|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
120-430 |
7.49e-131 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 382.73 E-value: 7.49e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 120 EKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCCQ-TNIEPIFEGYISALRRQLDCVSGDRVRLESELCSLQ 198
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 199 AALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEEICLLQSQISETSVIVKMD 278
Cdd:pfam00038 82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 279 NSRELDVDSIIAEIKAQYDDIASRSKAEAEAWYQCRYEELRVTAGNHCDNLRNRKNEILEMNKLIQWLQQETENVKAQRC 358
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468491673 359 KLEGAIAEAEQQGEAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 430
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
61-116 |
1.21e-11 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 62.75 E-value: 1.21e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2468491673 61 GFGRPRVASRCGGTlPGFGYRLG---ATCGPSAcITPVTINESLLVPLALEIDPTVQRV 116
Cdd:pfam16208 100 GFGGGGYGGGGFGG-GGFGGRGGfggPPCPPGG-IQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-439 |
5.95e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 118 RDEKEQIKclnNRFASFINKVRFLEQKNKLLETKWNFMQQQRccQTNIEPI--FEGYISALRRQLDCVSGDRVRLESELC 195
Cdd:TIGR02169 694 QSELRRIE---NRLDELSQELSDASRKIGEIEKEIEQLEQEE--EKLKERLeeLEEDLSSLEQEIENVKSELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 196 SLQAALEgykkKYEEELslrpcvenefvalkkdvdtaflmkADLETN-AEALVQEIDFLKSLYEEEICLLQSQISETSVI 274
Cdd:TIGR02169 769 ELEEDLH----KLEEAL------------------------NDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 275 VKMDNSRELDVDSIIAEIKAQYDDIASRSKAEAEawyqcRYEELRVTAGNHCDNLRNRKNEILEMNKLIQWLQQETENVK 354
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK-----EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 355 AQRCKLEgaiaEAEQQGEAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEvMNSKLGLDIEIATYRRLLEGEEHRLcEG 434
Cdd:TIGR02169 896 AQLRELE----RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-DEEIPEEELSLEDVQAELQRVEEEI-RA 969
|
....*
gi 2468491673 435 IGPVN 439
Cdd:TIGR02169 970 LEPVN 974
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
145-406 |
1.57e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 145 NKLLEtkwNFMQQQRccQTNIEPIfEGYISALRRQLDcvsgdrvRLESELCSLQAALEGYKKKyeeelslrpcveNEFVA 224
Cdd:COG3206 155 NALAE---AYLEQNL--ELRREEA-RKALEFLEEQLP-------ELRKELEEAEAALEEFRQK------------NGLVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 225 LKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEeiclLQSQISETSvivkmDNSRELDVDSIIAEIKAQYddiasrsk 304
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGSGP-----DALPELLQSPVIQQLRAQL-------- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 305 AEAEAwyqcRYEELRVTAG-NHCD--NLRNRKNEIL-----EMNKLIQWLQQETENVKAQRCKLEGAIAEAEQQGeAALN 376
Cdd:COG3206 273 AELEA----ELAELSARYTpNHPDviALRAQIAALRaqlqqEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELP 347
|
250 260 270
....*....|....*....|....*....|
gi 2468491673 377 DAKCKLAGLEEALQKAKQDMACLLKEYQEV 406
Cdd:COG3206 348 ELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
108-428 |
4.92e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 108 EIDPTVQRVKRDE-KEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCC--------QTNIEPIFEGY---ISA 175
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCpvcgttlgEEKSNHIINHYnekKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 176 LRRQLDCVSGDRVRLESE---LCSLQAALEGYK-KKYEEELSLRPCVENEFVALKKDVDTAflmkADLETNAEALVQE-- 249
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKivdLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINEL----KDKHDKYEEIKNRyk 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 250 ---IDFLKSLYEEEICLLqSQISetsvIVKMDNSReldvdSIIAEIKAQYDDIASRSK------AEAEAWYQCRYEELRv 320
Cdd:PRK01156 557 slkLEDLDSKRTSWLNAL-AVIS----LIDIETNR-----SRSNEIKKQLNDLESRLQeieigfPDDKSYIDKSIREIE- 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 321 tagNHCDNLRNRKNEILEMNKLIQWLQQETENVKAQRCKLEGaIAEAEQQGEAALNDAKCKLAGLEEALQKAKQDMAcLL 400
Cdd:PRK01156 626 ---NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS-IIPDLKEITSRINDIEDNLKKSRKALDDAKANRA-RL 700
|
330 340
....*....|....*....|....*....
