAREE 243
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
904-1195 3.02e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 44.83  E-value: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  904 ELTQYKTKCENQSGFILQL--------KQLLAcGNTKFEALTVVIQHLLSEREEALKQHKTLSQElvnlrGELVTASttc 975
Cdd:PRK04778   127 ELQELLESEEKNREEVEQLkdlyrelrKSLLA-NRFSFGPALDELEKQLENLEEEFSQFVELTES-----GDYVEAR--- 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  976 EKLEKARNELQTVyeafvqQHQAEK-----TERENRLKEfytrEYEKLRDTYIE-EAEKYK---MQLQEQFDNLNAAHET 1046
Cdd:PRK04778   198 EILDQLEEELAAL------EQIMEEipellKELQTELPD----QLQELKAGYRElVEEGYHldhLDIEKEIQDLKEQIDE 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1047 -----SKLEIEAShSEKLELLKKA----YEASLSEIKKGHEIEKKS--LEDLLS-------------------------- 1089
Cdd:PRK04778   268 nlallEELDLDEA-EEKNEEIQERidqlYDILEREVKARKYVEKNSdtLPDFLEhakeqnkelkeeidrvkqsytlnese 346
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1090 -EKQESLEKQINDLKSENDALNEKLksEEQKRRAREkanlknpqimyLEQELESLKAVL-EIKNEklhQQDIK--LMKME 1165
Cdd:PRK04778   347 lESVRQLEKQLESLEKQYDEITERI--AEQEIAYSE-----------LQEELEEILKQLeEIEKE---QEKLSemLQGLR 410
                          330       340       350
                   ....*....|....*....|....*....|
gi 1386876319 1166 KlvDNNTALvDKLKRFQQENEELKARMDKH 1195
Cdd:PRK04778   411 K--DELEAR-EKLERYRNKLHEIKRYLEKS 437
fliH PRK06669
flagellar assembly protein H; Validated
1006-1149 4.21e-04

flagellar assembly protein H; Validated


Pssm-ID: 235850 [Multi-domain]  Cd Length: 281  Bit Score: 43.85  E-value: 4.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1006 RLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSE--KLELLKKAYEASLSEIKKGHEIEK-- 1081
Cdd:PRK06669    26 RFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEeaKEELLKKTDEASSIIEKLQMQIEReq 105
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876319 1082 -KSLEDLLSEKQESLEKQIND--LKSENDALNEKLKSEEQKRRAREKANLK-NPQIMYLEQELESLkaVLEI 1149
Cdd:PRK06669   106 eEWEEELERLIEEAKAEGYEEgyEKGREEGLEEVRELIEQLNKIIEKLIKKrEEILESSEEEIVEL--ALDI 175
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
900-1215 4.47e-04

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 44.29  E-value: 4.47e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  900 EKTLEltQYKTKCENQSGFILQLKQLLacgntkfEALTVVIQHLLSEREEALK------QHKTLSQELVNLRGELVTAST 973
Cdd:pfam05622  134 EATVE--TYKKKLEDLGDLRRQVKLLE-------ERNAEYMQRTLQLEEELKKanalrgQLETYKRQVQELHGKLSEESK 204
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  974 TCEKLEKARNELQTVYEAFVQqhqaektERENRLKEfytreyeklRDTYIEEAEKYK-MQLQEqfdnlnaAHETSKLEIE 1052
Cdd:pfam05622  205 KADKLEFEYKKLEEKLEALQK-------EKERLIIE---------RDTLRETNEELRcAQLQQ-------AELSQADALL 261
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1053 ASHSEKLELLkkAYEASLSEIKKghEIEKKSLED-LLSEKQE-SLEKQINDLKSENDalneklKSEEQKRRAREKANLKN 1130
Cdd:pfam05622  262 SPSSDPGDNL--AAEIMPAEIRE--KLIRLQHENkMLRLGQEgSYRERLTELQQLLE------DANRRKNELETQNRLAN 331
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1131 PQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKArmdkhmAISRQLSTEQAVLQ 1210
Cdd:pfam05622  332 QRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEP------KQDSNLAQKIDELQ 405

                   ....*
gi 1386876319 1211 ESLEK 1215
Cdd:pfam05622  406 EALRK 410
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
1023-1166 4.67e-04

