|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
368-526 |
7.15e-46 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 159.78 E-value: 7.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 368 WEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRS------------------- 428
Cdd:pfam06818 3 WEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSktlelevcenelqrkknea 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 429 --LQEQAPREEAP-----------------GSCETDDCKSRGLLGEAGGSEARDsAEQLRAELLQERLRGQEQALRFEQE 489
Cdd:pfam06818 83 elLREKVGKLEEEvsglrealsdvspsgyeSVYESDEAKEQRQEEADLGSLRRE-VERLRAELREERQRRERQASSFEQE 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1351503585 490 RRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELR 526
Cdd:pfam06818 162 RRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
278-530 |
3.08e-10 |
|
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: 63.15 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 278 GSNPFTQVLEERQRlwlaELkrlyvERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEAD 357
Cdd:TIGR02168 664 GSAKTNSSILERRR----EI-----EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 358 PSARPEEEARW---------EVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQD-------AELVQ 421
Cdd:TIGR02168 735 LARLEAEVEQLeeriaqlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRealdelrAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 422 LREAVRSLQEQAPREEApgscETDDCKSRGLLGEAGGSEARDSAEQLRAEL--LQERLRGQEQALRFEQERRTWQEEKER 499
Cdd:TIGR02168 815 LNEEAANLRERLESLER----RIAATERRLEDLEEQIEELSEDIESLAAEIeeLEELIEELESELEALLNERASLEEALA 890
|
250 260 270
....*....|....*....|....*....|..
gi 1351503585 500 VLRYQREIQGGYM-DMYRRNQALEQELRALRE 530
Cdd:TIGR02168 891 LLRSELEELSEELrELESKRSELRRELEELRE 922
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
284-530 |
1.78e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 284 QVLEERQRLWLAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELraqqglapeprapgtlpeadpsarpe 363
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL-------------------------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 364 EEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEApgsce 443
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 444 tddcKSRGLLGEAGGSEA-RDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALE 522
Cdd:COG1196 345 ----ELEEAEEELEEAEAeLAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
....*...
gi 1351503585 523 QELRALRE 530
Cdd:COG1196 421 EELEELEE 428
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
287-508 |
1.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 287 EERQRLWLAELKRLYVERLHEVTQKAERSERNLQlQLFMAQQEQRRlRKELRAQqglAPEPRAPGTLPEADPSARPEEEA 366
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKK-ADEAKKK---AEEKKKADEAKKKAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 367 RWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEAPGSCETDD 446
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351503585 447 CKSRGLLGEAGGSEARDSAEQLRAellQERLRGQEQALRFEQERRTwQEEKERVLRYQREIQ 508
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKK---AEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAK 1587
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
286-435 |
1.42e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.55 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 286 LEERQRLWLAELKRLYvERLHEVTQKAERSERNLQL---QLFMAQQEQRRLRKELRAQQGLAPepRAPGTLPEAD----- 357
Cdd:pfam05667 329 LQQQREEELEELQEQL-EDLESSIQELEKEIKKLESsikQVEEELEELKEQNEELEKQYKVKK--KTLDLLPDAEeniak 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 358 -------PSARPEE-EARWEVCQKT--AEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVR 427
Cdd:pfam05667 406 lqalvdaSAQRLVElAGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYE 485
|
....*...
gi 1351503585 428 SLQEQAPR 435
Cdd:pfam05667 486 RLPKDVSR 493
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
284-432 |
1.68e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.80 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 284 QVLEERQRLWLAELKrlyVERLhEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEprapGTLPEADpsarpE 363
Cdd:COG1566 84 ALAQAEAQLAAAEAQ---LARL-EAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKK----GAVSQQE-----L 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351503585 364 EEARwevcqktaeisllkQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQdAELVQLREAVRSLQEQ 432
Cdd:COG1566 151 DEAR--------------AALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQ-AQVAQAEAALAQAELN 204
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
372-432 |
7.69e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 36.00 E-value: 7.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351503585 372 QKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQ 432
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEK 61
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Fez1 |
pfam06818 |
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper ... |
368-526 |
7.15e-46 |
|
Fez1; This family represents the eukaryotic Fez1 protein. Fez1 contains a leucine-zipper region with similarity to the DNA-binding domain of the cAMP-responsive activating-transcription factor 5. There is evidence that Fez1 inhibits cancer cell growth through regulation of mitosis, and that its alterations result in abnormal cell growth. Note that some family members contain more than one copy of this region.
