|
Name |
Accession |
Description |
Interval |
E-value |
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
489-693 |
7.64e-71 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 229.18 E-value: 7.64e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 489 FSQRNLDEQRQRLQknfeNEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQAVKLMITEKDKDKQQKQAEIDRLKEQ 568
Cdd:pfam05010 1 YSQKDMDAALEKAR----NEIEEKELEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 569 LDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAHAETKLDEANVEIARVRA 648
Cdd:pfam05010 77 KDQALADLNSVEKSFSDLFKRYEKQKEVISGYKKNEESLKKCAQDYLARIKKEEQRYQALKAHAEEKLDQANEEIAQVRS 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 328772091 649 SYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQELTKICDDLV 693
Cdd:pfam05010 157 KAKAETAALQASLRKEQMKVQSLERQLEQKTKENEELTKICDELI 201
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
473-665 |
2.54e-09 |
|
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: 60.85 E-value: 2.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 473 LLDVVVPISTPNSILKFSQRNLDEQRQRLQKNFEnEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQAVKLM---IT 549
Cdd:TIGR02169 296 IGELEAEIASLERSIAEKERELEDAEERLAKLEA-EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLraeLE 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 550 EKDKDKQQKQAEIDRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATgnqrfdslr 629
Cdd:TIGR02169 375 EVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED--------- 445
|
170 180 190
....*....|....*....|....*....|....*..
gi 328772091 630 AHAETKLDEANVE-IARVRASYEKEAAAMRAKLSRVE 665
Cdd:TIGR02169 446 KALEIKKQEWKLEqLAADLSKYEQELYDLKEEYDRVE 482
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
491-697 |
2.91e-08 |
|
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: 56.31 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 491 QRNLDEQRQRLQKNfENEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQAVKLMITEKDKDKQQKQAEIDRLKEQLD 570
Cdd:COG4942 33 QQEIAELEKELAAL-KKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLR 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 571 LAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAHAEtKLDEANVEIARVRASY 650
Cdd:COG4942 112 ALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA-ELEALLAELEEERAAL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 328772091 651 EKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQELTKICDDLVSQME 697
Cdd:COG4942 191 EALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
494-661 |
6.31e-08 |
|
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: 54.16 E-value: 6.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 494 LDEQRQRLQKNFENefevAQLEIQDLTLSSQNLERENQKMKDTLKQWEQAVKlmitEKDKDKQQKQAEIDRLKEQLDLAY 573
Cdd:COG1579 15 LDSELDRLEHRLKE----LPAELAELEDELAALEARLEAAKTELEDLEKEIK----RLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 574 AERnESK---KELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAHAETKLDEANVEIARVRASY 650
Cdd:COG1579 87 NNK-EYEalqKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
170
....*....|.
gi 328772091 651 EKEAAAMRAKL 661
Cdd:COG1579 166 EELAAKIPPEL 176
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
531-699 |
9.85e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.71 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 531 QKMKDTLKQWEQAVKLM-ITEKDKDKQQKQAEIDRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQRE 609
Cdd:COG1196 216 RELKEELKELEAELLLLkLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 610 QISELEQTVATGNQRfdslRAHAETKLDEANVEIARVRASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQELTKIC 689
Cdd:COG1196 296 ELARLEQDIARLEER----RRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170
....*....|
gi 328772091 690 DDLVSQMESI 699
Cdd:COG1196 372 AELAEAEEEL 381
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
491-684 |
1.00e-07 |
|
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: 55.41 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 491 QRNLDEQRQRLQKnFENEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQAVKLMITEKD-KDKQQK---------QA 560
Cdd:TIGR04523 362 QRELEEKQNEIEK-LKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKElLEKEIErlketiiknNS 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 561 EIDRLKEQ---LDLAYAE----RNESKKELDQMSLKYKQLRVDISDL-KELDERQRE------QISELEQTVATGNQRFD 626
Cdd:TIGR04523 441 EIKDLTNQdsvKELIIKNldntRESLETQLKVLSRSINKIKQNLEQKqKELKSKEKElkklneEKKELEEKVKDLTKKIS 520
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 328772091 627 SLrahaETKLDEANVEIArvrasyEKEaaamrAKLSRVEIQMQTLD-----CNLKTKVQENQE 684
Cdd:TIGR04523 521 SL----KEKIEKLESEKK------EKE-----SKISDLEDELNKDDfelkkENLEKEIDEKNK 568
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
496-672 |
1.28e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 55.33 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 496 EQRQRLQKNFENEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQAvklmITEKDKDKQQKQAEIDRLKEQLDLAYAE 575
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD----IARLEERRRELEERLEELEEELAELEEE 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 576 RNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAHAETKLDEANVEIARvRASYEKEAA 655
Cdd:COG1196 332 LEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEE 410
|
170
....*....|....*..
gi 328772091 656 AMRAKLSRVEIQMQTLD 672
Cdd:COG1196 411 ALLERLERLEEELEELE 427
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
494-687 |
1.52e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.94 E-value: 1.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 494 LDEQRQRLQKnFENEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQA---VKLMITEKDKDKQQKQAEIDRLKEQLD 570
Cdd:COG1196 269 LEELRLELEE-LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERleeLEEELAELEEELEELEEELEELEEELE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 571 LAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAHAETKLDEANvEIARVRASY 650
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE-RLEEELEEL 426
|
170 180 190
....*....|....*....|....*....|....*..
