|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
182-493 |
1.45e-135 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 396.21 E-value: 1.45e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 182 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKL-QFYQNRECCQSNLEPLFEGYIETLRREAECVEADSGRLASELNHV 260
Cdd:pfam00038 1 NEKEQLQELNDRLASYIDKVRFLEQQNKLLETKIsELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 261 QEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEIRVLQSHISDTSVVVKL 340
Cdd:pfam00038 81 RLAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 341 DNSRDLNMDCIIAEIKAQYDDIVTRSRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQN 420
Cdd:pfam00038 161 DAARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530400236 421 SKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQR 493
Cdd:pfam00038 241 ASLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
81-179 |
4.99e-15 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 72.77 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 81 GSYCGGRAF---SCISACGPR---PGRCCITAAPYRGISCYRGLTGGFGSHS---VCGGFRAGSCGRS------------ 139
Cdd:pfam16208 32 GGGGGGGGFgsrSLYNLGGSKsisISVAGGGSRPGSGFGFGGGGGGGFGGGFgggGGGGFGGGGGFGGgfggggyggggf 111
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 530400236 140 ----FGYRSGGVCGPSPP-CITTVSVNESLLTPLNLEIDPNAQCV 179
Cdd:pfam16208 112 ggggFGGRGGFGGPPCPPgGIQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
182-513 |
1.78e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 70.48 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 182 EEKEQIKSLNSRFAAFIDKVRflEQQNKLLETKLQFYQNRECcQSNLEPlFEGYI-----ETLRREAECVEADSGRLASE 256
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKR--QQLERLRREREKAERYQAL-LKEKRE-YEGYEllkekEALERQKEAIERQLASLEEE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 257 LNHVQEVLEGYKKKYEEEVSLRATA--------ENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFL---RRLYEEEIR 325
Cdd:TIGR02169 253 LEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAeerLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 326 VLQSHISDTSVVVKLDNSRDLNMDCIIAEIKAQYDDIVTRSRAEAESWYRSKCEEMKATvirhgETLRRTKEEINELNRM 405
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYR-----EKLEKLKREINELKRE 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 406 IQRLTAEVENAKCQNSKLEAAVAQSEQ---QGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMN---------SK 473
Cdd:TIGR02169 408 LDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEeydrvekelSK 487
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 530400236 474 LGLDIEIATYRRLLEGEEQRlceGVGSVNVCVSSSRGGVV 513
Cdd:TIGR02169 488 LQRELAEAEAQARASEERVR---GGRAVEEVLKASIQGVH 524
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
181-502 |
1.13e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 55.06 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 181 QEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQN-------RECCQSNLEPLFEGYIETLRREAECVEADSGRL 253
Cdd:TIGR02168 673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEeleqlrkELEELSRQISALRKDLARLEAEVEQLEERIAQL 752
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 254 ASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLY---EEEIRVLQSH 330
Cdd:TIGR02168 753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERR 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 331 ISDT--SVVVKLDNSRDLNMDciIAEIKAQYDDIVT---RSRAEAESWYRSKcEEMKATVIRHGETLRRTKEEINELNRM 405
Cdd:TIGR02168 833 IAATerRLEDLEEQIEELSED--IESLAAEIEELEElieELESELEALLNER-ASLEEALALLRSELEELSEELRELESK 909
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 406 IQRLTAEVENAKCQNSKLEAAVAQSEQQgeaalsdarckLAELEGALqkakqdMACLIREYQEVMNSKLGLDIEIATYRR 485
Cdd:TIGR02168 910 RSELRRELEELREKLAQLELRLEGLEVR-----------IDNLQERL------SEEYSLTLEEAEALENKIEDDEEEARR 972
|
330 340
....*....|....*....|
gi 530400236 486 ---LLEGEEQRLcegvGSVN 502
Cdd:TIGR02168 973 rlkRLENKIKEL----GPVN 988
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
238-455 |
2.27e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 238 TLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALiqeidflr 317
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKL-------- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 318 rlyEEEIRVLQSHISDtsVVVKLDNSRDL--NM-------DCIIAE---IKAQYDDivTRSRAEAESwyRSKceEMKA-T 384
Cdd:pfam01576 572 ---EKTKNRLQQELDD--LLVDLDHQRQLvsNLekkqkkfDQMLAEekaISARYAE--ERDRAEAEA--REK--ETRAlS 640