Pssm-ID: 462015 [Multi-domain] Cd Length: 198 Bit Score: 159.78 E-value: 7.15e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 368 WEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRS------------------- 428
Cdd:pfam06818 3 WEVCQKSGEISLLKQQLKDSQAEVTQKLNEIVALRAQLRELRAKLEEKEEQIQELEDSLRSktlelevcenelqrkknea 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 429 --LQEQAPREEAP-----------------GSCETDDCKSRGLLGEAGGSEARDsAEQLRAELLQERLRGQEQALRFEQE 489
Cdd:pfam06818 83 elLREKVGKLEEEvsglrealsdvspsgyeSVYESDEAKEQRQEEADLGSLRRE-VERLRAELREERQRRERQASSFEQE 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 1351503585 490 RRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELR 526
Cdd:pfam06818 162 RRTWQEEKEKVIRYQKQLQLNYVQMYRRNQALERELK 198
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
278-530 |
3.08e-10 |
|
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: 63.15 E-value: 3.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 278 GSNPFTQVLEERQRlwlaELkrlyvERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEAD 357
Cdd:TIGR02168 664 GSAKTNSSILERRR----EI-----EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKD 734
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 358 PSARPEEEARW---------EVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQD-------AELVQ 421
Cdd:TIGR02168 735 LARLEAEVEQLeeriaqlskELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRealdelrAELTL 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 422 LREAVRSLQEQAPREEApgscETDDCKSRGLLGEAGGSEARDSAEQLRAEL--LQERLRGQEQALRFEQERRTWQEEKER 499
Cdd:TIGR02168 815 LNEEAANLRERLESLER----RIAATERRLEDLEEQIEELSEDIESLAAEIeeLEELIEELESELEALLNERASLEEALA 890
|
250 260 270
....*....|....*....|....*....|..
gi 1351503585 500 VLRYQREIQGGYM-DMYRRNQALEQELRALRE 530
Cdd:TIGR02168 891 LLRSELEELSEELrELESKRSELRRELEELRE 922
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
284-530 |
1.78e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.72 E-value: 1.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 284 QVLEERQRLWLAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELraqqglapeprapgtlpeadpsarpe 363
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEL-------------------------- 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 364 EEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEApgsce 443
Cdd:COG1196 270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE----- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 444 tddcKSRGLLGEAGGSEA-RDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALE 522
Cdd:COG1196 345 ----ELEEAEEELEEAEAeLAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLE 420
|
....*...
gi 1351503585 523 QELRALRE 530
Cdd:COG1196 421 EELEELEE 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
284-530 |
3.43e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.57 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 284 QVLEERQRLWLAELkrlyvERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEprapgtlpeadpSARPE 363
Cdd:COG1196 256 EELEAELAELEAEL-----EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE------------LEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 364 EEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEApgscE 443
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR----A 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 444 TDDCKSRgllgEAGGSEARDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQggymdmyRRNQALEQ 523
Cdd:COG1196 395 AAELAAQ----LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE-------EEEEALLE 463
|
....*..
gi 1351503585 524 ELRALRE 530
Cdd:COG1196 464 LLAELLE 470
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
287-529 |
2.29e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 2.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 287 EERQRLWLAELKRLYVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLApeprapgtlpeadpsARPEEEA 366
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAEL---------------ARLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 367 RwevcQKTAEISLLKQQLREAQAELAQ-KLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPreeapgscetd 445
Cdd:COG4913 312 E----RLEARLDALREELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLP----------- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 446 dcksrglLGEAGGSEARDSAEQLRAELlqERLRGQEQALRFEQERRTWQEEKERvlryqreiqggymdmyrrnQALEQEL 525
Cdd:COG4913 377 -------ASAEEFAALRAEAAALLEAL--EEELEALEEALAEAEAALRDLRREL-------------------RELEAEI 428
|
....
