|
Name |
Accession |
Description |
Interval |
E-value |
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
306-459 |
2.44e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 306 ENQYLRVSLEKEEKALSSLQEELNKLREQIRILEDKGTSTELVKENQKLKQHLEEEKQKKHSF---LSQRETLLTEAKML 382
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELeerLEELRELEEELEEL 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75677585 383 KRELERERlvtTALRGELQQLSGSQLHGKSDSPNVYTE-KKEIAILRERLTELERKLTFEQQRSDLWERLYVEAKDQN 459
Cdd:COG4717 169 EAELAELQ---EELEELLEQLSLATEEELQDLAEELEElQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-450 |
5.09e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 242 KRQQLVRKIHEDELNdMKDYLSQCQQEQESFIDYKSLKENLARCWTLTEAEKMSFETQKTNLATENQYLRVSLEKEEKAL 321
Cdd:TIGR02169 302 EIASLERSIAEKERE-LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 322 SSLQEELNKLREQIRILEDKgtstelVKENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRELERERLVT----TALR 397
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKRE------INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleiKKQE 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 75677585 398 GELQQLSGSQlhgKSDSPNVYTEKKEIAILRERLTELERKLTFEQQRSDLWER 450
Cdd:TIGR02169 455 WKLEQLAADL---SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
249-376 |
8.00e-04 |
|
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: 41.43 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 249 KIHEDELNDMKDYLSQCQQEQESFIdyKSLKENLArcwtltEAEKMSFETQKT--NLATENQYLRVSLEKEEKALSSLQE 326
Cdd:pfam13851 4 KNHEKAFNEIKNYYNDITRNNLELI--KSLKEEIA------ELKKKEERNEKLmsEIQQENKRLTEPLQKAQEEVEELRK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 75677585 327 EL---NKLREQIRILEDKGTSTElvKENQKLKQHLEEEKQKKHSFLSQRETLL 376
Cdd:pfam13851 76 QLenyEKDKQSLKNLKARLKVLE--KELKDLKWEHEVLEQRFEKVERERDELY 126
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
488-546 |
2.80e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 38.03 E-value: 2.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 75677585 488 SVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDE 546
Cdd:COG4980 35 KLKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEE 93
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
301-524 |
3.82e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 301 TNLATENQYLRVSLEKEEKALSSLQEELNKLREQIRILEDKgtstelVKENQKLKqhleeEKQKKHSFLSQ-RETLLTEA 379
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK------VKELKELK-----EKAEEYIKLSEfYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 380 KMLKRELERERLVTTALRGELQQLSgsqlhgksdspnvyTEKKEIAILRERLTELERKLtfeqQRSDLWERLYVEAKDQN 459
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELE--------------EKEERLEELKKKLKELEKRL----EELEERHELYEEAKAKK 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75677585 460 GKQGTDGKKKGGRGSHRAKNKSKEtfLGSVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKEnLKK 524
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEE--LEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-LKK 433
|
|
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
84-231 |
4.86e-03 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 40.36 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 84 EAEEQKIPEDSI--YIGTASDDSDIVTLEPPKleeignQEVVIVEEAQSSEDFNMGSSSSSQYTFCQPETVFS--SQPSD 159
Cdd:PLN02328 4 ETKEPEDPADNVndVVSEASSPETDLSLSPSQ------SEQNIENDGQNSPETQSPLTELQPSPLPPNTTLDApvSDSQG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75677585 160 DESSSDETSNQPSPAFRRRRARKKtvsasESEDRLVAEQETEPSkeLSKRQFSSGLNKCVILALVIAISMGF 231
Cdd:PLN02328 78 DESSSEQQPQNPNSTEPAPPPKKR-----RRRKRFFTEINANPA--FRRHRVRGGLGKEVDVEALIAISVGF 142
|
|
| YtxH |
pfam12732 |
YtxH-like protein; This family of proteins is found in bacteria. Proteins in this family are ... |
477-530 |
9.32e-03 |
|
YtxH-like protein; This family of proteins is found in bacteria. Proteins in this family are typically between 100 and 143 amino acids in length. The N-terminal region is the most conserved. Proteins is this family are functionally uncharacterized.