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 44.43  E-value: 4.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1023 IEEAEKYKMQLQEQFDNLnaahetskleIEASHSEKLELLKKAYEASlsEIKKGHEIEKKSLEDLLSEKQESLEKQINDL 1102
Cdd:PRK00409   504 IEEAKKLIGEDKEKLNEL----------IASLEELERELEQKAEEAE--ALLKEAEKLKEELEEKKEKLQEEEDKLLEEA 571
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876319 1103 KSE-NDALNE-KLKSEEQKRRAREKANLKNPQIMylEQELESLKAVLEIKNEKLHQQDIKLMKMEK 1166
Cdd:PRK00409   572 EKEaQQAIKEaKKEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKEKQE 635
PTZ00121 PTZ00121
MAEBL; Provisional
944-1216 7.21e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 7.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  944 LSEREEALKQHKTLSQELVNLRGELVTAsttcEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTYI 1023
Cdd:PTZ00121  1527 AKKAEEAKKADEAKKAEEKKKADELKKA----EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1024 EEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLK 1103
Cdd:PTZ00121  1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE-EAKKAEEDKKKAEEAK 1681
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1104 SENDalNEKLKSEEQKRRAREKANLKNPQimylEQELESLKAVLEIKNEKlHQQDIKLMKMEKLVDNNTALVDKLKRFQQ 1183
Cdd:PTZ00121  1682 KAEE--DEKKAAEALKKEAEEAKKAEELK----KKEAEEKKKAEELKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1386876319 1184 ENEELKARMDKHMAISRQLSTE-QAVLQESLEKE 1216
Cdd:PTZ00121  1755 EKKKIAHLKKEEEKKAEEIRKEkEAVIEEELDEE 1788
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
980-1127 7.46e-04

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 41.84  E-value: 7.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  980 KARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYE----KLRDtyiEEAEKYKM--QLQEQFDNLNAAHETSKLEIEA 1053
Cdd:pfam08614   20 EAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllaQLRE---ELAELYRSrgELAQRLVDLNEELQELEKKLRE 96
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876319 1054 ShSEKLELLkkayEASLSEIkkghEIEKKSLEDLLSEKQesleKQINDLKSENDALNEKLKSEEQKRRAREKAN 1127
Cdd:pfam08614   97 D-ERRLAAL----EAERAQL----EEKLKDREEELREKR----KLNQDLQDELVALQLQLNMAEEKLRKLEKEN 157
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
1048-1166 7.68e-04

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 43.92  E-value: 7.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1048 KLEIEASHSEKLELlkkayEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE----EQKRRAR 1123
Cdd:COG0542    403 RMEIDSKPEELDEL-----ERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEkeliEEIQELK 477
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876319 1124 EKANLKNPQIMYLEQELESLKAVLEIKNEKLHQ----QDI---------------------KLMKMEK 1166
Cdd:COG0542    478 EELEQRYGKIPELEKELAELEEELAELAPLLREevteEDIaevvsrwtgipvgkllegereKLLNLEE 545
mukB PRK04863
chromosome partition protein MukB;
944-1230 8.51e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 43.79  E-value: 8.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  944 LSEREEALKQHKTLSQELVNLRGEL-VTASTTCEKLEKARNELQTVYEAF-VQQ------HQA----EKTERENRLKEFy 1011
Cdd:PRK04863   357 LEELEERLEEQNEVVEEADEQQEENeARAEAAEEEVDELKSQLADYQQALdVQQtraiqyQQAvqalERAKQLCGLPDL- 435
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1012 trEYEKLRDtYIEEaekYKMQLQEQFDNLNAAHEtsKLEIEASHSEKLEllkKAYEASLS-----EIKKGHEIEKKSLED 1086
Cdd:PRK04863   436 --TADNAED-WLEE---FQAKEQEATEELLSLEQ--KLSVAQAAHSQFE---QAYQLVRKiagevSRSEAWDVARELLRR 504
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1087 LlsEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQdiklmkMEK 1166
Cdd:PRK04863   505 L--REQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES------VSE 576
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876319 1167 LVDNNTALVDKLKRFQQENEELKAR----MDKHMAISR-------QLSTEQAV---LQESLEKEskvnKRLSMENEEL 1230
Cdd:PRK04863   577 ARERRMALRQQLEQLQARIQRLAARapawLAAQDALARlreqsgeEFEDSQDVteyMQQLLERE----RELTVERDEL 650
PTZ00121 PTZ00121
MAEBL; Provisional
976-1223 8.91e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 8.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  976 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKmQLQEQFDNLNAAHETSKLEIEASH 1055
Cdd:PTZ00121  1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK-AEEAKKAD-EAKKKAEEAKKAEEAKKKAEEAKK 1471
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1056 SEklELLKKAYEASLS-EIKKGHEIEKKSLEDLlsEKQESLEKQINDL-KSENDALNEKLKSEEQKRRARE--KA-NLKN 1130
Cdd:PTZ00121  1472 AD--EAKKKAEEAKKAdEAKKKAEEAKKKADEA--KKAAEAKKKADEAkKAEEAKKADEAKKAEEAKKADEakKAeEKKK 1547
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1131 PQIMYLEQELESLKAVLEIKNEKLHQQD--IKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHmaisrqlSTEQAV 1208
Cdd:PTZ00121  1548 ADELKKAEELKKAEEKKKAEEAKKAEEDknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-------AEEAKI 1620
                          250
                   ....*....|....*
gi 1386876319 1209 LQESLEKESKVNKRL 1223
Cdd:PTZ00121  1621 KAEELKKAEEEKKKV 1635
COG5022 COG5022
Myosin heavy chain [General function prediction only];
977-1230 9.32e-04

