|
Name |
Accession |
Description |
Interval |
E-value |
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
38-707 |
5.88e-55 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 202.39 E-value: 5.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 38 SPLFYVRIVVTWLGMVSLDAMTGFRFELLWPTWLMIRAAAESIQMRnqhcvttianptAARFSVLFICVTATSDLICYLF 117
Cdd:pfam09726 26 STFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLLIRSVYDSFKYQ------------GLAFSVFFVCIAFTSDIICLLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 118 IPIRMLIFLATTYVWISLYYHTQGGFlrSLATVyggerlqSWPIVFitcfiVIFELFLRIRShpiLISFFPNVAEyagvs 197
Cdd:pfam09726 94 IPVQWLFFAASTYVWVQYVWHTEKGI--CLPTV-------SLWILF-----VYIEAAIRFKD---LKNFHVDLCR----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 198 pvwPrslnafFGAHSIGYPVILITVSMHYYFNeWKLR-RKQCDVSNRNEQLFRILVEGLPAEyegpkdytsQQCLEDdly 276
Cdd:pfam09726 152 ---P------FAAHCIGYPVVTLGFGFKSYVS-YKMRlRKQREVQKENEFYMQLLQQALPKE---------QQMLDR--- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 277 yldppvQTLQPMQAIQAASATPPTSSKKNGiHKRNGDVTSSTTTSSRKKKHNgNSGFNSTPPNDKKKGKSIRDVDMDDGD 356
Cdd:pfam09726 210 ------QERETSETAKGLSEVDPLALNQNG-HSLNKKDSTLQLPELEYREKK-NSGTSSGSDSKKSHNHNIHNLNHVDSK 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 357 DSDDDYSYRDTSSSTIEDQRRGGGISIIRFIFSSAAwlfsfvfESSTPSENSLSNQQidddedyedgdgDKKNGRTDSMT 436
Cdd:pfam09726 282 LQEKEYMENHSNSKRLNISTSPGSEEDLLVRESVSS-------KSSSSSSSSNKNYK------------NASGGSANSSN 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 437 STTKGRANTMPSTTRsqnnnnsqkqqkqsngkshhqhSSHQNNHQKSNGnsnGHARGFAAVRDSSHDTNASNETDIRSMS 516
Cdd:pfam09726 343 SSPRSHSHNSGSVTS----------------------SSSSKNSKKQKG---PGGKSGARHKDPAENCIPNNQLSKPDAL 397
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 517 RELES----LRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERKYADL 592
Cdd:pfam09726 398 VRLEQdikkLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEKRLKAE 477
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 593 LGKKAEIEATLSAERKAR-MEVTSKKYDVA----------EHQRERERQLESEIDKLRIELKSKDESNMRMESELHGLRN 661
Cdd:pfam09726 478 QEARASAEKQLAEEKKRKkEEEATAARAVAlaaasrgectESLKQRKRELESEIKKLTHDIKLKEEQIRELEIKVQELRK 557
|
650 660 670 680
....*....|....*....|....*....|....*....|....*..
gi 392885956 662 YKE-ENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDAR 707
Cdd:pfam09726 558 YKEsEKDTEVLMSALSAMQDKNQHLENSLSAETRIKLDLFSALGDAK 604
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
507-723 |
2.51e-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: 61.24 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 507 SNETDIRSMSRELESLRSEISSRRSQEEDfkLQVSMHESNETR--LSQQLSNM--------RLKVEQMEIKCSSIERHRE 576
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISE--LEKRLEEIEQLLeeLNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIA 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 577 SDKHQLEQAERKYADLlgkKAEIEATLSAERKARMEVTSKKYDVAEHQrERERQLESEIDKLRIELKSKDESNMRMESEL 656
Cdd:TIGR02169 312 EKERELEDAEERLAKL---EAEIDKLLAEIEELEREIEEERKRRDKLT-EEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 657 HGLRNYKEE--NDIDSLNMELRFVRDKSHQMEESLAG-ENKLKqslfkclgDARDTIKSLERRVQEFQIK 723
Cdd:TIGR02169 388 KDYREKLEKlkREINELKRELDRLQEELQRLSEELADlNAAIA--------GIEAKINELEEEKEDKALE 449
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
503-723 |
8.67e-08 |
|
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: 56.28 E-value: 8.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 503 DTNASNETDIRSMSRELESLRSEISSRRSqeedfkLQVSMHESNETRLSQQLSNMRLKVEQMEiKCSSIERHRESDKHQL 582
Cdd:pfam15921 405 DRDTGNSITIDHLRRELDDRNMEVQRLEA------LLKAMKSECQGQMERQMAAIQGKNESLE-KVSSLTAQLESTKEML 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 583 EQAerkYADLLGKKAEIEatlSAERKARmevtskkyDVAEHQRERERQLE---SEIDKL--RIELKSKDESNMRMESElH 657
Cdd:pfam15921 478 RKV---VEELTAKKMTLE---SSERTVS--------DLTASLQEKERAIEatnAEITKLrsRVDLKLQELQHLKNEGD-H 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 658 gLRNYKEENDIDSLNME-----LRFVRDKSHQMEEsLAGEN---------------------KLKQSLFKCLGDARDT-I 710
Cdd:pfam15921 543 -LRNVQTECEALKLQMAekdkvIEILRQQIENMTQ-LVGQHgrtagamqvekaqlekeindrRLELQEFKILKDKKDAkI 620
|
250
....*....|...
gi 392885956 711 KSLERRVQEFQIK 723
Cdd:pfam15921 621 RELEARVSDLELE 633
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
509-701 |
1.08e-07 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 56.06 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 509 ETDIRSMSRELESLRSEISSRRSQEEDFKLQVS----MHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQ 584
Cdd:PRK01156 362 EMDYNSYLKSIESLKKKIEEYSKNIERMSAFISeilkIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDE 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 585 AERKYADLLGK-KAEIEATLSAERKARmevtskkyDVAEHQRERERQLESEIDKLRIELKSKDESNMRMESelhgLRNYK 663
Cdd:PRK01156 442 LSRNMEMLNGQsVCPVCGTTLGEEKSN--------HIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK----RKEYL 509
|
170 180 190
....*....|....*....|....*....|....*...