Pssm-ID: 432750 [Multi-domain] Cd Length: 71 Bit Score: 35.66 E-value: 9.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 75677585 477 AKNKSKETFlGSVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVK 530
Cdd:pfam12732 19 APKSGKETR-KDLKDKAEDLKDKAKDLAEEAKEKAEDLKEKVKEKADELKEKVK 71
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
306-459 |
2.44e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 2.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 306 ENQYLRVSLEKEEKALSSLQEELNKLREQIRILEDKGTSTELVKENQKLKQHLEEEKQKKHSF---LSQRETLLTEAKML 382
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELeerLEELRELEEELEEL 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75677585 383 KRELERERlvtTALRGELQQLSGSQLHGKSDSPNVYTE-KKEIAILRERLTELERKLTFEQQRSDLWERLYVEAKDQN 459
Cdd:COG4717 169 EAELAELQ---EELEELLEQLSLATEEELQDLAEELEElQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
290-517 |
4.30e-06 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 50.32 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 290 EAEKMSFETQKTNLATENQYLRVSLEKEEKALSSLQEELNKLREQI-RILEDKGTSTELVKENQKLKQHLEEEKQKKHSF 368
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELaRLEQDIARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 369 LSQRETLLTEAKMLKRELERERlvtTALRGELQQLsgsqlhgksdspnvytEKKEIAILRERLTELERKLTFEQQRSDLW 448
Cdd:COG1196 332 LEELEEELEELEEELEEAEEEL---EEAEAELAEA----------------EEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75677585 449 ERLYVEAKDQNGKQGTDGKKKGGRGSHRAKNKSKETFLGSVKETFDAMKNSTKEFVRHHKEKIKQAKEA 517
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
242-450 |
5.09e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.07 E-value: 5.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 242 KRQQLVRKIHEDELNdMKDYLSQCQQEQESFIDYKSLKENLARCWTLTEAEKMSFETQKTNLATENQYLRVSLEKEEKAL 321
Cdd:TIGR02169 302 EIASLERSIAEKERE-LEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 322 SSLQEELNKLREQIRILEDKgtstelVKENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRELERERLVT----TALR 397
Cdd:TIGR02169 381 AETRDELKDYREKLEKLKRE------INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKaleiKKQE 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 75677585 398 GELQQLSGSQlhgKSDSPNVYTEKKEIAILRERLTELERKLTFEQQRSDLWER 450
Cdd:TIGR02169 455 WKLEQLAADL---SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEE 504
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
314-403 |
1.83e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 48.32 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 314 LEKEEKALSSLQEELNKLREQIRILEDKgtSTELVKENQKLKQHLEEEKQKKHS-FLSQRE--TLLTEAKMLKRELERER 390
Cdd:COG2433 408 LTEEEEEIRRLEEQVERLEAEVEELEAE--LEEKDERIERLERELSEARSEERReIRKDREisRLDREIERLERELEEER 485
|
90
....*....|...
gi 75677585 391 LVTTALRGELQQL 403
Cdd:COG2433 486 ERIEELKRKLERL 498
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
262-522 |
2.04e-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: 48.13 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 262 LSQCQQEQESfiDYKSLKENLARcwtlteaekmsFETQKTNLATENQYLRVSLEKEEKALSSLQEELNKLREQIRILEDK 341
Cdd:TIGR02168 682 LEEKIEELEE--KIAELEKALAE-----------LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 342 -----GTSTELVKENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRELERERLVTTALRGELQQLSGSQLHGKSDSPN 416
Cdd:TIGR02168 749 iaqlsKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLES 828
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 417 VYTEKKEIAILRERLTELERKLT-----FEQQRSDLWERLYVEAKDQNGKQGTDGKKKGGRGSHRAKNKSKETFLGSVKE 491
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSediesLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
250 260 270
....*....|....*....|....*....|.