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 43.91  E-value: 9.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  977 KLEKARNELQTVYEAFVQQHQAEKTERENR---LKEFYTREYEKLRDTYIEEaeKYKMQLQEQFDNLNAAHETSKLEIEA 1053
Cdd:COG5022    814 SYLACIIKLQKTIKREKKLRETEEVEFSLKaevLIQKFGRSLKAKKRFSLLK--KETIYLQSAQRVELAERQLQELKIDV 891
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1054 SHSEKLELLKKAYEASLSEIKKgheiekkSLEDLLSEKqeslekqiNDLKSENDALNEKLKSEEQKRRAREKANLKNPQI 1133
Cdd:COG5022    892 KSISSLKLVNLELESEIIELKK-------SLSSDLIEN--------LEFKTELIARLKKLLNNIDLEEGPSIEYVKLPEL 956
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1134 MYLEQELESLKAVLEIKNEKLHQQDI-------KLMKMEKLVDNNTALVDKLKRFQQENEELKARMDK---HMAISRQLS 1203
Cdd:COG5022    957 NKLHEVESKLKETSEEYEDLLKKSTIlvregnkANSELKNFKKELAELSKQYGALQESTKQLKELPVEvaeLQSASKIIS 1036
                          250       260
                   ....*....|....*....|....*..
gi 1386876319 1204 TEQAVLQeSLEKESKVNKRLSMENEEL 1230
Cdd:COG5022   1037 SESTELS-ILKPLQKLKGLLLLENNQL 1062
PTZ00440 PTZ00440
reticulocyte binding protein 2-like protein; Provisional
955-1229 1.07e-03

reticulocyte binding protein 2-like protein; Provisional


Pssm-ID: 240419 [Multi-domain]  Cd Length: 2722  Bit Score: 43.67  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  955 KTLSQELVNLRGELVtasttcEKLEKARNELQTvyEAFVQQHqaEKTERENRLKEFYTREYEKLRDTYIEEaekYKMQLQ 1034
Cdd:PTZ00440   896 KQLVEHLLNNKIDLK------NKLEQHMKIINT--DNIIQKN--EKLNLLNNLNKEKEKIEKQLSDTKINN---LKMQIE 962
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1035 EQFDnlnaAHETSKLEIEA---SHSEKLELLKKAYEASLSEIKK---GHEIEKKSLEDLLSE-KQESLEKQINDLKSEND 1107
Cdd:PTZ00440   963 KTLE----YYDKSKENINGndgTHLEKLDKEKDEWEHFKSEIDKlnvNYNILNKKIDDLIKKqHDDIIELIDKLIKEKGK 1038
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1108 ALNEKLKSeeqkrrarekanlknpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE 1187
Cdd:PTZ00440  1039 EIEEKVDQ----------------YISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIE 1102
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1386876319 1188 LKARMDKHMAISRQLSTEQAVL----QESLEK-----ESKVNKRLSMENEE 1229
Cdd:PTZ00440  1103 IKNKSHEHVVNADKEKNKQTEHynkkKKSLEKiykqmEKTLKELENMNLED 1153
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
990-1215 1.09e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  990 EAFVQQHQAEKT---ERENRLKEFYtREYEKLRDTYIEEAEKYKM--QLQEQFDNLNAAHET-SKLEIEASH------SE 1057
Cdd:COG4913    210 DDFVREYMLEEPdtfEAADALVEHF-DDLERAHEALEDAREQIELlePIRELAERYAAARERlAELEYLRAAlrlwfaQR 288
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1058 KLELLKKAYEASLSEIKKgHEIEKKSLEDLLSEKQESLE-----------KQINDLKSENDALNEKLkseEQKRRAREKa 1126
Cdd:COG4913    289 RLELLEAELEELRAELAR-LEAELERLEARLDALREELDeleaqirgnggDRLEQLEREIERLEREL---EERERRRAR- 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1127 nlknpqimyLEQELESLKavLEIKNEKlhqqdiklmkmEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQ 1206
Cdd:COG4913    364 ---------LEALLAALG--LPLPASA-----------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
                          250
                   ....*....|..
gi 1386876319 1207 AVLQ---ESLEK 1215
Cdd:COG4913    422 RELEaeiASLER 433
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
903-1124 1.14e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  903 LELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELvtasttcEKLEKAR 982
Cdd:TIGR02169  329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-------EKLKREI 401
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  983 NELQtvyeafvqqhqaekterenrlkefytREYEKLRDTyieeaekyKMQLQEQFDNLNAAHETSKLEIEASHSEKLELL 1062
Cdd:TIGR02169  402 NELK--------------------------RELDRLQEE--------LQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876319 1063 K--KAYEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLKSENDALneklksEEQKRRARE 1124
Cdd:TIGR02169  448 LeiKKQEWKLEQLAADLSKYEQELYD-LKEEYDRVEKELSKLQRELAEA------EAQARASEE 504
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
940-1158 1.57e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  940 IQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVyEAFVQQHQAEKTERENRLKEFYtreyeklr 1019
Cdd:COG3883     18 IQAKQKELSELQAELEAAQAELDALQAELEELN---EEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERR-------- 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1020 dtyieeaEKYKMQLQEQFDNLNAaheTSKLE-IEASHS-----EKLELLKKAYEASLSEIKkgheiEKKSLEDLLSEKQE 1093
Cdd:COG3883     86 -------EELGERARALYRSGGS---VSYLDvLLGSESfsdflDRLSALSKIADADADLLE-----ELKADKAELEAKKA 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876319 1094 SLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQD 1158
Cdd:COG3883    151 ELEAKLAELEALKAELEAAKAElEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
916-1242 1.64e-03

