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Conserved domains on  [gi|674591750|emb|CDS29410|]
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growth arrest specific protein 8 [Hymenolepis microstoma]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GAS super family cl25894
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
221-419 1.45e-21

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.


The actual alignment was detected with superfamily member pfam13851:

Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 92.28  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  221 QLEMAHDKELNNMRTYYNDITLGNVNVIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLF 300
Cdd:pfam13851   1 ELMKNHEKAFNEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  301 ESEFSAHNVTKADLRVAVKAKNSNEILYNIAQTRLEEAENEIKRMTEGVVTALLDIKKKSSLKCALLEKKLVQLVDILEN 380
Cdd:pfam13851  81 EKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEKKLQALGETLEK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 674591750  381 MQTEIDALV-ASNADPSNANELRKNIEKVMKKKNTDIKGL 419
Cdd:pfam13851 161 KEAQLNEVLaAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
77-347 2.84e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750    77 LRRKERELEDTEERQEMELQIYRQKAKHLMFEHNAKQSDAQQeatifINAQTERARKEVKDILNENNTLKAQMRLKQLES 156
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-----LSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   157 EDIIKLLKSQHE--TEMTSLRQDFIQQAEELEQRLSKKEAQLRADLETQRACEIHATEERKNLHIKQLEMA-HDKELNNM 233
Cdd:TIGR02168  757 TELEAEIEELEErlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLEsLERRIAAT 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   234 RTYYNDItlgnVNVIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFESEFSAHNVTKAD 313
Cdd:TIGR02168  837 ERRLEDL----EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
                          250       260       270
                   ....*....|....*....|....*....|....
gi 674591750   314 LRVAVKAKNSneiLYNIAQTRLEEAENEIKRMTE 347
Cdd:TIGR02168  913 LRRELEELRE---KLAQLELRLEGLEVRIDNLQE 943
 
Name Accession Description Interval E-value
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
221-419 1.45e-21

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: 92.28  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  221 QLEMAHDKELNNMRTYYNDITLGNVNVIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLF 300
Cdd:pfam13851   1 ELMKNHEKAFNEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  301 ESEFSAHNVTKADLRVAVKAKNSNEILYNIAQTRLEEAENEIKRMTEGVVTALLDIKKKSSLKCALLEKKLVQLVDILEN 380
Cdd:pfam13851  81 EKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEKKLQALGETLEK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 674591750  381 MQTEIDALV-ASNADPSNANELRKNIEKVMKKKNTDIKGL 419
Cdd:pfam13851 161 KEAQLNEVLaAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
170-444 2.56e-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: 2.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   170 EMTSLRQDFIQQAEELEQRLSKKEAQLRaDLETQRAcEIHATEERKNLHIKQLEMAHDKELNNMRTYYNDITLGNVNV-- 247
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELE-ELEEELE-QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELte 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   248 ----IKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFESEFSAHNVTKADLRVAVKAKns 323
Cdd:TIGR02168  759 leaeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT-- 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   324 neilyniaQTRLEEAENEIKRMTEGVVTALLDIkKKSSLKCALLEKKLVQLVDILENMQTEIDALvasNADPSNANELRK 403
Cdd:TIGR02168  837 --------ERRLEDLEEQIEELSEDIESLAAEI-EELEELIEELESELEALLNERASLEEALALL---RSELEELSEELR 904
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 674591750   404 NIEKVMKKKNTDIKGLQLQIS----RINKAYMDLWNVcQEKLSEE 444
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAqlelRLEGLEVRIDNL-QERLSEE 948
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
108-339 1.46e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 108 EHNAKQSDAQQEATIFINAQTERARKEVKDILNENNTLKAQMRLKQLESEdiikllKSQHETEMTSLRQDFIQ---QAEE 184
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE------AKLLLQQLSELESQLAEaraELAE 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 185 LEQRLSKKEAQLRADLETQRACEIHATEERKNLHIKQLEMahdkELNNMRTYYNDitlgNVNVIKTLKENIEELQFKLST 264
Cdd:COG3206  238 AEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEA----ELAELSARYTP----NHPDVIALRAQIAALRAQLQQ 309
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 674591750 265 -SERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFesefsahNVTKADLRVAVKAKNSNEILYNIAQTRLEEAE 339
Cdd:COG3206  310 eAQRILASLEAELEALQAREASLQAQLAQLEARLAEL-------PELEAELRRLEREVEVARELYESLLQRLEEAR 378
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
77-347 2.84e-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: 46.97  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750    77 LRRKERELEDTEERQEMELQIYRQKAKHLMFEHNAKQSDAQQeatifINAQTERARKEVKDILNENNTLKAQMRLKQLES 156
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-----LSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   157 EDIIKLLKSQHE--TEMTSLRQDFIQQAEELEQRLSKKEAQLRADLETQRACEIHATEERKNLHIKQLEMA-HDKELNNM 233
Cdd:TIGR02168  757 TELEAEIEELEErlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLEsLERRIAAT 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   234 RTYYNDItlgnVNVIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFESEFSAHNVTKAD 313
Cdd:TIGR02168  837 ERRLEDL----EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
                          250       260       270
                   ....*....|....*....|....*....|....
gi 674591750   314 LRVAVKAKNSneiLYNIAQTRLEEAENEIKRMTE 347
Cdd:TIGR02168  913 LRRELEELRE---KLAQLELRLEGLEVRIDNLQE 943
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-344 2.88e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  78 RRKE--RELEDTEE--------RQEMELQI---YRQKAKhlmfehnAKQSDA-QQEATIfinAQTERARKEVKDILNENN 143
Cdd:COG1196  173 RKEEaeRKLEATEEnlerlediLGELERQLeplERQAEK-------AERYRElKEELKE---LEAELLLLKLRELEAELE 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 144 TLKAQMRLKQLESEDIIKLLkSQHETEMTSLRQDfIQQAEELEQRLSKKEAQLRADLETQRACEIHATEERKNLHIKQLE 223
Cdd:COG1196  243 ELEAELEELEAELEELEAEL-AELEAELEELRLE-LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 224 mahdkelnnmrtyynditlgnvnviktLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFESE 303
Cdd:COG1196  321 ---------------------------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 674591750 304 FSAHNVTKADLRVAVKAKNSNEILYNIAQTRLEEAENEIKR 344
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
69-291 1.80e-03