gi 392885956 664 EENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFK 701
Cdd:PRK01156 510 ESEEINKSINEYNKIESARADLEDIKIKINELKDKHDK 547
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
498-717 |
2.68e-07 |
|
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: 54.80 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 498 RDSSHDTNASNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQlsnmrlkVEQMEIKCSSIERHRES 577
Cdd:pfam01576 863 RDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQ-------VEQLTTELAAERSTSQK 935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 578 DKHQLEQAERKYADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRE---RERQLESEIDKlRIELKSKdESNMRMES 654
Cdd:pfam01576 936 SESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEqesRERQAANKLVR-RTEKKLK-EVLLQVED 1013
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392885956 655 ELHGLRNYKEEndIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRV 717
Cdd:pfam01576 1014 ERRHADQYKDQ--AEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREV 1074
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
504-712 |
3.45e-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: 54.26 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 504 TNASNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLE 583
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 584 QAERKYADllgKKAEIEaTLSAERKARMEVTSKKYDVAEHQRERERQLESEIDKLRIELKSKDESNMRMESELHGlRNYK 663
Cdd:TIGR04523 486 QKQKELKS---KEKELK-KLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK-ENLE 560
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 392885956 664 EEndIDSLNMELrfvrDKSHQMEESLAGENKLKQSLFKCLGDARDTIKS 712
Cdd:TIGR04523 561 KE--IDEKNKEI----EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIK 603
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
515-655 |
1.44e-06 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 52.22 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 515 MSRELESLRSEISS---RRSQEEDFKLQVSMHESNEtrLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERKYA- 590
Cdd:pfam15964 365 LERQKERLEKELASqqeKRAQEKEALRKEMKKEREE--LGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLAs 442
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392885956 591 ---DLLGKKAEIEATLSaerKARMEVTSKKYDVAEHQRERERQLE---SEIDKLRIELkskDESNMRMESE 655
Cdd:pfam15964 443 qemDVTKVCGEMRYQLN---QTKMKKDEAEKEHREYRTKTGRQLEikdQEIEKLGLEL---SESKQRLEQA 507
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
509-719 |
1.95e-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: 51.99 E-value: 1.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 509 ETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSnmRLKVEQMEIKCSSIERHRESDKHQLEQAERK 588
Cdd:TIGR02169 743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQK 820
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 589 YADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRE---RERQLESEIDKLRIELKSkdesnmrMESELHGLrnykeE 665
Cdd:TIGR02169 821 LNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENlngKKEELEEELEELEAALRD-------LESRLGDL-----K 888
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 392885956 666 NDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQE 719
Cdd:TIGR02169 889 KERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGE 942
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
512-714 |
2.26e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.60 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 512 IRSMSRELESLRSEISSRRSQEEDFKLQVSMHESN-----ETR-----LSQQLSNMRLKVEQMEIKCSSIERHRESDKHQ 581
Cdd:PRK03918 195 IKEKEKELEEVLREINEISSELPELREELEKLEKEvkeleELKeeieeLEKELESLEGSKRKLEEKIRELEERIEELKKE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 582 LEQAERK--------------------YADLLGKKAEIE---ATLSAERKA---RMEVTSKKYDVAEHQRERERQLESEI 635
Cdd:PRK03918 275 IEELEEKvkelkelkekaeeyiklsefYEEYLDELREIEkrlSRLEEEINGieeRIKELEEKEERLEELKKKLKELEKRL 354
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392885956 636 DKLRIELKSKDESnMRMESELHGLRNYKEENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLE 714
Cdd:PRK03918 355 EELEERHELYEEA-KAKKEELERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELK 432
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
517-690 |
2.59e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 517 RELESLRSEISSRRSQEEDFK-LQVSMHESNE--TRLSQQLSNMRLKVEQMEIKCS---------SIERHRESDKHQLEQ 584
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAeLQEELEELEEelEELEAELEELREELEKLEKLLQllplyqeleALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 585 AERKYADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESEIDKLRIELKskdesnmRMESELHGLRNYKE 664
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA-------ELEEELEEAQEELE 223
|
170 180
....*....|....*....|....*...
gi 392885956 665 --ENDIDSLNMELRfvrdkSHQMEESLA 690
Cdd:COG4717 224 elEEELEQLENELE-----AAALEERLK 246
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
497-718 |
2.79e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 497 VRDSSH-DTNASNETDIRSMSRELESLRSEISSRRSQEEDFK------LQVSMHESNETRLSQQLSNMRLKVEQMEIKCS 569
Cdd:PRK02224 461 VEGSPHvETIEEDRERVEELEAELEDLEEEVEEVEERLERAEdlveaeDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 570 SI-----------ERHRESDKHQLEQAER---KYADLLGKKAEIEATLSA-----------------------ERKARME 612
Cdd:PRK02224 541 ELreraaeleaeaEEKREAAAEAEEEAEEareEVAELNSKLAELKERIESlerirtllaaiadaedeierlreKREALAE 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 613 VTSKKYDVAEHQRERERQLESEIDKLRIElkskdesnmrmeselhGLRNYKE--ENDIDSLNMELRFVRDKSHQMEESLA 690
Cdd:PRK02224 621 LNDERRERLAEKRERKRELEAEFDEARIE----------------EAREDKEraEEYLEQVEEKLDELREERDDLQAEIG 684
|
250 260
....*....|....*....|....*....
gi 392885956 691 G-ENKLKQslfkcLGDARDTIKSLERRVQ 718
Cdd:PRK02224 685 AvENELEE-----LEELRERREALENRVE 708
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
508-719 |
2.96e-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: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 508 NETDIRSMSRELESLRSEissrRSQEEDFK-LQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAE 586
Cdd:TIGR02169 189 LDLIIDEKRQQLERLRRE----REKAERYQaLLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 587 RKYAdllgkkaEIEATLSAERKARMEVTSKKYDVAehqRERERQLESEIDKLRielKSKDESNMRMESELHGLRNYKEEn 666
Cdd:TIGR02169 265 KRLE-------EIEQLLEELNKKIKDLGEEEQLRV---KEKIGELEAEIASLE---RSIAEKERELEDAEERLAKLEAE- 330
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 392885956 667 dIDSLNMELRfvrdkshQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQE 719
Cdd:TIGR02169 331 -IDKLLAEIE-------ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
506-685 |
3.52e-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: 51.21 E-value: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 506 ASNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHE-------SNETRLSQQLSNMRLKVEQMEIKCSSIERHRESD 578
Cdd:TIGR02168 340 AELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqletlrSKVAQLELQIASLNNEIERLEARLERLEDRRERL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 579 KHQLEQAERKYADLlgKKAEIEATLSAERKARMEVTSKKYDV---AEHQRERERQLESEIDKLRIELKSKDesnmrmeSE 655
Cdd:TIGR02168 420 QQEIEELLKKLEEA--ELKELQAELEELEEELEELQEELERLeeaLEELREELEEAEQALDAAERELAQLQ-------AR 490
|
170 180 190
....*....|....*....|....*....|
gi 392885956 656 LHGLRNYKEENdiDSLNMELRFVRDKSHQM 685
Cdd:TIGR02168 491 LDSLERLQENL--EGFSEGVKALLKNQSGL 518
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
513-723 |
3.55e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.94 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 513 RSMSRELESLRSEIS-------------SRRSQEEDfKLQVSMHEsnETRL-SQQLSNMRLKVEQmeikcsSIERHREsd 578
Cdd:pfam01576 295 RDLGEELEALKTELEdtldttaaqqelrSKREQEVT-ELKKALEE--ETRShEAQLQEMRQKHTQ------ALEELTE-- 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 579 khQLEQAERKYADLLGKKAEIE---ATLSAERKArmeVTSKKYDVaEHQRER-ERQLE------SEIDKLRIELKSKDEs 648
Cdd:pfam01576 364 --QLEQAKRNKANLEKAKQALEsenAELQAELRT---LQQAKQDS-EHKRKKlEGQLQelqarlSESERQRAELAEKLS- 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 649 nmRMESELHGL---------RNYKEENDIDSLNMELrfvRDKSHQMEES----LAGENKLKQ------SLFKCLGDARDT 709
Cdd:pfam01576 437 --KLQSELESVssllneaegKNIKLSKDVSSLESQL---QDTQELLQEEtrqkLNLSTRLRQledernSLQEQLEEEEEA 511
|
250
....*....|....