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530400236 385 VIRHGETLRRTKEEINELNRMiqrLTAEVE---NAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKA 455
Cdd:pfam01576 641 LARALEEALEAKEELERTNKQ---LRAEMEdlvSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQAT 711
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
236-485 |
2.53e-06 |
|
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: 49.76 E-value: 2.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 236 IETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVdcaylrkSDLEANVEALIQEIDF 315
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-------AELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 316 LRRLYEEEIRVLQSHISDTSVVVKLdNSRDLNmdciIAEIKAQYDDIVTRSRAEaeswyrskceemkatvirHGETLRRT 395
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALLL-SPEDFL----DAVRRLQYLKYLAPARRE------------------QAEELRAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 396 KEEINELNRMIQRLTAEVEnakcqnsKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLG 475
Cdd:COG4942 159 LAELAALRAELEAERAELE-------ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
250
....*....|
gi 530400236 476 LDIEIATYRR 485
Cdd:COG4942 232 LEAEAAAAAE 241
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
168-488 |
1.30e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.14 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 168 LNLEIDPNAQCVKQEE--KEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNReccQSNLEPLFEgYIETLRREAEC 245
Cdd:PRK03918 174 IKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKE---VKELEELKE-EIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 246 VEADSGRLASELNHVQEVLEGYKKKYEEevsLRATAEnEFVALKKDVDcAYLRKSDLEANVEALIQEIDFLRRLYEEEIR 325
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEE---LEEKVK-ELKELKEKAE-EYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 326 VLQSHISDTSVvvklDNSRDLNMDCIIAEIKAQYDDIVTRSR---------AEAESWYRSKCEEMKATVIRHGETLRRTK 396
Cdd:PRK03918 325 GIEERIKELEE----KEERLEELKKKLKELEKRLEELEERHElyeeakakkEELERLKKRLTGLTPEKLEKELEELEKAK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 397 EE----INELNRMIQRLTAEVENAKCQNSKLEAAVAQ--------SEQQGEAALSDARCKLAELEGALQKAKQDMACLIR 464
Cdd:PRK03918 401 EEieeeISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
330 340
....*....|....*....|....
gi 530400236 465 EYQEVmNSKLGLDIEIATYRRLLE 488
Cdd:PRK03918 481 ELREL-EKVLKKESELIKLKELAE 503
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
267-494 |
1.57e-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: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 267 YKKKYEE-EVSLRATAEN----EFVA--LKKDVDcaylrksDLEANVEALIQEIDflrrlYEEEIRVLQSHISDTSVVVK 339
Cdd:TIGR02168 170 YKERRKEtERKLERTRENldrlEDILneLERQLK-------SLERQAEKAERYKE-----LKAELRELELALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 340 LDNSRDLNMdcIIAEIKAQYDDIVTRSRAEAESW--YRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAK 417
Cdd:TIGR02168 238 REELEELQE--ELKEAEEELEELTAELQELEEKLeeLRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 418 CQNSKLEAAVAQSEQQGE---AALSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQRL 494
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDelaEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
180-470 |
8.01e-05 |
|
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: 45.27 E-value: 8.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 180 KQEEKEQIKSLNSRfAAFIDKVRFLEQQNKLLETKLQfyQNREccqsNLEPLFEGYIETLRREAECVEADSGRLASELNH 259
Cdd:pfam07888 55 RQREKEKERYKRDR-EQWERQRRELESRVAELKEELR--QSRE----KHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 260 VQEVLE-------GYKKKYEEEVSLRATAE--NEFVALKKDVdcaYLRKSDLEANVEALIQEidfLRRLYEE-------- 322
Cdd:pfam07888 128 EARIREleediktLTQRVLERETELERMKEraKKAGAQRKEE---EAERKQLQAKLQQTEEE---LRSLSKEfqelrnsl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 323 -----EIRVLQSHISDTSVVVKLDNSRDLNMDCIIAE-----------------IKAQYDDIVT-RSRAEAEsWYRSKCE 379
Cdd:pfam07888 202 aqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrslqerlnaserkvegLGEELSSMAAqRDRTQAE-LHQARLQ 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 380 ----------------EMKATVIRHGETLRRT----KEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALS 439
Cdd:pfam07888 281 aaqltlqladaslalrEGRARWAQERETLQQSaeadKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLS 360
|
330 340 350
....*....|....*....|....*....|.