gi 75677585 492 TFDAMKNSTKEfVRHHKEKIKQAKEAVKENL 522
Cdd:TIGR02168 909 KRSELRRELEE-LREKLAQLELRLEGLEVRI 938
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
307-444 |
2.86e-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: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 307 NQYLRVSLEKE----EKALSSLQEELNKLREQIRILEDKgtstelvkenqklkqhLEEEKQKKHSFLSQRETLLTEAKM- 381
Cdd:COG3206 159 EAYLEQNLELRreeaRKALEFLEEQLPELRKELEEAEAA----------------LEEFRQKNGLVDLSEEAKLLLQQLs 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75677585 382 -LKRELERERLVTTALRGELQQLSgSQLHGKSDSPNVYTEKKEIAILRERLTELERKLTFEQQR 444
Cdd:COG3206 223 eLESQLAEARAELAEAEARLAALR-AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSAR 285
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
238-458 |
6.86e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 6.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 238 IQIQKRQQLVRKIHEDELNDMKDYLSQCQQEQESFIDYKSLKENLARcwTLTEAEKMSFETQKTNLATENQYLRVS---L 314
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE--ELEEAEEELEEAEAELAEAEEALLEAEaelA 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 315 EKEEKALSSLQEELNKLREQIriledkgtstELVKENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRELERERLVTT 394
Cdd:COG1196 376 EAEEELEELAEELLEALRAAA----------ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75677585 395 ALRGELQQLSGSQLHGKSDspnVYTEKKEIAILRERLTELERKLtfEQQRSDLWERLYVEAKDQ 458
Cdd:COG1196 446 EAAEEEAELEEEEEALLEL---LAELLEEAALLEAALAELLEEL--AEAAARLLLLLEAEADYE 504
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
252-461 |
4.28e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.89 E-value: 4.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 252 EDELNDMKDYLSQCQQEQESF--------IDYKSLK---ENLARCWTLTEAEKMSFETQKTNLATEnqylrvsLEKEEKA 320
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELsrqisalrKDLARLEaevEQLEERIAQLSKELTELEAEIEELEER-------LEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 321 LSSLQEELNKLREQI-----RILEDKGTSTELVKENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRELERERLVTTA 395
Cdd:TIGR02168 777 LAEAEAEIEELEAQIeqlkeELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75677585 396 LRGEL--QQLSGSQLHGKSDS-PNVYTEKKE-IAILRERLTELERKL-TFEQQRSDLwERLYVEAKDQNGK 461
Cdd:TIGR02168 857 LAAEIeeLEELIEELESELEAlLNERASLEEaLALLRSELEELSEELrELESKRSEL-RRELEELREKLAQ 926
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
240-454 |
4.69e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 43.90 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 240 IQKRQQLVRKIHE---DELNDMKDYLSQCQQEQESFIDykSLKENLARCWTLTEA-----------EKMSFETQKTNLAT 305
Cdd:TIGR02169 721 IEKEIEQLEQEEEklkERLEELEEDLSSLEQEIENVKS--ELKELEARIEELEEDlhkleealndlEARLSHSRIPEIQA 798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 306 ENQYLRVSLEKEEKALSSLQEELNKLREQIRILEDkgtstelvkENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRE 385
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK---------EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75677585 386 LERERLVTTALRGELQQLSGSQLHGKSDSPNVYTEKKEIAI----LRERLTELERKLTFEQQRSDLWERLYVE 454