gi 1351503585 526 RALR 529
Cdd:COG4913 429 ASLE 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
288-530 |
2.60e-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: 47.36 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 288 ERQRLWLAELKRLYVERLHEV-TQKAERSERNLQLQ--LFMAQQEQRRLRKELRAQQglapeprapgtlpeadpsaRPEE 364
Cdd:TIGR02168 252 EEELEELTAELQELEEKLEELrLEVSELEEEIEELQkeLYALANEISRLEQQKQILR-------------------ERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 365 EARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEApgscET 444
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS----KV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 445 DDCKSRGLLGEAGGSEARDSAEQL--RAELLQERLRGQEQALRfEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALE 522
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLedRRERLQQEIEELLKKLE-EAELKELQAELEELEEELEELQEELERLEEALEELR 467
|
....*...
gi 1351503585 523 QELRALRE 530
Cdd:TIGR02168 468 EELEEAEQ 475
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
283-543 |
3.21e-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: 46.98 E-value: 3.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 283 TQVLEERQRLWLAELKRLY--VERLHEVTQKAER--SERNLQLQLFMA--QQEQRRLRKELRAQQglapeprapgtlPEA 356
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEeiEQLLEELNKKIKDlgEEEQLRVKEKIGelEAEIASLERSIAEKE------------REL 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 357 DPSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQ---EQA 433
Cdd:TIGR02169 318 EDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYReklEKL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 434 PREEAPGSCETDDCKSRGLLGEAGGSEARDSAEQLRAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREI---QGG 510
Cdd:TIGR02169 398 KREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELydlKEE 477
|
250 260 270
....*....|....*....|....*....|...
gi 1351503585 511 YMDMYRRNQALEQELRALREPPTPWSPRLESSK 543
Cdd:TIGR02169 478 YDRVEKELSKLQRELAEAEAQARASEERVRGGR 510
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
287-508 |
1.62e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 287 EERQRLWLAELKRLYVERLHEVTQKAERSERNLQlQLFMAQQEQRRlRKELRAQqglAPEPRAPGTLPEADPSARPEEEA 366
Cdd:PTZ00121 1375 EAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAAKKK-ADEAKKK---AEEKKKADEAKKKAEEAKKADEA 1449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 367 RWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEAPGSCETDD 446
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351503585 447 CKSRGLLGEAGGSEARDSAEQLRAellQERLRGQEQALRFEQERRTwQEEKERVLRYQREIQ 508
Cdd:PTZ00121 1530 AEEAKKADEAKKAEEKKKADELKK---AEELKKAEEKKKAEEAKKA-EEDKNMALRKAEEAK 1587
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
250-508 |
2.38e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 250 FSCSSAEEMGAVLPETCEELKRGLGDEDGSNPFTQVLEERQrlwlAELKRL--YVERLHEVTQKAERSERNLQLQLFMAQ 327
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE----TELERMkeRAKKAGAQRKEEEAERKQLQAKLQQTE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 328 QEQRRLRKELRAqqglapeprAPGTLPEADPSArpeeearwevcqktaeisllkQQLREAQAELAQKLAeifslktqlrg 407
Cdd:pfam07888 185 EELRSLSKEFQE---------LRNSLAQRDTQV---------------------LQLQDTITTLTQKLT----------- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 408 sraQAQAQDAELVQLREAVRSLQEQAPREEAPGSCETDDCKSRGLLGEAGGSE---ARDSAEQLRAELLQERLRGQEQAL 484
Cdd:pfam07888 224 ---TAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAElhqARLQAAQLTLQLADASLALREGRA 300
|
250 260
....*....|....*....|....*...