gi 530400236 440 DARCKLAELEGALQKAKQDMACLIREYQEVM 470
Cdd:pfam07888 361 ESRRELQELKASLRVAQKEKEQLQAEKQELL 391
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
169-468 |
1.15e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.28 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 169 NLEIDPNAQcVKQEEKEQIKSLnsRFAAFIDKVRFLEQQNKLL-ETKLQFYQNRECCQSNLEPLfEGYIETLrrEAECVE 247
Cdd:PLN02939 108 IAAIDNEQQ-TNSKDGEQLSDF--QLEDLVGMIQNAEKNILLLnQARLQALEDLEKILTEKEAL-QGKINIL--EMRLSE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 248 ADSG-RLASELNHVQEVLEGYKKKYEEEVSLRATAENEFV-ALKKDVDCAYLRKSDLEANVEALIQEIdflrrlyeeeir 325
Cdd:PLN02939 182 TDARiKLAAQEKIHVEILEEQLEKLRNELLIRGATEGLCVhSLSKELDVLKEENMLLKDDIQFLKAEL------------ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 326 vlqSHISDT-SVVVKLDNSRDLnMDCIIAEIKAQY----DDIVTRSRAEAESWYrskceemkatvirhgetlrrtkEEIN 400
Cdd:PLN02939 250 ---IEVAETeERVFKLEKERSL-LDASLRELESKFivaqEDVSKLSPLQYDCWW----------------------EKVE 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 401 ELNRMIQRLTAEVENAKC---QNSKLEAAVAQSEQQ-GEAALSDARC--------KLAELEGALQKAKQDMACLIREYQE 468
Cdd:PLN02939 304 NLQDLLDRATNQVEKAALvldQNQDLRDKVDKLEASlKEANVSKFSSykvellqqKLKLLEERLQASDHEIHSYIQLYQE 383
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
182-494 |
2.35e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 182 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLET-------------KLQFYQNRECC--QSNLEPLFEGYiETLRREAECV 246
Cdd:TIGR04523 93 KNKDKINKLNSDLSKINSEIKNDKEQKNKLEVelnklekqkkenkKNIDKFLTEIKkkEKELEKLNNKY-NDLKKQKEEL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 247 EADSGRLASELNHVQE-----------------VLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEAL 309
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKnidkiknkllklelllsNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 310 IQEIDFLRRLYEEEIRVLQSHISDtsvvVKLDNSRDLNMDCIIAEIKAQYDDIVTRSRAEAESWYRSKCEEMKATVIRHG 389
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKE----LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 390 ETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEgALQKAKQDMACLIREYQEV 469
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIK-NLESQINDLESKIQNQEKL 406
|
330 340
....*....|....*....|....*...