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: 41.26  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750    69 QNEETCGLLRRKERELEDTEERQEMELQ---IYRQKAKHLMFEHNAKQSDAQQEATIFINAQTERARKeVKDILNENNTL 145
Cdd:pfam15921  580 QHGRTAGAMQVEKAQLEKEINDRRLELQefkILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRA-VKDIKQERDQL 658
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   146 KAQMRlkqlESEDIIKLLKSQHETemtsLRQDFIQQAEELEQRLSKKEAQLR-ADLETQRACEIHATEERKNLHIKQLEM 224
Cdd:pfam15921  659 LNEVK----TSRNELNSLSEDYEV----LKRNFRNKSEEMETTTNKLKMQLKsAQSELEQTRNTLKSMEGSDGHAMKVAM 730
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 674591750   225 AHDKELNNMRtyynditlgnvNVIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNE-SEEQNK 291
Cdd:pfam15921  731 GMQKQITAKR-----------GQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNK 787
PTZ00121 PTZ00121
MAEBL; Provisional
1-302 2.07e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750    1 MKKSQPQKSRQSRTKQAPHVVEPSEMTRQELEKFVSRLQEELERERSERNKTALERDKITQFWEI-SKQQNEETCGLLRR 79
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAeEAKKAEEDKNMALR 1581
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   80 KERELEDTEERQEMELQIYRQKAKHLMFEHNAKQSDAQQEATIFINAQTERARKEVKDILNENNTLKAQmRLKQLESEDI 159
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE-ELKKAEEENK 1660
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  160 IKLLKSQHETEMTSLRQDFIQQAEELEQRlsKKEAQLRADLETQRACEIHATEERKNLHIKQLEMAHDkelnnmrtyynd 239
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKK--AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE------------ 1726
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 674591750  240 itlgnVNVIKtlkenIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFES 302
Cdd:PTZ00121 1727 -----ENKIK-----AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
248-388 5.22e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 5.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 248 IKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKaaklfESEFSAHNVTKADLRVAVKAKNSNEIL 327
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLA-----EAGLDDADAEAVEARREELEDRDEELR 327
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 674591750 328 YNIAQTRL--EEAENEIKRMTEGvVTALLDIKKKSSLKCALLEKKLVQLVDILENMQTEIDAL 388
Cdd:PRK02224 328 DRLEECRVaaQAHNEEAESLRED-ADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
 