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAqiekKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
241-391 |
6.03e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.22 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 241 QKRQQLVRKIHEDELNDMKDYLSQCQQEQESFIDYKSLKENLARcwTLTEAEKMSFETQKTNLATENQYLRVSLEKEEKA 320
Cdd:COG4717 370 QEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE--LLGELEELLEALDEEELEEELEELEEELEELEEE 447
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75677585 321 LSSLQEELNKLREQIRILEDKGTSTELVKENQKLKQHLEEEkQKKHSFLSQRETLLTEAkmlKRELERERL 391
Cdd:COG4717 448 LEELREELAELEAELEQLEEDGELAELLQELEELKAELREL-AEEWAALKLALELLEEA---REEYREERL 514
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
249-376 |
8.00e-04 |
|
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: 41.43 E-value: 8.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 249 KIHEDELNDMKDYLSQCQQEQESFIdyKSLKENLArcwtltEAEKMSFETQKT--NLATENQYLRVSLEKEEKALSSLQE 326
Cdd:pfam13851 4 KNHEKAFNEIKNYYNDITRNNLELI--KSLKEEIA------ELKKKEERNEKLmsEIQQENKRLTEPLQKAQEEVEELRK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 75677585 327 EL---NKLREQIRILEDKGTSTElvKENQKLKQHLEEEKQKKHSFLSQRETLL 376
Cdd:pfam13851 76 QLenyEKDKQSLKNLKARLKVLE--KELKDLKWEHEVLEQRFEKVERERDELY 126
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
239-408 |
2.25e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 239 QIQKRQQLVRKIHEdELNDMKDYLSQCQQEQESFID-YKSLKENLARcwtlTEAEKMSFETQKTNLATENQYLRVSLEKE 317
Cdd:COG4372 74 ELEQLEEELEELNE-QLQAAQAELAQAQEELESLQEeAEELQEELEE----LQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 318 EKALSSLQEELNKLREQIRILEDKGTSTELVKENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRELERERLVTTALR 397
Cdd:COG4372 149 EEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170
....*....|.
gi 75677585 398 GELQQLSGSQL 408
Cdd:COG4372 229 AKLGLALSALL 239
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
252-457 |
2.26e-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: 2.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 252 EDELNDMKDYLsqcQQEQESFIDYKSLKENL--ARCWTLTeAEKMSFETQKtnlatenqylrvslEKEEKALSSLQEELN 329
Cdd:TIGR02169 193 IDEKRQQLERL---RREREKAERYQALLKEKreYEGYELL-KEKEALERQK--------------EAIERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 330 KLREQIriledkgtsTELVKENQKLKQHLEEEkQKKHSFLSQRETLLTEAKMLKRELERERLVTT--ALRGELQQLSGSQ 407
Cdd:TIGR02169 255 KLTEEI---------SELEKRLEEIEQLLEEL-NKKIKDLGEEEQLRVKEKIGELEAEIASLERSiaEKERELEDAEERL 324
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 75677585 408 LHGKSdspnvytekkEIAILRERLTELERKLTFEQQRSDLWERLYVEAKD 457
Cdd:TIGR02169 325 AKLEA----------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKE 364
|
|
| GvpP |
COG4980 |
Gas vesicle protein YhaH [General function prediction only]; |
488-546 |
2.80e-03 |
|
Gas vesicle protein YhaH [General function prediction only];
Pssm-ID: 444004 [Multi-domain] Cd Length: 106 Bit Score: 38.03 E-value: 2.80e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 75677585 488 SVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFDE 546
Cdd:COG4980 35 KLKDKADDLKDKAEDLKDELKEKASELSEEAKEKLDELIEEIKEKIEELKEEVEPKIEE 93