gi 530400236 470 MNSKlglDIEIATY---RRLLEGEEQRL 494
Cdd:TIGR04523 407 NQQK---DEQIKKLqqeKELLEKEIERL 431
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
275-468 |
2.92e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 2.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 275 VSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLY---EEEIRVLQSHISDTSvvvklDNSRDLNmdci 351
Cdd:COG3883 8 APTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYnelQAELEALQAEIDKLQ-----AEIAEAE---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 352 iAEIKAQYDDIVTRSRAEAESWYRSKCEEM------KATVIRHGETLRR----TKEEINELNRMIQRLT---AEVENAKC 418
Cdd:COG3883 79 -AEIEERREELGERARALYRSGGSVSYLDVllgsesFSDFLDRLSALSKiadaDADLLEELKADKAELEakkAELEAKLA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 530400236 419 QNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMACLIREYQE 468
Cdd:COG3883 158 ELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAA 207
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
233-449 |
3.50e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.47 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 233 EGYIETLrreaecVEADSGRLASELNHVQEVLEGYKKKYEE-EVSLRA-TAENEFVALKKDVDCAYLRKSDLEANVEALI 310
Cdd:COG3206 159 EAYLEQN------LELRREEARKALEFLEEQLPELRKELEEaEAALEEfRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 311 QEIDFLRRLYEEeirvLQSHISDTSvvvklDNSRDLNMDCIIAEIKAQYDDIVTRsRAEAESWYRSKCEEMKATVirhgE 390
Cdd:COG3206 233 AELAEAEARLAA----LRAQLGSGP-----DALPELLQSPVIQQLRAQLAELEAE-LAELSARYTPNHPDVIALR----A 298
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 391 TLRRTKEEIN-ELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGeAALSDARCKLAELE 449
Cdd:COG3206 299 QIAALRAQLQqEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELPELEAELRRLE 357
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
237-502 |
3.74e-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: 43.52 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 237 ETLRREAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFL 316
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 317 RRL-----------------YEEEIRVLQSHISDTSVVVKLDNSRDLNMdcIIAEIKAQYDDI----------------- 362
Cdd:TIGR02169 757 KSElkelearieeleedlhkLEEALNDLEARLSHSRIPEIQAELSKLEE--EVSRIEARLREIeqklnrltlekeyleke 834
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 363 ---VTRSRAEAESWYRSKCEEMKATVIRHGETLRRTKEEINELNRMIQR---LTAEVENAKCQNSKLEaavaQSEQQGEA 436
Cdd:TIGR02169 835 iqeLQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELE----RKIEELEA 910
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530400236 437 ALSDARCKLAELEGALQKAKQDMACL---IREYQEVMNSKLGLDIEIATYRRLlegeEQRLcEGVGSVN 502
Cdd:TIGR02169 911 QIEKKRKRLSELKAKLEALEEELSEIedpKGEDEEIPEEELSLEDVQAELQRV----EEEI-RALEPVN 974
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
351-468 |
4.18e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 351 IIAEIKAQYDDIvtrsRAEAESWYRSKCEEMKA---TVIRHGETLRRTKEEI----NELNRMIQRLTAEVENAKCQNSKL 423
Cdd:PRK12704 58 ALLEAKEEIHKL----RNEFEKELRERRNELQKlekRLLQKEENLDRKLELLekreEELEKKEKELEQKQQELEKKEEEL 133
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 530400236 424 EAAVAQSEQQGE--AALS--DARCKLaeLEGALQKAKQDMACLIREYQE 468
Cdd:PRK12704 134 EELIEEQLQELEriSGLTaeEAKEIL--LEKVEEEARHEAAVLIKEIEE 180
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
181-456 |
4.75e-04 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 43.09 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 181 QEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFyqnreccQSNLEPLFEGYIETLRREAECVEADSGRLASELNHV 260
Cdd:TIGR04523 366 EEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQN-------QEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKN 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 261 QEVLEGYKKK-------YEEEVSLRATAENEFVALKKDVDCAylrKSDLEANVEAL---IQEIDFL---RRLYEEEIRVL 327
Cdd:TIGR04523 439 NSEIKDLTNQdsvkeliIKNLDNTRESLETQLKVLSRSINKI---KQNLEQKQKELkskEKELKKLneeKKELEEKVKDL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 328 QSHISDTsvvvkLDNSRDLNMDciIAEIKAQYDDIvtrsraeaeswyRSKCEEMKatvirhgETLRRT--KEEINELNRM 405
Cdd:TIGR04523 516 TKKISSL-----KEKIEKLESE--KKEKESKISDL------------EDELNKDD-------FELKKEnlEKEIDEKNKE 569