Name Accession Description Interval E-value
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
221-419 1.45e-21

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: 92.28  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  221 QLEMAHDKELNNMRTYYNDITLGNVNVIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLF 300
Cdd:pfam13851   1 ELMKNHEKAFNEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEKLMSEIQQENKRLTEPLQKAQEEVEELRKQLENY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  301 ESEFSAHNVTKADLRVAVKAKNSNEILYNIAQTRLEEAENEIKRMTEGVVTALLDIKKKSSLKCALLEKKLVQLVDILEN 380
Cdd:pfam13851  81 EKDKQSLKNLKARLKVLEKELKDLKWEHEVLEQRFEKVERERDELYDKFEAAIQDVQQKTGLKNLLLEKKLQALGETLEK 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 674591750  381 MQTEIDALV-ASNADPSNANELRKNIEKVMKKKNTDIKGL 419
Cdd:pfam13851 161 KEAQLNEVLaAANLDPDALQAVTEKLEDVLESKNQLIKDL 200
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
170-444 2.56e-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: 2.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   170 EMTSLRQDFIQQAEELEQRLSKKEAQLRaDLETQRAcEIHATEERKNLHIKQLEMAHDKELNNMRTYYNDITLGNVNV-- 247
Cdd:TIGR02168  681 ELEEKIEELEEKIAELEKALAELRKELE-ELEEELE-QLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELte 758
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   248 ----IKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFESEFSAHNVTKADLRVAVKAKns 323
Cdd:TIGR02168  759 leaeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAAT-- 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   324 neilyniaQTRLEEAENEIKRMTEGVVTALLDIkKKSSLKCALLEKKLVQLVDILENMQTEIDALvasNADPSNANELRK 403
Cdd:TIGR02168  837 --------ERRLEDLEEQIEELSEDIESLAAEI-EELEELIEELESELEALLNERASLEEALALL---RSELEELSEELR 904
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 674591750   404 NIEKVMKKKNTDIKGLQLQIS----RINKAYMDLWNVcQEKLSEE 444
Cdd:TIGR02168  905 ELESKRSELRRELEELREKLAqlelRLEGLEVRIDNL-QERLSEE 948
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
108-339 1.46e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.70  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 108 EHNAKQSDAQQEATIFINAQTERARKEVKDILNENNTLKAQMRLKQLESEdiikllKSQHETEMTSLRQDFIQ---QAEE 184
Cdd:COG3206  164 QNLELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLVDLSEE------AKLLLQQLSELESQLAEaraELAE 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 185 LEQRLSKKEAQLRADLETQRACEIHATEERKNLHIKQLEMahdkELNNMRTYYNDitlgNVNVIKTLKENIEELQFKLST 264
Cdd:COG3206  238 AEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEA----ELAELSARYTP----NHPDVIALRAQIAALRAQLQQ 309
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 674591750 265 -SERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFesefsahNVTKADLRVAVKAKNSNEILYNIAQTRLEEAE 339
Cdd:COG3206  310 eAQRILASLEAELEALQAREASLQAQLAQLEARLAEL-------PELEAELRRLEREVEVARELYESLLQRLEEAR 378
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
77-347 2.84e-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: 46.97  E-value: 2.84e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750    77 LRRKERELEDTEERQEMELQIYRQKAKHLMFEHNAKQSDAQQeatifINAQTERARKEVKDILNENNTLKAQMRLKQLES 156
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-----LSRQISALRKDLARLEAEVEQLEERIAQLSKEL 756
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   157 EDIIKLLKSQHE--TEMTSLRQDFIQQAEELEQRLSKKEAQLRADLETQRACEIHATEERKNLHIKQLEMA-HDKELNNM 233
Cdd:TIGR02168  757 TELEAEIEELEErlEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLEsLERRIAAT 836
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   234 RTYYNDItlgnVNVIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFESEFSAHNVTKAD 313
Cdd:TIGR02168  837 ERRLEDL----EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSE 912
                          250       260       270
                   ....*....|....*....|....*....|....
gi 674591750   314 LRVAVKAKNSneiLYNIAQTRLEEAENEIKRMTE 347
Cdd:TIGR02168  913 LRRELEELRE---KLAQLELRLEGLEVRIDNLQE 943
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
78-344 2.88e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.85  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  78 RRKE--RELEDTEE--------RQEMELQI---YRQKAKhlmfehnAKQSDA-QQEATIfinAQTERARKEVKDILNENN 143
Cdd:COG1196  173 RKEEaeRKLEATEEnlerlediLGELERQLeplERQAEK-------AERYRElKEELKE---LEAELLLLKLRELEAELE 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 144 TLKAQMRLKQLESEDIIKLLkSQHETEMTSLRQDfIQQAEELEQRLSKKEAQLRADLETQRACEIHATEERKNLHIKQLE 223
Cdd:COG1196  243 ELEAELEELEAELEELEAEL-AELEAELEELRLE-LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE 320
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 224 mahdkelnnmrtyynditlgnvnviktLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFESE 303
Cdd:COG1196  321 ---------------------------LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 674591750 304 FSAHNVTKADLRVAVKAKNSNEILYNIAQTRLEEAENEIKR 344
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE 414
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
30-430 3.96e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.60  E-value: 3.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750    30 ELEKFVSRLQEELERERSERNKTALERDKITQFWEISKQQNEETCGLLRRKERELEdtEERQEMELQIYRQKAKHLMFEH 109
Cdd:TIGR02169  181 EVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALE--RQKEAIERQLASLEEELEKLTE 258
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   110 NAKQSDAQQEAtifINAQTERARKEVKDiLNENNTLKAQMRLKQLESEdIIKLLKSQHETEmtslrqdfiQQAEELEQRL 189
Cdd:TIGR02169  259 EISELEKRLEE---IEQLLEELNKKIKD-LGEEEQLRVKEKIGELEAE-IASLERSIAEKE---------RELEDAEERL 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   190 SKKEAQLRADLETQRACEIHATEERKNLHIKQLEMAHDKElnnmrtyynditlgnvnVIKTLKENIEELQFKLSTSEREL 269
Cdd:TIGR02169  325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE-----------------ELEDLRAELEEVDKEFAETRDEL 387
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   270 EAYKTEIEEYKKKLNESEEQNKSLRKAAKLFESEFSAHNVTKADLRVAVKAknsneilyniAQTRLEEAENEIKRmTEGV 349
Cdd:TIGR02169  388 KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINE----------LEEEKEDKALEIKK-QEWK 456
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   350 VTALLDIKKKSSLKCALLEKKLVQLVDILENMQTEIDALVASNADPSNANELRKNIEKVMKKKNTDIKGLQLQISRINKA 429
Cdd:TIGR02169  457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGER 536