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 1.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  916 SGFILQLKQLLACGNTKFEALTVVIQHL------LSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVY 989
Cdd:TIGR00618  204 QLLTLCTPCMPDTYHERKQVLEKELKHLrealqqTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  990 EAFVQQHQAEKterenrlkefYTREYEKLrdTYIE-EAEKYKMQLQEQFDNLNAA--HETSKLEIEASHSEKLELLKKAY 1066
Cdd:TIGR00618  284 ERINRARKAAP----------LAAHIKAV--TQIEqQAQRIHTELQSKMRSRAKLlmKRAAHVKQQSSIEEQRRLLQTLH 351
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1067 EASlSEIKKGHEIEKKSLEDllSEKQESLEKQINDLKSENDALNEKLKSEEQK----RRAREKANLKNPQIMYLEQELES 1142
Cdd:TIGR00618  352 SQE-IHIRDAHEVATSIREI--SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEldilQREQATIDTRTSAFRDLQGQLAH 428
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1143 LKAVLEIKNEKLHQQDIKLMK-MEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNK 1221
Cdd:TIGR00618  429 AKKQQELQQRYAELCAAAITCtAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCG 508
                          330       340
                   ....*....|....*....|.
gi 1386876319 1222 RLSMENEELLWKLHNGDLCSP 1242
Cdd:TIGR00618  509 SCIHPNPARQDIDNPGPLTRR 529
PRK01156 PRK01156
chromosome segregation protein; Provisional
904-1187 2.07e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 42.58  E-value: 2.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  904 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHllsereeALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 983
Cdd:PRK01156   191 KLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN-------AMDDYNNLKSALNELSSLEDMKNRYESEIKTAES 263
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  984 ELQTVYEAFVQQhqAEKTERENRL---KEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKleieashseKLE 1060
Cdd:PRK01156   264 DLSMELEKNNYY--KELEERHMKIindPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIK---------KLS 332
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1061 LLKKAYEAslseikkgHEIEKKSLEDLlsekqeslEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQI-MYLEQE 1139
Cdd:PRK01156   333 VLQKDYND--------YIKKKSRYDDL--------NNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsAFISEI 396
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1386876319 1140 LESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE 1187
Cdd:PRK01156   397 LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSR 444
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1047-1227 2.11e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1047 SKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLE---KQINDLKSENDALNEKLKS-EEQKRRA 1122
Cdd:COG4372      6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEqarEELEQLEEELEQARSELEQlEEELEEL 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1123 REKANLKNPQIMYLEQELESLKAvleiKNEKLHQQdiklmkMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQL 1202
Cdd:COG4372     86 NEQLQAAQAELAQAQEELESLQE----EAEELQEE------LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
                          170       180
                   ....*....|....*....|....*
gi 1386876319 1203 STEQAVLQESLEKESKVNKRLSMEN 1227
Cdd:COG4372    156 EEQLESLQEELAALEQELQALSEAE 180
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
940-1230 2.39e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.25  E-value: 2.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  940 IQHLLSEREEALKQHKT----LSQELVNLRG-----ELVTASTTCEKLEKARNELQTVYEA--FVQQHQaektereNRLk 1008
Cdd:COG3096    848 LERELAQHRAQEQQLRQqldqLKEQLQLLNKllpqaNLLADETLADRLEELREELDAAQEAqaFIQQHG-------KAL- 919
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1009 efytREYEKLRDTyieeaekykmqLQ---EQFDNLNAAHETSKleieashsEKLELLKKAYEAsLSEIKKgheiekkSLE 1085
Cdd:COG3096    920 ----AQLEPLVAV-----------LQsdpEQFEQLQADYLQAK--------EQQRRLKQQIFA-LSEVVQ-------RRP 968
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1086 DLLSEKQESLEKQINDLkseNDALNEKLKSEEQKR-RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM 1164
Cdd:COG3096    969 HFSYEDAVGLLGENSDL---NEKLRARLEQAEEARrEAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1165 EKLVDNNTAlvdklKRFQQENEELKARMDKHMAISRQLSTEQAVL---QESLEKE-SKVNKRLSMENEEL 1230
Cdd:COG3096   1046 GVQADAEAE-----ERARIRRDELHEELSQNRSRRSQLEKQLTRCeaeMDSLQKRlRKAERDYKQEREQV 1110
PspA_IM30 pfam04012
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ...
940-1145 2.51e-03

PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.


