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Conserved domains on  [gi|385198093|ref|NP_001245227|]
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shootin-1 isoform c [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 ...
 80-290 4.04e-09

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 4.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093    80 CQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEkcnrvsmlavEEYEEMQV 159
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   160 NLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIpdqqLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETL 239
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 385198093   240 HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 200-455 5.47e-03

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 200 QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLenETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKhsvD 279
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRI--AALARRIRALEQELAALEAELAELEKEIAELRAELEAQK---E 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 280 ELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMirkrshpsgsgakkeKATQPETTEEVTDLKRQAVEemMDRIKK 359
Cdd:COG4942  105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL---------------KYLAPARREQAEELRADLAE--LAALRA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 360 GVHLRPVNQTARPKTKPESSKGCESAVDELKGILGTLNKSTSSRSLKSLDPENSETELERILRR-RKVTAEADSSSPTGI 438
Cdd:COG4942  168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARlEAEAAAAAERTPAAG 247

                        250
                 ....*....|....*...
gi 385198093 439 LATSESK-SMPVLGSVSS 455
Cdd:COG4942  248 FAALKGKlPWPVSGRVVR 265
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 80-290 4.04e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 4.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093    80 CQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEkcnrvsmlavEEYEEMQV 159
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   160 NLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIpdqqLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETL 239
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 385198093   240 HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 81-290 1.35e-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: 54.00  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVN 160
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 161 LELEKDLRKKAESFAQEMFieqNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENE--T 238
Cdd:COG4942  113 LYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraA 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385198093 239 LHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:COG4942  190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
PRK12704 PRK12704
phosphodiesterase; Provisional
 165-284 3.49e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 165 KDLRKKAESFAQEMFIEQNKLKRQshlllqssipdqQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEN--ETLHKE 242
Cdd:PRK12704  34 KEAEEEAKRILEEAKKEAEAIKKE------------ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkeENLDRK 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 385198093 243 IHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKR 284
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 156-289 3.84e-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: 43.63  E-value: 3.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   156 EMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQ-----------QLLKALDENAKL-TQQLEEERIQH 223
Cdd:pfam01576  275 ELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQelrskreqevtELKKALEEETRShEAQLQEMRQKH 354

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385198093   224 QQKVKELEEQLEN-----ETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 289
Cdd:pfam01576  355 TQALEELTEQLEQakrnkANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESE 425
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 200-455 5.47e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 200 QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLenETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKhsvD 279
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRI--AALARRIRALEQELAALEAELAELEKEIAELRAELEAQK---E 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 280 ELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMirkrshpsgsgakkeKATQPETTEEVTDLKRQAVEemMDRIKK 359
Cdd:COG4942  105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL---------------KYLAPARREQAEELRADLAE--LAALRA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 360 GVHLRPVNQTARPKTKPESSKGCESAVDELKGILGTLNKSTSSRSLKSLDPENSETELERILRR-RKVTAEADSSSPTGI 438
Cdd:COG4942  168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARlEAEAAAAAERTPAAG 247

                        250
                 ....*....|....*...
gi 385198093 439 LATSESK-SMPVLGSVSS 455
Cdd:COG4942  248 FAALKGKlPWPVSGRVVR 265
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 80-290 4.04e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 59.69  E-value: 4.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093    80 CQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEkcnrvsmlavEEYEEMQV 159
Cdd:TIGR02168  300 LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----------ELEAELEE 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   160 NLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIpdqqLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETL 239
Cdd:TIGR02168  370 LESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA----RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEL 445

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 385198093   240 HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:TIGR02168  446 EEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 80-289 4.30e-08

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: 56.23  E-value: 4.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093    80 CQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKC-----NRVSMLAVEEY 154
Cdd:TIGR02169  714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLeealnDLEARLSHSRI 793

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   155 EEMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQ-----------LEEERIQH 223
Cdd:TIGR02169  794 PEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKeienlngkkeeLEEELEEL 873

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 385198093   224 QQKVKELEEQLENetLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 289
Cdd:TIGR02169  874 EAALRDLESRLGD--LKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 81-290 1.35e-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: 54.00  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVN 160
Cdd:COG4942   33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 161 LELEKDLRKKAESFAQEMFieqNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENE--T 238
Cdd:COG4942  113 LYRLGRQPPLALLLSPEDF---LDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEEraA 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385198093 239 LHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:COG4942  190 LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 70-289 5.26e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 5.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093    70 GAAETCVSVQCQKQ-IKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRvsm 148
Cdd:TIGR02168  664 GSAKTNSSILERRReIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA--- 740