gi 1351503585 485 RFEQERRTWQE----EKERVLRYQREIQ 508
Cdd:pfam07888 301 RWAQERETLQQsaeaDKDRIEKLSAELQ 328
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
301-529 |
4.02e-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: 43.51 E-value: 4.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 301 YVERLHEVTQKAERSERNL------------QLQLFMAQQEQ----RRLRKELRAqqglapeprapgtlpeadpsarpee 364
Cdd:TIGR02168 170 YKERRKETERKLERTRENLdrledilnelerQLKSLERQAEKaeryKELKAELRE------------------------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 365 earwevcqktAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAprEEAPG---- 440
Cdd:TIGR02168 225 ----------LELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEI--EELQKelya 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 441 -SCETDDCKSRGLLGEAGGSEARDSAEQL---RAELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYR 516
Cdd:TIGR02168 293 lANEISRLEQQKQILRERLANLERQLEELeaqLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
250
....*....|...
gi 1351503585 517 RNQALEQELRALR 529
Cdd:TIGR02168 373 RLEELEEQLETLR 385
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
312-530 |
5.39e-04 |
|
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: 42.44 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 312 AERSERNLQLQLFMAQQEQRRLRKELRAQQglapeprapgtlpeadpsaRPEEEARWEVCQKTAEISLLKQQLREAQAEL 391
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALK-------------------KEEKALLKQLAALERRIAALARRIRALEQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 392 AQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEAPGSCETDDCKSRGLLGEAGGSEARDSAEQLRA- 470
Cdd:COG4942 79 AALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRAd 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1351503585 471 --ELLQERLRGQEQALRFEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELRALRE 530
Cdd:COG4942 159 laELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
283-539 |
6.88e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 283 TQVLEERQRLWLAELKRLYVERLHEVTQKA----ERSErnlqlqlfmAQQEQRRLRKELRAQQGLAP-EPRAPGTLPEAD 357
Cdd:COG3096 455 EEVLELEQKLSVADAARRQFEKAYELVCKIagevERSQ---------AWQTARELLRRYRSQQALAQrLQQLRAQLAELE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 358 PSARPEEEARW---EVCQKTA-------EISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVR 427
Cdd:COG3096 526 QRLRQQQNAERlleEFCQRIGqqldaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWL 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 428 SLQEQAPReeapgscetddcksrglLGEAGGSEARDSAE--QLRAELLqerlrgqeqalrfEQERRTWQEEKERVlryqr 505
Cdd:COG3096 606 AAQDALER-----------------LREQSGEALADSQEvtAAMQQLL-------------EREREATVERDELA----- 650
|
250 260 270
....*....|....*....|....*....|....
gi 1351503585 506 eiqggymdmyRRNQALEQELRALREPPTPWSPRL 539
Cdd:COG3096 651 ----------ARKQALESQIERLSQPGGAEDPRL 674
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
296-499 |
8.77e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.44 E-value: 8.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 296 ELKRLYVERLHEVTQKAERSERNLQLQLFMAQQ-EQRRLRKELRAQQGL--APEPRAPGTLPEADPSARPEEEAR-WEVC 371
Cdd:PTZ00121 1241 EAKKAEEERNNEEIRKFEEARMAHFARRQAAIKaEEARKADELKKAEEKkkADEAKKAEEKKKADEAKKKAEEAKkADEA 1320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 372 QKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLR---------EAVRSLQEQAPREEAPGSC 442
Cdd:PTZ00121 1321 KKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkeeakkkadAAKKKAEEKKKADEAKKKA 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1351503585 443 ETDDCKSRGLLGEAggsEARDSAEQLRAEllQERLRGQEQALRFEQERRTWQEEKER 499
Cdd:PTZ00121 1401 EEDKKKADELKKAA---AAKKKADEAKKK--AEEKKKADEAKKKAEEAKKADEAKKK 1452
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
287-495 |
9.70e-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: 41.97 E-value: 9.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 287 EERQRLWLAELKRLYVERLHEVTQKAERSERNL-QLQLFMAQQEQRR--LRKELRAQQGLAPEPRApgtlpEADPSARPE 363
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIeELEAQIEQLKEELkaLREALDELRAELTLLNE-----EAANLRERL 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 364 EEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQApreeapgscE 443
Cdd:TIGR02168 827 ESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL---------E 897
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1351503585 444 TDDCKSRGLLGEAggSEARDSAEQLRAELLQERLRGQEqalrFEQERRTWQE 495
Cdd:TIGR02168 898 ELSEELRELESKR--SELRRELEELREKLAQLELRLEG----LEVRIDNLQE 943
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
284-530 |
1.37e-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: 41.65 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 284 QVLEERQRLWLAELKRLYVERLHEV-----TQKAERSERNLQLQLFMAQQEQRRL-RKELRAQQglaPEPRAPGTLPEAD 357
Cdd:pfam17380 326 QAEMDRQAAIYAEQERMAMERERELerirqEERKRELERIRQEEIAMEISRMRELeRLQMERQQ---KNERVRQELEAAR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 358 PSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREE 437
Cdd:pfam17380 403 KVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKE 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 438 APGSCETDDCKSRGLLGEAGGSEARDSAEQLRAELLQERLRGQEQALRFEQERRTWQEE--KERVLRYQREIQGGYM--- 512
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEErrKQQEMEERRRIQEQMRkat 562
|
250
....*....|....*...