gi 328772091 651 EKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQELTK 687
Cdd:COG1196 427 EEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
494-683 |
2.39e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 494 LDEQRQRLQKNFENEFEVAQLEIQDLTL---SSQNLERENQKMKDTLKQWEQAvklmITEKDKDKQQKQAEIDRLKEQLD 570
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKELEEelkEAEEKEEEYAELQEELEELEEE----LEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 571 L--AYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAHAETKLDEANVEIARVR- 647
Cdd:COG4717 127 LlpLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQq 206
|
170 180 190
....*....|....*....|....*....|....*...
gi 328772091 648 --ASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQ 683
Cdd:COG4717 207 rlAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
491-672 |
2.74e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 491 QRNLDEQRQRLQKnfenefEVAQLEiQDLTLSSQNLERENQKMKDTLKQWEQAVKLMITEKDKDKQQKQAEIDRLKEQLD 570
Cdd:COG1196 311 RRELEERLEELEE------ELAELE-EELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 571 LAYAERNESKKELDQMSlKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAHAETKLDEANVEIARVRASy 650
Cdd:COG1196 384 LAEELLEALRAAAELAA-QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL- 461
|
170 180
....*....|....*....|..
gi 328772091 651 EKEAAAMRAKLSRVEIQMQTLD 672
Cdd:COG1196 462 LELLAELLEEAALLEAALAELL 483
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
494-668 |
4.06e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 494 LDEQRQRLQKnfenEFEVAQLEIQDLtlssQNLERENQKMKDTLKQWEQ---------AVKLMITEKDKDKQQKQA---E 561
Cdd:COG4913 615 LEAELAELEE----ELAEAEERLEAL----EAELDALQERREALQRLAEyswdeidvaSAEREIAELEAELERLDAssdD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 562 IDRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGnqrfdsLRAHAETKLDEANV 641
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE------LRALLEERFAAALG 760
|
170 180
....*....|....*....|....*....
gi 328772091 642 E--IARVRASYEKEAAAMRAKLSRVEIQM 668
Cdd:COG4913 761 DavERELRENLEERIDALRARLNRAEEEL 789
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
526-699 |
4.11e-07 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 52.23 E-value: 4.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 526 LERENQKMKDTLKQWEQAVKlmiTEKDKDKQQKQAEIDRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDlkELDE 605
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKG---AEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYED--ELNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 606 RQreqisELEQTVATGNQRFDSL---RAHAETKLDEANVEIARVRASYEKEAAAMRAklsrveiQMQTLDCNLKTKVQEN 682
Cdd:pfam00038 98 RT-----SAENDLVGLRKDLDEAtlaRVDLEAKIESLKEELAFLKKNHEEEVRELQA-------QVSDTQVNVEMDAARK 165
|
170
....*....|....*..
gi 328772091 683 QELTKICDDLVSQMESI 699
Cdd:pfam00038 166 LDLTSALAEIRAQYEEI 182
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
487-684 |
6.52e-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: 53.14 E-value: 6.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 487 LKFSQRNLDEQRQRLQKNFENEfevAQLEIQDLTLSSQNLERENQKMKDTLKQweqavklmITEKDKDKQQKQAEIDRLK 566
Cdd:TIGR02168 198 LERQLKSLERQAEKAERYKELK---AELRELELALLVLRLEELREELEELQEE--------LKEAEEELEELTAELQELE 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 567 EQLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRfdslRAHAETKLDEANVEIARV 646
Cdd:TIGR02168 267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ----LEELESKLDELAEELAEL 342
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 328772091 647 RASYE---KEAAAMRAKLSRVEIQMQtldcNLKTKVQENQE 684
Cdd:TIGR02168 343 EEKLEelkEELESLEAELEELEAELE----ELESRLEELEE 379
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
493-687 |
6.67e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 6.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 493 NLDEQRQRLQKNFENEFEvaqlEIQDLTLSSQNLERENQKMKDTLKQWEQAVKLmITEKDKDKQQKQAEIDRLKEQLDLA 572
Cdd:PRK03918 162 NAYKNLGEVIKEIKRRIE----RLEKFIKRTENIEELIKEKEKELEEVLREINE-ISSELPELREELEKLEKEVKELEEL 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 573 YAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVAtgnqRFDSLRAHAET--KLDEANVEIARVRASY 650
Cdd:PRK03918 237 KEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVK----ELKELKEKAEEyiKLSEFYEEYLDELREI 312
|
170 180 190
....*....|....*....|....*....|....*..
gi 328772091 651 EKEAAAMRAKLSRVEIQMQtldcNLKTKVQENQELTK 687
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIK----ELEEKEERLEELKK 345
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
485-697 |
1.09e-06 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 52.37 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 485 SILKFSQRNLDEQRQRLQKNFE---NEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQA---VKLMITEKDKDKQQK 558
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYalaNEISRLEQQKQILRERLANLERQLEELEAQLEELESKldeLAEELAELEEKLEEL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 559 QAEIDRLKEQLDLAYAERNESK-------KELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVatgnQRFDSLRAH 631
Cdd:TIGR02168 350 KEELESLEAELEELEAELEELEsrleeleEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR----ERLQQEIEE 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 328772091 632 AETKLDEANV--------EIARVRASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQELTKICDDLVSQME 697
Cdd:TIGR02168 426 LLKKLEEAELkelqaeleELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
492-666 |
1.16e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.69 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 492 RNLDEQRQRLQKNFENEFEVAQL--EIQDLTLSSQNLERENQKMKDTLKQWEQAVKL-MITEKDKDKQQKQAEIDRLKEQ 568
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELqeELEELEEELEELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 569 LDLAYAERNESKKELDQMSLKYKQLRVDISDLKE-LDERQREQISELEQTVATGNQRFDSLR---AHAETKLDEANVEIA 644
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEqLSLATEEELQDLAEELEELQQRLAELEeelEEAQEELEELEEELE 230
|
170 180
....*....|....*....|..