gi 392885956 710 IKSLERRVQEFQIK 723
Cdd:pfam01576 512 KRNVERQLSTLQAQ 525
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
509-724 |
3.72e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 50.82 E-value: 3.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 509 ETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLK--------------VEQMEIKCSSIERH 574
Cdd:TIGR00606 701 QSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKlqkvnrdiqrlkndIEEQETLLGTIMPE 780
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 575 RESDK-------------HQLEQAERKYADLLGKKAEIEATLSAErkarmEVTSKKydvaEHQRERERQLESEIDKLRIE 641
Cdd:TIGR00606 781 EESAKvcltdvtimerfqMELKDVERKIAQQAAKLQGSDLDRTVQ-----QVNQEK----QEKQHELDTVVSKIELNRKL 851
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 642 LKSKDESNMRMESELhglrnykeeNDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQEFQ 721
Cdd:TIGR00606 852 IQDQQEQIQHLKSKT---------NELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQ 922
|
...
gi 392885956 722 IKN 724
Cdd:TIGR00606 923 QEK 925
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
544-723 |
3.76e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.84 E-value: 3.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 544 ESNETRLSQQLSNMRLKVEQMEI-------KCSSIERHRESDKHQLEQAERKYADLlgkKAEIEATLSAERKARMEVTSK 616
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRelsslqsELRRIENRLDELSQELSDASRKIGEI---EKEIEQLEQEEEKLKERLEEL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 617 KYDVAEHQRERErQLESEIDKLRIELKSKDESNMRMESELHGLRNYKEENDIDSLNMELRFVRDKSHQMEESLAG-ENKL 695
Cdd:TIGR02169 743 EEDLSSLEQEIE-NVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREiEQKL 821
|
170 180
....*....|....*....|....*...
gi 392885956 696 KQSLFKcLGDARDTIKSLERRVQEFQIK 723
Cdd:TIGR02169 822 NRLTLE-KEYLEKEIQELQEQRIDLKEQ 848
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
512-722 |
4.04e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.90 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 512 IRSMSRELESLRSEISSRRSQEEDFKLQVSmhesnetRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERKYAD 591
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELE-------QLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 592 LLGKKAEIEATLSAERKARMEVtskkydvaehqRERERQLESEIDKLRIELKSKDESNMRMESELHGLRNYKEENDIDSL 671
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDL-----------EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 392885956 672 NMELRFVRdksHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQEFQI 722
Cdd:COG4372 175 ALSEAEAE---QALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLE 222
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
517-715 |
7.19e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.06 E-value: 7.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 517 RELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHR---ESDKHQLEQAERKYADLL 593
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVkelEELKEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 594 GKKAEIEATLSaERKARMEVTSKKYDVAEHQRERERQLE------SEIDKLRIELKSK----DESNMRMESELHGLRnyK 663
Cdd:PRK03918 252 GSKRKLEEKIR-ELEERIEELKKEIEELEEKVKELKELKekaeeyIKLSEFYEEYLDElreiEKRLSRLEEEINGIE--E 328
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 392885956 664 EENDIDSLNMELRFVRDKSHQMEESLageNKLKQSLfKCLGDARDTIKSLER 715
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRL---EELEERH-ELYEEAKAKKEELER 376
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
509-645 |
1.11e-05 |
|
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: 47.61 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 509 ETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMR----LKVEQMEIkcssierhrESDKHQLEQ 584
Cdd:COG1579 37 EDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeYEALQKEI---------ESLKRRISD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392885956 585 AERKYADLLGKKAEIEATLSAERKarmEVTSKKYDVAEHQRERERQLEsEIDKLRIELKSK 645
Cdd:COG1579 108 LEDEILELMERIEELEEELAELEA---ELAELEAELEEKKAELDEELA-ELEAELEELEAE 164
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
518-694 |
1.13e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.19 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 518 ELESLRSEISSRRSQEE--DFKLQVsmhESNETRLSQQLSNMRLK----VEQMEIKCSSIERHRESDKHQLEQAERKYAD 591
Cdd:COG5185 362 EIENIVGEVELSKSSEEldSFKDTI---ESTKESLDEIPQNQRGYaqeiLATLEDTLKAADRQIEELQRQIEQATSSNEE 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 592 LlgKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESEIDKLRIELKskdesnmRMESELHGLRNyKEENDIDSL 671
Cdd:COG5185 439 V--SKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELT-------QIESRVSTLKA-TLEKLRAKL 508
|
170 180
....*....|....*....|...
gi 392885956 672 NMELRFVRDKSHQMEESLAGENK 694
Cdd:COG5185 509 ERQLEGVRSKLDQVAESLKDFMR 531
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
509-675 |
1.46e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 509 ETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQ----LSNMRLKVEQME------IKCSSIERHRESD 578
Cdd:PRK03918 538 KGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEpfyneyLELKDAEKELERE 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 579 KHQLEQAERKYADLLGKKAEIEATLSaERKARMEVTSKKYDVAEHQRERER--QLESEIDKLRIELKSKDESNMRMESEL 656
Cdd:PRK03918 618 EKELKKLEEELDKAFEELAETEKRLE-ELRKELEELEKKYSEEEYEELREEylELSRELAGLRAELEELEKRREEIKKTL 696
|
170
....*....|....*....
gi 392885956 657 HGLRNYKEEndIDSLNMEL 675
Cdd:PRK03918 697 EKLKEELEE--REKAKKEL 713
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
494-719 |
2.03e-05 |
|
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: 47.84 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 494 FAAVRDSSHDTNASNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIER 573
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 574 HRESDKHQLEQAERKYADLL------GKKAEIEATLSAERKARMEVTSKKYD-VAEHQRERERQLESEIDKLRIELKSKD 646
Cdd:COG4942 91 EIAELRAELEAQKEELAELLralyrlGRQPPLALLLSPEDFLDAVRRLQYLKyLAPARREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 392885956 647 ESNMRMESELHGLRNYKEEndidsLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQE 719
Cdd:COG4942 171 AERAELEALLAELEEERAA-----LEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
434-717 |
2.77e-05 |
|
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: 47.79 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 434 SMTSTTKGRANTMPSTTRSQNNNNSQKQQKQSNGKSHHQHSSHQNNHQKSNGNSNGHARGFAAVrDSSHDTNASNETDIR 513
Cdd:pfam05483 24 AKSNLSKNGENIDSDPAFQKLNFLPMLEQVANSGDCHYQEGLKDSDFENSEGLSRLYSKLYKEA-EKIKKWKVSIEAELK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 514 SMSRELESLRSEISSRRS--QEEDF-------KLQVSMHESN----ETRLSQQLSNMrLKveqmEIKCSSIERhreSDKH 580
Cdd:pfam05483 103 QKENKLQENRKIIEAQRKaiQELQFenekvslKLEEEIQENKdlikENNATRHLCNL-LK----ETCARSAEK---TKKY 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 581 QLEQAERK--YADLlgkKAEIEATLSAERKARMEVTSKKYDV---AEHQRERERQLESEIDKlriELKSKDEsnmrmESE 655
Cdd:pfam05483 175 EYEREETRqvYMDL---NNNIEKMILAFEELRVQAENARLEMhfkLKEDHEKIQHLEEEYKK---EINDKEK-----QVS 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392885956 656 LHGLRNYKEENDIDSLNMELRFVRDKSHQMEE--SLAGENkLKQSLFK---CLGDARDTIKSLERRV 717
Cdd:pfam05483 244 LLLIQITEKENKMKDLTFLLEESRDKANQLEEktKLQDEN-LKELIEKkdhLTKELEDIKMSLQRSM 309
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
510-721 |
2.91e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.13 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 510 TDIRS-MSRELESLR--SEISSR----RSQEEDFKLQVSMHESNEtrLSQQLSNMRLKVEQMEIKCSSIERhresdkhQL 582
Cdd:TIGR02168 192 EDILNeLERQLKSLErqAEKAERykelKAELRELELALLVLRLEE--LREELEELQEELKEAEEELEELTA-------EL 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 583 EQAERKYADLLGKKAEIEATLSAERKARMEVTSKKYDV---AEHQRERERQLESEIDKLRIELKSKDESNMRMESELHGL 659
Cdd:TIGR02168 263 QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqKQILRERLANLERQLEELEAQLEELESKLDELAEELAEL 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 660 RNYKEE--NDIDSL------------NMELRF---------VRDKSHQMEESLAGENKLKQSLfkclgdaRDTIKSLERR 716
Cdd:TIGR02168 343 EEKLEElkEELESLeaeleeleaeleELESRLeeleeqletLRSKVAQLELQIASLNNEIERL-------EARLERLEDR 415
|
....*
gi 392885956 717 VQEFQ 721
Cdd:TIGR02168 416 RERLQ 420
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
513-755 |
3.56e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 3.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 513 RSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSnmrlKVEQMEIKCSSIERHRESDKH-----QLEQAER 587
Cdd:PTZ00121 1571 KAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK----KAEEAKIKAEELKKAEEEKKKveqlkKKEAEEK 1646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 588 KYADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESEIDKLRIELKSKDESNMRMESELHG---LRNYKE 664
Cdd:PTZ00121 1647 KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKaeeLKKAEE 1726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 665 ENDI--DSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKS----LERRVQEFQIKNGSSIGGGSSETLMN 738
Cdd:PTZ00121 1727 ENKIkaEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEkeavIEEELDEEDEKRRMEVDKKIKDIFDN 1806
|
250
....*....|....*..