gi 1351503585 513 DMYRRNQALEQELRALRE 530
Cdd:pfam17380 563 EERSRLEAMEREREMMRQ 580
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
302-496 |
1.38e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.44 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 302 VERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEADpsarpEEEARWEVcQKTA------ 375
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE-----REIAELEA-ELERldassd 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 376 EISLLKQQLREAQAELAQKLAEIfslkTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEAPGSCETDDCKSRGLLGE 455
Cdd:COG4913 686 DLAALEEQLEELEAELEELEEEL----DELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGD 761
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1351503585 456 AGGSEARDSAEQLRAElLQERLRGQEQALR--FEQERRTWQEE 496
Cdd:COG4913 762 AVERELRENLEERIDA-LRARLNRAEEELEraMRAFNREWPAE 803
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
286-435 |
1.42e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 41.55 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 286 LEERQRLWLAELKRLYvERLHEVTQKAERSERNLQL---QLFMAQQEQRRLRKELRAQQGLAPepRAPGTLPEAD----- 357
Cdd:pfam05667 329 LQQQREEELEELQEQL-EDLESSIQELEKEIKKLESsikQVEEELEELKEQNEELEKQYKVKK--KTLDLLPDAEeniak 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 358 -------PSARPEE-EARWEVCQKT--AEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVR 427
Cdd:pfam05667 406 lqalvdaSAQRLVElAGQWEKHRVPliEEYRALKEAKSNKEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYE 485
|
....*...
gi 1351503585 428 SLQEQAPR 435
Cdd:pfam05667 486 RLPKDVSR 493
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
284-432 |
1.68e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 40.80 E-value: 1.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 284 QVLEERQRLWLAELKrlyVERLhEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEprapGTLPEADpsarpE 363
Cdd:COG1566 84 ALAQAEAQLAAAEAQ---LARL-EAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKK----GAVSQQE-----L 150
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351503585 364 EEARwevcqktaeisllkQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQdAELVQLREAVRSLQEQ 432
Cdd:COG1566 151 DEAR--------------AALDAAQAQLEAAQAQLAQAQAGLREEEELAAAQ-AQVAQAEAALAQAELN 204
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
296-529 |
2.50e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 40.98 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 296 ELKRLYVERLHEVTQ----KAERSERNLQLQLFMAQQEQRRL---RKELRAQQglAPEPRAPGTLPEADPSARP---EEE 365
Cdd:pfam12128 586 DLKRIDVPEWAASEEelreRLDKAEEALQSAREKQAAAEEQLvqaNGELEKAS--REETFARTALKNARLDLRRlfdEKQ 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 366 ARWEVCQK--TAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQ------------DAELVQLREAVRSLQE 431
Cdd:pfam12128 664 SEKDKKNKalAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEkqaywqvvegalDAQLALLKAAIAARRS 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 432 QAPREEApgSCETD---DCKSRGLLGEAGGSEARDSAEqLRAELLQERLRGQE-------QALRFEQERRTWQEEKERVL 501
Cdd:pfam12128 744 GAKAELK--ALETWykrDLASLGVDPDVIAKLKREIRT-LERKIERIAVRRQEvlryfdwYQETWLQRRPRLATQLSNIE 820
|
250 260 270
....*....|....*....|....*....|..