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   149 lAVEEYEEMQVNLELE-KDLRKKAESFAQEMFIEQNKLKRQSHLLLQSsipDQQLLKALDENAKLTQQLEEERIQHQ--- 224
Cdd:TIGR02168  741 -EVEQLEERIAQLSKElTELEAEIEELEERLEEAEEELAEAEAEIEEL---EAQIEQLKEELKALREALDELRAELTlln 816

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   225 ---QKVKELEEQLENET--LHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 289
Cdd:TIGR02168  817 eeaANLRERLESLERRIaaTERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLE 886
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-292 5.82e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 5.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKcnrvsmLAVEEYEEMQVN 160
Cdd:COG1196  273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEE------LEEELEELEEEL 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 161 LELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQL-ENETL 239
Cdd:COG1196  347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEeELEEL 426

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 385198093 240 HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSV 292
Cdd:COG1196  427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAAL 479
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-290 6.18e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 6.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLE-KCNRVSMLAVEEYEEMQV 159
Cdd:COG1196  245 EAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArLEERRRELEERLEELEEE 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 160 NLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENET- 238
Cdd:COG1196  325 LAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEe 404

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385198093 239 LHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:COG1196  405 LEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-356 1.59e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVN 160
Cdd:COG1196  224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 161 LELEKDLRKKAESFAQEMfIEQNKLKRQSHLLLQSSIpdQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEN---- 236
Cdd:COG1196  304 IARLEERRRELEERLEEL-EEELAELEEELEELEEEL--EELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEaeee 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 237 -ETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMS 315
Cdd:COG1196  381 lEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 385198093 316 MIRKRSHPSGSGAKKEKATQPETTEEVTDLKRQAVEEMMDR 356
Cdd:COG1196  461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-265 1.62e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.09  E-value: 1.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRvsmLAVEEYEEMQVN 160
Cdd:COG1196  322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE---ELLEALRAAAEL 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 161 LELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEN---- 236
Cdd:COG1196  399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALleaa 478

                        170       180       190
                 ....*....|....*....|....*....|
gi 385198093 237 -ETLHKEIHNLKQQLELLEEDKKELELKYQ 265
Cdd:COG1196  479 lAELLEELAEAAARLLLLLEAEADYEGFLE 508
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 14-290 3.18e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 3.18e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093    14 EIEK--TCRESAEALATKLNKENKTLkRISMLYMAKLGPDVITEEINIDDEDSTTDTDGAAETCVSVQCQKQIKELRDQI 91
Cdd:TIGR02168  678 EIEEleEKIEELEEKIAELEKALAEL-RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093    92 VSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEkcnrvsmlaveeyeemqvnlELEKDLRKKA 171
Cdd:TIGR02168  757 TELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD--------------------ELRAELTLLN 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   172 ESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEEriqhQQKVKELEEQLENETlhKEIHNLKQQLE 251
Cdd:TIGR02168  817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL----EELIEELESELEALL--NERASLEEALA 890

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 385198093   252 LLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSEN 290
Cdd:TIGR02168  891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLEL 929
PRK12704 PRK12704
phosphodiesterase; Provisional
 165-284 3.49e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 165 KDLRKKAESFAQEMFIEQNKLKRQshlllqssipdqQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEN--ETLHKE 242
Cdd:PRK12704  34 KEAEEEAKRILEEAKKEAEAIKKE------------ALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQkeENLDRK 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 385198093 243 IHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKR 284
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQE 143
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 79-289 2.12e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 47.13  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  79 QCQKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCN-RVSMLAVEEYEEM 157
Cdd:COG3883   20 AKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERReELGERARALYRSG 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 158 QVNLELEKDLrkKAESFAQemFIEQnklkrqshLLLQSSIPDQQlLKALDENAKLTQQLEEERIQHQQKVKELEEQLenE 237
Cdd:COG3883  100 GSVSYLDVLL--GSESFSD--FLDR--------LSALSKIADAD-ADLLEELKADKAELEAKKAELEAKLAELEALK--A 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 385198093 238 TLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 289
Cdd:COG3883  165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 82-353 7.79e-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: 45.82  E-value: 7.79e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093    82 KQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLE-QRKVLEKCNRVSmlaveeyeemqvn 160
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElQKELYALANEIS------------- 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   161 lELEKDLRKKAESFAQemfIEQNKLKRQSHLllqssipdQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENetLH 240
Cdd:TIGR02168  299 -RLEQQKQILRERLAN---LERQLEELEAQL--------EELESKLDELAEELAELEEKLEELKEELESLEAELEE--LE 364