gi 392885956 739 GRSSTEANNENDTTASD 755
Cdd:PTZ00121 1807 FANIIEGGKEGNLVIND 1823
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
506-718 |
3.70e-05 |
|
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: 47.81 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 506 ASNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRlsqQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQa 585
Cdd:pfam15921 274 SEHEVEITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR---QLSDLESTVSQLRSELREAKRMYEDKIEELEK- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 586 ERKYADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESE---------------IDKLRIELKSKDESNM 650
Cdd:pfam15921 350 QLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKEqnkrlwdrdtgnsitIDHLRRELDDRNMEVQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 651 RMESELHGLRNY--------------KEEN--DIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLE 714
Cdd:pfam15921 430 RLEALLKAMKSEcqgqmerqmaaiqgKNESleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKE 509
|
....
gi 392885956 715 RRVQ 718
Cdd:pfam15921 510 RAIE 513
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
571-721 |
4.78e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 4.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 571 IERHRESDKHQLEQAERkYADL--LGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERE------RQLESEIDKLRIEL 642
Cdd:COG1196 198 LERQLEPLERQAEKAER-YRELkeELKELEAELLLLKLRELEAELEELEAELEELEAELEeleaelAELEAELEELRLEL 276
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392885956 643 KSKDEsnmrmESELHGLRNYKEENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQEFQ 721
Cdd:COG1196 277 EELEL-----ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAE 350
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
514-723 |
5.33e-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: 47.09 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 514 SMSRELES-LRSEISSRRSQEedfKLQVSMH-ESNETR-----LSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAE 586
Cdd:pfam01576 187 AMISDLEErLKKEEKGRQELE---KAKRKLEgESTDLQeqiaeLQAQIAELRAQLAKKEEELQAALARLEEETAQKNNAL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 587 RKYADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESEIDK--LRIELKSKDESNMRM------------ 652
Cdd:pfam01576 264 KKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTtaAQQELRSKREQEVTElkkaleeetrsh 343
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392885956 653 ESELHGLRNyKEENDIDSLNMEL-RFVRDKS--HQMEESLAGENKLKQSLFKCL----GDARDTIKSLERRVQEFQIK 723
Cdd:pfam01576 344 EAQLQEMRQ-KHTQALEELTEQLeQAKRNKAnlEKAKQALESENAELQAELRTLqqakQDSEHKRKKLEGQLQELQAR 420
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
504-721 |
5.38e-05 |
|
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: 47.04 E-value: 5.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 504 TNASNETDIRSMSReleSLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSierhresdkHQLE 583
Cdd:pfam05557 94 EKESQLADAREVIS---CLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN---------LEKQ 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 584 QAERKYADLLGKKAEIEATLSAERKARME-VTSKKYDVAEHQRERERQLEsEIDKLRiELKskdESNMRMESELHGLRN- 661
Cdd:pfam05557 162 QSSLAEAEQRIKELEFEIQSQEQDSEIVKnSKSELARIPELEKELERLRE-HNKHLN-ENI---ENKLLLKEEVEDLKRk 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392885956 662 -YKEENDIDSL-NMELrfvrDKSHqMEESLAGENKLKQSlfKCLgdardTIKS---LERRVQEFQ 721
Cdd:pfam05557 237 lEREEKYREEAaTLEL----EKEK-LEQELQSWVKLAQD--TGL-----NLRSpedLSRRIEQLQ 289
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
512-719 |
5.52e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 47.24 E-value: 5.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 512 IRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQM----------EIKCSSIERHRESDKHQ 581
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAqaeeyellaeLARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 582 LEQAERKY--------ADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESEIDKLRiELKSKDESNMRME 653
Cdd:COG1196 314 LEERLEELeeelaeleEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-ELEELAEELLEAL 392
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392885956 654 SELHGLRNYKE--ENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQE 719
Cdd:COG1196 393 RAAAELAAQLEelEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
510-724 |
6.30e-05 |
|
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: 46.94 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 510 TDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSI----ERHR---------E 576
Cdd:TIGR04523 145 TEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLkkkiQKNKslesqiselK 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 577 SDKHQLE-QAERKYADLLGKKAEIEatlsaerkarmEVTSKKYDVAEHQRERERQLE---SEIDKLRIELKSKDESNMRM 652
Cdd:TIGR04523 225 KQNNQLKdNIEKKQQEINEKTTEIS-----------NTQTQLNQLKDEQNKIKKQLSekqKELEQNNKKIKELEKQLNQL 293
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392885956 653 ESELHGLRNYKEENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLfkclgdaRDTIKSLERRVQEFQIKN 724
Cdd:TIGR04523 294 KSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQL-------NEQISQLKKELTNSESEN 358
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
495-723 |
6.39e-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: 6.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 495 AAVRD--SSHDTNASNETDIRSMSRELESLRSEISSRRSQEedfKLQVSMHESNETR--LSQQLSNMRLKVEQMEIKCSS 570
Cdd:pfam15905 112 AAVREktSLSASVASLEKQLLELTRVNELLKAKFSEDGTQK---KMSSLSMELMKLRnkLEAKMKEVMAKQEGMEGKLQV 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 571 IERHRESDKHQLEQAERK----YADLLGKKAEIE------ATLSAERKaRMEVTSKKYDVAEhqrERERQLESEIDKLRI 640
Cdd:pfam15905 189 TQKNLEHSKGKVAQLEEKlvstEKEKIEEKSETEklleyiTELSCVSE-QVEKYKLDIAQLE---ELLKEKNDEIESLKQ 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 641 ELKSKDEsnmrmesELhglrnYKEENDIDSLNMELRfvrdksHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQEF 720
Cdd:pfam15905 265 SLEEKEQ-------EL-----SKQIKDLNEKCKLLE------SEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKL 326
|
...
gi 392885956 721 QIK 723
Cdd:pfam15905 327 QQK 329
|
|
| CCDC144C |
pfam14915 |
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ... |
490-634 |
7.20e-05 |
|
CCDC144C protein coiled-coil region; This family includes the human protein CCDC144C and the ankyrin repeat domain-containing protein 26-like 1 found in eukaryotes. Its function remains unknown, however, it is known to contain a coiled-coil domain which corresponds to this region. The ankyrin repeat which features in this protein is a common amino acid motif.