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 530400236 406 IQRLTAEVENAKCQNSKLEAAVAQSEQQ-----GEAALSDArcKLAELEGALQKAK 456
Cdd:TIGR04523 570 IEELKQTQKSLKKKQEEKQELIDQKEKEkkdliKEIEEKEK--KISSLEKELEKAK 623
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
180-452 |
5.14e-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: 43.12 E-value: 5.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 180 KQEEKEQIKSLNSRFAAFIDKV-----RFLEQQNKL--LETKLQFYQNR-ECCQSNLEPLfEGYIETLRREAECVEADSG 251
Cdd:TIGR02168 262 LQELEEKLEELRLEVSELEEEIeelqkELYALANEIsrLEQQKQILRERlANLERQLEEL-EAQLEELESKLDELAEELA 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 252 RLASELNHVQEVLEGYKKKYEEEVSLRATAEN-------EFVALKKDVDCAYL--------------RKSDLEANVEALI 310
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESrleeleeQLETLRSKVAQLELqiaslnneierleaRLERLEDRRERLQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 311 QEIDFLRRLYEEeirvlqshisdtsvvvkldnsrdlnmdciiAEIKAQYDDIVTRSRAEaeswyrskcEEMKATVIRHGE 390
Cdd:TIGR02168 421 QEIEELLKKLEE------------------------------AELKELQAELEELEEEL---------EELQEELERLEE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530400236 391 TLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAV--AQSEQQGEAALSDARCKLAELEGAL 452
Cdd:TIGR02168 462 ALEELREELEEAEQALDAAERELAQLQARLDSLERLQenLEGFSEGVKALLKNQSGLSGILGVL 525
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-494 |
1.26e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 352 IAEIKAQYDDIVTRSRAEAESW--YRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQ 429
Cdd:COG1196 248 LEELEAELEELEAELAELEAELeeLRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAE 327
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530400236 430 SEQQGEAALSdarcKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEIATYRRLLEGEEQRL 494
Cdd:COG1196 328 LEEELEELEE----ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
189-442 |
1.42e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 41.54 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 189 SLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNReccqsnleplfegyIETLRREAECVEadsgrLASELNHVQEVLEGYK 268
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEAEAA--------------LEEFRQKNGLVD-----LSEEAKLLLQQLSELE 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 269 KKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEAN--VEALIQEIDFLRRLYEEEIRVLQShisDTSVVVKLDNSrdl 346
Cdd:COG3206 226 SQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSpvIQQLRAQLAELEAELAELSARYTP---NHPDVIALRAQ--- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 347 nmdciIAEIKAQYDDIVTRSRAEAESWYrskcEEMKATVIRHGETLRRTKEEINELNRM---IQRLTAEVENAKCQNSKL 423
Cdd:COG3206 300 -----IAALRAQLQQEAQRILASLEAEL----EALQAREASLQAQLAQLEARLAELPELeaeLRRLEREVEVARELYESL 370
|
250
....*....|....*....
gi 530400236 424 EAAVAQSEQQGEAALSDAR 442
Cdd:COG3206 371 LQRLEEARLAEALTVGNVR 389
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
379-494 |
1.43e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 41.38 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 379 EEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVEnakcqnsKLEAAVAQSEQQgeaalsdarckLAELEGALQKAKQD 458
Cdd:COG2433 395 PEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVE-------ELEAELEEKDER-----------IERLERELSEARSE 456
|
90 100 110
....*....|....*....|....*....|....*.
gi 530400236 459 MACLIREYQEVMNsklgLDIEIATYRRLLEGEEQRL 494
Cdd:COG2433 457 ERREIRKDREISR----LDREIERLERELEEERERI 488
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
169-485 |
1.47e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 169 NLEIDPNAQCVKQEEK------EQIKSLNSRFAAFIDKVRFLEQQ----NKLLETKLQFYQNRECCQSNLEPLFEGYIET 238
Cdd:PRK01156 196 NLELENIKKQIADDEKshsitlKEIERLSIEYNNAMDDYNNLKSAlnelSSLEDMKNRYESEIKTAESDLSMELEKNNYY 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 239 LRREAECVEADSGRLASELNHV-------------QEVLEGYK---KKYEEEVSLRATAE---NEFVALKKDVDCAYLRK 299
Cdd:PRK01156 276 KELEERHMKIINDPVYKNRNYIndyfkykndienkKQILSNIDaeiNKYHAIIKKLSVLQkdyNDYIKKKSRYDDLNNQI 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 300 SDL---EANVEALIQEIDFL---RRLYEEEIRVLQSHISDTSVVVKLDNSRdlnMDCIIAEIKAQYDDIVTR-------- 365