                   .
gi 674591750   430 Y 430
Cdd:TIGR02169  537 Y 537
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
175-359 6.98e-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: 6.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  175 RQDFIQQAEELEQRLSKKEAQLrADLETQRAceihATEERKNLHIKQLEM--------AHDKELNNMRTYYNDITLGNvN 246
Cdd:COG4913   612 LAALEAELAELEEELAEAEERL-EALEAELD----ALQERREALQRLAEYswdeidvaSAEREIAELEAELERLDASS-D 685
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  247 VIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFESEFSAHNVTKADLRV--AVKAKNSN 324
Cdd:COG4913   686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFaaALGDAVER 765
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 674591750  325 EILYNIaQTRLEEAENEIKRMTEGVVTALLDIKKK 359
Cdd:COG4913   766 ELRENL-EERIDALRARLNRAEEELERAMRAFNRE 799
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
64-347 4.43e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  64 EISKQQNEETCGLLRRKERELEDTEERQ---EMELQIYRQKAKhlmfEHNAKQSDAQQEATIFINAQTERARKEVKDILN 140
Cdd:COG1196  247 ELEELEAELEELEAELAELEAELEELRLeleELELELEEAQAE----EYELLAELARLEQDIARLEERRRELEERLEELE 322
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 141 ENNTLKAQMRLKQLESEDIIKLLKSQHETEMTSLRQDFIQQAEELEQRLSKKEAQLRADLETQRAcEIHATEERKNLHIK 220
Cdd:COG1196  323 EELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE-LLEALRAAAELAAQ 401
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 221 QLEMAHDKELNNMRtyynditlgnvnvIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLF 300
Cdd:COG1196  402 LEELEEAEEALLER-------------LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 674591750 301 ESEFSAHNVTKADLRVAVKAKNSNEILYNIAQTRLEEAENEIKRMTE 347
Cdd:COG1196  469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
53-295 1.18e-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: 41.59  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750    53 ALERDKITQFWEISKQQNE--ETCGLLRRKERELEDTEERQEMeLQIYRQKAKHLMFEHNAKQSdaqqeatifinaQTER 130
Cdd:TIGR02169  685 GLKRELSSLQSELRRIENRldELSQELSDASRKIGEIEKEIEQ-LEQEEEKLKERLEELEEDLS------------SLEQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   131 ARKEVKDILNENNTLKAQMRLKQLESEDIIKLLKSqhetemtSLRQDFIQQAEELEQRLSKKEAQLRADLEtqracEIHA 210
Cdd:TIGR02169  752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEA-------RLSHSRIPEIQAELSKLEEEVSRIEARLR-----EIEQ 819
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   211 TEERKNLHIKQLEmahdKELNNMRTYYNDITlgnvNVIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQN 290
Cdd:TIGR02169  820 KLNRLTLEKEYLE----KEIQELQEQRIDLK----EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKER 891

