|
Name |
Accession |
Description |
Interval |
E-value |
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
548-952 |
1.29e-15 |
|
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: 81.99 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 548 DLMNKHKQLQLQLNAKITEIQnlQANGaaaqrpeqpnyepELLALRQQLAHLQSELQTAHAQRQEfeihyhqirELAEQK 627
Cdd:TIGR04523 257 QLKDEQNKIKKQLSEKQKELE--QNNK-------------KIKELEKQLNQLKSEISDLNNQKEQ---------DWNKEL 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 628 DHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQIyvkidnlTAENRDLTDK 707
Cdd:TIGR04523 313 KSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKL-------KKENQSYKQE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 708 IAQLQVSDSLELEELEELRNKNLELQEQVKQL---KEELEKEKSVAGSGNSGGWSDIDDNEVVEAVQPI---ETTPISSE 781
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLqqeKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELiikNLDNTRES 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 782 NSENLKKFEAEIAELKASLEKTEKELTkyrnlynEKLTAIsDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKE-- 859
Cdd:TIGR04523 466 LETQLKVLSRSINKIKQNLEQKQKELK-------SKEKEL-KKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEke 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 860 -----LSDRLNEMLKNL------------NQSMQKSAENDKML----TQLREEAFAKEKQLLEHDSVLRKKDDKIRELDA 918
Cdd:TIGR04523 538 skisdLEDELNKDDFELkkenlekeidekNKEIEELKQTQKSLkkkqEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
410 420 430
....*....|....*....|....*....|....
gi 32565309 919 EFKRVKMEYVKLETKsfhdVRKLNMDVEELKTQL 952
Cdd:TIGR04523 618 ELEKAKKENEKLSSI----IKNIKSKKNKLKQEV 647
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
548-931 |
1.65e-13 |
|
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: 75.06 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 548 DLMNKHKQLQLQLNAKITEIQNLQAngaaaqrpEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQK 627
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKK--------ENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 628 DHQIAQL---TEQANDYQERLEKSQSELQELARHVDSARAELmDSQTSDYGRQ-----QELMEKQAELEQIYVKIDNLTA 699
Cdd:TIGR04523 425 EKEIERLketIIKNNSEIKDLTNQDSVKELIIKNLDNTRESL-ETQLKVLSRSinkikQNLEQKQKELKSKEKELKKLNE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 700 ENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEELEKEKSVAGSGNSGGWSDIDDNEVVEAVQpiETTPIS 779
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKQ--TQKSLK 581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 780 SENSE---NLKKFEAEIAELKASLEKTEKELTKYrnlynEKLTAISDKENRSQIEMEHKLKNAESDLQEakrRAEEIGAE 856
Cdd:TIGR04523 582 KKQEEkqeLIDQKEKEKKDLIKEIEEKEKKISSL-----EKELEKAKKENEKLSSIIKNIKSKKNKLKQ---EVKQIKET 653
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32565309 857 KKELSDRLNEMLKNLNQSMQKSAE-NDKMLTQLREEAFAKEKQLLEHdsvLRKKDdkIRELDAEFKRVKMEYVKLE 931
Cdd:TIGR04523 654 IKEIRNKWPEIIKKIKESKTKIDDiIELMKDWLKELSLHYKKYITRM---IRIKD--LPKLEEKYKEIEKELKKLD 724
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
589-952 |
1.83e-13 |
|
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: 75.15 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 589 LLALRQQLAHLQSELQtahaQRQEFEIHYHQ--IRELAEQKDHQIAQLTE-------QANDYQERLEKSQSE-------- 651
Cdd:pfam15921 240 IFPVEDQLEALKSESQ----NKIELLLQQHQdrIEQLISEHEVEITGLTEkassarsQANSIQSQLEIIQEQarnqnsmy 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 652 ---LQELARHVDSARAELMDSQTSdYGRQQELMEKQ-----AELEQIYVKIDNLTAENRDLTDKIAQL--QVSDSLELEE 721
Cdd:pfam15921 316 mrqLSDLESTVSQLRSELREAKRM-YEDKIEELEKQlvlanSELTEARTERDQFSQESGNLDDQLQKLlaDLHKREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 722 LEELRNKNL----------------ELQE---QVKQLKEELEKEKSVAGSGNSGGWSDID-DNEVVEAVQPIeTTPISSe 781
Cdd:pfam15921 395 LEKEQNKRLwdrdtgnsitidhlrrELDDrnmEVQRLEALLKAMKSECQGQMERQMAAIQgKNESLEKVSSL-TAQLES- 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 782 NSENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKEN-----RSQI-----EMEHkLKNAESDLQEAKRRAE 851
Cdd:pfam15921 473 TKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAeitklRSRVdlklqELQH-LKNEGDHLRNVQTECE 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 852 EIG---AEKKELSDRLNEMLKNLNQSMQKSAENDKML----TQLREEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKRVK 924
Cdd:pfam15921 552 ALKlqmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMqvekAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLE 631
|
410 420
....*....|....*....|....*...
gi 32565309 925 MEYVKLETKSFHDVRKLNmDVEELKTQL 952
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVK-DIKQERDQL 658
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
567-924 |
5.20e-13 |
|
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: 73.94 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 567 IQNLQANGAAAQRpeqpnyepeLLALRQQLAHLQSELQTAHAQrqEFEIHYHQIRELAEQKDHQIAQLTEQANDYQERLE 646
Cdd:TIGR02168 202 LKSLERQAEKAER---------YKELKAELRELELALLVLRLE--ELREELEELQEELKEAEEELEELTAELQELEEKLE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 647 KSQSELQELARHVDSARAELmdsqtsdYGRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELR 726
Cdd:TIGR02168 271 ELRLEVSELEEEIEELQKEL-------YALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 727 NKNLELQEQVKQLKEELEKEKsvagsgnsggwsdiddnevvEAVQPIETTPISSEnsENLKKFEAEIAELKASLEKTEKE 806
Cdd:TIGR02168 344 EKLEELKEELESLEAELEELE--------------------AELEELESRLEELE--EQLETLRSKVAQLELQIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 807 LTKYRnlynEKLTAISD-KENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLnqsmqksAENDKML 885
Cdd:TIGR02168 402 IERLE----ARLERLEDrRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL-------EELREEL 470
|
330 340 350
....*....|....*....|....*....|....*....
gi 32565309 886 TQLREEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKRVK 924
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
543-860 |
7.42e-13 |
|
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: 73.17 E-value: 7.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 543 RQAHFDLMNKHKQLQLQLNAKITEIQNLQANGAAAQRpEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRE 622
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEA-EVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEA 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 623 LAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLTAENR 702
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 703 DLTDKIAQLQvsdsleleeleELRNKNLELQEQVKQLKEELEKEKSVAGsgnsggwSDIDDNEvveavqpiettpissen 782
Cdd:TIGR02168 863 ELEELIEELE-----------SELEALLNERASLEEALALLRSELEELS-------EELRELE----------------- 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32565309 783 sENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKEL 860
Cdd:TIGR02168 908 -SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
592-955 |
7.63e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 7.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 592 LRQQLAHLqsELQTAHAQRqefeihYHQIRELAEQKDHQIAQLteQANDYQERLEKSQSELQELARHVDSARAELMDsqt 671
Cdd:COG1196 198 LERQLEPL--ERQAEKAER------YRELKEELKELEAELLLL--KLRELEAELEELEAELEELEAELEELEAELAE--- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 672 sdygRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEELEKEksvag 751
Cdd:COG1196 265 ----LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEEL----- 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 752 sgnsggwsdiddnevveavqpiettpissensenlkkfEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKEnRSQIE 831
Cdd:COG1196 336 --------------------------------------EEELEELEEELEEAEEELEEAEAELAEAEEALLEAE-AELAE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 832 MEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEAFAKEKQLLEHDSVLRKKDD 911
Cdd:COG1196 377 AEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 32565309 912 KIRELDAEFKRVKMEYVKLETKSFHDVRKLNMDVEELKTQLSMA 955
Cdd:COG1196 457 EEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
589-940 |
9.02e-13 |
|
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: 73.17 E-value: 9.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 589 LLALRQQLAHL-------QSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDS 661
Cdd:TIGR02168 672 ILERRREIEELeekieelEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 662 ARAELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLqvsdsleleeleelRNKNLELQEQVKQLKE 741
Cdd:TIGR02168 752 LSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAL--------------REALDELRAELTLLNE 817
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 742 ELEKEKSVAGSgnsggwsdiDDNEVVEAVQPIETTP-ISSENSENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTA 820
Cdd:TIGR02168 818 EAANLRERLES---------LERRIAATERRLEDLEeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 821 IsDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKSAENDKMLTqlrEEAFAKEKQLL 900
Cdd:TIGR02168 889 L-ALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL---EEAEALENKIE 964
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 32565309 901 EHDSVLRKKDDKIRE---------LDA--EFKRVKMEYVKLeTKSFHDVRK 940
Cdd:TIGR02168 965 DDEEEARRRLKRLENkikelgpvnLAAieEYEELKERYDFL-TAQKEDLTE 1014
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
588-880 |
6.89e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 6.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 588 ELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELM 667
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 668 DSQTSDYGRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEELEKEK 747
Cdd:COG1196 313 ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 748 svagsgnsggwsdiddNEVVEAVQPIETTpisSENSENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKENR 827
Cdd:COG1196 393 ----------------RAAAELAAQLEEL---EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 32565309 828 SQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNemLKNLNQSMQKSAE 880
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAA--RLLLLLEAEADYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
543-750 |
1.51e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 65.73 E-value: 1.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 543 RQAHFDLMNKHKQLQLQLNAKITEIQNLQANGAAAQRpEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIhyhQIRE 622