gi 2468491673 401 KEYQEVMNSKLG-LDIEIATYRRLLEGEE 428
Cdd:PRK01156 701 ESTIEILRTRINeLSDRINDINETLESMK 729
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Filament |
pfam00038 |
Intermediate filament protein; |
120-430 |
7.49e-131 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 382.73 E-value: 7.49e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 120 EKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCCQ-TNIEPIFEGYISALRRQLDCVSGDRVRLESELCSLQ 198
Cdd:pfam00038 2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEpSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 199 AALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEEICLLQSQISETSVIVKMD 278
Cdd:pfam00038 82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 279 NSRELDVDSIIAEIKAQYDDIASRSKAEAEAWYQCRYEELRVTAGNHCDNLRNRKNEILEMNKLIQWLQQETENVKAQRC 358
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468491673 359 KLEGAIAEAEQQGEAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRLLEGEEHR 430
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
|
|
| Keratin_2_head |
pfam16208 |
Keratin type II head; |
61-116 |
1.21e-11 |
|
Keratin type II head;
Pssm-ID: 465068 [Multi-domain] Cd Length: 156 Bit Score: 62.75 E-value: 1.21e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2468491673 61 GFGRPRVASRCGGTlPGFGYRLG---ATCGPSAcITPVTINESLLVPLALEIDPTVQRV 116
Cdd:pfam16208 100 GFGGGGYGGGGFGG-GGFGGRGGfggPPCPPGG-IQEVTVNQSLLQPLNLEIDPEIQRV 156
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
98-410 |
1.55e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.96 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 98 NESLLVPLALEIdptvQRVKRDEKEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCCQTNiEPIFEGYISALR 177
Cdd:pfam05483 375 NEDQLKIITMEL----QKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGK-EQELIFLLQARE 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 178 RQLDcvsgdrvRLESELCSLQAALEGYKKKYEEelsLRPCVENEfvALKKDVDTAFLMKADLETnaEALVQEI-DFLKSL 256
Cdd:pfam05483 450 KEIH-------DLEIQLTAIKTSEEHYLKEVED---LKTELEKE--KLKNIELTAHCDKLLLEN--KELTQEAsDMTLEL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 257 YEEEICLLQSQISETSVIVKMDNSRELD------VDSIIAEIKAQYDDIASRSKAEAEAWYQCRYEELRVTAG-----NH 325
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIENLEEKEmnlrdeLESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQmkileNK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 326 CDNLRNrknEILEMNKLIQWLQQETENVKAQrcklegAIAEAEQqgeaaLNDAKCKLAGLEEALQKAKQDMACLLKEYQE 405
Cdd:pfam05483 596 CNNLKK---QIENKNKNIEELHQENKALKKK------GSAENKQ-----LNAYEIKVNKLELELASAKQKFEEIIDNYQK 661
|
....*
gi 2468491673 406 VMNSK 410
Cdd:pfam05483 662 EIEDK 666
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
118-439 |
5.95e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.30 E-value: 5.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 118 RDEKEQIKclnNRFASFINKVRFLEQKNKLLETKWNFMQQQRccQTNIEPI--FEGYISALRRQLDCVSGDRVRLESELC 195
Cdd:TIGR02169 694 QSELRRIE---NRLDELSQELSDASRKIGEIEKEIEQLEQEE--EKLKERLeeLEEDLSSLEQEIENVKSELKELEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 196 SLQAALEgykkKYEEELslrpcvenefvalkkdvdtaflmkADLETN-AEALVQEIDFLKSLYEEEICLLQSQISETSVI 274
Cdd:TIGR02169 769 ELEEDLH----KLEEAL------------------------NDLEARlSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 275 VKMDNSRELDVDSIIAEIKAQYDDIASRSKAEAEawyqcRYEELRVTAGNHCDNLRNRKNEILEMNKLIQWLQQETENVK 354
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK-----EIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 355 AQRCKLEgaiaEAEQQGEAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEvMNSKLGLDIEIATYRRLLEGEEHRLcEG 434
Cdd:TIGR02169 896 AQLRELE----RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE-DEEIPEEELSLEDVQAELQRVEEEI-RA 969
|
....*
gi 2468491673 435 IGPVN 439
Cdd:TIGR02169 970 LEPVN 974
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
112-357 |
1.02e-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: 48.53 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 112 TVQRVKRDEKEQIKCLNNRFASfinKVRFLEQKNKLLETKWNfmQQQRCCQTNIEPI------FEGYISALRRQLDCVSG 185
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEE---IEQLLEELNKKIKDLGE--EEQLRVKEKIGELeaeiasLERSIAEKERELEDAEE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 186 DRVRLESELCSLQAALEGYKKKYEEELSLRPCVENEFVALKKDVDTAFLMKADLETNAEALVQEIDFLK---SLYEEEIC 262
Cdd:TIGR02169 323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYReklEKLKREIN 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 263 LLQSQISETSVIVKMDNSRELDVDSIIAEIKAQYDDIASRSKAEAEAWYQCRY--EELRVTAGNHCDNLRNRKNEILEMN 340
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWklEQLAADLSKYEQELYDLKEEYDRVE 482
|
250
....*....|....*..