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
290-530 |
2.90e-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: 41.20 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 290 EAEKMSFETQKTNLATENQYLRVSLEKEEKALSSLQEELNKLREQIRILEDKGTSTELVKENQKLKQHLEEEKQKKHSFL 369
Cdd:TIGR02168 278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 370 SQRETLLTEAKMLKRELERERLVTTALRGELQQLSGSQlhgksdspnvYTEKKEIAILRERLTELERKLT-FEQQRSDLW 448
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQI----------ASLNNEIERLEARLERLEDRRErLQQEIEELL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 449 ERLyvEAKDQNGKQGTDGKKKGGRGSHRAKNKSKETFLGSVKETFDAMKN---STKEFVRHHKEKIKqAKEAVKENLKKF 525
Cdd:TIGR02168 428 KKL--EEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQaldAAERELAQLQARLD-SLERLQENLEGF 504
|
....*
gi 75677585 526 SDSVK 530
Cdd:TIGR02168 505 SEGVK 509
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
266-496 |
3.02e-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: 40.88 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 266 QQEQESFIDYKSLK-ENLARCWTLTEAEKMSFETQKTNLATENQYLRVSLEKEEKALSSLQEELNKLREQIRiledkgtS 344
Cdd:pfam17380 295 KMEQERLRQEKEEKaREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIR-------Q 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 345 TELVKENQKLKQ--HLEEEKQKKHSFLSQRETLLTEAKMLkrELERERLVTTALRgELQQLSGSQLHGKSDSPNVYTEkk 422
Cdd:pfam17380 368 EEIAMEISRMREleRLQMERQQKNERVRQELEAARKVKIL--EEERQRKIQQQKV-EMEQIRAEQEEARQREVRRLEE-- 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75677585 423 eiailrERLTELERKLTFEQQRSDLWERLYVEAKDQNGKQGTDGKKKggRGSHRAKNKSKETFLGSVKETFDAM 496
Cdd:pfam17380 443 ------ERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK--RDRKRAEEQRRKILEKELEERKQAM 508
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
238-549 |
3.12e-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: 3.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 238 IQIQKRQQLVRKIHEDELNDMKDYLSQCQQEQESFIDYKSL-------KENLARCWTLTEAEKMSFETQKTNLATenqyL 310
Cdd:pfam15921 426 MEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLtaqlestKEMLRKVVEELTAKKMTLESSERTVSD----L 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 311 RVSLEKEEKALSSLQEELNKLREQIRIledkgtstelvkENQKLkQHLEEEKQkkhsflsQRETLLTEAKMLKRELERER 390
Cdd:pfam15921 502 TASLQEKERAIEATNAEITKLRSRVDL------------KLQEL-QHLKNEGD-------HLRNVQTECEALKLQMAEKD 561
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 391 LVTTALRGELQ---QLSGSqlHGKS-------------DSPNVYTEKKEIAILRERLTELERKLTFEQQRSDLWERLYVE 454
Cdd:pfam15921 562 KVIEILRQQIEnmtQLVGQ--HGRTagamqvekaqlekEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVN 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 455 AKDQNGKQGTDGKKKGGRGSHRAKNKSKEtfLGSVKETFDAMKNStkefVRHHKEKIKQAKEAVKENLKkfsdSVKSTFR 534
Cdd:pfam15921 640 AGSERLRAVKDIKQERDQLLNEVKTSRNE--LNSLSEDYEVLKRN----FRNKSEEMETTTNKLKMQLK----SAQSELE 709
|
330
....*....|....*
gi 75677585 535 HFKDTTKNIFDEKGN 549
Cdd:pfam15921 710 QTRNTLKSMEGSDGH 724
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
301-524 |