gi 1351503585 502 RYQREIQGGY----MDMYRRNQALEQELRALR 529
Cdd:pfam12128 821 RAISELQQQLarliADTKLRRAKLEMERKASE 852
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
284-509 |
3.81e-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: 40.04 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 284 QVLEERQRLWLAELKRLYVERlhevtQKAERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRApgtlpeadpsARPE 363
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQL-----EELESKLDELAEELAELEEKLEELKEELESLEAELEELEA----------ELEE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 364 EEARWEVCQKTAEisllkqQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEAPGSCE 443
Cdd:TIGR02168 370 LESRLEELEEQLE------TLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1351503585 444 TDDcksrgllGEAGGSEARDSAEQLRAELLQERLRGQEQALR-FEQERRTWQEEKERVLRYQREIQG 509
Cdd:TIGR02168 444 ELE-------EELEELQEELERLEEALEELREELEEAEQALDaAERELAQLQARLDSLERLQENLEG 503
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
380-530 |
3.90e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 40.00 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 380 LKQQLREAQAELAQKLAEI--FSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQ-----APREEAPGSCETDDCKSRGL 452
Cdd:COG3206 180 LEEQLPELRKELEEAEAALeeFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAElaeaeARLAALRAQLGSGPDALPEL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 453 LGEAGGSEARDSAEQLRAELLQERLRGQE-----QALRfEQERRTWQEEKERVLRYQREIQGGYMDMYRRNQALEQELRA 527
Cdd:COG3206 260 LQSPVIQQLRAQLAELEAELAELSARYTPnhpdvIALR-AQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQ 338
|
...
gi 1351503585 528 LRE 530
Cdd:COG3206 339 LEA 341
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
377-530 |
4.10e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.50 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 377 ISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEApgscETDDCKSRGLLGEA 456
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE----QLQAAQAELAQAQE 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1351503585 457 GGSEARDSAEQLRAELlqERLRGQEQALrfeqerrtwQEEKERVLRYQREIQGGYMDMYRRNQALEQELRALRE 530
Cdd:COG4372 102 ELESLQEEAEELQEEL--EELQKERQDL---------EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
347-543 |
4.75e-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: 39.95 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 347 PRAPGTLPEADPSARPEEEARWEVCQKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRgsraQAQAQDAELVQLREAV 426
Cdd:TIGR00618 211 PCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIE----ELRAQEAVLEETQERI 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 427 RSLQEQAPREEAPGSCETDDCKSRGLLGEAggsearDSAEQLRAELLQERLRGQEQALRFEQERR---TWQEEKERvLRY 503
Cdd:TIGR00618 287 NRARKAAPLAAHIKAVTQIEQQAQRIHTEL------QSKMRSRAKLLMKRAAHVKQQSSIEEQRRllqTLHSQEIH-IRD 359
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1351503585 504 QREIQGGYMDMYRRNQALEQELRALREPPTPWSPRLESSK 543
Cdd:TIGR00618 360 AHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLC 399
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
286-438 |
4.87e-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: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 286 LEERQRLWLAELKRL--YVERLHEVTQKAERSERNLQLQLFMAQQEQRRLRKELRAQQG-LAPEPRAPGTLPEADP---- 358
Cdd:COG4942 46 LKKEEKALLKQLAALerRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEeLAELLRALYRLGRQPPlall 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 359 --SARPEEEARWEVCQKTAEISLLKQ--QLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAP 434
Cdd:COG4942 126 lsPEDFLDAVRRLQYLKYLAPARREQaeELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLE 205
|
....