Pssm-ID: 464371 [Multi-domain] Cd Length: 304 Bit Score: 45.75 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 490 HARGFAAVRDssHDTNASNETDIrsmsreleslrsEISSRRSQEEDFKLQVSMH-------ESNETrLSQQLSNMRLKVE 562
Cdd:pfam14915 97 RSRLAAAIQD--HEQSQTSKRDL------------ELAFQRERDEWLRLQDKMNfdvsnlrDENEI-LSQQLSKAESKAN 161
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392885956 563 QMEIKCssierHRESDKHQ-----LEQAERKYADLLGKKAEIEATLSAERKARMEVTSKKydvaEHQRERERQLESE 634
Cdd:pfam14915 162 SLENEL-----HRTRDALRektllLESVQRDLSQAQCQKKELEHMYQNEQDKVNKYIGKQ----ESLEERLAQLQSE 229
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
579-697 |
8.43e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.39 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 579 KHQLEQAERK---YADLLGKKAE------IEATLSAERKARMEVTSKKYDVAEH--------QRERERQLESEIDKLRIE 641
Cdd:COG2433 349 KNKFERVEKKvppDVDRDEVKARvirglsIEEALEELIEKELPEEEPEAEREKEheerelteEEEEIRRLEEQVERLEAE 428
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392885956 642 -------LKSKDESNMRMESELHGLRN--YKE----------ENDIDSLNMELRFVRDKSHQMEESLAgenKLKQ 697
Cdd:COG2433 429 veeleaeLEEKDERIERLERELSEARSeeRREirkdreisrlDREIERLERELEEERERIEELKRKLE---RLKE 500
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
525-718 |
8.49e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 46.04 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 525 EISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERKYADLLGKKAEIE---A 601
Cdd:pfam07888 60 EKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEediK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 602 TLSA---ERKARMEVTSKKYDVAEHQRERErqlESEIDKLRIELKSKDESNMRMESELHGLRNYKEENDIDSLNMelrfv 678
Cdd:pfam07888 140 TLTQrvlERETELERMKERAKKAGAQRKEE---EAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQL----- 211
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 392885956 679 RDKSHQMEESLAGENKLK---QSLFKCLGDARDTIKSLERRVQ 718
Cdd:pfam07888 212 QDTITTLTQKLTTAHRKEaenEALLEELRSLQERLNASERKVE 254
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
509-675 |
9.04e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 9.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 509 ETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERK 588
Cdd:COG4372 65 EEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 589 YADLLGKKAEIEATLSAERK--ARMEVTSKKYDVAEHQRERERQLESEIDKLRIELKSKDESNMRMESELHGLRNYKEEN 666
Cdd:COG4372 145 IAEREEELKELEEQLESLQEelAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAK 224
|
....*....
gi 392885956 667 DIDSLNMEL 675
Cdd:COG4372 225 DSLEAKLGL 233
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
510-719 |
9.80e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 46.19 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 510 TDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERky 589
Cdd:PRK02224 251 EELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRD-- 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 590 aDLLGKKAEIEATLS-----AERKARMEvtskkyDVAEHQRERERQLESEIDKLRIELKSKDESNMRMESELHGLRNYKE 664
Cdd:PRK02224 329 -RLEECRVAAQAHNEeaeslREDADDLE------ERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 392885956 665 ENDIDslnmelrfvRDKSHQMEESLAGE-NKLKQSlfkcLGDARDTIKSLERRVQE 719
Cdd:PRK02224 402 DAPVD---------LGNAEDFLEELREErDELRER----EAELEATLRTARERVEE 444
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
512-724 |
1.54e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 512 IRSMSRELESLRSEISsrrsQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHR---ESDKHQLEQAERK 588
Cdd:PRK03918 171 IKEIKRRIERLEKFIK----RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVkelEELKEEIEELEKE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 589 YADLLGKKAEIEATLSAERKARMEVtskkydvaehqRERERQLESEIDKLRiELKSKDESNMRMESELhglRNYKEEndi 668
Cdd:PRK03918 247 LESLEGSKRKLEEKIRELEERIEEL-----------KKEIEELEEKVKELK-ELKEKAEEYIKLSEFY---EEYLDE--- 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 392885956 669 dslnmelrfvrdkshqmeeslagenklKQSLFKCLGDARDTIKSLERRVQEFQIKN 724
Cdd:PRK03918 309 ---------------------------LREIEKRLSRLEEEINGIEERIKELEEKE 337
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
509-655 |
1.62e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 509 ETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERK 588
Cdd:COG4372 44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392885956 589 YADLLGKKAEIEAtlsaerkarmEVTSKKYDVAEHQRERErQLESEIDKLRIELKSKDESNMRMESE 655
Cdd:COG4372 124 RQDLEQQRKQLEA----------QIAELQSEIAEREEELK-ELEEQLESLQEELAALEQELQALSEA 179
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
507-715 |
1.86e-04 |
|
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: 45.55 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 507 SNETDIRSMSRELESLRSEIssrrSQEEDFKLQVSMHESNetrLSQQLSNMRLKVEQMeikCSSIErhresdkhQLEQAE 586
Cdd:pfam01576 486 NLSTRLRQLEDERNSLQEQL----EEEEEAKRNVERQLST---LQAQLSDMKKKLEED---AGTLE--------ALEEGK 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 587 RKYadllgkKAEIEATLSaerkaRMEVTSKKYDVAEHQRERERQlesEIDKLRIELKSKDE--SNMRmeselhglrnyKE 664
Cdd:pfam01576 548 KRL------QRELEALTQ-----QLEEKAAAYDKLEKTKNRLQQ---ELDDLLVDLDHQRQlvSNLE-----------KK 602
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 392885956 665 ENDIDSLNMELRFV-------RDKShqmeESLAGENKLKQ-SLFKCLGDARDTIKSLER 715
Cdd:pfam01576 603 QKKFDQMLAEEKAIsaryaeeRDRA----EAEAREKETRAlSLARALEEALEAKEELER 657
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
529-642 |
2.65e-04 |
|
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: 44.14 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 529 RRSQEEDFKLQvsmhesnETRLSQQLSNMRLKVEQMEIKcssiERHRESDKHQLEQAERKYADLLGKKAEIEATLSAERK 608
Cdd:pfam13868 108 ERIQEEDQAEA-------EEKLEKQRQLREEIDEFNEEQ----AEWKELEKEEEREEDERILEYLKEKAEREEEREAERE 176
|
90 100 110
....*....|....*....|....*....|....