gi 328772091 645 RVRAsyEKEAAAMRAKLSRVEI 666
Cdd:COG4717 231 QLEN--ELEAAALEERLKEARL 250
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
494-692 |
2.48e-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: 51.22 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 494 LDEQRQRLQKNFENEFEVAQLEIQDLTLSSQNLERE----NQKMKDTLKQWEQA------VKLMITEKDKDKQQKQAEID 563
Cdd:TIGR02169 274 LEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSiaekERELEDAEERLAKLeaeidkLLAEIEELEREIEEERKRRD 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 564 RLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVatgnQRFDSLRAHAETKLDEANVEI 643
Cdd:TIGR02169 354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKREL----DRLQEELQRLSEELADLNAAI 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 328772091 644 ARVRASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQELTKICDDL 692
Cdd:TIGR02169 430 AGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY 478
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
485-698 |
3.82e-06 |
|
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: 50.49 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 485 SILKFSQRNLDEQRQrlqknFENEFEVAQLEIQDLTLSSQNLERENQKM-------KDTLKQWEQAVKLMITEKDKDKQq 557
Cdd:pfam05483 412 KILAEDEKLLDEKKQ-----FEKIAEELKGKEQELIFLLQAREKEIHDLeiqltaiKTSEEHYLKEVEDLKTELEKEKL- 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 558 KQAEIDRLKEQLDLayaERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTvatgnqrfdslrahaETKLD 637
Cdd:pfam05483 486 KNIELTAHCDKLLL---ENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK---------------EMNLR 547
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 328772091 638 EanvEIARVRASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQELTKICDDLVSQMES 698
Cdd:pfam05483 548 D---ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
489-685 |
5.12e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.15 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 489 FSQRNLDEQRQRLqkNFENEFEVAQLEIQDLTLSSQNLERENQKMKDTL----KQWEQAVKLMitEKDKDKQQKQAEIDR 564
Cdd:pfam00038 87 FRQKYEDELNLRT--SAENDLVGLRKDLDEATLARVDLEAKIESLKEELaflkKNHEEEVREL--QAQVSDTQVNVEMDA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 565 LKeQLDLAYAeRNESKKELDQMSLKYKQ-----LRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAHAETKLDE- 638
Cdd:pfam00038 163 AR-KLDLTSA-LAEIRAQYEEIAAKNREeaeewYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQk 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 328772091 639 ANVE--IARVRASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQEL 685
Cdd:pfam00038 241 ASLErqLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQEL 289
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
487-696 |
9.84e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 9.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 487 LKFSQRNLDEQRQRLqKNFENEFEVAQLEIQDLTLSSQNLERENQK--------MKDTLKQWEQAVKLMITEKD--KDKQ 556
Cdd:PRK03918 537 LKGEIKSLKKELEKL-EELKKKLAELEKKLDELEEELAELLKELEElgfesveeLEERLKELEPFYNEYLELKDaeKELE 615
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 557 QKQAEIDRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDlkELDERQREQISELEQTVATGNQRFDSLRAHAET-- 634
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE--EEYEELREEYLELSRELAGLRAELEELEKRREEik 693
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 328772091 635 ----KLDEANVEIARVRASYEKEAAAM------RAKLSRveiqmqtldcnLKTKVQEN--QELTKICDDLVSQM 696
Cdd:PRK03918 694 ktleKLKEELEEREKAKKELEKLEKALerveelREKVKK-----------YKALLKERalSKVGEIASEIFEEL 756
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
481-699 |
2.86e-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: 47.74 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 481 STPNSILkFSQRNLDEQRQRLQKnFENEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQAVKLMitekDKDKQQKQA 560
Cdd:TIGR02168 667 KTNSSIL-ERRREIEELEEKIEE-LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISAL----RKDLARLEA 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 561 EIDRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAhaetKLDEAN 640
Cdd:TIGR02168 741 EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA----ELTLLN 816
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 328772091 641 VEIARVRASYEKeaaaMRAKLSRVEIQMQTLDCNLKTKVQENQELTKICDDLVSQMESI 699
Cdd:TIGR02168 817 EEAANLRERLES----LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
548-685 |
4.41e-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: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 548 ITEKDKDKQQKQAEIDRLKEQLDLAYAERNESKKELDQMS------LKYKQLRVDISDL--------KELDERQRE---- 609
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRrerekaERYQALLKEKREYegyellkeKEALERQKEaier 244
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 328772091 610 QISELEQTVATGNQRFDSLRAHAETKLDEANVEIARVRASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQEL 685
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDA 320
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
484-699 |
4.90e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 484 NSILKFSQRNLDEQRQRLQKNfENEFEVAQLEIQDLtlsSQNLERENQKMKDTLKQWEQAVKLmITEKDKDKQQKQAEID 563
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESL-ERRIAATERRLEDL---EEQIEELSEDIESLAAEIEELEEL-IEELESELEALLNERA 883
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 564 RLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRfdsLRAHAETKLDEANVEI 643
Cdd:TIGR02168 884 SLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER---LSEEYSLTLEEAEALE 960
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 328772091 644 ARVrasyEKEAAAMRAKLSRVEIQMQTL-DCNLkTKVQENQELTKICDDLVSQMESI 699
Cdd:TIGR02168 961 NKI----EDDEEEARRRLKRLENKIKELgPVNL-AAIEEYEELKERYDFLTAQKEDL 1012
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
532-687 |
5.66e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 45.96 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 532 KMKDTL-KQWEQAVKLMITEKDKdkQQKQAEIDRLKEQLDLAYAERNESKKELDQMsLKYKQlrvDISDLKELDERQREQ 610
Cdd:pfam15905 171 KMKEVMaKQEGMEGKLQVTQKNL--EHSKGKVAQLEEKLVSTEKEKIEEKSETEKL-LEYIT---ELSCVSEQVEKYKLD 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 611 ISELEQTVATGNQRFDSLRA-------HAETKLDEANVEIARVRASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQ 683
Cdd:pfam15905 245 IAQLEELLKEKNDEIESLKQsleekeqELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQ 324
|
....