Cdd:COG1196 273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEE-RRRELEERLEELEEELAELEEELEELEEELEELEE---ELEE 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 623 LAEQKDHQIAQLTEQAndyqERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLTAENR 702
Cdd:COG1196 349 AEEELEEAEAELAEAE----EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 32565309 703 DLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEELEKEKSVA 750
Cdd:COG1196 425 ELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
586-953 |
1.70e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 586 EPELLALRQQLAHLQSELQTAHAQRQEFEihyhQIRELAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVdsARAE 665
Cdd:PRK03918 213 SSELPELREELEKLEKEVKELEELKEEIE----ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV--KELK 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 666 LMDSQTSDYGRQQELMEK-QAELEQIYVKIDNLTAENRDLTDKIAQLQvsdsleleeleelrNKNLELQEqVKQLKEELE 744
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEyLDELREIEKRLSRLEEEINGIEERIKELE--------------EKEERLEE-LKKKLKELE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 745 KEKsvagsgnsggwsdiddNEVVEAVQPIETTPISSENSENLKKFEA--EIAELKASLEKTEKELTKYRNLYNEKLTAIS 822
Cdd:PRK03918 352 KRL----------------EELEERHELYEEAKAKKEELERLKKRLTglTPEKLEKELEELEKAKEEIEEEISKITARIG 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 823 DKENRSQiemehKLKNAESDLQEAKRRAEEIGAE-----KKELsdrLNEMLKNLNQSMQKSAENDKMLTQLREEAFAKEK 897
Cdd:PRK03918 416 ELKKEIK-----ELKKAIEELKKAKGKCPVCGRElteehRKEL---LEEYTAELKRIEKELKEIEEKERKLRKELRELEK 487
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 32565309 898 QLLEHDSVLRKKD--DKIRELDAEFKRVKMEYVKLETKSFhdvRKLNMDVEELKTQLS 953
Cdd:PRK03918 488 VLKKESELIKLKElaEQLKELEEKLKKYNLEELEKKAEEY---EKLKEKLIKLKGEIK 542
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
543-920 |
5.18e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 63.91 E-value: 5.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 543 RQAHFDLMNKHKQLQLQLNAKITEIQNLQANGAAAQRpEQPNYEPELLALRQQLAHLQSEL--------------QTAHA 608
Cdd:PRK02224 236 RDEADEVLEEHEERREELETLEAEIEDLRETIAETER-EREELAEEVRDLRERLEELEEERddllaeaglddadaEAVEA 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 609 QRQEFEIHYHQIREL-------AEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDsqtsdygRQQELM 681
Cdd:PRK02224 315 RREELEDRDEELRDRleecrvaAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVED-------RREEIE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 682 EKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEELEKEK------SVAGSGNS 755
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqPVEGSPHV 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 756 GGWSDIDDN--EVVEAVQPIETTPISSEN----SENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKENRSQ 829
Cdd:PRK02224 468 ETIEEDRERveELEAELEDLEEEVEEVEErlerAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAA 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 830 iEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEM------LKNLNQSMQKSAENDKMLTQLRE--EAFA-KEKQLL 900
Cdd:PRK02224 548 -ELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELkeriesLERIRTLLAAIADAEDEIERLREkrEALAeLNDERR 626
|
410 420
....*....|....*....|
gi 32565309 901 EHdsvLRKKDDKIRELDAEF 920
Cdd:PRK02224 627 ER---LAEKRERKRELEAEF 643
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
591-872 |
1.33e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.63 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 591 ALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAE----------------QKDHQIAQLTEQandyQERLEKSQSELQE 654
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREalqrlaeyswdeidvaSAEREIAELEAE----LERLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 655 LARHVDSARAELMDSQtsdyGRQQELMEKQAELEQiyvKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQE 734
Cdd:COG4913 690 LEEQLEELEAELEELE----EELDELKGEIGRLEK---ELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDA 762
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 735 QVKQLKEELEKEKSVAGSGNSGGWsdiddNEVVEAVqpiettpissenSENLKKFEAEIAELKASLEKTEKELTKYRNLY 814
Cdd:COG4913 763 VERELRENLEERIDALRARLNRAE-----EELERAM------------RAFNREWPAETADLDADLESLPEYLALLDRLE 825
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 815 NEKLTAISDKENRSQIE-MEHKLKNAESDLQEAKRRAEE-IgaekkelsDRLNEMLKNLN 872
Cdd:COG4913 826 EDGLPEYEERFKELLNEnSIEFVADLLSKLRRAIREIKErI--------DPLNDSLKRIP 877
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
586-873 |
1.37e-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: 62.78 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 586 EPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTE-QANDYQERLEKSQSELQELARHVDSARA 664
Cdd:TIGR02169 236 ERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeEQLRVKEKIGELEAEIASLERSIAEKER 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 665 ELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEELE 744
Cdd:TIGR02169 316 ELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 745 KEKsvagsgnsggwsdiddnevvEAVQPIETTpiSSENSENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAISdk 824
Cdd:TIGR02169 396 KLK--------------------REINELKRE--LDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIK-- 451
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 32565309 825 enrsqiEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLNQ 873
Cdd:TIGR02169 452 ------KQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE 494
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
552-932 |
1.93e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 61.71 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 552 KHKQLQLQLNAKITEIQNLQANGAAAQR---------PEQPNYEpELLALRQQLAHLQSELQTAHAQRQEFEihyHQIRE 622
Cdd:COG4717 89 EYAELQEELEELEEELEELEAELEELREeleklekllQLLPLYQ-ELEALEAELAELPERLEELEERLEELR---ELEEE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 623 LAEQKDhQIAQLTEQANDYQERL-EKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLTAEN 701
Cdd:COG4717 165 LEELEA-ELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 702 R-------------------------DLTDKIAQ-LQVSDSLELEELEELRNKNLELQEQVKQL-----KEELEKEKSVA 750
Cdd:COG4717 244 RlkearlllliaaallallglggsllSLILTIAGvLFLVLGLLALLFLLLAREKASLGKEAEELqalpaLEELEEEELEE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 751 GSGNSGGWSDIDDNEVVEAVQPIETtpissensenLKKFEAEIAELKASLEKTEKELTKYRNLynEKLTAISDKENRSQI 830
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEE----------LQELLREAEELEEELQLEELEQEIAALL--AEAGVEDEEELRAAL 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 831 EMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLN--EMLKNLNQSMQKSAENDKMLTQLREE--AFAKEKQLLEHDSVL 906
Cdd:COG4717 392 EQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEELEEELEELEEELEELREElaELEAELEQLEEDGEL 471
|
410 420
....*....|....*....|....*.
gi 32565309 907 RKKDDKIRELDAEFKRVKMEYVKLET 932
Cdd:COG4717 472 AELLQELEELKAELRELAEEWAALKL 497
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
589-953 |
2.02e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 589 LLALRQQLAHLQSELQ-------TAHAQRQEFEihyhQIRELAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDS 661
Cdd:PRK02224 208 LNGLESELAELDEEIEryeeqreQARETRDEAD----EVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRD 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 662 ARAELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKE 741
Cdd:PRK02224 284 LRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 742 ---ELEKEKSVAGSGNSGGWSDID--DNEVVEAVQPIETTPISSENS--------ENLKKFEAEIAELKASLEKTEKELT 808
Cdd:PRK02224 364 eaaELESELEEAREAVEDRREEIEelEEEIEELRERFGDAPVDLGNAedfleelrEERDELREREAELEATLRTARERVE 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 809 KYRNLYNE--------------KLTAISDKENR--------SQIEMEH-----KLKNAEsDLQEAKRRAEEIGAEKKELS 861
Cdd:PRK02224 444 EAEALLEAgkcpecgqpvegspHVETIEEDRERveeleaelEDLEEEVeeveeRLERAE-DLVEAEDRIERLEERREDLE 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 862 DRLNEMLKNLNQSMQKSAENDKMLTQLREEAFAKEKQLLEhdsvLRKKDDKIRELDAEFKRvKMEYVKLETKSFHDVRKL 941
Cdd:PRK02224 523 ELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAE----AEEEAEEAREEVAELNS-KLAELKERIESLERIRTL 597
|
410
....*....|..
gi 32565309 942 NMDVEELKTQLS 953
Cdd:PRK02224 598 LAAIADAEDEIE 609
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
643-953 |
2.88e-09 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 59.54 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 643 ERLEKSQSELQELARHVDSARAELMDSQtsdygrqQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEEL 722
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELK-------EKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 723 EELRNKNLELQEQVKQLKEELEKEKSVAGSGNSGGwsdIDDNEVVEAVQPIE----TTPISSENSenlKKFEAEIAELKA 798
Cdd:COG1340 74 KELKEERDELNEKLNELREELDELRKELAELNKAG---GSIDKLRKEIERLEwrqqTEVLSPEEE---KELVEKIKELEK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 799 SLEKTEKeltkyrnlynekltaisdkenrsQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDR----LNEMLKNLNQS 874
Cdd:COG1340 148 ELEKAKK-----------------------ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEaqelHEEMIELYKEA 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32565309 875 MQKSAENDKMLTQLREeafaKEKQLLEHDSVLRKKDDKIRELDAEFKRVKMEYVKLETKSfhDVRKLNMDVEELKTQLS 953
Cdd:COG1340 205 DELRKEADELHKEIVE----AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREK--EKEELEEKAEEIFEKLK 277
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
619-933 |
4.52e-09 |
|
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: 60.84 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 619 QIRELAEQKDHQIAQLTEQA---NDYQERLEKSQSELQE----LARhVDSARAELmdsqtsdyGRQQELMEKQAELEQIY 691
Cdd:TIGR02168 145 KISEIIEAKPEERRAIFEEAagiSKYKERRKETERKLERtrenLDR-LEDILNEL--------ERQLKSLERQAEKAERY 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 692 ---------VKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLK---EELEKEKSVAGSGNSGGWS 759
Cdd:TIGR02168 216 kelkaelreLELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRlevSELEEEIEELQKELYALAN 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 760 DIDDNEVVEAVQpiettpissenSENLKKFEAEIAELKASLEKTEKEltkyRNLYNEKLTAISDKENRSQIEME---HKL 836
Cdd:TIGR02168 296 EISRLEQQKQIL-----------RERLANLERQLEELEAQLEELESK----LDELAEELAELEEKLEELKEELEsleAEL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 837 KNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEafaKEKQLLEHDSVLRKKDD-KIRE 915
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDR---RERLQQEIEELLKKLEEaELKE 437
|
330
....*....|....*...