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   241 KEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMIRKR 320
Cdd:TIGR02168  365 AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444

                          250       260       270
                   ....*....|....*....|....*....|...
gi 385198093   321 SHPSGSGAKKEKATQPETTEEVTDLKRQAVEEM 353
Cdd:TIGR02168  445 LEEELEELQEELERLEEALEELREELEEAEQAL 477
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
132-280 8.77e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 8.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  132 EVLEQRKVLEKCNRvsmlAVEEYEEMQVNLELEKDLRKKAESFAQEMFIEqnklkrqshlLLQSSIpdQQLLKALDENAK 211
Cdd:COG4913   246 DAREQIELLEPIRE----LAERYAAARERLAELEYLRAALRLWFAQRRLE----------LLEAEL--EELRAELARLEA 309

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 385198093  212 LTQQLEEERIQHQQKVKELEEQLENETLhKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDE 280
Cdd:COG4913   310 ELERLEARLDALREELDELEAQIRGNGG-DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPA 377
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
151-349 9.03e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 9.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 151 VEEYeeMQVNLELEKDLRKKAESFAQEMFIE--------QNKLK--RQSHLLLQSSIPDQQLLKALDENAKLTQQLEEER 220
Cdd:COG3206  158 AEAY--LEQNLELRREEARKALEFLEEQLPElrkeleeaEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAEL 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 221 IQHQQKVKELEEQLENETL-------HKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVP 293
Cdd:COG3206  236 AEAEARLAALRAQLGSGPDalpellqSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 385198093 294 PPPPPPPPLPPPPPNPIRSLMSMIRKRShpsgsgakkekATQPETTEEVTDLKRQA 349
Cdd:COG3206  316 ASLEAELEALQAREASLQAQLAQLEARL-----------AELPELEAELRRLEREV 360
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
79-251 1.04e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  79 QCQKQIKELRDQ---IVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKtvlnsEVLEQRKVLEKCNRVSMLAVEEYE 155
Cdd:COG4717   75 ELEEELKEAEEKeeeYAELQEELEELEEELEELEAELEELREELEKLEKLL-----QLLPLYQELEALEAELAELPERLE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 156 EMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPD-QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQL 234
Cdd:COG4717  150 ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229

                        170
                 ....*....|....*..
gi 385198093 235 ENETLHKEIHNLKQQLE 251
Cdd:COG4717  230 EQLENELEAAALEERLK 246
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
131-289 1.36e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.91  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  131 SEVLEQRKVLEKCNRVSMLaVEEYEEMQVNLELEKD-------LRKKAESFaQEMFIEQNKLKRQSHLL--LQSSIPDQQ 201
Cdd:COG4913   215 EYMLEEPDTFEAADALVEH-FDDLERAHEALEDAREqiellepIRELAERY-AAARERLAELEYLRAALrlWFAQRRLEL 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  202 LLKALDENAKLTQQLEEERIQHQQKVKELEEQLENetLHKEIHNLK-QQLELLEEDKKELELKYQNSEEKARNLKHSVDE 280
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEARLDALREELDE--LEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAA 370