gi 1351503585 435 REEA 438
Cdd:COG4942 206 KELA 209
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
296-524 |
5.62e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 39.74 E-value: 5.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 296 ELKRLYVERLHEVTQKAERSERNLQLQlFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEADpSARPEEEARW--EVCQK 373
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDK-NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIkaEELKK 1627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 374 TAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEAPGSCETDDCKSRGLL 453
Cdd:PTZ00121 1628 AEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEEL 1707
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1351503585 454 GEAGGSEARdSAEQLRAELlQERLRGQEQALRFEQE--------RRTwQEEKERVLRYQREIQGGYMDMYRRNQALEQE 524
Cdd:PTZ00121 1708 KKKEAEEKK-KAEELKKAE-EENKIKAEEAKKEAEEdkkkaeeaKKD-EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE 1783
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
314-539 |
6.11e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 39.56 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 314 RSERNLQLQLFMAQQEQRRLRKELRAQQGLapeprapgtlpeadpsarpeEEARWEVCQKtAEISLLKQQlrEAQAELAQ 393
Cdd:PRK04863 506 REQRHLAEQLQQLRMRLSELEQRLRQQQRA--------------------ERLLAEFCKR-LGKNLDDED--ELEQLQEE 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 394 KLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEApgscetddcksrgllgeaggseARDSAEQLRaELL 473
Cdd:PRK04863 563 LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLA----------------------AQDALARLR-EQS 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1351503585 474 QERLRGQEQALRFEQErrtwQEEKERVLRYQREiqggymDMYRRNQALEQELRALREPPTPWSPRL 539
Cdd:PRK04863 620 GEEFEDSQDVTEYMQQ----LLERERELTVERD------ELAARKQALDEEIERLSQPGGSEDPRL 675
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
411-530 |
6.59e-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: 6.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 411 QAQAQDAELVQLREAVRSLQEQAPR-EEAPGSCET-DDCKSRGLLGEAGGSEARDSAEQLRAELLQERLRGQEQAL---- 484
Cdd:COG4913 229 ALVEHFDDLERAHEALEDAREQIELlEPIRELAERyAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELarle 308
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1351503585 485 ----RFEQERRTwQEEKERVLRYQREIQGGymdmyRRNQALEQELRALRE 530
Cdd:COG4913 309 aeleRLEARLDA-LREELDELEAQIRGNGG-----DRLEQLEREIERLER 352
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
376-492 |
6.82e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 39.04 E-value: 6.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 376 EISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAE----LVQLREAVRSLQEQAPREEAPGSCETDDCKSRG 451
Cdd:COG3883 137 ELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEqealLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1351503585 452 LLGEAGGSEARDSAEQLRAELLQERLRGQEQALRFEQERRT 492
Cdd:COG3883 217 AAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
|
| Atg16_CCD |
cd22887 |
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ... |
372-432 |
7.69e-03 |
|
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.
Pssm-ID: 439196 [Multi-domain] Cd Length: 91 Bit Score: 36.00 E-value: 7.69e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1351503585 372 QKTAEISLLKQQLREAQAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQ 432
Cdd:cd22887 1 ELESELQELEKRLAELEAELASLEEEIKDLEEELKEKNKANEILNDELIALQIENNLLEEK 61
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
302-499 |
9.70e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 38.97 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 302 VERLHEVTQK---AERSERNLQLQLFMAQQEQRRLRKELRAQQGLAPEPRAPGTLPEADPSARPEEEARWEVCQKTAEis 378
Cdd:PTZ00121 1229 VKKAEEAKKDaeeAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADE-- 1306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1351503585 379 lLKQQLREA-QAELAQKLAEIFSLKTQLRGSRAQAQAQDAELVQLREAVRSLQEQAPREEApgscETDDCKSrgllgeag 457
Cdd:PTZ00121 1307 -AKKKAEEAkKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA----EAAEKKK-------- 1373
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1351503585 458 gSEARDSAEQLRAElLQERLRGQEQALRFEQERRTWQEEKER 499
Cdd:PTZ00121 1374 -EEAKKKADAAKKK-AEEKKKADEAKKKAEEDKKKADELKKA 1413
|
|
| |