gi 392885956 609 ARMEVTSKKYDVAEHQRERERQLESEIDKLRIEL 642
Cdd:pfam13868 177 EIEEEKEREIARLRAQQEKAQDEKAERDELRAKL 210
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
513-719 |
3.28e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.67 E-value: 3.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 513 RSMSRELESLRSEISS------RRSQEEDFKLQvsmHESNEtrLSQQLSNMRLKVEQMEikcsSIERHRESDKHQLEQAE 586
Cdd:PRK03918 499 KELAEQLKELEEKLKKynleelEKKAEEYEKLK---EKLIK--LKGEIKSLKKELEKLE----ELKKKLAELEKKLDELE 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 587 RKYADLLGK--------KAEIEATLSAERKARMEVTSKKYDVAEHQRERERQ--LESEIDKLRIELKSKDESNMRMESEL 656
Cdd:PRK03918 570 EELAELLKEleelgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKELkkLEEELDKAFEELAETEKRLEELRKEL 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392885956 657 HGL-RNYKEEndidslnmELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQE 719
Cdd:PRK03918 650 EELeKKYSEE--------EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
549-697 |
3.56e-04 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 44.28 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 549 RLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERKYADLlgkKAEIEATLSAERKARMEVtskkydvaEHQRERE 628
Cdd:pfam05911 685 RLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAEL---RSELASLKESNSLAETQL--------KCMAESY 753
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 392885956 629 RQLESEIDKLRIELKSKDESNMRMESELHGLRNYKEENDIDSLNMELRFVRDKSHQMEESLAG--ENKLKQ 697
Cdd:pfam05911 754 EDLETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAKCLELQEQLERNEKKESSNCDADqeDKKLQQ 824
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
507-644 |
3.59e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 507 SNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQ--QLSNMRLKVEQMEIKCSSIERhRESDKHQleq 584
Cdd:COG3206 216 LLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSA-RYTPNHP--- 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 585 aerKYADLLGKKAEIEATLSAERKARMEVTSKKYDVAehqRERERQLESEIDKLRIELKS 644
Cdd:COG3206 292 ---DVIALRAQIAALRAQLQQEAQRILASLEAELEAL---QAREASLQAQLAQLEARLAE 345
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
499-608 |
3.80e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 499 DSSHDTNASNETDIRSMSRELESLRSEISSRRSQEEdfKLQVSMHESnETRLSQQLSNMRLKVEQMEIKCSSIerhresd 578
Cdd:pfam00038 206 ARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA--SLERQLAET-EERYELQLADYQELISELEAELQET------- 275
|
90 100 110
....*....|....*....|....*....|
gi 392885956 579 KHQLEQAERKYADLLGKKAEIEATLSAERK 608
Cdd:pfam00038 276 RQEMARQLREYQELLNVKLALDIEIATYRK 305
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
511-720 |
4.61e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.90 E-value: 4.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 511 DIRSMSRELESLRSEISSRRSQEEDFKLQVSMHEsnetRLSQQLSNMR--------LKVEQMEIKCSSIERHRESDKHQL 582
Cdd:PRK03918 332 ELEEKEERLEELKKKLKELEKRLEELEERHELYE----EAKAKKEELErlkkrltgLTPEKLEKELEELEKAKEEIEEEI 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 583 EQAERKYADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQR----------------------ERERQLESEIDKLRI 640
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRkelleeytaelkriekelkeieEKERKLRKELRELEK 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 641 ELKSKDE-SNMR--------MESELHGL------------RNYKEE---------------NDIDSLNMELRFVRDKSHQ 684
Cdd:PRK03918 488 VLKKESElIKLKelaeqlkeLEEKLKKYnleelekkaeeyEKLKEKliklkgeikslkkelEKLEELKKKLAELEKKLDE 567
|
250 260 270
....*....|....*....|....*....|....*..
gi 392885956 685 MEESLAG-ENKLKQSLFKCLGDARDTIKSLERRVQEF 720
Cdd:PRK03918 568 LEEELAElLKELEELGFESVEELEERLKELEPFYNEY 604
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
572-664 |
5.34e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 41.18 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 572 ERHR----ESDKHQLEQAERKYADLLGKKAEIEATLSAERKARMEV-TSKKYDVAEHQRERERQLESEIDKLRIELKSK- 645
Cdd:pfam05672 31 EQERlekeEEERLRKEELRRRAEEERARREEEARRLEEERRREEEErQRKAEEEAEEREQREQEEQERLQKQKEEAEAKa 110
|
90 100
....*....|....*....|.
gi 392885956 646 --DESNMRMESELHGLRNYKE 664
Cdd:pfam05672 111 reEAERQRQEREKIMQQEEQE 131
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
490-720 |
7.73e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 43.21 E-value: 7.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 490 HARGFAAVRDSSHDTNASNETDirsMSRELESLRSEIS------SRRSQEEDFKLQVSMHEsNETRLSQQLSNMRLKVEQ 563
Cdd:pfam09731 237 KAQSLAKLVDQYKELVASERIV---FQQELVSIFPDIIpvlkedNLLSNDDLNSLIAHAHR-EIDQLSKKLAELKKREEK 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 564 meikcsSIERHRESDKHQLEQAERKyadllgkkaeieatLSAERKARMEVTSKKYDvAEHQRERERQLESEIDKLRIELK 643
Cdd:pfam09731 313 ------HIERALEKQKEELDKLAEE--------------LSARLEEVRAADEAQLR-LEFEREREEIRESYEEKLRTELE 371
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 392885956 644 SKDESNmrmesELHgLRNYKEENDIDslnMELRFVRD-KSHQMEESlagENKLKQslfkcLGDARDTIKSLERRVQEF 720
Cdd:pfam09731 372 RQAEAH-----EEH-LKDVLVEQEIE---LQREFLQDiKEKVEEER---AGRLLK-----LNELLANLKGLEKATSSH 432
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
514-719 |
8.17e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.12 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 514 SMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQL-------SNMRLKVEQMEIKCSSIERHRESDKHQLEQAE 586
Cdd:TIGR02168 660 VITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALaelrkelEELEEELEQLRKELEELSRQISALRKDLARLE 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 587 RKYADLLGKKAEIEATLSAERKARMEVTSK--KYDVAEHQRERER-QLESEIDKLRIELKSKDEsnmrmeselhglrnyk 663
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELEAEIEELEERleEAEEELAEAEAEIeELEAQIEQLKEELKALRE---------------- 803
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 392885956 664 eenDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQE 719
Cdd:TIGR02168 804 ---ALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
520-689 |
1.08e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 41.55 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 520 ESLRSEISS--RRSQ--EEDFklqvsmhESNETRL---SQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERKYadl 592
Cdd:pfam00261 32 EKAEAEVAAlnRRIQllEEEL-------ERTEERLaeaLEKLEEAEKAADESERGRKVLENRALKDEEKMEILEAQL--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 593 lgkKAEIEATLSAERKArMEVTSKKYDVA---EHQRERERQLESEIDKLRIELK-----------SKDESNMRMESELHG 658
Cdd:pfam00261 102 ---KEAKEIAEEADRKY-EEVARKLVVVEgdlERAEERAELAESKIVELEEELKvvgnnlksleaSEEKASEREDKYEEQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 392885956 659 LRNYKE-------------------ENDIDSLNMELRFVRDKSHQMEESL 689
Cdd:pfam00261 178 IRFLTEklkeaetraefaersvqklEKEVDRLEDELEAEKEKYKAISEEL 227
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
508-660 |
1.18e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.59 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 508 NETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSN------MRLK--VEQMEIKCSSIERHRESDK 579
Cdd:COG4913 286 AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggdrlEQLEreIERLERELEERERRRARLE 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 580 HQLEQAERKY----ADLLGKKAEIEATLSAERKARMEVTSKKYDvaehQRERERQLESEIDKLRIELKSKDESNMRMESE 655
Cdd:COG4913 366 ALLAALGLPLpasaEEFAALRAEAAALLEALEEELEALEEALAE----AEAALRDLRRELRELEAEIASLERRKSNIPAR 441
|
....*
gi 392885956 656 LHGLR 660
Cdd:COG4913 442 LLALR 446
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
518-719 |
1.25e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 42.72 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 518 ELESLRSEISSRRSQEEDfklqvsmhesnetrLSQQLSNMRLKVEQMEIKCSSIERHREsdkhqlEQAERKyADLLGKKA 597