                  ....*....
gi 385198093  281 LQKRVNQSE 289
Cdd:COG4913   371 LGLPLPASA 379
PLN02939 PLN02939
transferase, transferring glycosyl groups
 94-281 1.51e-04

transferase, transferring glycosyl groups


Pssm-ID: 215507 [Multi-domain]  Cd Length: 977  Bit Score: 44.89  E-value: 1.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  94 VQEEKKILAIELENLKSKLVEVI---EEVNKVKQEKTVLNSEV--LEQRKVL--EKCNRVSMLAVEEYEEMQVNLELEKD 166
Cdd:PLN02939 231 LKEENMLLKDDIQFLKAELIEVAeteERVFKLEKERSLLDASLreLESKFIVaqEDVSKLSPLQYDCWWEKVENLQDLLD 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 167 -LRKKAESFAqeMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTqqleeeriqhQQKVKELEEQLENEtlHKEIHN 245
Cdd:PLN02939 311 rATNQVEKAA--LVLDQNQDLRDKVDKLEASLKEANVSKFSSYKVELL----------QQKLKLLEERLQAS--DHEIHS 376

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 385198093 246 lkqQLELLEEDKKELE--LKYQNSEEKARNLKHSVDEL 281
Cdd:PLN02939 377 ---YIQLYQESIKEFQdtLSKLKEESKKRSLEHPADDM 411
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 156-289 3.84e-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: 43.63  E-value: 3.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   156 EMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQ-----------QLLKALDENAKL-TQQLEEERIQH 223
Cdd:pfam01576  275 ELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQelrskreqevtELKKALEEETRShEAQLQEMRQKH 354

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 385198093   224 QQKVKELEEQLEN-----ETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 289
Cdd:pfam01576  355 TQALEELTEQLEQakrnkANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESE 425
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
150-263 6.20e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 42.34  E-value: 6.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 150 AVEEYEEMQVNLELEKDLRKKAESFAQ---EMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQK 226
Cdd:COG1566   95 AEAQLARLEAELGAEAEIAAAEAQLAAaqaQLDLAQRELERYQALYKKGAVSQQELDEARAALDAAQAQLEAAQAQLAQA 174

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 385198093 227 VKELEEQLENETLHKEIHNLKQQLELLEEDKKELELK 263
Cdd:COG1566  175 QAGLREEEELAAAQAQVAQAEAALAQAELNLARTTIR 211
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
200-283 6.55e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 6.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 200 QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVD 279
Cdd:COG4717   91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEA 170


                 ....
gi 385198093 280 ELQK 283
Cdd:COG4717  171 ELAE 174
PRK12704 PRK12704
phosphodiesterase; Provisional
 98-272 1.23e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  98 KKILAIELENLKSKLVEVIEEVNKvkqektvlNSEVLEQRKVLEkcnrvsmlAVEEYEEMQvnLELEKDLR-KKAESFAQ 176
Cdd:PRK12704  26 KKIAEAKIKEAEEEAKRILEEAKK--------EAEAIKKEALLE--------AKEEIHKLR--NEFEKELReRRNELQKL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 177 EMFIEQNK--LKRQSHLLLQSsipDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLEnetlhkEIHNL-----KQQ 249
Cdd:PRK12704  88 EKRLLQKEenLDRKLELLEKR---EEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE------RISGLtaeeaKEI 158

                        170       180
                 ....*....|....*....|....*
gi 385198093 250 L--ELLEEDKKELELKYQNSEEKAR 272
Cdd:PRK12704 159 LleKVEEEARHEAAVLIKEIEEEAK 183
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 82-235 1.95e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  82 KQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKcNRVSMLAV---EEYEEMQ 158
Cdd:COG1579   17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVrnnKEYEALQ 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 385198093 159 VNLELEKDLRKKAESFAQEMFIEQNKLKrqshlllqssipdQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLE 235
Cdd:COG1579   96 KEIESLKRRISDLEDEILELMERIEELE-------------EELAELEAELAELEAELEEKKAELDEELAELEAELE 159
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-249 3.02e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVK-QEKTVLNSEVLEQRKVLEKCNRvsmlAVEEYEEMQV 159
Cdd:COG4913   294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERER----RRARLEALLA 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  160 NLELEKDLrkKAESFAqemfieqnKLKRQShlllqssipdQQLLKALDEnakLTQQLEEERIQHQQKVKELEEQLenETL 239
Cdd:COG4913   370 ALGLPLPA--SAEEFA--------ALRAEA----------AALLEALEE---ELEALEEALAEAEAALRDLRREL--REL 424