Pssm-ID: 461130 [Multi-domain]  Cd Length: 215  Bit Score: 40.82  E-value: 2.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  940 IQHLLSEREEALKQhktLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAfvQQHQAEKteRENRLKEFYTREYEKLR 1019
Cdd:pfam04012   13 IHEGLDKAEDPEKM---LEQAIRDMQSELVKARQALAQTIARQKQLERRLEQ--QTEQAKK--LEEKAQAALTKGNEELA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1020 DTYIEEAEKYKMQ---LQEQFDNLNAAHETSKLEIEASHS--EKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES 1094
Cdd:pfam04012   86 REALAEKKSLEKQaeaLETQLAQQRSAVEQLRKQLAALETkiQQLKAKKNLLKARLKAAKAQEAVQTSLGSLSTSSATDS 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876319 1095 LEK---QINDLKSENDALNE--KLKSEEQKRRArEKANLKNPqimylEQELESLKA 1145
Cdd:pfam04012  166 FERieeKIEEREARADAAAElaSAVDLDAKLEQ-AGIQMEVS-----EDVLARLKA 215
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
921-1065 2.99e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 2.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  921 QLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTC------EKLEKARNELQTVYEAfVQ 994
Cdd:COG4717    371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeleEELEELEEELEELEEE-LE 449
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876319  995 QHQAEKTERENRLKEFYT-REYEKLRDTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEASHSEKL-ELLKKA 1065
Cdd:COG4717    450 ELREELAELEAELEQLEEdGELAELLQELEELKAELR-ELAEEWAALKLALELLEEAREEYREERLpPVLERA 521
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
976-1156 3.78e-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: 41.06  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  976 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYE-KLRDTYIEEAEKYKMQLQEqfdnLNAAHETSKLEIEAS 1054
Cdd:pfam13868  176 EEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQErKERQKEREEAEKKARQRQE----LQQAREEQIELKERR 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1055 HSEKLELLKKAYEASLSEIKKGHEIEKKSLED---LLSEKQESLEKQINdlksendalneklksEEQKRRAREKANLKNP 1131
Cdd:pfam13868  252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKrrmKRLEHRRELEKQIE---------------EREEQRAAEREEELEE 316
                          170       180
                   ....*....|....*....|....*
gi 1386876319 1132 QIMYLEQELESLKAVLEIKNEKLHQ 1156
Cdd:pfam13868  317 GERLREEEAERRERIEEERQKKLKE 341
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
944-1156 3.98e-03