                   ....*
gi 674591750   291 KSLRK 295
Cdd:TIGR02169  892 DELEA 896
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
69-291 1.80e-03

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: 41.26  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750    69 QNEETCGLLRRKERELEDTEERQEMELQ---IYRQKAKHLMFEHNAKQSDAQQEATIFINAQTERARKeVKDILNENNTL 145
Cdd:pfam15921  580 QHGRTAGAMQVEKAQLEKEINDRRLELQefkILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRA-VKDIKQERDQL 658
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   146 KAQMRlkqlESEDIIKLLKSQHETemtsLRQDFIQQAEELEQRLSKKEAQLR-ADLETQRACEIHATEERKNLHIKQLEM 224
Cdd:pfam15921  659 LNEVK----TSRNELNSLSEDYEV----LKRNFRNKSEEMETTTNKLKMQLKsAQSELEQTRNTLKSMEGSDGHAMKVAM 730
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 674591750   225 AHDKELNNMRtyynditlgnvNVIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNE-SEEQNK 291
Cdd:pfam15921  731 GMQKQITAKR-----------GQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTvATEKNK 787
PTZ00121 PTZ00121
MAEBL; Provisional
1-302 2.07e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.89  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750    1 MKKSQPQKSRQSRTKQAPHVVEPSEMTRQELEKFVSRLQEELERERSERNKTALERDKITQFWEI-SKQQNEETCGLLRR 79
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAeEAKKAEEDKNMALR 1581
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   80 KERELEDTEERQEMELQIYRQKAKHLMFEHNAKQSDAQQEATIFINAQTERARKEVKDILNENNTLKAQmRLKQLESEDI 159
Cdd:PTZ00121 1582 KAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAE-ELKKAEEENK 1660
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  160 IKLLKSQHETEMTSLRQDFIQQAEELEQRlsKKEAQLRADLETQRACEIHATEERKNLHIKQLEMAHDkelnnmrtyynd 239
Cdd:PTZ00121 1661 IKAAEEAKKAEEDKKKAEEAKKAEEDEKK--AAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE------------ 1726
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 674591750  240 itlgnVNVIKtlkenIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFES 302
Cdd:PTZ00121 1727 -----ENKIK-----AEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
126-345 2.77e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  126 AQTERARKEVKDILN-ENNTLKAQMRLKQLE-----SEDIIKLL--KSQHETEMTSLRQDFIQQAEELeqrLSKKEAQLR 197
Cdd:COG4913   225 EAADALVEHFDDLERaHEALEDAREQIELLEpirelAERYAAARerLAELEYLRAALRLWFAQRRLEL---LEAELEELR 301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  198 ADLETQRAcEIHATEERKNLHIKQLEMAHDKELNNmrtyynditlgNVNVIKTLKENIEELQFKLSTSERELEAYKTEIE 277
Cdd:COG4913   302 AELARLEA-ELERLEARLDALREELDELEAQIRGN-----------GGDRLEQLEREIERLERELEERERRRARLEALLA 369
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 674591750  278 EYKKKLNESEEQNKSLRKAAKLF----ESEFSAHNVTKADLRVAVKAknsneilyniAQTRLEEAENEIKRM 345
Cdd:COG4913   370 ALGLPLPASAEEFAALRAEAAALlealEEELEALEEALAEAEAALRD----------LRRELRELEAEIASL 431
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
5-291 3.20e-03