gi 32565309 916 LDAEFKRVKMEYVKLETK 933
Cdd:TIGR02168 438 LQAELEELEEELEELQEE 455
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
555-952 |
6.06e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 60.34 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 555 QLQLQLNAKITEIQNLQANGAAAQRpEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQL 634
Cdd:COG1196 320 ELEEELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 635 TEQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVS 714
Cdd:COG1196 399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 715 DSLELEELEELRNKNLELQEQVKQLKEELEKEKSVAGSGNSGGWSD-----IDDNEVVEAVQPIETTPISSE-NSENLKK 788
Cdd:COG1196 479 LAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGavavlIGVEAAYEAALEAALAAALQNiVVEDDEV 558
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 789 FEAEIAELK-------------------------------------ASLEKTEKELTKYRNLYNEKLTAISDKENRSQIE 831
Cdd:COG1196 559 AAAAIEYLKaakagratflpldkiraraalaaalargaigaavdlvASDLREADARYYVLGDTLLGRTLVAARLEAALRR 638
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 832 M---EHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEAFAKEKQLLEHDSVLR- 907
Cdd:COG1196 639 AvtlAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLe 718
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 32565309 908 ------KKDDKIRELDAEFKRVKMEYVKLETKSFHDVRKLNMDVEELKTQL 952
Cdd:COG1196 719 eeleeeALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELEREL 769
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
643-949 |
9.50e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 643 ERLEKSQSELQELARHVDSARAELMD--SQTSDYGRQqeLMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQvsdslele 720
Cdd:PRK03918 158 DDYENAYKNLGEVIKEIKRRIERLEKfiKRTENIEEL--IKEKEKELEEVLREINEISSELPELREELEKLE-------- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 721 eleeLRNKNLE-LQEQVKQLKEELEK-EKSVAGSgnsggwsdidDNEVVEAVQPIEttpissENSENLKKFEAEIAELKa 798
Cdd:PRK03918 228 ----KEVKELEeLKEEIEELEKELESlEGSKRKL----------EEKIRELEERIE------ELKKEIEELEEKVKELK- 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 799 SLEKTEKELTKYRNLYNEKLTAISDKENRSQIeMEHKLKNAE---SDLQEAKRRAEEIGAEKKELSDRLNEM---LKNLN 872
Cdd:PRK03918 287 ELKEKAEEYIKLSEFYEEYLDELREIEKRLSR-LEEEINGIEeriKELEEKEERLEELKKKLKELEKRLEELeerHELYE 365
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32565309 873 QSMQKSAENDKMLTQLREEAFAKEKQLLEHdsvLRKKDDKIREldaEFKRVKMEYVKLETKsfhdVRKLNMDVEELK 949
Cdd:PRK03918 366 EAKAKKEELERLKKRLTGLTPEKLEKELEE---LEKAKEEIEE---EISKITARIGELKKE----IKELKKAIEELK 432
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
731-953 |
2.55e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.15 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 731 ELQEQVKQLKEELEKEKSVAGSGNSggwSDIDDNEVVEAVqpiettpisSENSENLKKFEAEIAELKASLEKTEKELTKY 810
Cdd:PRK03918 190 NIEELIKEKEKELEEVLREINEISS---ELPELREELEKL---------EKEVKELEELKEEIEELEKELESLEGSKRKL 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 811 RnlynEKLtaisdKENRSQIEmehKLKNAESDLQEAKRRAEEIgAEKKELSDRLNEMLKNLNqsmQKSAENDKMLTQLRE 890
Cdd:PRK03918 258 E----EKI-----RELEERIE---ELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYEEYL---DELREIEKRLSRLEE 321
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32565309 891 EAFAKEKQLLEhdsvLRKKDDKIRELDAEFKRVKMEYVKLET--KSFHDVRKLNMDVEELKTQLS 953
Cdd:PRK03918 322 EINGIEERIKE----LEEKEERLEELKKKLKELEKRLEELEErhELYEEAKAKKEELERLKKRLT 382
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
619-922 |
3.88e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.83 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 619 QIRELAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLT 698
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 699 AENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEELEK-EKSVAGSGNSGGWSDIDdnEVVEAVQPIETTP 777
Cdd:COG4372 122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAlEQELQALSEAEAEQALD--ELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 778 ISSENSENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEK 857
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32565309 858 KELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKR 922
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
556-863 |
1.10e-07 |
|
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: 56.23 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 556 LQLQLNAKITEIQNLQANGAAAQRpEQPNYEPELLALRQQLAHLQSELQTAHAQ-RQEFEIHYHQIRELAEQKDHQIAQL 634
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEE-ELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 635 TEQANDYQERLEKSQSELQELARHVDSARAELMDSQTsdygrqqELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVs 714
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELER-------EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDK- 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 715 dsleleeleelrnKNLELQEQVKQLKEELEKEKSVAGSGNSGGWSDIDDNEVVEAVQpiettpisSENSENLKKFEAEIA 794
Cdd:TIGR02169 379 -------------EFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEEL--------ADLNAAIAGIEAKIN 437
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 795 ELKASLEKTEKEL-TKYRNLynEKLTAISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDR 863
Cdd:TIGR02169 438 ELEEEKEDKALEIkKQEWKL--EQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER 505
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
632-953 |
1.31e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 632 AQLTEQANDYQER---LEKSQSELQELARHVDSARAELMDSQTsDYGRQQELMEKQAELEQIYVKIDNLTAEnrDLTDKI 708
Cdd:PRK03918 317 SRLEEEINGIEERikeLEEKEERLEELKKKLKELEKRLEELEE-RHELYEEAKAKKEELERLKKRLTGLTPE--KLEKEL 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 709 AQLQVSDSLELEELEELRNKNLELQEQVKQLKEELEKEKSVAGSGNSGGwSDIDDNEVVEAVQpiETTPISSENSENLKK 788
Cdd:PRK03918 394 EELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCG-RELTEEHRKELLE--EYTAELKRIEKELKE 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 789 FEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKENRSQ-----------------------IEMEHKLKNAESDL-- 843
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKlkkynleelekkaeeyeklkeklIKLKGEIKSLKKELek 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 844 -QEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEAfakekqlleHDSVLRKKDDKiRELDAEFKR 922
Cdd:PRK03918 551 lEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPF---------YNEYLELKDAE-KELEREEKE 620
|
330 340 350
....*....|....*....|....*....|.
gi 32565309 923 VKMEYVKLEtKSFHDVRKLNMDVEELKTQLS 953
Cdd:PRK03918 621 LKKLEEELD-KAFEELAETEKRLEELRKELE 650
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
593-877 |
1.82e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 593 RQQLAHLQSELQTAHAQRQEFEIhyhQIRELAEQKDhqiaQLTEQANDYQERLEKSQSEL--QELARHVDSARAELMDSQ 670
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEE---RLEALEAELD----ALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 671 TSDygrqQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQvsdsleleeleelrNKNLELQEQVKQLKEELEkekSVA 750
Cdd:COG4913 682 ASS----DDLAALEEQLEELEAELEELEEELDELKGEIGRLE--------------KELEQAEEELDELQDRLE---AAE 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 751 GSGNSGGWSDIDdnEVVEAVQPIETTpissenSENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTA------ISDK 824
Cdd:COG4913 741 DLARLELRALLE--ERFAAALGDAVE------RELRENLEERIDALRARLNRAEEELERAMRAFNREWPAetadldADLE 812
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32565309 825 ENRSQIEMEHKLKN-----AESDLQEAKRRAE---------EIGAEKKELSDRLNEmlknLNQSMQK 877
Cdd:COG4913 813 SLPEYLALLDRLEEdglpeYEERFKELLNENSiefvadllsKLRRAIREIKERIDP----LNDSLKR 875
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
585-901 |
2.15e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 585 YEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKD--HQIAQLTEQANDYQ-ERLEKSQSELQELARHVDS 661
Cdd:PRK03918 457 YTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKElaEQLKELEEKLKKYNlEELEKKAEEYEKLKEKLIK 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 662 ARAELMdSQTSDYGRQQELMEKQAELEQiyvKIDNLTAENRDLTDKIAQLQVSDSLeleeleelrnknlELQEQVKQLKE 741
Cdd:PRK03918 537 LKGEIK-SLKKELEKLEELKKKLAELEK---KLDELEEELAELLKELEELGFESVE-------------ELEERLKELEP 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 742 ELEKEksvagsgnsggwsdiddNEVVEAVQPIEttpissENSENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAI 821
Cdd:PRK03918 600 FYNEY-----------------LELKDAEKELE------REEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKY 656
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 822 SDKENRSQ----IEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEM------LKNLNQSMQKsaendkmLTQLREE 891
Cdd:PRK03918 657 SEEEYEELreeyLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERekakkeLEKLEKALER-------VEELREK 729
|
330
....*....|
gi 32565309 892 aFAKEKQLLE 901
Cdd:PRK03918 730 -VKKYKALLK 738
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
570-812 |
4.31e-07 |
|
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: 53.61 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 570 LQANGAAAQRPEQPNYEPELLALRQQLAHLQSELQTAHAQRQEfeihyhQIRELAEQkDHQIAQLTEQANDYQERLEKSQ 649
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKA------LLKQLAAL-ERRIAALARRIRALEQELAALE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 650 SELQELARHVDSARAELmDSQTSDY----------GRQQELM-----EKQAELEQIYVKIDNLTAENRDLTDKIAQLQVS 714
Cdd:COG4942 83 AELAELEKEIAELRAEL-EAQKEELaellralyrlGRQPPLAlllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 715 DSLELEELEELRNKNLELQEQVKQLKEELEKEKsvagsgnsggwsdiddNEVVEAVQPIETTpiSSENSENLKKFEAEIA 794
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAALEALK----------------AERQKLLARLEKE--LAELAAELAELQQEAE 223
|
250
....*....|....*...