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


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.12  E-value: 3.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  944 LSEREEALKQHKTLSQELVNLRGELvtasttceklekarNELQTVYEAFVQQHQAEKTERENRLKEFyTREYEKLRDTYI 1023
Cdd:cd00176     32 LESVEALLKKHEALEAELAAHEERV--------------EALNELGEQLIEEGHPDAEEIQERLEEL-NQRWEELRELAE 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1024 EEAEKYK--MQLQEQFDNLnaahetskLEIEASHSEKlellkkayEASLSEIKKGHEIEkkSLEDLLsEKQESLEKQIND 1101
Cdd:cd00176     97 ERRQRLEeaLDLQQFFRDA--------DDLEQWLEEK--------EAALASEDLGKDLE--SVEELL-KKHKELEEELEA 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1386876319 1102 LKSENDALNEKLKSEEQKRRAREKANLKNPQIMyLEQELESLKAVLEIKNEKLHQ 1156
Cdd:cd00176    158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEE-LNERWEELLELAEERQKKLEE 211
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
978-1228 4.48e-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: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  978 LEKARNELQTVyeafVQQHQAEKTERENRLKEFYTR---EYEKLRdtyieeaekykmqlqeqfdnlNAAHETSKLEIEAS 1054
Cdd:TIGR01612  673 IDALYNELSSI----VKENAIDNTEDKAKLDDLKSKidkEYDKIQ---------------------NMETATVELHLSNI 727
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1055 HSEKLELLkkayeASLSEIKKG--HEIEK---KSLEDLLSeKQESLEKQINDLKSENDALNE-KLKSEEQKRRAREKANL 1128
Cdd:TIGR01612  728 ENKKNELL-----DIIVEIKKHihGEINKdlnKILEDFKN-KEKELSNKINDYAKEKDELNKyKSKISEIKNHYNDQINI 801
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1129 KNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE-LKARMDKHMAISRQLSTEqa 1207
Cdd:TIGR01612  802 DNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEkIDSEHEQFAELTNKIKAE-- 879
                          250       260
                   ....*....|....*....|..
gi 1386876319 1208 VLQESLEK-ESKVNKRLSMENE 1228
Cdd:TIGR01612  880 ISDDKLNDyEKKFNDSKSLINE 901
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
947-1218 4.48e-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: 41.10  E-value: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  947 REEALKQHKTLSQELVNLRGELVTA-STTCEKLE--KARNELQTVYEAFVQQHQA--EKTERENRLKEFYT------REY 1015
Cdd:COG5185    266 RLEKLGENAESSKRLNENANNLIKQfENTKEKIAeyTKSIDIKKATESLEEQLAAaeAEQELEESKRETETgiqnltAEI 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1016 EKLRDTYIEEAEKYKM------------QLQEQFDNLNAAHETSKLEIEASH---SEKLELLKKAYEASLSEIKKGHEIE 1080
Cdd:COG5185    346 EQGQESLTENLEAIKEeienivgevelsKSSEELDSFKDTIESTKESLDEIPqnqRGYAQEILATLEDTLKAADRQIEEL 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1081 KKSLEDLLSEKQES------LEKQINDLKSENDALNEKLKSEEQK---RRAREKANLKNPQIMYLEQELESLKAVLEIKN 1151
Cdd:COG5185    426 QRQIEQATSSNEEVskllneLISELNKVMREADEESQSRLEEAYDeinRSVRSKKEDLNEELTQIESRVSTLKATLEKLR 505
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876319 1152 EKLHQQdikLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESK 1218
Cdd:COG5185    506 AKLERQ---LEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAV 569
DUF4200 pfam13863
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ...
1058-1166 4.48e-03

Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.


Pssm-ID: 464003 [Multi-domain]  Cd Length: 119  Bit Score: 38.32  E-value: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1058 KLELLKKAYEASLSEIKKgheiekksLEDLLSEKQESLEKQINDLKSENDALNEKLK-SEEQKRRAREKANLKNPQIMYL 1136
Cdd:pfam13863    7 EMFLVQLALDAKREEIER--------LEELLKQREEELEKKEQELKEDLIKFDKFLKeNDAKRRRALKKAEEETKLKKEK 78
                           90       100       110
                   ....*....|....*....|....*....|
gi 1386876319 1137 EQELESLKAVLEIKNEKLHQQDIKLMKMEK 1166
Cdd:pfam13863   79 EKEIKKLTAQIEELKSEISKLEEKLEEYKP 108
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
959-1218 4.66e-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: 41.28  E-value: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  959 QELVNLRGELVTASTTCEKlEKARNELQTV-YEAFVQQHQAEKTERENRLKEFYTREY--EKLRDTYIEEAEKYKMQLQE 1035
Cdd:pfam07111   73 QELRRLEEEVRLLRETSLQ-QKMRLEAQAMeLDALAVAEKAGQAEAEGLRAALAGAEMvrKNLEEGSQRELEEIQRLHQE 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1036 QFDNLNAAHETSkLEIEASHSEKLELLKKAYEASLS-EIKKGHEIEKKS--LEDLLSEKQESLEKQINDLKSENDALNEK 1112
Cdd:pfam07111  152 QLSSLTQAHEEA-LSSLTSKAEGLEKSLNSLETKRAgEAKQLAEAQKEAelLRKQLSKTQEELEAQVTLVESLRKYVGEQ 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1113 LKSE------EQKRRA---------REKANLKnPQIMYLEQELESLKAVLEIKNEKLHQqdiKLMKMEKLVDNNTALVDK 1177
Cdd:pfam07111  231 VPPEvhsqtwELERQElldtmqhlqEDRADLQ-ATVELLQVRVQSLTHMLALQEEELTR---KIQPSDSLEPEFPKKCRS 306
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1386876319 1178 LKRFQQENE-----ELKARMDKHMAISRQLSTEQAVLQESLEKESK 1218
Cdd:pfam07111  307 LLNRWREKVfalmvQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQ 352
Ctf13_LRR_LRR-insertion cd19611
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein ...
1069-1156 4.85e-03

leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein complex CBF3 subunit C (Ctf13); Ctf13, is an F-box protein of the leucine-rich-repeat superfamily; it is a component of CEN binding factor 3 (CBF3), a complex that recognizes point centromeres found in budding yeast, associating specifically with the third centromere DNA element (CDEIII) DNA. CBF3 is comprised of two homodimers of Cep3 and Ndc10, and a Ctf13-Skp1 heterodimer. The Skp1-Ctf13 heterodimer interacts with Cep3, Ndc10 and CDEIII at a completely conserved G, centrally positioned between the TGC/CCG sites. The eight leucine-rich repeat (LRR) motifs of Ctf13 (LRR 1-8) form a solenoid structure. At the N-terminus of the Ctf13 LRR is an expanded F-box, and at the C-terminal end, an alpha-beta domain formed by insertions within the latter LRRs of Ctf13 (LRR insertion domain). This domain model includes the LLR domain and the LRR insertion domain.