Cdd:PRK01156 356 LELegyEMDYNSYLKSIESLkkkIEEYSKNIERMSAFISEILKIQEIDPDA---IKKELNEINVKLQDISSKvsslnqri 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 366 ----------SRAEAESWYRSKC--------EEMKATVIRH-GETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAA 426
Cdd:PRK01156 433 ralrenldelSRNMEMLNGQSVCpvcgttlgEEKSNHIINHyNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEYLESE 512
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 530400236 427 VAQSEQQGEAALSDARCKLAELEGALQKAKQDMAclirEYQEVMNSKLGLDIEIATYRR 485
Cdd:PRK01156 513 EINKSINEYNKIESARADLEDIKIKINELKDKHD----KYEEIKNRYKSLKLEDLDSKR 567
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
236-458 |
1.79e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 236 IETLRREAECVEADSGRLASELNHVQEVlegykKKYEEEVSLRATAENEFVALKKDVdcaylRKSDLEANVEAlIQEIDF 315
Cdd:PTZ00121 1166 AEEARKAEDAKKAEAARKAEEVRKAEEL-----RKAEDARKAEAARKAEEERKAEEA-----RKAEDAKKAEA-VKKAEE 1234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 316 LRRLYEEEIRVlqSHISDTSVVVKLDNSRDLNMDCIIAEIKAQYDDIVTRSRAEAEswyRSKCEEM-KATVIRHGETLRR 394
Cdd:PTZ00121 1235 AKKDAEEAKKA--EEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEE---KKKADEAkKAEEKKKADEAKK 1309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530400236 395 TKEEinelNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQD 458
Cdd:PTZ00121 1310 KAEE----AKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA 1369
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
246-494 |
2.41e-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: 40.81 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 246 VEADSGRLA--SELNHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRR---LY 320
Cdd:TIGR02168 666 AKTNSSILErrREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAeveQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 321 EEEIRVLQSHISDTSVVVKLDNSRDLNMDCIIAEIKAQyddivtrsRAEAESWYRSKCEEMKATvirhGETLRRTKEEIN 400
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE--------IEELEAQIEQLKEELKAL----REALDELRAELT 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 401 ELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMACLIREYQEVMNSKLGLDIEI 480
Cdd:TIGR02168 814 LLNEEAANLRERLESLERRIAATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
250
....*....|....
gi 530400236 481 ATYRRLLEGEEQRL 494
Cdd:TIGR02168 890 ALLRSELEELSEEL 903
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
390-474 |
2.63e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 390 ETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMACLIREYQEV 469
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE----IAEREEELKELEEQLESLQEELAALEQELQAL 176
|
....*
gi 530400236 470 MNSKL 474
Cdd:COG4372 177 SEAEA 181
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
302-494 |
2.95e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 302 LEANVEALIQEIDFLRRLyEEEIRVLQSHISdtsvvvKLDNSRDLnmdciIAEIKAQYDDIVTRSRAEAEswYRSKCEEM 381
Cdd:COG4717 83 AEEKEEEYAELQEELEEL-EEELEELEAELE------ELREELEK-----LEKLLQLLPLYQELEALEAE--LAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 382 katvirhgETLRRTKEEINELNRMIQRLTAEVENAKcqnSKLEAAVAQSEQQGEAALSDARCKLAELEGALQKAKQDMAC 461
Cdd:COG4717 149 --------EELEERLEELRELEEELEELEAELAELQ---EELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEE 217
|
170 180 190
....*....|....*....|....*....|...
gi 530400236 462 LIREYQEVMNsklglDIEIATYRRLLEGEEQRL 494
Cdd:COG4717 218 AQEELEELEE-----ELEQLENELEAAALEERL 245
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
392-494 |
3.08e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 3.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 392 LRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQ---GEAALSDARCKLAELEGALQKAKQDMACLIREYQE 468
Cdd:COG4372 47 LEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQlqaAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126
|
90 100
....*....|....*....|....*.
gi 530400236 469 VMNSKLGLDIEIATYRRLLEGEEQRL 494
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEEL 152
|
|
| TMCO5 |
pfam14992 |
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing ... |
303-490 |
3.41e-03 |
|
TMCO5 family; The TMCO5 family includes human transmembrane and coiled-coil domain-containing proteins 5A and 5B.