gi 32565309 795 ELKASLEKTEKELTKYRN 812
Cdd:COG4942 224 ELEALIARLEAEAAAAAE 241
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
554-940 |
5.94e-07 |
|
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: 53.90 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 554 KQLQLQLNAKITEIQ-------NLQANGAAAQRpEQPNYEPELLALRQQLAHLQSELQTAhAQRQEFEIHYHQIRELAEQ 626
Cdd:TIGR00606 573 KQLEDWLHSKSKEINqtrdrlaKLNKELASLEQ-NKNHINNELESKEEQLSSYEDKLFDV-CGSQDEESDLERLKEEIEK 650
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 627 KDHQIAQLTEQANDYQERLEKSQSELQE---LARHVDSARAELMDSQTSDYGRQQELMEKQAELEQIYVKIDnltaENRD 703
Cdd:TIGR00606 651 SSKQRAMLAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKE----KRRD 726
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 704 LTDKIAQLQVSD-SLELEELEELRNKNLELQEQVKQLKEELEKEKSVAGSGNSGGWSDIDDNEVVEAVQPIETtpissEN 782
Cdd:TIGR00606 727 EMLGLAPGRQSIiDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQM-----EL 801
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 783 SENLKKFEAEIAELKAS-LEKTEKELTKYRNLYNEKLTAISdkenrSQIEMEHKL-KNAESDLQEAKRRAEEIGAEKKEL 860
Cdd:TIGR00606 802 KDVERKIAQQAAKLQGSdLDRTVQQVNQEKQEKQHELDTVV-----SKIELNRKLiQDQQEQIQHLKSKTNELKSEKLQI 876
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 861 SDRLNEMLKNLNQSMQKSAENDKMLTQLRE--EAFAKEKQLLEHDsvLRKKDDKIRELDAEFKRVKMEY--VKLETKSFH 936
Cdd:TIGR00606 877 GTNLQRRQQFEEQLVELSTEVQSLIREIKDakEQDSPLETFLEKD--QQEKEELISSKETSNKKAQDKVndIKEKVKNIH 954
|
....
gi 32565309 937 DVRK 940
Cdd:TIGR00606 955 GYMK 958
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
548-953 |
5.95e-07 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 54.29 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 548 DLMNKHKQLQLQLN-------------AKITEIQ---NLQANGAAAQRPE-QPNYEpellalrqqlahlQSELQTAHAQR 610
Cdd:TIGR01612 759 DFKNKEKELSNKINdyakekdelnkykSKISEIKnhyNDQINIDNIKDEDaKQNYD-------------KSKEYIKTISI 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 611 QEFEIhYHQIRELAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGR-----QQELMEKQA 685
Cdd:TIGR01612 826 KEDEI-FKIINEMKFMKDDFLNKVDKFINFENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDYEKkfndsKSLINEINK 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 686 ELEQIYVKIDNLTAENrdltdkiAQLQVSDSlELEELEELRNKNLELQEQVKQLKEELEKEKSVAGSGNSGGWSDIDD-- 763
Cdd:TIGR01612 905 SIEEEYQNINTLKKVD-------EYIKICEN-TKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKFDNTLIDki 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 764 NEVVEAVQPIETTPISSENSENLKKFEaeiaELKASLeKTEKELTKYRNlYNEKLTAISDKENRSqIEMEHKLKNAESDL 843
Cdd:TIGR01612 977 NELDKAFKDASLNDYEAKNNELIKYFN----DLKANL-GKNKENMLYHQ-FDEKEKATNDIEQKI-EDANKNIPNIEIAI 1049
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 844 QEAKRR-AEEIGAEKKELSDRLN-EMLKNLNQSMQKSAENDKMLTQLREEAFAKEKQLLEHDSVLRKKDDkIRELDAEFK 921
Cdd:TIGR01612 1050 HTSIYNiIDEIEKEIGKNIELLNkEILEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYADEINKIKDD-IKNLDQKID 1128
|
410 420 430
....*....|....*....|....*....|..
gi 32565309 922 RVKMEYVKLETKSfhdvrklNMDVEELKTQLS 953
Cdd:TIGR01612 1129 HHIKALEEIKKKS-------ENYIDEIKAQIN 1153
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
588-922 |
1.07e-06 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 53.05 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 588 ELLALRQQLAHLQSELQTAHAQR-----QEFEIHYHQIRELAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSA 662
Cdd:pfam02463 177 KLIEETENLAELIIDLEELKLQElklkeQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 663 RAELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKE- 741
Cdd:pfam02463 257 KQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEe 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 742 --ELEKEKSVAGSgnsggwSDIDDNEVVEAVQPIETTPISSENsENLKKFEAEIAELKASLEKTEKELTKyrnLYNEKLT 819
Cdd:pfam02463 337 ieELEKELKELEI------KREAEEEEEEELEKLQEKLEQLEE-ELLAKKKLESERLSSAAKLKEEELEL---KSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 820 AISDKENRSQIEMEHKLKNAESDlqeakrrAEEIGAEKKELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEAFAKEKQL 899
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEEL-------EILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
330 340
....*....|....*....|...
gi 32565309 900 LEHDSVLRKKDDKIRELDAEFKR 922
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKE 502
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
594-747 |
1.12e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 594 QQLAHLQSELQTAHAQRQEfeihYHQIRELAEQKDHQIAQLTEQANDYQERLEK--SQSELQELARHVDSARAELMDSQT 671
Cdd:COG4717 71 KELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKleKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32565309 672 sdygRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLE-LQEQVKQLKEELEKEK 747
Cdd:COG4717 147 ----RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEeLQQRLAELEEELEEAQ 219
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
559-902 |
1.19e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.21 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 559 QLNAKITEIQNLQANGAAAQRpEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTEQA 638
Cdd:COG4372 32 QLRKALFELDKLQEELEQLRE-ELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 639 NDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLE 718
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 719 LEELEELRNKNLELQEQVKQLKEELEKEKSVAGSGNSGgwsdIDDNEVVEAVQPIETTPISSENSENLKKFEAEIAELKA 798
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLE----AKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 799 SLEKTEKELTKYRNLYNEKLTAISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKS 878
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLL 346
|
330 340
....*....|....*....|....
gi 32565309 879 AENDKMLTQLREEAFAKEKQLLEH 902
Cdd:COG4372 347 LVGLLDNDVLELLSKGAEAGVADG 370
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
539-746 |
1.20e-06 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 52.38 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 539 DILDRQA-HFDLMNKHKQLQLQLNAKITEIQNLQANGAAAQRPE---------------QPNYEPELLALRQQLAH---L 599
Cdd:COG0497 145 ELLDAFAgLEELLEEYREAYRAWRALKKELEELRADEAERARELdllrfqleeleaaalQPGEEEELEEERRRLSNaekL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 600 QSELQTAHAQRQEFEIH-YHQIRElAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSaraeLMDSQTSDYGRQQ 678
Cdd:COG0497 225 REALQEALEALSGGEGGaLDLLGQ-ALRALERLAEYDPSLAELAERLESALIELEEAASELRR----YLDSLEFDPERLE 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32565309 679 ELMEKQAELEQI---Y-VKIDNLTAENRDLTDKIAQLQVSDSLELeeleelrnknlELQEQVKQLKEELEKE 746
Cdd:COG0497 300 EVEERLALLRRLarkYgVTVEELLAYAEELRAELAELENSDERLE-----------ELEAELAEAEAELLEA 360
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
586-745 |
1.60e-06 |
|
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: 50.69 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 586 EPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTEQANDYQERLE--KSQSELQELARHVDSAR 663
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGnvRNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 664 AELMDSQTsdygRQQELMEKQAELEQiyvKIDNLTAENRDLTDKIAQLQVsdsleleeleelrnknlELQEQVKQLKEEL 743
Cdd:COG1579 103 RRISDLED----EILELMERIEELEE---ELAELEAELAELEAELEEKKA-----------------ELDEELAELEAEL 158
|
..