Pssm-ID: 381623  Cd Length: 290  Bit Score: 40.40  E-value: 4.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1069 SLSEIKK-GHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK--A 1145
Cdd:cd19611     14 NPNMVKKiLKVLEKKELLDLVSEVFFGQDEEESDEEDEDDSSKNDRKKLTDDDVKEKSYKLNDPSIIRIISSLESMKnlR 93
                           90
                   ....*....|.
gi 1386876319 1146 VLEIKNEKLHQ 1156
Cdd:cd19611     94 KLSVRGDNLYE 104
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
1062-1203 5.00e-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: 5.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1062 LKKAYEASLSEIKKGHEIEKKSLEDllSEKQESLEKQINDLksendaLNEKLKSEEQkrrarekanlkNPQIMYLEQELE 1141
Cdd:TIGR01612  546 LKESYELAKNWKKLIHEIKKELEEE--NEDSIHLEKEIKDL------FDKYLEIDDE-----------IIYINKLKLELK 606
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876319 1142 SLKAVLEIKNEKLHqqdiKLMKMEKLVDNNTALVDKLKRFQ--QENEELKARMDKHMAISRQLS 1203
Cdd:TIGR01612  607 EKIKNISDKNEYIK----KAIDLKKIIENNNAYIDELAKISpyQVPEHLKNKDKIYSTIKSELS 666
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
931-1126 5.01e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.97  E-value: 5.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  931 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeAFVQQHQAEKTERENRLKEF 1010
Cdd:COG3883     16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ----AEIAEAEAEIEERREELGER 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1011 YTREYEKLRD-TYIE---EAEKYKmQLQEQFDNLNAAHETSKLEIEASHSEKLELlkKAYEASLSEIKKGHEIEKKSLED 1086
Cdd:COG3883     92 ARALYRSGGSvSYLDvllGSESFS-DFLDRLSALSKIADADADLLEELKADKAEL--EAKKAELEAKLAELEALKAELEA 168
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1386876319 1087 LLSE---KQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1126
Cdd:COG3883    169 AKAEleaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
936-1223 5.87e-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: 40.88  E-value: 5.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  936 LTVVIQHLLSEREEalkqhkTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTEREnRLKEFYTREY 1015
Cdd:pfam05557  273 LNLRSPEDLSRRIE------QLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLK-RHKALVRRLQ 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1016 EKLRdTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEasHSEKLELLKKAYEASLSEIKkgHEIEKkSLEDLLSEKQ--E 1093
Cdd:pfam05557  346 RRVL-LLTKERDGYR-AILESYDKELTMSNYSPQLLE--RIEEAEDMTQKMQAHNEEME--AQLSV-AEEELGGYKQqaQ 418
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1094 SLEKQINDLKSENDaLNEKLKSEEQKRRARekanLKNPQIMYLEQELESLKAVLEIKNEKLHQQ---DIKLMKMEKLVDN 1170
Cdd:pfam05557  419 TLERELQALRQQES-LADPSYSKEEVDSLR----RKLETLELERQRLREQKNELEMELERRCLQgdyDPKKTKVLHLSMN 493
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386876319 1171 NTALV-----DKLKRFQQENEELKARMDKHMAISRQLST-----------EQAVLQESLEKESKVNKRL 1223
Cdd:pfam05557  494 PAAEAyqqrkNQLEKLQAEIERLKRLLKKLEDDLEQVLRlpettstmnfkEVLDLRKELESAELKNQRL 562
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
940-1223 6.13e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 40.18  E-value: 6.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  940 IQHLLSEREEALKQHKTLSQELVNLRGELVTA-------STTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLkefYT 1012
Cdd:pfam15905   82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAvrektslSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSS---LS 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1013 REYEKLRDTyIEEAEKYKMQLQEqfdnlnaahetsKLEIeashseKLELLKKAYEASLSEIKKgheiekksledlLSEKQ 1092
Cdd:pfam15905  159 MELMKLRNK-LEAKMKEVMAKQE------------GMEG------KLQVTQKNLEHSKGKVAQ------------LEEKL 207
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1093 ESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpqIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKlvdnnt 1172
Cdd:pfam15905  208 VSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLD---IAQLEELLKEKNDEIESLKQSLEEKEQELSKQIK------ 278
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1386876319 1173 ALVDKLKRFQQENEELKARmdkHMAISRQLSTEQAVLQESLEKESKVNKRL 1223
Cdd:pfam15905  279 DLNEKCKLLESEKEELLRE---YEEKEQTLNAELEELKEKLTLEEQEHQKL 326
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
978-1188 6.14e-03