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 40.11  E-value: 3.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750    5 QPQKSRQSRTKQAPHVVEPSEMTRQELEKFVSRLQEELERERSERNKTALERDKITQFWEISKQQNEETCGL--LRRKER 82
Cdd:pfam17380 279 QHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELerIRQEER 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   83 ELEDTEERQE---MELQIYRQkAKHLMFEHNAKQSDAQQE---ATIFINAQTERARKEVKDILNENNTLKAQMRLKQLEs 156
Cdd:pfam17380 359 KRELERIRQEeiaMEISRMRE-LERLQMERQQKNERVRQEleaARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQRE- 436
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  157 ediIKLLKSQHETEMTSLRQDFIQQAEELEQRLSKKEAQLRADLETQRACEIHATEERKNLHIKQLEMAHDKElnnmrty 236
Cdd:pfam17380 437 ---VRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQ------- 506
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 674591750  237 yndITLGNVNVIKTLKENIEELQFKLSTSERELEAykteiEEYKKKLNESEEQNK 291
Cdd:pfam17380 507 ---AMIEEERKRKLLEKEMEERQKAIYEEERRREA-----EEERRKQQEMEERRR 553
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
248-388 5.22e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 5.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 248 IKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKaaklfESEFSAHNVTKADLRVAVKAKNSNEIL 327
Cdd:PRK02224 253 LETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLA-----EAGLDDADAEAVEARREELEDRDEELR 327
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 674591750 328 YNIAQTRL--EEAENEIKRMTEGvVTALLDIKKKSSLKCALLEKKLVQLVDILENMQTEIDAL 388
Cdd:PRK02224 328 DRLEECRVaaQAHNEEAESLRED-ADDLEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
129-301 5.86e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 5.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 129 ERARKEVKDILNENNTLKAqmRLKQLESE-DIIKLLKSQHETEMTSLRQdfIQQAEELEQRLSKKEAQLRADLETQRACE 207
Cdd:COG4717   77 EEELKEAEEKEEEYAELQE--ELEELEEElEELEAELEELREELEKLEK--LLQLLPLYQELEALEAELAELPERLEELE 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 208 IHATEERKNLH-IKQLEMAHDKELNNMRTYYNDITLGNVNVIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNES 286
Cdd:COG4717  153 ERLEELRELEEeLEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL 232
                        170
                 ....*....|....*
gi 674591750 287 EEQNKSLRKAAKLFE 301
Cdd:COG4717  233 ENELEAAALEERLKE 247
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
25-288 5.94e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 39.27  E-value: 5.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750    25 EMTRQELEKFVSRLQEELERERSErnKTALERDKITQFWEISKQQNEETCGLLRRKERELEDTE-ERQEMELQIYRQKAK 103
Cdd:TIGR02168  697 EKALAELRKELEELEEELEQLRKE--LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTElEAEIEELEERLEEAE 774
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   104 HLMFEHNAKQSDAQQEATIFINA--QTERARKEVKDILNENNTLKAQMRLKQLESEDIIKLLksqhETEMTSLRQDFIQQ 181
Cdd:TIGR02168  775 EELAEAEAEIEELEAQIEQLKEElkALREALDELRAELTLLNEEAANLRERLESLERRIAAT----ERRLEDLEEQIEEL 850
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   182 AEELEqRLSKKEAQLRADLETQRACEIHATEERKNlhIKQLEMAHDKELNNMRTYYNDITlgnvNVIKTLKENIEELQFK 261
Cdd:TIGR02168  851 SEDIE-SLAAEIEELEELIEELESELEALLNERAS--LEEALALLRSELEELSEELRELE----SKRSELRRELEELREK 923
                          250       260
                   ....*....|....*....|....*..
gi 674591750   262 LSTSERELEAYKTEIEEYKKKLNESEE 288
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDNLQERLSEEYS 950
TMPIT pfam07851
TMPIT-like protein; A number of members of this family are annotated as being transmembrane ...
152-284 6.41e-03

TMPIT-like protein; A number of members of this family are annotated as being transmembrane proteins induced by tumour necrosis factor alpha, but no literature was found to support this.