gi 32565309 744 EK 745
Cdd:COG1579 159 EE 160
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
551-754 |
1.63e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 51.69 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 551 NKHKQLQLQLNAKITEIQNLQANGAAAQRpEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEihyHQIRELAEQKDHQ 630
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKK-EEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 631 IAQLTEQANDYQERLEK--------------SQSELQELAR------HVDSARAELMDSQTSDygrQQELMEKQAELEQI 690
Cdd:COG4942 96 RAELEAQKEELAELLRAlyrlgrqpplalllSPEDFLDAVRrlqylkYLAPARREQAEELRAD---LAELAALRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32565309 691 YVKIDNLTAENRDLTDKIAQLQ------VSDSLELEELEELRNKNL-----ELQEQVKQLKEELEKEKSVAGSGN 754
Cdd:COG4942 173 RAELEALLAELEEERAALEALKaerqklLARLEKELAELAAELAELqqeaeELEALIARLEAEAAAAAERTPAAG 247
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
651-933 |
1.99e-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: 52.38 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 651 ELQELARHVDSARAELMDSQtsdygrqQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEelrnknl 730
Cdd:TIGR02169 675 ELQRLRERLEGLKRELSSLQ-------SELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLE------- 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 731 ELQEQVKQLKEELEKEKsvagsgnsggwSDIDDNEVVEAvqpiettpissENSENLKKFEAEIAELKASL--------EK 802
Cdd:TIGR02169 741 ELEEDLSSLEQEIENVK-----------SELKELEARIE-----------ELEEDLHKLEEALNDLEARLshsripeiQA 798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 803 TEKELTKYRNLYNEKLTAISDKENRSQIEMEHklknAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKSAEND 882
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEY----LEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 32565309 883 KMLTQLREEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKRVKMEYVKLETK 933
Cdd:TIGR02169 875 AALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAK 925
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
584-949 |
4.19e-06 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 50.99 E-value: 4.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 584 NYEPELLALRQQLAHLQSELQtahaqrqEFEihyhqirELAEQKDHqiaqltEQANDYQERLEKSQSELQELARHVDSAR 663
Cdd:PRK04778 162 SFGPALDELEKQLENLEEEFS-------QFV-------ELTESGDY------VEAREILDQLEEELAALEQIMEEIPELL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 664 AELmdsQTSDYGRQQELMEKQAELE---------QIYVKIDNLTAENRDLTDKIAQLQVSDsleleeleeLRNKNLELQE 734
Cdd:PRK04778 222 KEL---QTELPDQLQELKAGYRELVeegyhldhlDIEKEIQDLKEQIDENLALLEELDLDE---------AEEKNEEIQE 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 735 QVKQLKEELEKEksvagsgnsggwsdIDDNEVVEAVQPIETTPIsSENSENLKKFEAEIAELKASLEKTEKELTKYRNLY 814
Cdd:PRK04778 290 RIDQLYDILERE--------------VKARKYVEKNSDTLPDFL-EHAKEQNKELKEEIDRVKQSYTLNESELESVRQLE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 815 NEkltaisdkenrsqiemehkLKNAESDLQEAkrrAEEIGAEKK---ELSDRLNEMLKNLNQSMQKSAENDKMLTQLR-E 890
Cdd:PRK04778 355 KQ-------------------LESLEKQYDEI---TERIAEQEIaysELQEELEEILKQLEEIEKEQEKLSEMLQGLRkD 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 891 EAFAKEK------QLLEHD----------------SVLRKKDDKIRELDAEF--KRVKMEYVKletksfHDVRKLNMDVE 946
Cdd:PRK04778 413 ELEAREKleryrnKLHEIKryleksnlpglpedylEMFFEVSDEIEALAEELeeKPINMEAVN------RLLEEATEDVE 486
|
...
gi 32565309 947 ELK 949
Cdd:PRK04778 487 TLE 489
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
582-852 |
4.36e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 582 QPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQ--------LTEQANDYQERLEKSQSELQ 653
Cdd:COG3096 831 APDPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQanlladetLADRLEELREELDAAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 654 ELARHVDSAR--AELMDSQTSD----YGRQQELMEKQAELEQIYVKIDNLTaenrDLTDKIAQLQVSDSLELEeleelrN 727
Cdd:COG3096 911 FIQQHGKALAqlEPLVAVLQSDpeqfEQLQADYLQAKEQQRRLKQQIFALS----EVVQRRPHFSYEDAVGLL------G 980
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 728 KNLELQEQVKQLKEELEKEKSVAGSGNSGGwsdidDNEVVEAVQPIETTPISSEN-SENLKKFEAEIAEL---------- 796
Cdd:COG3096 981 ENSDLNEKLRARLEQAEEARREAREQLRQA-----QAQYSQYNQVLASLKSSRDAkQQTLQELEQELEELgvqadaeaee 1055
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32565309 797 KASLEKTE--KELTKYRNLYNEKLTAISdkenRSQIEMEH---KLKNAESDLQEAKRRAEE 852
Cdd:COG3096 1056 RARIRRDElhEELSQNRSRRSQLEKQLT----RCEAEMDSlqkRLRKAERDYKQEREQVVQ 1112
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
676-885 |
4.80e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.80 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 676 RQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLqvsdsleleeleelRNKNLELQEQVKQLKEELEKEKsvagsgns 755
Cdd:pfam05667 333 REEELEELQEQLEDLESSIQELEKEIKKLESSIKQV--------------EEELEELKEQNEELEKQYKVKK-------- 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 756 ggwsdiddnevveavQPIETTPissENSENLKKFEAEIAELKASLEKTEKELTKYR----NLYNEKLTAISDKENRSQIE 831
Cdd:pfam05667 391 ---------------KTLDLLP---DAEENIAKLQALVDASAQRLVELAGQWEKHRvpliEEYRALKEAKSNKEDESQRK 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 32565309 832 MEhklknaesDLQEAKRRAEEIGAE---KKELSDRLNEMLKNLNQSMQKSAENDKML 885
Cdd:pfam05667 453 LE--------EIKELREKIKEVAEEakqKEELYKQLVAEYERLPKDVSRSAYTRRIL 501
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
578-921 |
5.14e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 50.99 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 578 QRPEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIR---ELAEQKDHQIAQLTEQANDYQERLEKSQSELQ- 653
Cdd:pfam12128 588 KRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANgelEKASREETFARTALKNARLDLRRLFDEKQSEKd 667
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 654 ----ELARHVDSARAELmdsQTSDYGRQQELMEKQAELEQIyvkiDNLTAENRdlTDKIAQLQVSDSleleeleelrnkn 729
Cdd:pfam12128 668 kknkALAERKDSANERL---NSLEAQLKQLDKKHQAWLEEQ----KEQKREAR--TEKQAYWQVVEG------------- 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 730 lELQEQVKQLKEELEKEKSVAGSGNSGGWSDIDDNEVVEAVQPiettpissensENLKKFEAEIAELKASLEKTEK---E 806
Cdd:pfam12128 726 -ALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDP-----------DVIAKLKREIRTLERKIERIAVrrqE 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 807 LTKYRNLYNEklTAISDKENRsqiemehklknaesdlqeaKRRAEEIGAEKKELSDRLNemlknlnqsmQKSAENDKMLT 886
Cdd:pfam12128 794 VLRYFDWYQE--TWLQRRPRL-------------------ATQLSNIERAISELQQQLA----------RLIADTKLRRA 842
|
330 340 350
....*....|....*....|....*....|....*
gi 32565309 887 QLREEAFAKEKQLLEHDSVLRKKDDKIRELdAEFK 921
Cdd:pfam12128 843 KLEMERKASEKQQVRLSENLRGLRCEMSKL-ATLK 876
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
640-952 |
5.96e-06 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 50.56 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 640 DYQERL---EKSQSELQELARHVDSARAELMDsQTSDYGRQ-----QELMEKQAELEQIYVKIDNLTAENRDLTDKIAQL 711
Cdd:pfam01576 191 DLEERLkkeEKGRQELEKAKRKLEGESTDLQE-QIAELQAQiaelrAQLAKKEEELQAALARLEEETAQKNNALKKIREL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 712 QVSDSLELEELEELRNKNLELQEQVKQLKEELEKEKsvagsgnsggwSDIDDNEVVEAVQ-------PIETTPISSENSE 784
Cdd:pfam01576 270 EAQISELQEDLESERAARNKAEKQRRDLGEELEALK-----------TELEDTLDTTAAQqelrskrEQEVTELKKALEE 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 785 NLKKFEAEIAEL---------------------KASLEKTEKELTKYRNLYNEKLTAISdkenRSQIEMEHKLKNAESDL 843
Cdd:pfam01576 339 ETRSHEAQLQEMrqkhtqaleelteqleqakrnKANLEKAKQALESENAELQAELRTLQ----QAKQDSEHKRKKLEGQL 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 844 QEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEAFAKEKQLLEHDSVL----RKK---DDKIREL 916
Cdd:pfam01576 415 QELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLqeetRQKlnlSTRLRQL 494
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 32565309 917 DAEfKRVKMEYVKLETKSFHDVRK----LNMDVEELKTQL 952
Cdd:pfam01576 495 EDE-RNSLQEQLEEEEEAKRNVERqlstLQAQLSDMKKKL 533
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
565-974 |
6.48e-06 |
|
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: 50.50 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 565 TEIQNLQANGAAAQRPEQPNYEPELLALRQQLAHLQSElqtaHAQRQeFEIHYHQIRELA-------EQKDHQIAQLTEQ 637
Cdd:pfam15921 37 TIIENTSSTGTFTQIPIFPKYEVELDSPRKIIAYPGKE----HIERV-LEEYSHQVKDLQrrlnesnELHEKQKFYLRQS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 638 ANDYQERLEKSQSE---------------------LQELARHVDSARA----ELMDSQT----------SDYGRQQELME 682
Cdd:pfam15921 112 VIDLQTKLQEMQMErdamadirrresqsqedlrnqLQNTVHELEAAKClkedMLEDSNTqieqlrkmmlSHEGVLQEIRS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 683 -----KQAELEQIYvKIDNLTAEN------------RDLTDKIAQLQ-----VSDSLELEELEELRNKNLELQEQVKQLK 740
Cdd:pfam15921 192 ilvdfEEASGKKIY-EHDSMSTMHfrslgsaiskilRELDTEISYLKgrifpVEDQLEALKSESQNKIELLLQQHQDRIE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 741 EEL-EKEKSVAGSGNSGGWSDIDDNEVVEAVQPIETTPiSSENSENLKkfeaEIAELKASLEKTEKELTKYRNLYNEKLT 819
Cdd:pfam15921 271 QLIsEHEVEITGLTEKASSARSQANSIQSQLEIIQEQA-RNQNSMYMR----QLSDLESTVSQLRSELREAKRMYEDKIE 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 820 aisdkenrsqiEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLNQsmqksaeNDKMLTQLREEafakEKQL 899
Cdd:pfam15921 346 -----------ELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHK-------REKELSLEKEQ----NKRL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 900 LEHDS--------VLRKKDDK---IRELDAEFKRVK----------MEYVKLETKSFHDVRKLNMDVEELKTQLS----- 953
Cdd:pfam15921 404 WDRDTgnsitidhLRRELDDRnmeVQRLEALLKAMKsecqgqmerqMAAIQGKNESLEKVSSLTAQLESTKEMLRkvvee 483