gi 328772091 684 ELTK 687
Cdd:pfam15905 325 KLQQ 328
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
488-656 |
1.38e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 488 KFSQRNLDEQRQRLQKNFENEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQAvklmITEKDKDKQQKQAEIDRLKE 567
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE----LEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 568 QLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRA---HAETKLDEANVEIA 644
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEelkELEEQLESLQEELA 167
|
170
....*....|..
gi 328772091 645 RVRASYEKEAAA 656
Cdd:COG4372 168 ALEQELQALSEA 179
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
512-698 |
1.52e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.11 E-value: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 512 AQLEIQDLTLSSQNLERENQkmkdtLKQWEQAVKLMITEKDKDKQQKQAEIDRLKEQLDLAYAERNESKKELDQMSLKYK 591
Cdd:pfam15921 299 SQLEIIQEQARNQNSMYMRQ-----LSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 592 QLRVDISD-LKELDERQREQISELEQTVA-----TGNQ-RFDSLRahaeTKLDEANVEIARVRasyekeaAAMRAKLSRV 664
Cdd:pfam15921 374 NLDDQLQKlLADLHKREKELSLEKEQNKRlwdrdTGNSiTIDHLR----RELDDRNMEVQRLE-------ALLKAMKSEC 442
|
170 180 190
....*....|....*....|....*....|....
gi 328772091 665 EIQMQTLDCNLKTKvqeNQELTKIcDDLVSQMES 698
Cdd:pfam15921 443 QGQMERQMAAIQGK---NESLEKV-SSLTAQLES 472
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
526-700 |
1.89e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 526 LERENQKMKDTLKQWEQAVKLMITEKDKDKQQKQAEIDRLKEQLDLAYAERNESKKELDQMSLKYKQLRvdisdlKELDE 605
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQAR------SELEQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 606 RQrEQISELEQTVATGNQRFDSLRAHAETKLDEANVEIARVrASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQEL 685
Cdd:COG4372 78 LE-EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEEL-EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170
....*....|....*
gi 328772091 686 TKICDDLVSQMESIG 700
Cdd:COG4372 156 EEQLESLQEELAALE 170
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
503-669 |
2.25e-04 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 44.46 E-value: 2.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 503 KNFENEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQAVKLMITEKDKDKQQKQAEIDRLKEqldlayaerneSKKE 582
Cdd:COG5283 10 KPFKSALESAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQALDQ-----------AGID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 583 LDQMSLKYKQLRVDISDLKELDERQREQISELEQT---VATGNQRFDSLRAHAETkldeaNVEIARVRASYEKEAAAMRA 659
Cdd:COG5283 79 TRQLSAAQRRLRSSLEQTNRQLERQQQRLARLGARqdrLKAARARLQRLAGAGAA-----AAAIGAALAASVKPAIDFED 153
|
170
....*....|
gi 328772091 660 KLSRVEIQMQ 669
Cdd:COG5283 154 AMADVAATVD 163
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
513-688 |
2.39e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 2.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 513 QLEIQDLTLSSQNLERENQKMKDTLKQWEQAV-----KLMITEKDKDKQQKQAEIDRLKEQLDLAYAERNESKKELDQMS 587
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALeefrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 588 LKYKQLRVDISDLKELDERQ--REQISELEQTVATGNQRFD-------SLRAHAETKLDEANVEIARVRASYEKEAAAMR 658
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQqlRAQLAELEAELAELSARYTpnhpdviALRAQIAALRAQLQQEAQRILASLEAELEALQ 326
|
170 180 190
....*....|....*....|....*....|
gi 328772091 659 AKLSRVEIQMQTLDCNLKTKVQENQELTKI 688
Cdd:COG3206 327 AREASLQAQLAQLEARLAELPELEAELRRL 356
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
491-592 |
2.73e-04 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 41.01 E-value: 2.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 491 QRNLDEQRQRLQKNFENEFEVAQLEIQDLTLSSQNLERENQKMKdtlkqwEQAVKLMITEKdKDKQQKQAEIDRLKEQLD 570
Cdd:pfam13863 18 KREEIERLEELLKQREEELEKKEQELKEDLIKFDKFLKENDAKR------RRALKKAEEET-KLKKEKEKEIKKLTAQIE 90
|
90 100
....*....|....*....|..
gi 328772091 571 LAYAERNESKKELDQMSlKYKQ 592
Cdd:pfam13863 91 ELKSEISKLEEKLEEYK-PYED 111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
494-672 |
2.99e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.26 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 494 LDEQRQRLQKNfeNEFEVAQLEIQDLTLSSQnleRENQKMKDTLKQWEQAVKLMITEKDKDKQQKQAEIDRLKEQLDLAY 573
Cdd:PRK02224 218 LDEEIERYEEQ--REQARETRDEADEVLEEH---EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 574 AERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAHAETkLDEANVEIARVRASYEKE 653
Cdd:PRK02224 293 EERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADD-LEERAEELREEAAELESE 371
|
170
....*....|....*....
gi 328772091 654 AAAMRAKLSRVEIQMQTLD 672
Cdd:PRK02224 372 LEEAREAVEDRREEIEELE 390
|
|
| BRE1 |
pfam08647 |
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a ... |
515-615 |
3.98e-04 |
|
BRE1 E3 ubiquitin ligase; BRE1 is an E3 ubiquitin ligase that has been shown to act as a transcriptional activator through direct activator interactions.