Cdd:PRK02224 371 ELEEAREAVEDRREEIEE--------------LEEEIEELRERFGDAPVDLGNAEDFLE------ELREER-DELREREA 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 598 EIEATLSAERKARMEVT-----------------SKKYDVAEHQRERERQLESEIDKLRIELKSKDESNMRM------ES 654
Cdd:PRK02224 430 ELEATLRTARERVEEAEalleagkcpecgqpvegSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAedlveaED 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392885956 655 ELHGLRNYKE---------ENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQE 719
Cdd:PRK02224 510 RIERLEERREdleeliaerRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAE 583
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
506-696 |
1.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 506 ASNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQA 585
Cdd:COG4372 69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 586 ERKYADLLGKKAEIEATLSA--ERKARMEVTSKKYDVAEHQRERERQLESEIDKLRIELKSKDESNMRMESELHGLRNYK 663
Cdd:COG4372 149 EEELKELEEQLESLQEELAAleQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE 228
|
170 180 190
....*....|....*....|....*....|....*
gi 392885956 664 EEND--IDSLNMELRFVRDKSHQMEESLAGENKLK 696
Cdd:COG4372 229 AKLGlaLSALLDALELEEDKEELLEEVILKEIEEL 263
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
491-653 |
1.35e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 42.82 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 491 ARGFAAVRDSSHDTNASNETDIRSMSRELESLRSEISSRRSQEE---------------DFKLQVSMHESNETRLSQQLS 555
Cdd:PTZ00121 1205 ARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEErnneeirkfeearmaHFARRQAAIKAEEARKADELK 1284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 556 NMRLKVEQMEIKCSSIERHRESDKHQLEQAER------------KYADLLGKKAEiEATLSAE-RKARMEVTSKKYDVAE 622
Cdd:PTZ00121 1285 KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKadeakkkaeeakKKADAAKKKAE-EAKKAAEaAKAEAEAAADEAEAAE 1363
|
170 180 190
....*....|....*....|....*....|.
gi 392885956 623 HQRERERQLESEIDKLRIELKSKDESNMRME 653
Cdd:PTZ00121 1364 EKAEAAEKKKEEAKKKADAAKKKAEEKKKAD 1394
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
515-645 |
1.48e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 515 MSRELE----SLRSEISSRRSQEEDFKLQVSMHESNEtRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERKYA 590
Cdd:pfam15709 374 MREELEleqqRRFEEIRLRKQRLEEERQRQEEEERKQ-RLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQ 452
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 392885956 591 dllgKKAEIEATLSAERKARMEVTSK---KYDVAEHQRERERQLESEIDKLRIELKSK 645
Cdd:pfam15709 453 ----RQKELEMQLAEEQKRLMEMAEEerlEYQRQKQEAEEKARLEAEERRQKEEEAAR 506
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
509-697 |
1.81e-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: 41.93 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 509 ETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERhresdkhQLEQAERK 588
Cdd:TIGR04523 355 ESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQ-------EKELLEKE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 589 YADLLGKKAEIEATLSAERKarmEVTSKKYDVAEHQRERERQ------LESEIDKLRIELKSKDESNMRMESELHGLRNY 662
Cdd:TIGR04523 428 IERLKETIIKNNSEIKDLTN---QDSVKELIIKNLDNTRESLetqlkvLSRSINKIKQNLEQKQKELKSKEKELKKLNEE 504
|
170 180 190
....*....|....*....|....*....|....*...
gi 392885956 663 KE--ENDIDSLNMELRFVRDKSHQME-ESLAGENKLKQ 697
Cdd:TIGR04523 505 KKelEEKVKDLTKKISSLKEKIEKLEsEKKEKESKISD 542
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
496-689 |
1.96e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 41.60 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 496 AVRDSSHDTNASnetdirsMSRELesLRSEISSR--RSQEEDFKLQVSMHESNETR---LSQQLSNMRLKVEQMEI---- 566
Cdd:pfam05622 259 ALLSPSSDPGDN-------LAAEI--MPAEIREKliRLQHENKMLRLGQEGSYRERlteLQQLLEDANRRKNELETqnrl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 567 ---KCSSIERHRESDKHQLEQAERKYADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESEIDKLRIELK 643
Cdd:pfam05622 330 anqRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEPKQDSNLAQKIDELQEALR 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 392885956 644 SKDESNMRME--------------------------SELHGLRNYKEEND--IDSLNMELrfvrDKS---HQMEESL 689
Cdd:pfam05622 410 KKDEDMKAMEerykkyvekaksviktldpkqnpaspPEIQALKNQLLEKDkkIEHLERDF----EKSklqREQEEKL 482
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
532-716 |
2.07e-03 |
|
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: 42.08 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 532 QEEDFKL---QVSMHESNETRLSQQLSNMRLKVEQMeikcsSIERHRESDKHQLEQ-----AERKYADLLGKKAEIEATL 603
Cdd:pfam01576 3 QEEEMQAkeeELQKVKERQQKAESELKELEKKHQQL-----CEEKNALQEQLQAETelcaeAEEMRARLAARKQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 604 SaERKARME--------VTSKKYDVAEHQRERERQLESEID---KLRIELKSKDESNMRMESELHGLrnykeENDIDSLN 672
Cdd:pfam01576 78 H-ELESRLEeeeersqqLQNEKKKMQQHIQDLEEQLDEEEAarqKLQLEKVTTEAKIKKLEEDILLL-----EDQNSKLS 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 392885956 673 MELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERR 716
Cdd:pfam01576 152 KERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEER 195
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
509-721 |
2.48e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 509 ETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEikcssierhresdkHQLEQAERK 588
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE--------------LELEEAQAE 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 589 YADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLES---EIDKLRIELKSKDESNMRMESELHGLRNYKEE 665
Cdd:COG1196 290 EYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEleeELEELEEELEEAEEELEEAEAELAEAEEALLE 369
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 392885956 666 NDIDSLNMELRFVRDKSHQMEESLAGENKLKQslfkcLGDARDTIKSLERRVQEFQ 721
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQ-----LEELEEAEEALLERLERLE 420
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
494-696 |
2.52e-03 |
|
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: 41.70 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 494 FAAVRDSSHDTNASNETDIRSMSRELE--------------SLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRL 559
Cdd:pfam01576 620 YAEERDRAEAEAREKETRALSLARALEealeakeelertnkQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVEEMKT 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 560 KVEQMEIKCSSIERHR-------ESDKHQL--------EQAERKYADLLGKKAEIEATLSAERKAR-MEVTSKKydvaeh 623
Cdd:pfam01576 700 QLEELEDELQATEDAKlrlevnmQALKAQFerdlqardEQGEEKRRQLVKQVRELEAELEDERKQRaQAVAAKK------ 773
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392885956 624 QRERE-RQLESEIDKLRielKSKDESNMRMESELHGLRNYKEENDidslnmELRFVRDKS-HQMEESlagENKLK 696
Cdd:pfam01576 774 KLELDlKELEAQIDAAN---KGREEAVKQLKKLQAQMKDLQRELE------EARASRDEIlAQSKES---EKKLK 836
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
506-724 |
4.06e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.79 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 506 ASNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQ- 584
Cdd:PRK02224 373 EEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAg 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 585 ---------AERKYADLLGKKAEIEATLSAER---KARMEVTSKKYDVAEHQRERERQLES------------------- 633
Cdd:PRK02224 453 kcpecgqpvEGSPHVETIEEDRERVEELEAELedlEEEVEEVEERLERAEDLVEAEDRIERleerredleeliaerreti 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 634 EIDKLRIELKSKDESNMRMESELHGLRNYKEENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKcLGDARDTIKSL 713
Cdd:PRK02224 533 EEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAA-IADAEDEIERL 611
|
250
....*....|.