Pssm-ID: 464427 [Multi-domain] Cd Length: 278 Bit Score: 39.70 E-value: 3.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 303 EANVEAL--IQEidflrrlYEEEIRVLQSHISDTSVVVKLDNSRDLNmdCIIAEikaqyddivtRSRAEAEswyrskCEE 380
Cdd:pfam14992 17 EANQVLLlkIQE-------KEEEIQSLEREITLTRSLAEDEEREELN--FTIME----------KEDALQE------LEL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 381 MKATVIRHGETLRRtkeEINELNRMIQRltAEVENAKCQNSKLEAAVAQSE---QQGEAALSDARCKLAELEGALQKAKQ 457
Cdd:pfam14992 72 ETAKLEKKNEILVK---SVMELQRKLSR--KSDKNTGLEQETLKQMLEELKvklQQSEESCADQEKELAKVESDYQSVHQ 146
|
170 180 190
....*....|....*....|....*....|....*.
gi 530400236 458 ---DMACLIREYQEVMNSklgldIEIATYRRLLEGE 490
Cdd:pfam14992 147 lceDQALCIKKYQEILRK-----MEEEKETRLLEKE 177
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
182-334 |
4.49e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 40.05 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 182 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQ---FYQNRECCQ--SNLEPLFEGYIE----------------TLR 240
Cdd:PRK03918 546 KELEKLEELKKKLAELEKKLDELEEELAELLKELEelgFESVEELEErlKELEPFYNEYLElkdaekelereekelkKLE 625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 241 REAECVEADSGRLASELNHVQEVLEGYKKKYEEEVSLRatAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFL---- 316
Cdd:PRK03918 626 EELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKLkeel 703
|
170 180
....*....|....*....|
gi 530400236 317 --RRLYEEEIRVLQSHISDT 334
Cdd:PRK03918 704 eeREKAKKELEKLEKALERV 723
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
181-494 |
5.07e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 181 QEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQF---YQNRECCQSNLEPLFEGYIETLRREAECVEA--DSGRLAS 255
Cdd:COG4717 91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLlplYQELEALEAELAELPERLEELEERLEELRELeeELEELEA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 256 ELNHVQEVLEgykkkyEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYE------------EE 323
Cdd:COG4717 171 ELAELQEELE------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEqleneleaaaleER 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 324 IRVLQSHISDTSVVVKLDNSRDLNMDCII---------------------------AEIKAQYDDIVTRSRAEAESW--- 373
Cdd:COG4717 245 LKEARLLLLIAAALLALLGLGGSLLSLILtiagvlflvlgllallflllarekaslGKEAEELQALPALEELEEEELeel 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 374 ---YRSKCEEMKATVIRHGETLRRTKEEINELNRMIQRLTAEVENAKcQNSKLEAAVAQSEQQGEAALSDARcKLAELEG 450
Cdd:COG4717 325 laaLGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE-IAALLAEAGVEDEEELRAALEQAE-EYQELKE 402
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 530400236 451 ALQKAKQDMACLIREYQEVM--NSKLGLDIEIATYRRLLEGEEQRL 494
Cdd:COG4717 403 ELEELEEQLEELLGELEELLeaLDEEELEEELEELEEELEELEEEL 448
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
180-458 |
6.02e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 39.56 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 180 KQEEKEQIKSLNSRFAAFIDKVRflEQQNKLLETKLQFYQNRECCQSNleplfegyIETLRREAECV--EADSGRLASEL 257
Cdd:COG5185 310 ATESLEEQLAAAEAEQELEESKR--ETETGIQNLTAEIEQGQESLTEN--------LEAIKEEIENIvgEVELSKSSEEL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 258 NHVQEVLEGYKKKYEEEVSLRATAENEFVALKKDvdcaylRKSDLEANVEALIQEIDFLRRLYEEEIRVLqshisdtsvv 337
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLED------TLKAADRQIEELQRQIEQATSSNEEVSKLL---------- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 338 VKLDNSRDLNMDCIIAEIKAQYDDivtrsraeaeswyrskceemkatviRHGETLRRTKEEINELNRMIQRLTAEVENAK 417
Cdd:COG5185 444 NELISELNKVMREADEESQSRLEE-------------------------AYDEINRSVRSKKEDLNEELTQIESRVSTLK 498
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 530400236 418 CQNSKLEAAvaqseqqGEAALSDARCKLAELEGALQKAKQD 458