                         170
                  ....*....|
gi 385198093  240 HKEIHNLKQQ 249
Cdd:COG4913   425 EAEIASLERR 434
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 82-362 4.32e-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: 40.05  E-value: 4.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093    82 KQIKELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEvlEQRKVLEKCNRVSMlaveEYEEMQVNL 161
Cdd:TIGR02169  237 RQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE--EQLRVKEKIGELEA----EIASLERSI 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   162 ELEKDLRKKAESFAQEMFIEQNKLKRQsHLLLQSSIPDQQLLKAL---------DENAKLTQQLEEERIQHQ---QKVKE 229
Cdd:TIGR02169  311 AEKERELEDAEERLAKLEAEIDKLLAE-IEELEREIEEERKRRDKlteeyaelkEELEDLRAELEEVDKEFAetrDELKD 389

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   230 LEEQLEN-----ETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVpPPPPPPPPLPP 304
Cdd:TIGR02169  390 YREKLEKlkreiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL-EQLAADLSKYE 468

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 385198093   305 PPPNPIRSLMSMIRKRSHPSGSGAKKEKATQPETTEEVTDlkRQAVEEMMDRIKKGVH 362
Cdd:TIGR02169  469 QELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG--GRAVEEVLKASIQGVH 524
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-292 4.55e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 4.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   81 QKQIKELRDQIVSVQEEKKILAIELENLKSKLvevieevnkvkqektvlnsEVLEQRKVLEKcnrvsmlAVEEYEEMQVN 160
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAEL-------------------DALQERREALQ-------RLAEYSWDEID 662

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  161 L-ELEKDLRKKaesfaqemfieQNKLKRqshllLQSSIPD-QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENet 238
Cdd:COG4913   663 VaSAEREIAEL-----------EAELER-----LDASSDDlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ-- 724

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 385198093  239 LHKEIHNLKQQLELLEEDKKEL-----------ELKYQNSEEKARNLKHSVDELQKRVNQSENSV 292
Cdd:COG4913   725 AEEELDELQDRLEAAEDLARLElralleerfaaALGDAVERELRENLEERIDALRARLNRAEEEL 789
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
100-287 4.82e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 100 ILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVNLeleKDLRKKAESFAQEMF 179
Cdd:COG4717  288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL---QELLREAEELEEELQ 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 180 IEQNKLKRQSHLLLQSSIPDQQLLKALDEnakltqqlEEERIQHQQKVKELEEQLEN--------------ETLHKEIHN 245
Cdd:COG4717  365 LEELEQEIAALLAEAGVEDEEELRAALEQ--------AEEYQELKEELEELEEQLEEllgeleellealdeEELEEELEE 436

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 385198093 246 LKQQLELLEEDKKEL---------ELKYQNSEEKARNLKHSVDELQKRVNQ 287
Cdd:COG4717  437 LEEELEELEEELEELreelaeleaELEQLEEDGELAELLQELEELKAELRE 487
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 200-455 5.47e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 200 QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLenETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKhsvD 279
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRI--AALARRIRALEQELAALEAELAELEKEIAELRAELEAQK---E 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 280 ELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLMSMirkrshpsgsgakkeKATQPETTEEVTDLKRQAVEemMDRIKK 359
Cdd:COG4942  105 ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL---------------KYLAPARREQAEELRADLAE--LAALRA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 360 GVHLRPVNQTARPKTKPESSKGCESAVDELKGILGTLNKSTSSRSLKSLDPENSETELERILRR-RKVTAEADSSSPTGI 438
Cdd:COG4942  168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARlEAEAAAAAERTPAAG 247

                        250
                 ....*....|....*...
gi 385198093 439 LATSESK-SMPVLGSVSS 455
Cdd:COG4942  248 FAALKGKlPWPVSGRVVR 265
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 152-349 6.10e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 6.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 152 EEYEEMQVNLELEKDLRKKAESFAQEMFIEQNKLKRQSHL----LLQSSIpDQQLLKALDENAKLTQQLEEERiQHQQKV 227
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEaelaELEAEL-EELRLELEELELELEEAQAEEY-ELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 228 KELEEQLENETlhKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPP 307
Cdd:COG1196  298 ARLEQDIARLE--ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 385198093 308 NPIRSLMSMIRKRSHPSGSGAKKEKATQPETTEEVTDLKRQA 349
Cdd:COG1196  376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 85-289 6.92e-03