gi 2468491673 341 KLIQWLQQETENVKAQR 357
Cdd:TIGR02169 483 KELSKLQRELAEAEAQA 499
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
145-406 |
1.57e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.70 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 145 NKLLEtkwNFMQQQRccQTNIEPIfEGYISALRRQLDcvsgdrvRLESELCSLQAALEGYKKKyeeelslrpcveNEFVA 224
Cdd:COG3206 155 NALAE---AYLEQNL--ELRREEA-RKALEFLEEQLP-------ELRKELEEAEAALEEFRQK------------NGLVD 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 225 LKKDVDTAFLMKADLETNAEALVQEIDFLKSLYEEeiclLQSQISETSvivkmDNSRELDVDSIIAEIKAQYddiasrsk 304
Cdd:COG3206 210 LSEEAKLLLQQLSELESQLAEARAELAEAEARLAA----LRAQLGSGP-----DALPELLQSPVIQQLRAQL-------- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 305 AEAEAwyqcRYEELRVTAG-NHCD--NLRNRKNEIL-----EMNKLIQWLQQETENVKAQRCKLEGAIAEAEQQGeAALN 376
Cdd:COG3206 273 AELEA----ELAELSARYTpNHPDviALRAQIAALRaqlqqEAQRILASLEAELEALQAREASLQAQLAQLEARL-AELP 347
|
250 260 270
....*....|....*....|....*....|
gi 2468491673 377 DAKCKLAGLEEALQKAKQDMACLLKEYQEV 406
Cdd:COG3206 348 ELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
175-430 |
2.04e-05 |
|
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: 47.48 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 175 ALRRQLDCVSGDRVRLESELCSLQAALEGYKKKYEEELSLRPCVENEFVALKKDVDTAflmKADLETNAEAlVQEIDFLK 254
Cdd:pfam01576 500 SLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAL---TQQLEEKAAA-YDKLEKTK 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 255 SLYEEEIcllqsqiseTSVIVKMDNSREL---------DVDSIIAE---IKAQYDDiaSRSKAEAEAwyqcRYEELRVTA 322
Cdd:pfam01576 576 NRLQQEL---------DDLLVDLDHQRQLvsnlekkqkKFDQMLAEekaISARYAE--ERDRAEAEA----REKETRALS 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 323 GNH-CDNLRNRKNEILEMNKLiqwlqqetenvkaQRCKLEGAIAEAEQQGEAALNDAKCKLAgLEEALQKAKQDMACLLK 401
Cdd:pfam01576 641 LARaLEEALEAKEELERTNKQ-------------LRAEMEDLVSSKDDVGKNVHELERSKRA-LEQQVEEMKTQLEELED 706
|
250 260 270
....*....|....*....|....*....|....*...