Cdd:COG5185 499 ATLEKLRAK-------LERQLEGVRSKLDQVAESLKDFMRA 532
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
182-502 |
6.62e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 39.34 E-value: 6.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 182 EEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQN--RECCQSNLEPlfegyiETLRREAECVeadsgrLASELNH 259
Cdd:pfam05557 228 EEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKlaQDTGLNLRSP------EDLSRRIEQL------QQREIVL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 260 VQEVLEGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSD------LEANVEALIQEIDFLRRLYEEEIRVLQSHISD 333
Cdd:pfam05557 296 KEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHkalvrrLQRRVLLLTKERDGYRAILESYDKELTMSNYS 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 334 TSVVVKLDNSRDL--NMDCIIAEIKAQYddivtrSRAEAE-SWYRSKCE--EMKATVIRHGETLR---RTKEEINELNRM 405
Cdd:pfam05557 376 PQLLERIEEAEDMtqKMQAHNEEMEAQL------SVAEEElGGYKQQAQtlERELQALRQQESLAdpsYSKEEVDSLRRK 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 406 IQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSdaRCKLAEL-EGALQKAKQDMACLIREYQEvmnsklgldiEIATYR 484
Cdd:pfam05557 450 LETLELERQRLREQKNELEMELERRCLQGDYDPK--KTKVLHLsMNPAAEAYQQRKNQLEKLQA----------EIERLK 517
|
330
....*....|....*...
gi 530400236 485 RLLEGEEQRLcEGVGSVN 502
Cdd:pfam05557 518 RLLKKLEDDL-EQVLRLP 534
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
390-487 |
8.09e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 38.59 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 390 ETLRRTKEEINELNRMIQRLTAEVENAKCQNSKLEAAVAQSEQQgeaaLSDARCKLAELEGALQKAKQDMACLIREYQEV 469
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR----IAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90
....*....|....*...
gi 530400236 470 MNSklgLDIEIATYRRLL 487
Cdd:COG4942 96 RAE---LEAQKEELAELL 110
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
156-318 |
9.31e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 39.13 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 156 TTVSVNESLLTPLNLEIdpnAQCVKQEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNRecCQSN----LEPL 231
Cdd:COG4913 269 ERLAELEYLRAALRLWF---AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQ--IRGNggdrLEQL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 232 fEGYIETLRREAECVEADSGRLASELNHVQEVL----EGYKKKYEEEVSLRATAENEFVALKKDVDCAYLRKSDLEANVE 307
Cdd:COG4913 344 -EREIERLERELEERERRRARLEALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170
....*....|.
gi 530400236 308 ALIQEIDFLRR 318
Cdd:COG4913 423 ELEAEIASLER 433
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
170-468 |
9.94e-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: 38.80 E-value: 9.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 170 LEIDPNAQCVKQEEKEQIKSLNSRFAAFIDKVRFLEQQNKLLETKLQFYQNReccQSNLEPLFEGY----IETLRREAEC 245
Cdd:TIGR00618 357 IRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQRE---QATIDTRTSAFrdlqGQLAHAKKQQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 246 vEADSGRLASELNHVQEVLEGYKKKYEEEVSL-RATAENEFvaLKKDVDCAYLRKSDLEANVEALIQEIDFLRRLYEEEI 324
Cdd:TIGR00618 434 -ELQQRYAELCAAAITCTAQCEKLEKIHLQESaQSLKEREQ--QLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSC 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 325 RVLQSHI-------SDTSVVVKLDNS--------RDLNMDCI-----IAEIKAQYDDIVTRSRAEAESWYRSKCEEMKAT 384
Cdd:TIGR00618 511 IHPNPARqdidnpgPLTRRMQRGEQTyaqletseEDVYHQLTserkqRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530400236 385 -----VIRHGETLRRTKEEINELNRmIQRLTAEVENAKCQNSKLEAAVAQSEQQGEAALSdarcklAELEGALQKAKQDM 459
Cdd:TIGR00618 591 nitvrLQDLTEKLSEAEDMLACEQH-ALLRKLQPEQDLQDVRLHLQQCSQELALKLTALH------ALQLTLTQERVREH 663
|
....*....
gi 530400236 460 ACLIREYQE 468
Cdd:TIGR00618 664 ALSIRVLPK 672
|
|
| |