3.82e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.82 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 301 TNLATENQYLRVSLEKEEKALSSLQEELNKLREQIRILEDKgtstelVKENQKLKqhleeEKQKKHSFLSQ-RETLLTEA 379
Cdd:PRK03918 241 EELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK------VKELKELK-----EKAEEYIKLSEfYEEYLDEL 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 380 KMLKRELERERLVTTALRGELQQLSgsqlhgksdspnvyTEKKEIAILRERLTELERKLtfeqQRSDLWERLYVEAKDQN 459
Cdd:PRK03918 310 REIEKRLSRLEEEINGIEERIKELE--------------EKEERLEELKKKLKELEKRL----EELEERHELYEEAKAKK 371
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75677585 460 GKQGTDGKKKGGRGSHRAKNKSKEtfLGSVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKEnLKK 524
Cdd:PRK03918 372 EELERLKKRLTGLTPEKLEKELEE--LEKAKEEIEEEISKITARIGELKKEIKELKKAIEE-LKK 433
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
242-557 |
4.39e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.89 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 242 KRQQLVRKIHEDELNDMKDYLSQCQQEQESfidyksLKENLARCWTLTEAEKMSFETQKTNLATENQYLRVSLEKEEKAL 321
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEED------KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 322 SSLQEELNKLREQIRILEDKGTSTELVKENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRELERERLVTTALRGELQ 401
Cdd:PTZ00121 1620 IKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE 1699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 402 qlsgsqlhgksdspnvytEKKEIAILRERLTELERKLtfEQQRsdlwerlyvEAKDQNGKQGTDGKKKGGRGSHRAKNKS 481
Cdd:PTZ00121 1700 ------------------EAKKAEELKKKEAEEKKKA--EELK---------KAEEENKIKAEEAKKEAEEDKKKAEEAK 1750
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75677585 482 KETflGSVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVKSTFRHFKDTTKNIFD--EKGNKRFGATKE 557
Cdd:PTZ00121 1751 KDE--EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEggKEGNLVINDSKE 1826
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
239-445 |
4.77e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 40.45 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 239 QIQKRQQLVRKI---HEDELNDMKDYLSQCQQEQESFI-DYKSLKENLARcwtLTEA-EKMSFETQKTNLATENQYLrVS 313
Cdd:COG5022 883 QLQELKIDVKSIsslKLVNLELESEIIELKKSLSSDLIeNLEFKTELIAR---LKKLlNNIDLEEGPSIEYVKLPEL-NK 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 314 LEKEEKALSSLQEELNKLREQIRILEDkgtstELVKENQKLKQHleeeKQKKHSFLSQRETLLTEAKMLKrELERERLVT 393
Cdd:COG5022 959 LHEVESKLKETSEEYEDLLKKSTILVR-----EGNKANSELKNF----KKELAELSKQYGALQESTKQLK-ELPVEVAEL 1028
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 394 TAL-------RGELQQLSGSQ-LHGKSDSPNVYTEKKEIAILRERLTELERKLTFEQQRS 445
Cdd:COG5022 1029 QSAskiisseSTELSILKPLQkLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLES 1088
|
|
| PLN02328 |
PLN02328 |
lysine-specific histone demethylase 1 homolog |
84-231 |
4.86e-03 |
|
lysine-specific histone demethylase 1 homolog
Pssm-ID: 215187 [Multi-domain] Cd Length: 808 Bit Score: 40.36 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 84 EAEEQKIPEDSI--YIGTASDDSDIVTLEPPKleeignQEVVIVEEAQSSEDFNMGSSSSSQYTFCQPETVFS--SQPSD 159