gi 392885956 714 ERRVQEFQIKN 724
Cdd:PRK02224 612 REKREALAELN 622
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
505-637 |
4.66e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 40.53 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 505 NASNETDIRSMSRELESlRSEISSRRSQ-EEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLE 583
Cdd:PRK12704 46 EAKKEAEAIKKEALLEA-KEEIHKLRNEfEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQ 124
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 392885956 584 QAERKYADLLGKKAEIE------ATLSAErKARMEVTSK-----KYDVAEHQRERERQLESEIDK 637
Cdd:PRK12704 125 ELEKKEEELEELIEEQLqeleriSGLTAE-EAKEILLEKveeeaRHEAAVLIKEIEEEAKEEADK 188
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
499-719 |
4.67e-03 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 40.40 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 499 DSSHDTNASNETDIRSMSRELESLRSEISSRRSQEEDF--KLQVSMHESNETR-----LSQQLSNMRLKVEQMEIKCSSI 571
Cdd:pfam05701 127 EVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAikRAEEAVSASKEIEktveeLTIELIATKESLESAHAAHLEA 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 572 ERHR-------ESDKHQ----LEQAE----RKYADLLGK---KAEIEAT------LSAERKARMEVTSKKYDVAEHQRER 627
Cdd:pfam05701 207 EEHRigaalarEQDKLNwekeLKQAEeelqRLNQQLLSAkdlKSKLETAsallldLKAELAAYMESKLKEEADGEGNEKK 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 628 -ERQLESEIDKLRIEL--------KSKDESN--------MRME-----SELHGLRnyKEEN----DIDSLNMELRFVRDK 681
Cdd:pfam05701 287 tSTSIQAALASAKKELeevkanieKAKDEVNclrvaaasLRSElekekAELASLR--QREGmasiAVSSLEAELNRTKSE 364
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 392885956 682 --SHQMEESLAGENKLKqsLFKCLGDAR---DTIKSLERRVQE 719
Cdd:pfam05701 365 iaLVQAKEKEAREKMVE--LPKQLQQAAqeaEEAKSLAQAARE 405
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
614-721 |
5.25e-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: 40.00 E-value: 5.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 614 TSKKYDVAEHQRERERQLESEI--------DKLRIELKSKDESNMRMESELHGLRNYKE--ENDIDSLNmelrfvrDKSH 683
Cdd:smart00787 177 LRDRKDALEEELRQLKQLEDELedcdptelDRAKEKLKKLLQEIMIKVKKLEELEEELQelESKIEDLT-------NKKS 249
|
90 100 110
....*....|....*....|....*....|....*...
gi 392885956 684 QMEESLageNKLKQSLFKCLGDARDTIKSLERRVQEFQ 721
Cdd:smart00787 250 ELNTEI---AEAEKKLEQCRGFTFKEIEKLKEQLKLLQ 284
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
517-642 |
6.11e-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: 39.90 E-value: 6.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 517 RELESLRSEISSRRSQEEDFKLQVsmhESNETRLSQQLSNMRLKVEQMeikcssIERHRESDKHQLEQAERKYADLLGKK 596
Cdd:pfam13868 222 KEREEAEKKARQRQELQQAREEQI---ELKERRLAEEAEREEEEFERM------LRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 392885956 597 AEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESEIDKLRIEL 642
Cdd:pfam13868 293 RELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| CENP-F_leu_zip |
pfam10473 |
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ... |
509-590 |
6.45e-03 |
|
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.
Pssm-ID: 463102 [Multi-domain] Cd Length: 140 Bit Score: 38.05 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 509 ETDIRSMSRELESLRSEISSRRSQEEDfklqvsmhesnetrLSQQLSNMRLKVEQMEIKCSSIE---RHRESDKHQLEQa 585
Cdd:pfam10473 58 KAEIEEMAQNLRDLELDLVTLRSEKEN--------------LTKELQKKQERVSELESLNSSLEnllEEKEQEKVQMKE- 122
|
....*
gi 392885956 586 ERKYA 590
Cdd:pfam10473 123 ESKTA 127
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
509-722 |
7.02e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 39.52 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 509 ETDIRSMSRELESLRS----EISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMeikcssIERHRESDKhqlEQ 584
Cdd:pfam00038 123 EAKIESLKEELAFLKKnheeEVRELQAQVSDTQVNVEMDAARKLDLTSALAEIRAQYEEI------AAKNREEAE---EW 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 585 AERKYADLlgkkaeieaTLSAERkarmevtskkydvaehQRERERQLESEIDKLRIELKSkdesnmrMESELHGLRNYKE 664
Cdd:pfam00038 194 YQSKLEEL---------QQAAAR----------------NGDALRSAKEEITELRRTIQS-------LEIELQSLKKQKA 241
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392885956 665 --ENDI----DSLNMELRFVRDKSHQMEESLAgenklkqslfkclgDARDTiksLERRVQEFQI 722
Cdd:pfam00038 242 slERQLaeteERYELQLADYQELISELEAELQ--------------ETRQE---MARQLREYQE 288
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
582-721 |
9.74e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 39.75 E-value: 9.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392885956 582 LEQAERKYADLL---GKKAEIEAT-LSAERKARMEVTSKKYDVAEHQRERErQLESEIDKLRIELKSKDESNMRMESELH 657
Cdd:COG4717 48 LERLEKEADELFkpqGRKPELNLKeLKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 392885956 658 GLRNYKEENDI-----------DSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGD----ARDTIKSLERRVQEFQ 721
Cdd:COG4717 127 LLPLYQELEALeaelaelperlEELEERLEELRELEEELEELEAELAELQEELEELLEQlslaTEEELQDLAEELEELQ 205
|
|
| |