Pssm-ID: 462547 [Multi-domain] Cd Length: 95 Bit Score: 39.87 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 515 EIQDLTLSSQNLERENQKMKDTLKQWEQAVKLMITEKDKDKqQKQAEIDRLKEQLDlayaerNESKKELDQMSlkyKQLR 594
Cdd:pfam08647 4 ELVKLEQAFEELSEQLDKKVKDLTILEEKKLRLEAEKAKAD-QKYFAAMRSKDALE------NENKKLNTLLS---KSSE 73
|
90 100
....*....|....*....|.
gi 328772091 595 VdISDLKELDERQREQISELE 615
Cdd:pfam08647 74 L-IEQLKETEKEFVRKLKNLE 93
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
490-618 |
5.24e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 490 SQRNLDEQRQRLQKnFENEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQAVKLMItEKDKDKQQKQAEIDRLKEQL 569
Cdd:COG2433 404 EERELTEEEEEIRR-LEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREI-RKDREISRLDREIERLEREL 481
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 328772091 570 DLAYAERNESKKELDQM-SLKYKQLRVDISDLKELDERQREQISELEQTV 618
Cdd:COG2433 482 EEERERIEELKRKLERLkELWKLEHSGELVPVKVVEKFTKEAIRRLEEEY 531
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
485-660 |
5.60e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 5.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 485 SILKFSQRNLDEQRQRLQKNFENEFEV----AQLEIQDLTLSSQN-LERENQKMKDTLKQWEQAVklmitekdkdkQQKQ 559
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAikkeALLEAKEEIHKLRNeFEKELRERRNELQKLEKRL-----------LQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 560 AEIDRLKEQLDlayaernESKKELDQMSLKYKQLRVDISDLK-ELDERQREQISELEQtVA--TGNQRFDSLRAHAEtkl 636
Cdd:PRK12704 96 ENLDRKLELLE-------KREEELEKKEKELEQKQQELEKKEeELEELIEEQLQELER-ISglTAEEAKEILLEKVE--- 164
|
170 180
....*....|....*....|....*..
gi 328772091 637 DEANVEIARVRASYEKEA---AAMRAK 660
Cdd:PRK12704 165 EEARHEAAVLIKEIEEEAkeeADKKAK 191
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
494-663 |
5.73e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 43.37 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 494 LDEQRQRLQknfeneFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQAVKLMITEKDKDKQQKQA----EIDRLKEQL 569
Cdd:COG4913 274 LEYLRAALR------LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdRLEQLEREI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 570 DLAYAERNESKKELDQMSLKYKQLRV----DISDLKELDERQREQISELEQTVATGNQRFDSLRA---HAETKLDEANVE 642
Cdd:COG4913 348 ERLERELEERERRRARLEALLAALGLplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAalrDLRRELRELEAE 427
|
170 180
....*....|....*....|....
gi 328772091 643 IARVRA---SYEKEAAAMRAKLSR 663
Cdd:COG4913 428 IASLERrksNIPARLLALRDALAE 451
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
548-700 |
6.79e-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: 43.13 E-value: 6.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 548 ITEKDKDKQQKQAEIDRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDS 627
Cdd:TIGR02169 683 LEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 628 LRA---HAETKLDEANVEIARVRASY--------EKEAAAMRAKLSRVEIQMQTLDCNLKTKVQEN-------QELTKIC 689
Cdd:TIGR02169 763 LEArieELEEDLHKLEEALNDLEARLshsripeiQAELSKLEEEVSRIEARLREIEQKLNRLTLEKeylekeiQELQEQR 842
|
170
....*....|.
gi 328772091 690 DDLVSQMESIG 700
Cdd:TIGR02169 843 IDLKEQIKSIE 853
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
556-697 |
9.44e-04 |
|
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: 41.45 E-value: 9.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 556 QQKQAEIDRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLR------ 629
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeye 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 630 -------------AHAETKLDEANVEIARVRASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQELTKICDDLVSQM 696
Cdd:COG1579 93 alqkeieslkrriSDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKI 172
|
.
gi 328772091 697 E 697
Cdd:COG1579 173 P 173
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
548-699 |
1.56e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 548 ITEKDKDKQQKQAEIDRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDS 627
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 628 L--------------RAHAETKLDEANVEI-----------ARVRASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQEN 682
Cdd:COG3883 105 LdvllgsesfsdfldRLSALSKIADADADLleelkadkaelEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALL 184
|
170
....*....|....*..