gi 2468491673 402 EYQEVMNSKLGLDIEI----ATYRRLLE-----GEEHR 430
Cdd:pfam01576 707 ELQATEDAKLRLEVNMqalkAQFERDLQardeqGEEKR 744
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
108-428 |
4.92e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 108 EIDPTVQRVKRDE-KEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRCC--------QTNIEPIFEGY---ISA 175
Cdd:PRK01156 401 EIDPDAIKKELNEiNVKLQDISSKVSSLNQRIRALRENLDELSRNMEMLNGQSVCpvcgttlgEEKSNHIINHYnekKSR 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 176 LRRQLDCVSGDRVRLESE---LCSLQAALEGYK-KKYEEELSLRPCVENEFVALKKDVDTAflmkADLETNAEALVQE-- 249
Cdd:PRK01156 481 LEEKIREIEIEVKDIDEKivdLKKRKEYLESEEiNKSINEYNKIESARADLEDIKIKINEL----KDKHDKYEEIKNRyk 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 250 ---IDFLKSLYEEEICLLqSQISetsvIVKMDNSReldvdSIIAEIKAQYDDIASRSK------AEAEAWYQCRYEELRv 320
Cdd:PRK01156 557 slkLEDLDSKRTSWLNAL-AVIS----LIDIETNR-----SRSNEIKKQLNDLESRLQeieigfPDDKSYIDKSIREIE- 625
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 321 tagNHCDNLRNRKNEILEMNKLIQWLQQETENVKAQRCKLEGaIAEAEQQGEAALNDAKCKLAGLEEALQKAKQDMAcLL 400
Cdd:PRK01156 626 ---NEANNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDS-IIPDLKEITSRINDIEDNLKKSRKALDDAKANRA-RL 700
|
330 340
....*....|....*....|....*....
gi 2468491673 401 KEYQEVMNSKLG-LDIEIATYRRLLEGEE 428
Cdd:PRK01156 701 ESTIEILRTRINeLSDRINDINETLESMK 729
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
121-428 |
1.09e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.05 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 121 KEQIKCLNNRFASFINKVRFLEQKNKLLETKWNFMQQQRccqTNIEPIFEgYISALRRQLDCVSGDRVRLESELCSLQAA 200
Cdd:PRK03918 192 EELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEELKE-EIEELEKELESLEGSKRKLEEKIRELEER 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 201 LEGYKKKYEEelsLRPCVEnEFVALKKDVDTAFLMKADLETNAEALvQEIDFLKSLYEEEICLLQSQISETSvivkmDNS 280
Cdd:PRK03918 268 IEELKKEIEE---LEEKVK-ELKELKEKAEEYIKLSEFYEEYLDEL-REIEKRLSRLEEEINGIEERIKELE-----EKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 281 RELDvdsiiaEIKAQYDDIaSRSKAEAEAWYQcRYEELRVTAGNhCDNLRNRK--NEILEMNKLIQWLQQETENVKAQRC 358
Cdd:PRK03918 338 ERLE------ELKKKLKEL-EKRLEELEERHE-LYEEAKAKKEE-LERLKKRLtgLTPEKLEKELEELEKAKEEIEEEIS 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 359 KLEGAIAEAEQQGE---AALND-----AKCKLAGLE-------EALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRRL 423
Cdd:PRK03918 409 KITARIGELKKEIKelkKAIEElkkakGKCPVCGRElteehrkELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKV 488
|
....*
gi 2468491673 424 LEGEE 428
Cdd:PRK03918 489 LKKES 493
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
222-416 |
2.80e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.75 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 222 FVALK--KDVDTAF----LMKADLETNAEALVQEIDFLKSLYEEeicllqsqisetsvIVKMDNSRELdvdsiIAEIKAQ 295
Cdd:COG4913 200 TQSFKpiGDLDDFVreymLEEPDTFEAADALVEHFDDLERAHEA--------------LEDAREQIEL-----LEPIREL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 296 YDDIAsRSKAEAEAWYQCRyEELRVTAGNHCDNLRnrKNEILEMNKLIQWLQQETENVKAQRCKLEGAIAEAEQQ----G 371
Cdd:COG4913 261 AERYA-AARERLAELEYLR-AALRLWFAQRRLELL--EAELEELRAELARLEAELERLEARLDALREELDELEAQirgnG 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2468491673 372 EAALNDAKCKLAGLEEALQKAKQDmaclLKEYQEVMNSkLGLDIE 416
Cdd:COG4913 337 GDRLEQLEREIERLERELEERERR----RARLEALLAA-LGLPLP 376
|
|
| Seryl_tRNA_N |
pfam02403 |
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA ... |
327-396 |
7.41e-04 |
|
Seryl-tRNA synthetase N-terminal domain; This domain is found associated with the Pfam tRNA synthetase class II domain (pfam00587) and represents the N-terminal domain of seryl-tRNA synthetase.