|
490 500
....*....|....*....|....*
gi 32565309 954 -MAGGVT---SSRSIPDrLVSPLQE 974
Cdd:pfam15921 484 lTAKKMTlesSERTVSD-LTASLQE 507
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
623-901 |
6.77e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 50.21 E-value: 6.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 623 LAEqKDHQIAQLTEQ-ANDYQERLEKSQS---ELQELARHVDSARAELMDSQTSdygrQQELMEKQAELEQIYVKIDN-- 696
Cdd:pfam10174 445 LSE-KERIIERLKEQrEREDRERLEELESlkkENKDLKEKVSALQPELTEKESS----LIDLKEHASSLASSGLKKDSkl 519
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 697 --LTAENRDLTDKIAQLQVSDSLELEELEELRnKNLELQEQVKQLKEELEKEKSVAGSGNSggwsdiDDNEVVEAVQpie 774
Cdd:pfam10174 520 ksLEIAVEQKKEECSKLENQLKKAHNAEEAVR-TNPEINDRIRLLEQEVARYKEESGKAQA------EVERLLGILR--- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 775 ttpiSSENSENLKkfEAEIAELKASLEKTEKELTKyrNLYNEKLTAISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIG 854
Cdd:pfam10174 590 ----EVENEKNDK--DKKIAELESLTLRQMKEQNK--KVANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELM 661
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 32565309 855 AEKKELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEafaKEKQLLE 901
Cdd:pfam10174 662 GALEKTRQELDATKARLSSTQQSLAEKDGHLTNLRAE---RRKQLEE 705
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
621-953 |
1.02e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 49.65 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 621 RELAEQKDHQIAQ-----LTEQANDYQERLEKSQSELQELARHVDSARAelmdsqtsdygRQQELMEKQAELEQIYVKID 695
Cdd:PRK02224 186 RGSLDQLKAQIEEkeekdLHERLNGLESELAELDEEIERYEEQREQARE-----------TRDEADEVLEEHEERREELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 696 NLTAENRDLTDKIAQL---------QVSDSLELEELEELRNKNL----EL----QEQVKQLKEELEKEKSVAgsgnsggw 758
Cdd:PRK02224 255 TLEAEIEDLRETIAETerereelaeEVRDLRERLEELEEERDDLlaeaGLddadAEAVEARREELEDRDEEL-------- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 759 sdidDNEVVEAVQPIETTPISSEN-SENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKEnrSQIE-MEHKL 836
Cdd:PRK02224 327 ----RDRLEECRVAAQAHNEEAESlREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE--EEIEeLRERF 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 837 KNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKSAENDkmltQLREEAFAKE-KQLLE---HDSVLRKKDDK 912
Cdd:PRK02224 401 GDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAE----ALLEAGKCPEcGQPVEgspHVETIEEDRER 476
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 32565309 913 IRELDAEFKRVKMEYVKLETK--SFHDVRKLNMDVEELKTQLS 953
Cdd:PRK02224 477 VEELEAELEDLEEEVEEVEERleRAEDLVEAEDRIERLEERRE 519
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
592-953 |
1.08e-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: 49.63 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 592 LRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQT 671
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 672 SdYGRQQELMEKQAELEQiyvKIDNLTAENRDLTDKIAQLQVSDSleleeleelrNKNLEL---QEQVKQLKEELEKEKs 748
Cdd:TIGR04523 202 L-LSNLKKKIQKNKSLES---QISELKKQNNQLKDNIEKKQQEIN----------EKTTEIsntQTQLNQLKDEQNKIK- 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 749 vagsgnsggwsdiddNEVVEAVQPIETTPISSENSEN-LKKFEAEIAEL------------KASLEKTEKELTKYRNLYN 815
Cdd:TIGR04523 267 ---------------KQLSEKQKELEQNNKKIKELEKqLNQLKSEISDLnnqkeqdwnkelKSELKNQEKKLEEIQNQIS 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 816 EKLTAISD-KENRSQIEMEhkLKNAESDLQEAKRRAEE----IGAEKKELSDRLNEMLK------NLNQSMQKsAENDKM 884
Cdd:TIGR04523 332 QNNKIISQlNEQISQLKKE--LTNSESENSEKQRELEEkqneIEKLKKENQSYKQEIKNlesqinDLESKIQN-QEKLNQ 408
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32565309 885 LTQLREEAFAKEKQLLEHDSVLRKKDdkIRELDAEFKRVKMEYVKLETKsfhdVRKLNMDVEELKTQLS 953
Cdd:TIGR04523 409 QKDEQIKKLQQEKELLEKEIERLKET--IIKNNSEIKDLTNQDSVKELI----IKNLDNTRESLETQLK 471
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
581-744 |
1.10e-05 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 48.96 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 581 EQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTE---QANDYQERLEKSQSELQEL-- 655
Cdd:pfam00529 52 DPTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAaqaAVKAAQAQLAQAQIDLARRrv 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 656 --------ARHVDSARAELMDSQTsdygrqqELMEKQAELEQIYVKIDNLTAENRDLTDKI---AQLQVSdsleleelee 724
Cdd:pfam00529 132 lapiggisRESLVTAGALVAQAQA-------NLLATVAQLDQIYVQITQSAAENQAEVRSElsgAQLQIA---------- 194
|
170 180
....*....|....*....|
gi 32565309 725 lrnknlELQEQVKQLKEELE 744
Cdd:pfam00529 195 ------EAEAELKLAKLDLE 208
|
|
| DUF3729 |
pfam12526 |
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins ... |
253-316 |
1.61e-05 |
|
Protein of unknown function (DUF3729); This family of proteins is found in viruses. Proteins in this family are typically between 145 and 1707 amino acids in length. The family is found in association with pfam01443, pfam01661, pfam05417, pfam01660, pfam00978. There is a single completely conserved residue L that may be functionally important.
Pssm-ID: 372164 [Multi-domain] Cd Length: 115 Bit Score: 45.07 E-value: 1.61e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32565309 253 PPLVLQSLPETPEAQKLPEePLEPVTPEPIPEAPVPiaqyiqEPTTTPAPLEAPAPVENAPNLP 316
Cdd:pfam12526 47 RPPVVDTPPPVSAVWVLPP-PSEPAAPEPDLVPPVT------GPAGPPSPLAPPAPAQKPPLPP 103
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
542-713 |
2.65e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 542 DRQAHFDLMNKHKQLQLQLNAKITEIQNLQANGAAAQRPEQpnyepELLALRQQLAHLQSELQTAHaqrqefeihyhqiR 621
Cdd:PRK11281 40 DVQAQLDALNKQKLLEAEDKLVQQDLEQTLALLDKIDRQKE-----ETEQLKQQLAQAPAKLRQAQ-------------A 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 622 ELAEQKDHQIAQLTEQANDY-----QERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQIYVKIDN 696
Cdd:PRK11281 102 ELEALKDDNDEETRETLSTLslrqlESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKG 181
|
170
....*....|....*...
gi 32565309 697 LTAENRDLT-DKIAQLQV 713
Cdd:PRK11281 182 GKVGGKALRpSQRVLLQA 199
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
779-952 |
2.66e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.47 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 779 SSENSENLKKFEAEIAELKASLEKTEKELTKYRNLYNekltaISDKENRSQIEMEhKLKNAESDLQEAKRRAEEIGAEKK 858
Cdd:COG3206 170 REEARKALEFLEEQLPELRKELEEAEAALEEFRQKNG-----LVDLSEEAKLLLQ-QLSELESQLAEARAELAEAEARLA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 859 ELSDRLNEMLKNLNQSMQksaenDKMLTQLREEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKRVKMEyvkLETKSFHDV 938
Cdd:COG3206 244 ALRAQLGSGPDALPELLQ-----SPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ---LQQEAQRIL 315
|
170
....*....|....
gi 32565309 939 RKLNMDVEELKTQL 952
Cdd:COG3206 316 ASLEAELEALQARE 329
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
585-864 |
2.91e-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: 48.20 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 585 YEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRE---LAEQKDH---QIAQLTEQANDYQERLEKSQSELQELARH 658
Cdd:pfam05557 25 HKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKreaEAEEALReqaELNRLKKKYLEALNKKLNEKESQLADARE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 659 VDSA-RAELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQ-- 735
Cdd:pfam05557 105 VISClKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQSQeq 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 736 ----VKQLKEEL------EKEKSVAGSGNSGGWSDIDDNEVV-EAVQPIETtpisseNSENLKKFEAEIAELKASLEKTE 804
Cdd:pfam05557 185 dseiVKNSKSELaripelEKELERLREHNKHLNENIENKLLLkEEVEDLKR------KLEREEKYREEAATLELEKEKLE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 805 KELTKYRNLY------------------------------NEKLTAISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIG 854
Cdd:pfam05557 259 QELQSWVKLAqdtglnlrspedlsrrieqlqqreivlkeeNSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHK 338
|
330
....*....|
gi 32565309 855 AEKKELSDRL 864
Cdd:pfam05557 339 ALVRRLQRRV 348
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
542-954 |
2.99e-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: 48.18 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 542 DRQAHFDLMNKHKQLQlqlNAKITEIQNLQANGAAAQRPEQ---PNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYH 618
Cdd:pfam05483 332 EKEAQMEELNKAKAAH---SFVVTEFEATTCSLEELLRTEQqrlEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELE 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 619 QIRELAEQKDHQIAQlTEQANDYQERLEKSQSEL----QELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQIYVKI 694
Cdd:pfam05483 409 ELKKILAEDEKLLDE-KKQFEKIAEELKGKEQELifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKN 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 695 DNLTA-------ENRDLTDKIAQLqvsdsleleeleelrnkNLELQEQVKQLKEELEKEKSVAgsgnsggwsdiddnEVV 767
Cdd:pfam05483 488 IELTAhcdklllENKELTQEASDM-----------------TLELKKHQEDIINCKKQEERML--------------KQI 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 768 EAVQPIETTpISSENSENLKKFEAEIAELKASLEKTEK--ELTKYRNLYNEKLTAI-SDKENRSQIEMEHKLKNAESDLQ 844
Cdd:pfam05483 537 ENLEEKEMN-LRDELESVREEFIQKGDEVKCKLDKSEEnaRSIEYEVLKKEKQMKIlENKCNNLKKQIENKNKNIEELHQ 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 845 EAKRRAEEIGAEKKELSD---RLNEMLKNLNQSMQKSAE-NDKMLTQLREEAFAKEKQLLEHDSVLRKKDDKI---RELD 917
Cdd:pfam05483 616 ENKALKKKGSAENKQLNAyeiKVNKLELELASAKQKFEEiIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVklqKEID 695
|
410 420 430
....*....|....*....|....*....|....*..