gi 328772091 683 QELTKICDDLVSQMESI 699
Cdd:COG3883 185 AQLSAEEAAAEAQLAEL 201
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
491-639 |
1.65e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.82 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 491 QRNLDEQRQRLQKNFENEF----------EVAQLE--IQDLTLSS-------QNLERENQKMKDTLKQWEQAVKLmITEK 551
Cdd:COG4913 640 LDALQERREALQRLAEYSWdeidvasaerEIAELEaeLERLDASSddlaaleEQLEELEAELEELEEELDELKGE-IGRL 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 552 DKDKQQKQAEIDRLKEQLD-LAYAERNESKKELDQM------SLKYKQLRVDISD-LKELDERQREQISELEQTVATGNQ 623
Cdd:COG4913 719 EKELEQAEEELDELQDRLEaAEDLARLELRALLEERfaaalgDAVERELRENLEErIDALRARLNRAEEELERAMRAFNR 798
|
170
....*....|....*.
gi 328772091 624 RFDSLRAHAETKLDEA 639
Cdd:COG4913 799 EWPAETADLDADLESL 814
|
|
| F-BAR_CIP4-like |
cd07653 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 ... |
484-619 |
1.66e-03 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Cdc42-Interacting Protein 4 and similar proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4), Formin Binding Protein 17 (FBP17), FormiN Binding Protein 1-Like (FNBP1L), and similar proteins. CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Members of this subfamily typically contain an N-terminal F-BAR domain and a C-terminal SH3 domain. In addition, some members such as FNBP1L contain a central Cdc42-binding HR1 domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153337 [Multi-domain] Cd Length: 251 Bit Score: 40.70 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 484 NSILKFSQRNLDEQRQRLQKNFEnefEVAQLEiQDLTLSSQNLERENQKMKDTLKQWEQAvkLMITEK-DKDKQQKQAEI 562
Cdd:cd07653 90 SNVCKELKTLISELRQERKKHLS---EGSKLQ-QKLESSIKQLEKSKKAYEKAFKEAEKA--KQKYEKaDADMNLTKADV 163
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 328772091 563 DRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDI---------SDLKELDERQREQISELEQTVA 619
Cdd:cd07653 164 EKAKANANLKTQAAEEAKNEYAAQLQKFNKEQRQHystdlpqifDKLQELDEKRINRTVELLLQAA 229
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
491-684 |
1.80e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.06 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 491 QRNLDEQRQRLQKNFENEFEvAQLEIQDLTLSSQNLERENQKMKDTLKQwEQAVKLMITEKDKDKQQKQAEIDRLKEQLD 570
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLD-EMMEEERERALEEEEEKEEERKEERKRY-RQELEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 571 LAY-AERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAHAETKLDEanvEIARVRAS 649
Cdd:pfam13868 105 EIVeRIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREA---EREEIEEE 181
|
170 180 190
....*....|....*....|....*....|....*
gi 328772091 650 YEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQE 684
Cdd:pfam13868 182 KEREIARLRAQQEKAQDEKAERDELRAKLYQEEQE 216
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
553-650 |
2.03e-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: 40.90 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 553 KDKQQKQAEIDRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAha 632
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA-- 97
|
90
....*....|....*....
gi 328772091 633 etKLDEANVEIA-RVRASY 650
Cdd:COG4942 98 --ELEAQKEELAeLLRALY 114
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
480-685 |
2.10e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 480 ISTPNSILKFSQRNLDEQRQRLQKNfENEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWEQAVKLMITEKDKDKQQ-- 557
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQL-REELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEEle 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 558 -KQAEIDRLKEQLdlayaerNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRA-HAETK 635
Cdd:COG4372 105 sLQEEAEELQEEL-------EELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQeLQALS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 328772091 636 LDEANVEIARVRASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQEL 685
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSL 227
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
527-660 |
2.62e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 40.63 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 527 ERENQKMKdtLKQWEQAVKLMITEKDKDKQQKQAEI----DRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDIsdlkE 602
Cdd:COG2268 220 NREAEEAE--LEQEREIETARIAEAEAELAKKKAEErreaETARAEAEAAYEIAEANAEREVQRQLEIAEREREI----E 293
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 328772091 603 LDERQREQisELEQTVATGNQRFDSLRAHAETKlDEANVEIARVRAsyEKEAAAMRAK 660
Cdd:COG2268 294 LQEKEAER--EEAELEADVRKPAEAEKQAAEAE-AEAEAEAIRAKG--LAEAEGKRAL 346
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
493-661 |
3.38e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.87 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 493 NLDEQRQRLQKNFENEFEVAQLEIQDLTLSSQNLERENQKMKDTLKQWE----QAVKL------MITEKDKDKQQKQAEI 562
Cdd:pfam15921 671 SLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsdgHAMKVamgmqkQITAKRGQIDALQSKI 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 563 DRLKEQLDLAYAERNESKKELDQMSlkykqlrvdiSDLKELDERQREQISELEqTVATGNQRFDSLRAHAETKLDEANVE 642
Cdd:pfam15921 751 QFLEEAMTNANKEKHFLKEEKNKLS----------QELSTVATEKNKMAGELE-VLRSQERRLKEKVANMEVALDKASLQ 819
|
170 180
....*....|....*....|
gi 328772091 643 IARVRASYEK-EAAAMRAKL 661
Cdd:pfam15921 820 FAECQDIIQRqEQESVRLKL 839
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
541-663 |
3.86e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 40.61 E-value: 3.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 541 EQAVKLMItEKDKDKQQKQAEIDRLKEQldlayAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVAT 620
Cdd:COG2433 379 EEALEELI-EKELPEEEPEAEREKEHEE-----RELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE 452
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 328772091 621 -GNQRFDSLRAHAE-TKLDEanvEIARVR---ASYEKEAAAMRAKLSR 663
Cdd:COG2433 453 aRSEERREIRKDREiSRLDR---EIERLErelEEERERIEELKRKLER 497
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
496-667 |
4.55e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 40.49 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 496 EQRQRLQKNFENEFEVAQLEIQDLTLSSQNLERENQKMKDtlkqweqaVKLMITEKDKDKQQKQAEIDRLKEQLDLAYAE 575
Cdd:pfam15921 461 EKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD--------LTASLQEKERAIEATNAEITKLRSRVDLKLQE 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 576 RNESKKELDQM---SLKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSL---RAHAETKLDEANVEIARVRAS 649
Cdd:pfam15921 533 LQHLKNEGDHLrnvQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMqveKAQLEKEINDRRLELQEFKIL 612
|
170 180
....*....|....*....|.