Cdd:PLN02328 4 ETKEPEDPADNVndVVSEASSPETDLSLSPSQ------SEQNIENDGQNSPETQSPLTELQPSPLPPNTTLDApvSDSQG 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75677585 160 DESSSDETSNQPSPAFRRRRARKKtvsasESEDRLVAEQETEPSkeLSKRQFSSGLNKCVILALVIAISMGF 231
Cdd:PLN02328 78 DESSSEQQPQNPNSTEPAPPPKKR-----RRRKRFFTEINANPA--FRRHRVRGGLGKEVDVEALIAISVGF 142
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
303-457 |
4.92e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.23 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 303 LATENQYLRVSLEKEEKALSSLQEELNKLREQIRiledkgtstELVKENQKLKQHLEEEKQkkhsflsqretlltEAKML 382
Cdd:COG2433 390 LPEEEPEAEREKEHEERELTEEEEEIRRLEEQVE---------RLEAEVEELEAELEEKDE--------------RIERL 446
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75677585 383 KRELERERlvtTALRGELQqlsgsqlhgksdspnvytEKKEIAILRERLTELERKLTFEQQRSDLWERLYVEAKD 457
Cdd:COG2433 447 ERELSEAR---SEERREIR------------------KDREISRLDREIERLERELEEERERIEELKRKLERLKE 500
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
239-445 |
5.37e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 39.75 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 239 QIQKRQQLVRKIhEDELNDMKDYLSQCQQEQESF-IDYKSLKENLARcwTLTEAEKMSFETQKTNLATENQYLRvsLEKE 317
Cdd:COG4942 63 RIAALARRIRAL-EQELAALEAELAELEKEIAELrAELEAQKEELAE--LLRALYRLGRQPPLALLLSPEDFLD--AVRR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 318 EKALSSLQEELNKLREQIRiledkgtstELVKENQKLKQHLEEEKQKKhsflsqrETLLTEAKMLKRELERERlvtTALR 397
Cdd:COG4942 138 LQYLKYLAPARREQAEELR---------ADLAELAALRAELEAERAEL-------EALLAELEEERAALEALK---AERQ 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 75677585 398 GELQQLSGSQlhgKSDSPNVYTEKKEIAILRERLTELERKLTFEQQRS 445
Cdd:COG4942 199 KLLARLEKEL---AELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
292-451 |
6.18e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 40.06 E-value: 6.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 292 EKMSFETQKTNLATENQYLRVSLEKEEKALSSLQ------EELNKLREQIRILEDKGT--------STELVKENQKLKQH 357
Cdd:pfam05622 105 ELTSLAEEAQALKDEMDILRESSDKVKKLEATVEtykkklEDLGDLRRQVKLLEERNAeymqrtlqLEEELKKANALRGQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 358 LE------EEKQKKHSFLSQR-ETLLTEAKMLKREL-----ERERLVTT--ALR--------GELQQ--LSGSQLHGKSD 413
Cdd:pfam05622 185 LEtykrqvQELHGKLSEESKKaDKLEFEYKKLEEKLealqkEKERLIIErdTLRetneelrcAQLQQaeLSQADALLSPS 264
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 75677585 414 SPNVYTEKKEI--AILRERLTELER--KLTFEQQRSDLWERL 451
Cdd:pfam05622 265 SDPGDNLAAEImpAEIREKLIRLQHenKMLRLGQEGSYRERL 306
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
313-458 |
6.62e-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: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 313 SLEKEEKALSSLQEELNKLREQIRILEDKgtSTELVKENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRELERERLV 392
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKE--EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 393 TTALRGEL-QQLSGSQLHGKSDSPNV-------------------YTE--KKEIAILRERLTELER-KLTFEQQRSDLwE 449
Cdd:COG4942 99 LEAQKEELaELLRALYRLGRQPPLALllspedfldavrrlqylkyLAParREQAEELRADLAELAAlRAELEAERAEL-E 177
|
....*....