gi 32565309 918 AEFKRVKMEYVKLETKSFHDVRKLnmdVEELKTQLSM 954
Cdd:pfam05483 696 KRCQHKIAEMVALMEKHKHQYDKI---IEERDSELGL 729
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
783-952 |
2.99e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.53 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 783 SENLKKFEAEIAELKASLEKTEKE---LTKYRNLYNEKLTAISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKE 859
Cdd:TIGR02169 183 EENIERLDLIIDEKRQQLERLRRErekAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISE 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 860 LSDRLNEMLKNLNQsmqksaENDKMLTQLREEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKRVKMEYVKLETksfhDVR 939
Cdd:TIGR02169 263 LEKRLEEIEQLLEE------LNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEA----EID 332
|
170
....*....|...
gi 32565309 940 KLNMDVEELKTQL 952
Cdd:TIGR02169 333 KLLAEIEELEREI 345
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
731-933 |
3.02e-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: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 731 ELQEQVKQLKEELEKEKSVAGSGNSggwsDID--DNEVVEAVQPIETTpissenSENLKKFEAEIAELKASLEKTEKELT 808
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLK----QLAalERRIAALARRIRAL------EQELAALEAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 809 KYRNLYNEKLTAISDKENRSQIEMehkLKNAESDLQEAKR-------------RAEEIGAEKKELSDRLNEMLKNLNQSM 875
Cdd:COG4942 101 AQKEELAELLRALYRLGRQPPLAL---LLSPEDFLDAVRRlqylkylaparreQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 32565309 876 QKSAENDKMLTQLREEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKRVKMEYVKLETK 933
Cdd:COG4942 178 ALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
620-853 |
3.35e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.93 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 620 IRELAEQK---DHQiaQLTEQANDYQERLEKSQSELQELarHVDSARAELMDSQTS----------DYGRQQELMEKQAE 686
Cdd:pfam06160 220 YREMEEEGyalEHL--NVDKEIQQLEEQLEENLALLENL--ELDEAEEALEEIEERidqlydllekEVDAKKYVEKNLPE 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 687 LEQIyvkIDNLTAENRDLTDKIAQLQvsDSLELEELEELRNKNLE-----LQEQVKQLKEELEKEKSVagsgnsggWSDI 761
Cdd:pfam06160 296 IEDY---LEHAEEQNKELKEELERVQ--QSYTLNENELERVRGLEkqleeLEKRYDEIVERLEEKEVA--------YSEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 762 DDN--EVVEAVQPIETTPISSENS------------ENLKKFEAEIAELKASLEKTE-----KELTKYRNLYNEKLTAIS 822
Cdd:pfam06160 363 QEEleEILEQLEEIEEEQEEFKESlqslrkdelearEKLDEFKLELREIKRLVEKSNlpglpESYLDYFFDVSDEIEDLA 442
|
250 260 270
....*....|....*....|....*....|....
gi 32565309 823 DKENRSQIEME---HKLKNAESDLQEAKRRAEEI 853
Cdd:pfam06160 443 DELNEVPLNMDevnRLLDEAQDDVDTLYEKTEEL 476
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
543-952 |
3.82e-05 |
|
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: 48.04 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 543 RQAHFDLMNKHKQLQlQLNAKITEIQNLQANGAAAQRPEQPNYEPELLALRQQL-AHLQSELQTAHAQRQEFEIHYHQir 621
Cdd:TIGR00618 465 AQSLKEREQQLQTKE-QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqDIDNPGPLTRRMQRGEQTYAQLE-- 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 622 ELAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAElMDSQTSDYGRQQELMEKQAELEQiyVKIDNLTAEN 701
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKED-IPNLQNITVRLQDLTEKLSEAED--MLACEQHALL 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 702 RDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEElEKEKSVAgsgnsggwSDIDDNEVVEAVQPIETTPISSE 781
Cdd:TIGR00618 619 RKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQER-VREHALS--------IRVLPKELLASRQLALQKMQSEK 689
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 782 nsENLKKFEAEIAELKASLEKTEKELTKYRNLYNEkltaISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELS 861
Cdd:TIGR00618 690 --EQLTYWKEMLAQCQTLLRELETHIEEYDREFNE----IENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAH 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 862 DRLNE---MLKNLNQSMQKSAENDKMLTQLREEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKRVKMEYV--KLE--TKS 934
Cdd:TIGR00618 764 FNNNEevtAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFlsRLEekSAT 843
|
410
....*....|....*...
gi 32565309 935 FHDVRKLNMDVEELKTQL 952
Cdd:TIGR00618 844 LGEITHQLLKYEECSKQL 861
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
544-707 |
4.28e-05 |
|
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.
Pssm-ID: 462536 [Multi-domain] Cd Length: 176 Bit Score: 45.31 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 544 QAHFDLMNKHKQLQlQLNAKIT-EIQNLQANGAAAQRPEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEihyHQIRE 622
Cdd:pfam08614 7 DAYNRLLDRTALLE-AENAKLQsEPESVLPSTSSSKLSKASPQSASIQSLEQLLAQLREELAELYRSRGELA---QRLVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 623 L----------AEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELmdsqtsdygrqQELmekQAELEQIYV 692
Cdd:pfam08614 83 LneelqelekkLREDERRLAALEAERAQLEEKLKDREEELREKRKLNQDLQDEL-----------VAL---QLQLNMAEE 148
|
170
....*....|....*
gi 32565309 693 KIDNLTAENRDLTDK 707
Cdd:pfam08614 149 KLRKLEKENRELVER 163
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
551-893 |
5.06e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 47.74 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 551 NKHKQLQLQLNAKITEIQNLQAngaaAQRPEQPNYEPELLALRQQL--AHLQSELQTAHAQRQEFEIHYHQIRE-LAEQK 627
Cdd:TIGR01612 938 NKQNILKEILNKNIDTIKESNL----IEKSYKDKFDNTLIDKINELdkAFKDASLNDYEAKNNELIKYFNDLKAnLGKNK 1013
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 628 D----HQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAeLEQIYVKIDNL------ 697
Cdd:TIGR01612 1014 EnmlyHQFDEKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNKEI-LEEAEINITNFneikek 1092
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 698 -----------------TAENRDLTDKIAQLQVSDSLELEELEELRNKNlelQEQVKQLKEELEKEKSVAGSGNSGgwsd 760
Cdd:TIGR01612 1093 lkhynfddfgkeenikyADEINKIKDDIKNLDQKIDHHIKALEEIKKKS---ENYIDEIKAQINDLEDVADKAISN---- 1165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 761 iDDNEVVEAVQPIETTPISSENS--ENLKKFEAEIAEL---KASLEKTEK-ELTKYRNLYNEKLTAISDKENRSqiemEH 834
Cdd:TIGR01612 1166 -DDPEEIEKKIENIVTKIDKKKNiyDEIKKLLNEIAEIekdKTSLEEVKGiNLSYGKNLGKLFLEKIDEEKKKS----EH 1240
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32565309 835 KLKNAES---DLQEAKRRAEEIGAEKKELSDRLNEM-LKNLNQSMQK-----SAENDKMLTQLREEAF 893
Cdd:TIGR01612 1241 MIKAMEAyieDLDEIKEKSPEIENEMGIEMDIKAEMeTFNISHDDDKdhhiiSKKHDENISDIREKSL 1308
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
614-807 |
5.73e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 5.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 614 EIHYHQIRELaEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAEL--MDSQTSDYGRQQELMEKQAELEQIY 691
Cdd:COG4717 67 ELNLKELKEL-EEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELekLEKLLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 692 VKIDNLTAENRDLTDKIAQLQvsdsleleeleelrnknlELQEQVKQLKEELEKEKSVAGSGNSGGWSDIDDnEVVEAVQ 771
Cdd:COG4717 146 ERLEELEERLEELRELEEELE------------------ELEAELAELQEELEELLEQLSLATEEELQDLAE-ELEELQQ 206
|
170 180 190
....*....|....*....|....*....|....*.