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 39.29  E-value: 6.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   85 KELRDQIVSVQEEKKILAIELENLKsklvEVIEEVNKVK-QEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEMQVNLEL 163
Cdd:pfam05622 214 KKLEEKLEALQKEKERLIIERDTLR----ETNEELRCAQlQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQH 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  164 E-KDLRKKAESFAQEMFIE-----------------QNKLKRQSHLLLQSSIPD-QQLLKALDENAKLTQQLEEERIQHQ 224
Cdd:pfam05622 290 EnKMLRLGQEGSYRERLTElqqlledanrrkneletQNRLANQRILELQQQVEElQKALQEQGSKAEDSSLLKQKLEEHL 369

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 385198093  225 QKVKELEEQLE-------------NETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 289
Cdd:pfam05622 370 EKLHEAQSELQkkkeqieelepkqDSNLAQKIDELQEALRKKDEDMKAMEERYKKYVEKAKSVIKTLDPKQNPASPPE 447
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 210-291 7.49e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.98  E-value: 7.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 210 AKLTQQLEEERIQHQQKVKELEEQLENetLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKRVNQSE 289
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAA--LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96


                 ..
gi 385198093 290 NS 291
Cdd:COG4942   97 AE 98
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 199-288 8.17e-03

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: 37.96  E-value: 8.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  199 DQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEI-HNLKQQLELLEEDKKELELKYQNSEEKARNLKHS 277
Cdd:pfam13851  42 EERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENYEKDKQSlKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERE 121

                          90
                  ....*....|.
gi 385198093  278 VDELQKRVNQS 288
Cdd:pfam13851 122 RDELYDKFEAA 132
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
104-287 8.42e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 8.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 104 ELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVlEKCNRVSMLAVEEYEEMQVNLELEKDLRKKAESFAQEMFIEQN 183
Cdd:COG4717  338 ELLELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLG 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 184 KLKRQSHLLLQSSIPD--QQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIHNLKQQLELLEEDKKELE 261
Cdd:COG4717  417 ELEELLEALDEEELEEelEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALK 496

                        170       180
                 ....*....|....*....|....*.
gi 385198093 262 LKYQNSEEKARNLKhsvDELQKRVNQ 287
Cdd:COG4717  497 LALELLEEAREEYR---EERLPPVLE 519
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 85-352 9.27e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.18  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093    85 KELRDQIVSVQEEKKILAIELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKCNRVSMLAVEEYEEmQVNLELE 164
Cdd:pfam02463  173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE-LLRDEQE 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   165 KDLRKKAESFAQEMFIEQNKLKRQSHLLLQSSIPDQQLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIH 244
Cdd:pfam02463  252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   245 NLKQQLELLEEDKKELELKYQ----------NSEEKARNLKHSVDELQKRVNQSENSVPPPPPPPPPLPPPPPNPIRSLM 314
Cdd:pfam02463  332 KEKEEIEELEKELKELEIKREaeeeeeeeleKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLL 411

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 385198093   315 SMIRKRSHPSGSGAKKEKATQPETTEEVTDLKRQAVEE 352
Cdd:pfam02463  412 ELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 201-289 9.79e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.98  E-value: 9.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093 201 QLLKALDENAKLTQQLEEERIQHQQKVKELEEQLENETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDE 280
Cdd:COG1579   49 AAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAE 128


                 ....*....
gi 385198093 281 LQKRVNQSE 289
Cdd:COG1579  129 LEAELAELE 137
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
82-284 9.82e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 9.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093   82 KQIKELRDQIVSVQEEKKILAiELENLKSKLVEVIEEVNKVKQEKTVLNSEVLEQRKVLEKcnrvsmLAVEEYEEMQVNL 161
Cdd:COG4913   235 DDLERAHEALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLE------AELEELRAELARL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 385198093  162 ELEKDLRKKAESFAQEmfiEQNKLKRQshlLLQSsipDQQLLKALdenAKLTQQLEEERIQHQQKVKELEEQLEN----- 236
Cdd:COG4913   308 EAELERLEARLDALRE---ELDELEAQ---IRGN---GGDRLEQL---EREIERLERELEERERRRARLEALLAAlglpl 375

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 385198093  237 -----------ETLHKEIHNLKQQLELLEEDKKELELKYQNSEEKARNLKHSVDELQKR 284
Cdd:COG4913   376 pasaeefaalrAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
 
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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