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 39.66  E-value: 6.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  978 LEKARNELQTV-YEAFVQQHQAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLnaahetsKLEIEASHS 1056
Cdd:pfam05010   10 LEKARNEIEEKeLEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKV-------LEEKDQALA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1057 EKLELlkkayEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLKsendalnEKLKSEEQ-----KRRAREKANLKNP 1131
Cdd:pfam05010   83 DLNSV-----EKSFSDLFKRYEKQKEVISG-YKKNEESLKKCAQDYL-------ARIKKEEQryqalKAHAEEKLDQANE 149
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876319 1132 QIMYLEQELESLKAVLEIkneKLHQQDIKLMKMEKLVDNNTalvdklkrfqQENEEL 1188
Cdd:pfam05010  150 EIAQVRSKAKAETAALQA---SLRKEQMKVQSLERQLEQKT----------KENEEL 193
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
994-1139 6.97e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 40.71  E-value: 6.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  994 QQHQAEKTERENRLKEFYTREYEK------LRDTYIE------EAEKYKMQLQEQfdnlnAAHETSKLEIEASHSEKLEL 1061
Cdd:pfam15709  361 RRLQQEQLERAEKMREELELEQQRrfeeirLRKQRLEeerqrqEEEERKQRLQLQ-----AAQERARQQQEEFRRKLQEL 435
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1062 LKKAYEASLsEIKKGHEIEKKSLEDLLSEKQ---------ESLEKQINDLKSENDAlneKLKSEEQKRRAREKANLKNPQ 1132
Cdd:pfam15709  436 QRKKQQEEA-ERAEAEKQRQKELEMQLAEEQkrlmemaeeERLEYQRQKQEAEEKA---RLEAEERRQKEEEAARLALEE 511

                   ....*..
gi 1386876319 1133 IMYLEQE 1139
Cdd:pfam15709  512 AMKQAQE 518
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
931-1234 7.44e-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: 40.54  E-value: 7.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  931 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvQQHQAEKTERENRLKEF 1010
Cdd:pfam01576  636 TRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALE-------QQVEEMKTQLEELEDEL 708
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1011 YTREYEKLR----------------DTYIEEAEKYKMQLQEQFDNLNAAHETSKLE--IEASHSEKLELLKKAYEASLSE 1072
Cdd:pfam01576  709 QATEDAKLRlevnmqalkaqferdlQARDEQGEEKRRQLVKQVRELEAELEDERKQraQAVAAKKKLELDLKELEAQIDA 788
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1073 IKKGHEIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQEL---ESLKAVLEI 1149
Cdd:pfam01576  789 ANKGREEAVKQLKKLQAQMKD-LQRELEEARASRDEILAQSKESEKKLKNLEA------ELLQLQEDLaasERARRQAQQ 861
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1150 KNEKLhQQDIK--LMKMEKLVDNNTALVDKLKRFQQENEE-------LKARMDKHMAISRQLSTEQAVLQESLEKESKVN 1220
Cdd:pfam01576  862 ERDEL-ADEIAsgASGKSALQDEKRRLEARIAQLEEELEEeqsntelLNDRLRKSTLQVEQLTTELAAERSTSQKSESAR 940
                          330
                   ....*....|....
gi 1386876319 1221 KRLSMENEELLWKL 1234
Cdd:pfam01576  941 QQLERQNKELKAKL 954
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
1057-1171 7.48e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 40.00  E-value: 7.48e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319  1057 EKLELLKKAYEaslsEIKKgHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQkrRAREKANLKNPQIMY- 1135
Cdd:smart00787  151 ENLEGLKEDYK----LLMK-ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD--RAKEKLKKLLQEIMIk 223
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|..
gi 1386876319  1136 ------LEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNN 1171
Cdd:smart00787  224 vkkleeLEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQC 265
PRK14160 PRK14160
heat shock protein GrpE; Provisional
1080-1194 7.81e-03

heat shock protein GrpE; Provisional


Pssm-ID: 237629 [Multi-domain]  Cd Length: 211  Bit Score: 39.35  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876319 1080 EKKSLEDLLSEKQESLEKQiNDLKSENDALNEKLKSEEQKrrAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQdi 1159
Cdd:PRK14160     2 EKECKDAKHENMEEDCCKE-NENKEEDKGKEEDLEFEEIE--KEEIIEDSEESNEVKIEELKDENNKLKEENKKLENE-- 76
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1386876319 1160 klmkMEklvdnntALVDKLKRFQQENEELKARMDK 1194
Cdd:PRK14160    77 ----LE-------ALKDRLLRTVAEYDNYRKRTAK 100
 
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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