Pssm-ID: 462288  Cd Length: 324  Bit Score: 38.73  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  152 KQLESEDiiKLLKSQHET------EMTSLRQDFIQQAEELEQRLSKKEAQLRAdletqraCEIHATEERKNLhIKQLEma 225
Cdd:pfam07851   5 EELEKEF--QQLQETHKEykqkleELSSLQTRCKKSIKHQKKRLKELKSSLKR-------LQRSSIEEDQSL-IKELQ-- 72
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 674591750  226 hdKELNNMRTYYND--------------ITLGNVNVIKTLKEnieelqfklstserELEAYKTEIEEYKKKLN 284
Cdd:pfam07851  73 --EEIKERKAQLFEmeallpkknglylnLILGNVNVSLLNKD--------------EKFKYKDEYEKFKLILT 129
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
111-357 7.79e-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: 38.59  E-value: 7.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 111 AKQSDAQQEATIFINAQTERARKEVKDILNENNTLKAQMRLKQLESEDIIKLLKSQhETEMTSLRQDfIQQAEELEQRLS 190
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAL-EQELAALEAE-LAELEKEIAELR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 191 KKEAQLRADLETQ-RACEIHATEERKNLHIKQLEMAhdkELNNMRTYYNDITlgnvnviKTLKENIEELQFKLSTSEREL 269
Cdd:COG4942   97 AELEAQKEELAELlRALYRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLA-------PARREQAEELRADLAELAALR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 270 EAYKTEIEEYKKKLNESEEQNKSLRKAAKLFESEFSAHNVTKADLRVAVKAKNSNEILYNIAQTRLEEAENEIKRMTEGV 349
Cdd:COG4942  167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246

                 ....*...
gi 674591750 350 VTALLDIK 357
Cdd:COG4942  247 GFAALKGK 254
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
66-308 8.09e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 38.88  E-value: 8.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750    66 SKQQNEETCGLLRRKERELEDTE-ERQEMELQIyrQKAKHLMFEHNAKQSDAQQEAtIFINAQTERARKEVKDiLNENNT 144
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRlEVSELEEEI--EELQKELYALANEISRLEQQK-QILRERLANLERQLEE-LEAQLE 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   145 LKAQMRLKQLESEDIIKLLKSQHETEMTSLRQDFIQQAEELEQRLSKKEAqLRADLETQRAcEIHATEERKNLHIKQLEM 224
Cdd:TIGR02168  327 ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE-LEEQLETLRS-KVAQLELQIASLNNEIER 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750   225 --AHDKELNNMRTyyNDITLGNVNVIKTLKENIEELQFKLSTSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFES 302
Cdd:TIGR02168  405 leARLERLEDRRE--RLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482

                   ....*.
gi 674591750   303 EFSAHN 308
Cdd:TIGR02168  483 ELAQLQ 488
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
76-301 8.71e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.60  E-value: 8.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750  76 LLRRKERELEDTEERQEMELQIYRQKAKHLMFEHNAKQSDAQQEAtifinaqteRARKEVKDILNENNTLKAQMRLKQLE 155
Cdd:COG4717  299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL---------DRIEELQELLREAEELEEELQLEELE 369
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674591750 156 SEdIIKLLKSQHETEMTSLRQ--DFIQQAEELEQRLSKKEAQLRADLETQRACEIHATEERKNLHIKQLEM---AHDKEL 230
Cdd:COG4717  370 QE-IAALLAEAGVEDEEELRAalEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEeleELEEEL 448
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674591750 231 NNMRTyynditlgnvnVIKTLKENIEELQfklstSERELEAYKTEIEEYKKKLNESEEQNKSLRKAAKLFE 301
Cdd:COG4717  449 EELRE-----------ELAELEAELEQLE-----EDGELAELLQELEELKAELRELAEEWAALKLALELLE 503
 
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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