Pssm-ID: 426757 [Multi-domain] Cd Length: 108 Bit Score: 39.11 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 327 DNLRNRKNEILEMNKLI----QW--LQQETENVKAQRCKLEGAIAEAEQQGE------AALNDAKCKLAGLEEALQKAKQ 394
Cdd:pfam02403 16 ESLKKRGVDVLDVDELLeldeKRreLQVELEELQAERNELSKEIGQAKKKKEdadaliAEVKELKDELKALEAELKELEA 95
|
..
gi 2468491673 395 DM 396
Cdd:pfam02403 96 EL 97
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
173-511 |
1.37e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 173 ISALRRQLDCVSGDRVRLESELCSLQAALEGYKKKYEEelslrpcVENEFVALKKDVDTAflmKADLETNAEALVQEID- 251
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNE-------LQAELEALQAEIDKL---QAEIAEAEAEIEERREe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 252 ---FLKSLYEEeicllQSQISETSVIVKMDN-----SRELDVDSII----AEIKAQYDDIASRSKAEAEAwyqcryEELR 319
Cdd:COG3883 88 lgeRARALYRS-----GGSVSYLDVLLGSESfsdflDRLSALSKIAdadaDLLEELKADKAELEAKKAEL------EAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 320 VTAGNHCDNLRNRKNEIL----EMNKLIQWLQQETENVKAQRCKLEGAIAEAEQQGEAALNDAKCKLAGLEEALQKAKQD 395
Cdd:COG3883 157 AELEALKAELEAAKAELEaqqaEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 396 MAcllKEYQEVMNSKLGLDIEIATYRRLLEGEEHRLCEGIGPVniSVSSSKGAFLYEPCGVSTPVLSTGVLRSNGGCSIV 475
Cdd:COG3883 237 AA---AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGA--AAASAAGGGAGGAGGGGGGGGAASGGSGGGSGGAG 311
|
330 340 350
....*....|....*....|....*....|....*.
gi 2468491673 476 GTGELYVPCEPQGLLSCGSGQKSSMTLGAGGSSPSH 511
Cdd:COG3883 312 GVGSGGGAGAVVGGASAGGGGGSGGGGGSSGGGSGG 347
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
252-408 |
2.06e-03 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 40.00 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 252 FLKSLYEEEICLLQSQISETSVIVKMDNSREldVDSIIAEIKAQYDDIASRSKAEAEAwyqcryEELRVTAgnhcdnlrn 331
Cdd:PRK06669 26 RFKVLSIKEKERLREEEEEQVEQLREEANDE--AKEIIEEAEEDAFEIVEAAEEEAKE------ELLKKTD--------- 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468491673 332 rkneilEMNKLIQWLQQETENvkaqrcklegAIAEAEQQGEAALNDAKCKlaGLEEALQKAKQDMaclLKEYQEVMN 408
Cdd:PRK06669 89 ------EASSIIEKLQMQIER----------EQEEWEEELERLIEEAKAE--GYEEGYEKGREEG---LEEVRELIE 144
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
196-422 |
2.34e-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: 40.13 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 196 SLQAALEGYKKKYEEelslrpcVENEFVALKKDVDTAFLMKADLETNAEALVQEIDflksLYEEEICLLQSQISETsviv 275
Cdd:COG4942 24 EAEAELEQLQQEIAE-------LEKELAALKKEEKALLKQLAALERRIAALARRIR----ALEQELAALEAELAEL---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 276 kmdnsrELDVDSIIAEIKAQYDDIASRSKAeAEAWYQCRYEELRVTAGNHCDNLRN----------RKNEILEMNKLIQW 345
Cdd:COG4942 89 ------EKEIAELRAELEAQKEELAELLRA-LYRLGRQPPLALLLSPEDFLDAVRRlqylkylapaRREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 346 LQQETENVKAQRCKLEGAIAEAEQQG---EAALNDAKCKLAGLEEALQKAKQDMACLLKEYQEVMNSKLGLDIEIATYRR 422
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERaalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
173-319 |
8.17e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 37.98 E-value: 8.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468491673 173 ISALRRQLDCVSGDRVRLESELCSLQAALEGYKKKYEEELSLRpcvenEFVALKKDVDTAFLMKADLETNAEALVQEIDF 252
Cdd:COG1579 47 LEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEE 121
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468491673 253 LKSLYEEeiclLQSQISETSVIVKmdnSRELDVDSIIAEIKAQYDDI-ASRSKAEA---EAWYQcRYEELR 319
Cdd:COG1579 122 LEEELAE----LEAELAELEAELE---EKKAELDEELAELEAELEELeAEREELAAkipPELLA-LYERIR 184
|
|
| |