gi 75677585 450 RLYVEAKDQ 458
Cdd:COG4942 178 ALLAELEEE 186
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
314-525 |
6.70e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 6.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 314 LEKEEKALSSLQEELNKLREQIRILEDKgtstelVKENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRELERErlVT 393
Cdd:PRK03918 520 LEKKAEEYEKLKEKLIKLKGEIKSLKKE------LEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEE--LE 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 394 TALRgELQQLSGSQLHGKSDSPNVYTEKKEIAILRERLTELERKLT-----FEQQRSDLWE--RLYVEAKDQNGKQGTDG 466
Cdd:PRK03918 592 ERLK-ELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAetekrLEELRKELEEleKKYSEEEYEELREEYLE 670
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 75677585 467 KKKGGRGShRAKNKSKETFLGSVKETFDAMKNSTKEFVRHHKE--KIKQAKEAVKENLKKF 525
Cdd:PRK03918 671 LSRELAGL-RAELEELEKRREEIKKTLEKLKEELEEREKAKKEleKLEKALERVEELREKV 730
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
252-456 |
8.28e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 8.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 252 EDELNDMKDYLSQCQQEQEsfidykslkenlarcWTLTEAEKMSFETQKTNLATENQYLRVSLEKEEKALSSLQEELNKL 331
Cdd:TIGR00618 225 EKELKHLREALQQTQQSHA---------------YLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 332 REQIRILedkgtstelvkENQKLKQHLEEEKQKKHSFLSQRETLLTEAKMLKRELERERLVTTALRGELQQLSGSQLHGK 411
Cdd:TIGR00618 290 RKAAPLA-----------AHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR 358
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 75677585 412 sDSPNVYTEKKEiaILRERLTELERKLTFEQQRSDLWERLYVEAK 456
Cdd:TIGR00618 359 -DAHEVATSIRE--ISCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
241-439 |
8.56e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 39.78 E-value: 8.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 241 QKRQQLvrKIHEDELNDMKdylSQCQQEQEsfidYKSLKENLAR------CWTLTEAEKMSFETQKTNLATENQYLRVSL 314
Cdd:PRK10246 465 EMRQRY--KEKTQQLADVK---TICEQEAR----IKDLEAQRAQlqagqpCPLCGSTSHPAVEAYQALEPGVNQSRLDAL 535
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 315 EKEEKAL----SSLQEELNKLREQIRILEDKGTSteLVKENQKLKQHLE-----------------------EEKQKKHS 367
Cdd:PRK10246 536 EKEVKKLgeegAALRGQLDALTKQLQRDESEAQS--LRQEEQALTQQWQavcaslnitlqpqddiqpwldaqEEHERQLR 613
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 368 FLSQRETL---LTEAKMLKRELERERLVT-TALRGELQQLS---------GSQLHGKSDSPNVYTEKK-EIAILRERLTE 433
Cdd:PRK10246 614 LLSQRHELqgqIAAHNQQIIQYQQQIEQRqQQLLTALAGYAltlpqedeeASWLATRQQEAQSWQQRQnELTALQNRIQQ 693
|
....*.
gi 75677585 434 LERKLT 439
Cdd:PRK10246 694 LTPLLE 699
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
239-402 |
9.14e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.51 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 239 QIQKRQQLVRKIHeDELNDMKDYLSQCQQEQESFIDYKSLKENLARcwtlTEAEKMSFETQKTNLATenqyLRVSLEKEE 318
Cdd:COG4913 628 EAEERLEALEAEL-DALQERREALQRLAEYSWDEIDVASAEREIAE----LEAELERLDASSDDLAA----LEEQLEELE 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75677585 319 KALSSLQEELNKLREQIRILEDK-GTSTELVKENQKLKQHLEEEKQKKHSFL--SQRETLLTEAKM--LKRELERERLVT 393
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKElEQAEEELDELQDRLEAAEDLARLELRALleERFAAALGDAVEreLRENLEERIDAL 778
|
....*....
gi 75677585 394 TALRGELQQ 402
Cdd:COG4913 779 RARLNRAEE 787
|
|
| YtxH |
pfam12732 |
YtxH-like protein; This family of proteins is found in bacteria. Proteins in this family are ... |
477-530 |
9.32e-03 |
|
YtxH-like protein; This family of proteins is found in bacteria. Proteins in this family are typically between 100 and 143 amino acids in length. The N-terminal region is the most conserved. Proteins is this family are functionally uncharacterized.
Pssm-ID: 432750 [Multi-domain] Cd Length: 71 Bit Score: 35.66 E-value: 9.32e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 75677585 477 AKNKSKETFlGSVKETFDAMKNSTKEFVRHHKEKIKQAKEAVKENLKKFSDSVK 530
Cdd:pfam12732 19 APKSGKETR-KDLKDKAEDLKDKAKDLAEEAKEKAEDLKEKVKEKADELKEKVK 71
|
|
| |