gi 328772091 650 YEKEAAAMR---AKLSRVEIQ 667
Cdd:pfam15921 613 KDKKDAKIReleARVSDLELE 633
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
494-699 |
4.81e-03 |
|
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: 40.09 E-value: 4.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 494 LDEQRQRLQkNFENEF--EVAQLEIQDLTLSSQNLERENqKMKDTLkqweqavklMITEKDKDKqqkqaeIDRLKEQLDL 571
Cdd:pfam05483 217 LKEDHEKIQ-HLEEEYkkEINDKEKQVSLLLIQITEKEN-KMKDLT---------FLLEESRDK------ANQLEEKTKL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 572 ayaeRNESKKELDQmslKYKQLRVDISDLKELDERQREQISELEQTVATGNQRFDSLRAHAETKLDEAN----------V 641
Cdd:pfam05483 280 ----QDENLKELIE---KKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNkakaahsfvvT 352
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 328772091 642 EIARVRASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQELTKICDDLVSQMESI 699
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEEL 410
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
513-695 |
4.92e-03 |
|
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: 40.39 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 513 QLEIQDLTLSsqNLERENQKMK------DTLKQWEQAVKLMITEKDKDKQQKQAEIDRLKEQLDLAYAERNESKKELDQM 586
Cdd:TIGR04523 195 KLLKLELLLS--NLKKKIQKNKslesqiSELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 587 SLK--------------YKQLRVDISDLK-------------ELDERQRE------QISELEQTVATGNQRFDSLRAHAE 633
Cdd:TIGR04523 273 QKEleqnnkkikelekqLNQLKSEISDLNnqkeqdwnkelksELKNQEKKleeiqnQISQNNKIISQLNEQISQLKKELT 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 634 TK----------LDEANVEIARVR---ASY-------EKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQELTKICDDLV 693
Cdd:TIGR04523 353 NSesensekqreLEEKQNEIEKLKkenQSYkqeiknlESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
..
gi 328772091 694 SQ 695
Cdd:TIGR04523 433 ET 434
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
543-670 |
5.38e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 543 AVKLMITEKDKDKQQKQAEIDRLKEQLDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVATGN 622
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 328772091 623 QRFDSLRAHAEtKLDEANVEIARVRASYEKeaaaMRAKLSRVEIQMQT 670
Cdd:COG1340 85 EKLNELREELD-ELRKELAELNKAGGSIDK----LRKEIERLEWRQQT 127
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
492-617 |
5.48e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 39.51 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 492 RNLDEQRQRLQKNFENEFEVAQLEIQDLTLSSQnLERENQKMKDTLKQWEQAVKLMITEKDkdkqqkqaEIDRLKEQLDL 571
Cdd:COG1340 143 KELEKELEKAKKALEKNEKLKELRAELKELRKE-AEEIHKKIKELAEEAQELHEEMIELYK--------EADELRKEADE 213
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 328772091 572 AYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQT 617
Cdd:COG1340 214 LHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKRE 259
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
496-616 |
6.22e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.23 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 496 EQRQRLQKNFENE-FEVAQLEIQDLTLSSQNLEREN------QKMKDTLKqwEQAVKLMITEKDKDkQQKQAEIDRLKEQ 568
Cdd:smart00787 136 EWRMKLLEGLKEGlDENLEGLKEDYKLLMKELELLNsikpklRDRKDALE--EELRQLKQLEDELE-DCDPTELDRAKEK 212
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 328772091 569 LDLAYAERNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQ 616
Cdd:smart00787 213 LKKLLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEK 260
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
492-665 |
7.34e-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: 39.72 E-value: 7.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 492 RNLDEQRQRLQKNFENEFEVAQLEIQDLTLSSQNLERENQK------MKDTLKQWEQAVKLMITEKDKDKQQKQAEIDRL 565
Cdd:pfam05557 58 RLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQladareVISCLKNELSELRRQIQRAELELQSTNSELEEL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 566 KEQLDlayaernESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQ------TVATGNQRFDSLrAHAETKLDEA 639
Cdd:pfam05557 138 QERLD-------LLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSqeqdseIVKNSKSELARI-PELEKELERL 209
|
170 180 190
....*....|....*....|....*....|..
gi 328772091 640 NVEIARVRAS------YEKEAAAMRAKLSRVE 665
Cdd:pfam05557 210 REHNKHLNENienkllLKEEVEDLKRKLEREE 241
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
548-646 |
7.51e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 39.68 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 548 ITEKDKDKQQKQAEIDRLKEQLDLAYAER--------NESKKELDQMSLKY---KQLRVDISDLKELDERQREQISELEQ 616
Cdd:COG0542 413 LDELERRLEQLEIEKEALKKEQDEASFERlaelrdelAELEEELEALKARWeaeKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110
....*....|....*....|....*....|
gi 328772091 617 TVATGNQRFDSLRAHAETKLDEAnvEIARV 646
Cdd:COG0542 493 ELAELEEELAELAPLLREEVTEE--DIAEV 520
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
486-697 |
7.78e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 39.57 E-value: 7.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 486 ILKFSQRNLDEQRQRLQKNFENEFEVA-QLEIQDLTLSSQNLERENQKMKDTLKQWEQAVKlmitekdkdkQQKQAEIDR 564
Cdd:TIGR00618 596 LQDLTEKLSEAEDMLACEQHALLRKLQpEQDLQDVRLHLQQCSQELALKLTALHALQLTLT----------QERVREHAL 665
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 565 LKEQLDLAYAERNEskKELDQMSLKYKQLRVDISDLKELDERQREQ---------------------ISELEQTVATGNQ 623
Cdd:TIGR00618 666 SIRVLPKELLASRQ--LALQKMQSEKEQLTYWKEMLAQCQTLLRELethieeydrefneienassslGSDLAAREDALNQ 743
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 328772091 624 RFDSLRAHAETKLDEAnvEIARVRASYEKEAAAMRAKlsrveiQMQTLDCNLKTKVQENQELTKICDDLVSQME 697
Cdd:TIGR00618 744 SLKELMHQARTVLKAR--TEAHFNNNEEVTAALQTGA------ELSHLAAEIQFFNRLREEDTHLLKTLEAEIG 809
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
326-538 |
8.12e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 39.72 E-value: 8.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 326 PSGVSSPQQRQHVSTKMPT----PLKQVLSLSDELASP---------TKTESHHLNNHIGALYERSRSLSLSTPsksssp 392
Cdd:pfam15921 877 PSSQSTASFLSHHSRKTNAlkedPTRDLKQLLQELRSVineeptvqlSKAEDKGRAPSLGALDDRVRDCIIESS------ 950
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 393 MNADI-PPSFNSKQTEASSqhaieSEHKHHRTPITSRTSQISefDPIGTipqdwmmrFESPAAASASVK------YGTHV 465
Cdd:pfam15921 951 LRSDIcHSSSNSLQTEGSK-----SSETCSREPVLLHAGELE--DPSSC--------FTFPSTASPSVKnsasrsFHSSP 1015
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 466 SSTPIQSLLDVVV--------------PISTPNSIlKFSQRNLDEQRQRLQKNFENEFEVAQLEIQDLTLSSQ------- 524
Cdd:pfam15921 1016 KKSPVHSLLTSSAegsigsssqyrsakTIHSPDSV-KDSQSLPIETTGKTCRKLQNRLESLQTLVEDLQLKNQamssmir 1094
|
250
....*....|....
gi 328772091 525 NLERENQKMKDTLK 538
Cdd:pfam15921 1095 NQEKRIQKVKDQEK 1108
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
480-658 |
9.59e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 38.91 E-value: 9.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 480 ISTPNSILKFSQRNLDEQRQRLQKNFENEFEVAQLEIQDLTLSSQNLERE----------NQKMKDTLKQWEQAVKLMIT 549
Cdd:PRK11637 105 IDELNASIAKLEQQQAAQERLLAAQLDAAFRQGEHTGLQLILSGEESQRGerilayfgylNQARQETIAELKQTREELAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 550 EK----DKDKQQKQAEIDRLKEQLDLAYAeRNESKKELDQMSLKYKQLRVDISDLKELDERQREQISELEQTVatgnqrf 625
Cdd:PRK11637 185 QKaeleEKQSQQKTLLYEQQAQQQKLEQA-RNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREA------- 256
|
170 180 190
....*....|....*....|....*....|...
gi 328772091 626 dslRAHAETKLDEAnveiARVRAsyeKEAAAMR 658
Cdd:PRK11637 257 ---KARAEREAREA----ARVRD---KQKQAKR 279
|
|
| MAP65_ASE1 |
pfam03999 |
Microtubule associated protein (MAP65/ASE1 family); |
483-694 |
9.75e-03 |
|
Microtubule associated protein (MAP65/ASE1 family);
Pssm-ID: 427641 [Multi-domain] Cd Length: 477 Bit Score: 39.21 E-value: 9.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 483 PNSILKFSQRNLDEQRqRLQKNFENEFEVAQLEIQDLTLSSQN----LERENQKMKD--TLKQWEQAVKLMITEKDKDKQ 556
Cdd:pfam03999 29 KDHIKEFYTDALSEEN-DKEQRILQSIADLRAEAAILCLYMRNrllhEERDPFEPKKgmSLLQKEKKLDTQLEHLRKEKA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 557 QKQAEIDRLKEQLD--------LAYAERNESKKELDQMSlkykQLRVDISDLKELDERQREQISEL-------------- 614
Cdd:pfam03999 108 PRLAEIKELLEQLQqlceelgeEPLPLLIDPLPSLEELE----SFRKHLENLRNEKERRLEEVNELkkqikllmeeldlv 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 328772091 615 -----EQTVATGNQRFDSLRAHAETKLDEANVEIARVRASYEKEAAAMRAKLSRVEIQMQTLDCNLKTKVQENQELTKIC 689
Cdd:pfam03999 184 pgtdfEEDLLCESEDNFCLSRENIDKLRKLIKQLEEQKAEREEKIDDLREKILELWNRLQVPQEEQESFVRENNSLSQDT 263
|
....*
gi 328772091 690 DDLVS 694
Cdd:pfam03999 264 IDALR 268
|
|
| |