gi 32565309 772 PIEttpissENSENLKKFEAEIAELKASLEKTEKEL 807
Cdd:COG4717 207 RLA------ELEEELEEAQEELEELEEELEQLENEL 236
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
544-926 |
6.45e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 47.12 E-value: 6.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 544 QAHFDLM-NKHKQLQLQLNAKITEIQNLQA------NGAAAQRPEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEI- 615
Cdd:pfam10174 281 KSHSKFMkNKIDQLKQELSKKESELLALQTkletltNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESf 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 616 ---HYHQIRELAEQKDHQIAQLTEQAN--DYQER----LEKSQSELQELARHVDSARAEL--------MDSQTSDYGRQQ 678
Cdd:pfam10174 361 lnkKTKQLQDLTEEKSTLAGEIRDLKDmlDVKERkinvLQKKIENLQEQLRDKDKQLAGLkervkslqTDSSNTDTALTT 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 679 eLMEKQAELEQIyvkIDNLTaENRDLTDKIAQLQVSDSleleeleelRNKNLELQEQVKQLKEEL-EKEKSVagsgnsgg 757
Cdd:pfam10174 441 -LEEALSEKERI---IERLK-EQREREDRERLEELESL---------KKENKDLKEKVSALQPELtEKESSL-------- 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 758 wsdiddNEVVEAVqpiettpiSSENSENLKKfEAEIAELKASLEKTEKELTKyrnLYNEKLTAISDKEN-RSQIEMEHKL 836
Cdd:pfam10174 499 ------IDLKEHA--------SSLASSGLKK-DSKLKSLEIAVEQKKEECSK---LENQLKKAHNAEEAvRTNPEINDRI 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 837 KNAEsdlQEAKRRAEEIGAEKKELsDRLNEMLKNL----NQSMQKSAENDKM-LTQLREEA-----------FAKEKQLL 900
Cdd:pfam10174 561 RLLE---QEVARYKEESGKAQAEV-ERLLGILREVenekNDKDKKIAELESLtLRQMKEQNkkvanikhgqqEMKKKGAQ 636
|
410 420 430
....*....|....*....|....*....|....
gi 32565309 901 EHDSVLRKKDD--------KIRELDAEFKRVKME 926
Cdd:pfam10174 637 LLEEARRREDNladnsqqlQLEELMGALEKTRQE 670
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
768-951 |
6.70e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 768 EAVQPIETTpissenSENLKKFEAEIAELKASLEKTEKE---LTKYRNLYNEkltaisdkenrsqiEMEHKLKNAESDLQ 844
Cdd:TIGR02168 176 ETERKLERT------RENLDRLEDILNELERQLKSLERQaekAERYKELKAE--------------LRELELALLVLRLE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 845 EAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKRVK 924
Cdd:TIGR02168 236 ELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315
|
170 180
....*....|....*....|....*..
gi 32565309 925 MEYVKLETKSFHDVRKLNMDVEELKTQ 951
Cdd:TIGR02168 316 RQLEELEAQLEELESKLDELAEELAEL 342
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
570-755 |
6.95e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 570 LQANGAAAQRPEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTEQANDYQERLEKSQ 649
Cdd:COG3883 6 LAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 650 SELQELARH--------------------------------VDSARAELMDSQTSDygrQQELMEKQAELEQiyvKIDNL 697
Cdd:COG3883 86 EELGERARAlyrsggsvsyldvllgsesfsdfldrlsalskIADADADLLEELKAD---KAELEAKKAELEA---KLAEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 32565309 698 TAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEELEKEKSVAGSGNS 755
Cdd:COG3883 160 EALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAA 217
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
554-953 |
7.30e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 554 KQLQLQLNAKITEIQN----LQANGAAAQRP---EQPNYEPELLALRQQLAHLQSELQTAH------AQRQEFEIHYHQI 620
Cdd:PRK01156 265 LSMELEKNNYYKELEErhmkIINDPVYKNRNyinDYFKYKNDIENKKQILSNIDAEINKYHaiikklSVLQKDYNDYIKK 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 621 RELAEQKDHQIAQLTEQANDYQERLEKSQSelQELARHVDSARAELMDSQTSDYGRQQELM--EKQAELEQIYVKIDnlt 698
Cdd:PRK01156 345 KSRYDDLNNQILELEGYEMDYNSYLKSIES--LKKKIEEYSKNIERMSAFISEILKIQEIDpdAIKKELNEINVKLQ--- 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 699 aenrDLTDKIAQLQVS-DSLELEELEELRNKN-LELQEQVKQLKEELEKEKSVA-----GSGNSGGWSDID--------- 762
Cdd:PRK01156 420 ----DISSKVSSLNQRiRALRENLDELSRNMEmLNGQSVCPVCGTTLGEEKSNHiinhyNEKKSRLEEKIReieievkdi 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 763 DNEVVEAVQP---IETTPIS-SENSEN--------LKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTA---------- 820
Cdd:PRK01156 496 DEKIVDLKKRkeyLESEEINkSINEYNkiesaradLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSkrtswlnala 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 821 ----ISDKENRSQI-EMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEAFAK 895
Cdd:PRK01156 576 vislIDIETNRSRSnEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIEKLRGKIDNY 655
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32565309 896 EKQLLEHDSVLRKKDD---KIRELDAEFKRVKMEYVKL-----ETKSFHDVrkLNMDVEELKTQLS 953
Cdd:PRK01156 656 KKQIAEIDSIIPDLKEitsRINDIEDNLKKSRKALDDAkanraRLESTIEI--LRTRINELSDRIN 719
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
543-922 |
7.40e-05 |
|
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: 46.61 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 543 RQAHFDLMNKHKQLQLQLNAKITEIQNLQANGAAAQRPEQPN--YEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQI 620
Cdd:pfam05622 13 AQRCHELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSGtpGGKKYLLLQKQLEQLQEENFRLETARDDYRIKCEEL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 621 -RELAEQKdHQIAQLT----------------EQANDYQERLE-------KSQSELQELARHV----------------- 659
Cdd:pfam05622 93 eKEVLELQ-HRNEELTslaeeaqalkdemdilRESSDKVKKLEatvetykKKLEDLGDLRRQVklleernaeymqrtlql 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 660 --DSARAELMDSQTSDYGRQ-QELmekQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLEL---Q 733
Cdd:pfam05622 172 eeELKKANALRGQLETYKRQvQEL---HGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLIIERDTLRETNEELrcaQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 734 EQVKQLKEELEKEKSVAGSGNSGGwSDIDDNEVVEAVQPIEttpisSENSENLKKFEA----EIAELKASLEKTEKEltk 809
Cdd:pfam05622 249 LQQAELSQADALLSPSSDPGDNLA-AEIMPAEIREKLIRLQ-----HENKMLRLGQEGsyreRLTELQQLLEDANRR--- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 810 yrnlyNEKLTAISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLnEMLKNLNQSMQKSAENDKMLTQLR 889
Cdd:pfam05622 320 -----KNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHL-EKLHEAQSELQKKKEQIEELEPKQ 393
|
410 420 430
....*....|....*....|....*....|...
gi 32565309 890 EEAFAKEKQLLEHdsVLRKKDDKIRELDAEFKR 922
Cdd:pfam05622 394 DSNLAQKIDELQE--ALRKKDEDMKAMEERYKK 424
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
588-748 |
8.41e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 588 ELLALRQQLAHLQ------SELQTAHAQRQEFEI------HYHQIRELAEQKDhQIAQLTEQANDYQERLEKSQSELQEL 655
Cdd:COG4913 243 ALEDAREQIELLEpirelaERYAAARERLAELEYlraalrLWFAQRRLELLEA-ELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 656 ARHVDSARAELMDSqtsDYGRQQELmekQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELeelrnknLELQEQ 735
Cdd:COG4913 322 REELDELEAQIRGN---GGDRLEQL---EREIERLERELEERERRRARLEALLAALGLPLPASAEEF-------AALRAE 388
|
170
....*....|...
gi 32565309 736 VKQLKEELEKEKS 748
Cdd:COG4913 389 AAALLEALEEELE 401
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
617-825 |
8.52e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.55 E-value: 8.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 617 YHQIRELAEQKDHQIAQLTEQaNDYQERLEKSQSE-LQELARHVDSARAELMDSqtsdygrQQELMEKQAELEQIYVKID 695
Cdd:PHA02562 180 NQQIQTLDMKIDHIQQQIKTY-NKNIEEQRKKNGEnIARKQNKYDELVEEAKTI-------KAEIEELTDELLNLVMDIE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 696 NLTAENRDLTDKIAQL--QVSD---------------------SLELEELEELRNKNLELQEQVKQLKEELEKEKSVAgs 752
Cdd:PHA02562 252 DPSAALNKLNTAAAKIksKIEQfqkvikmyekggvcptctqqiSEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIM-- 329
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32565309 753 gnsggwSDIDDN--EVVEAVQPIET--TPISSENSENlKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKE 825
Cdd:PHA02562 330 ------DEFNEQskKLLELKNKISTnkQSLITLVDKA-KKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELV 399
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
543-750 |
8.75e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 8.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 543 RQAHFDLMNKHKQLQLQLNAKITEIQNlQANGAAAQRPEQPNYEPELLALRQQLAHLQSELQTA-HAQRQEFEIhYHQIR 621
Cdd:COG1340 66 RDELNEKVKELKEERDELNEKLNELRE-ELDELRKELAELNKAGGSIDKLRKEIERLEWRQQTEvLSPEEEKEL-VEKIK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 622 ELAEQ---------KDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSqtsdygrQQELMEKQAELEQIYV 692
Cdd:COG1340 144 ELEKElekakkaleKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIEL-------YKEADELRKEADELHK 216
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 32565309 693 KIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKqlKEELEKEKSVA 750
Cdd:COG1340 217 EIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKE--KEELEEKAEEI 272
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
548-688 |
1.16e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.52 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 548 DLMNKHKQLQLQLNAKITEIQNLQANgaaAQRPEQpNYEPELLALRQQLAHLQSELQTAHAQRQEFEihyHQIRELAEQK 627
Cdd:pfam09787 51 ELRQERDLLREEIQKLRGQIQQLRTE---LQELEA-QQQEEAESSREQLQELEEQLATERSARREAE---AELERLQEEL 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32565309 628 DHQIAQLTEQANDYQERLEKSQSELQELarhvdsaRAELMDSQTSDYGRQQ----------ELMEKQAELE 688
Cdd:pfam09787 124 RYLEEELRRSKATLQSRIKDREAEIEKL-------RNQLTSKSQSSSSQSElenrlhqlteTLIQKQTMLE 187
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
492-712 |
1.47e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 492 LIELIRSSLGLGNITDSSVL-------------LVVNLtfVAASFLVYII-IRSLSSGGESDILDRQAhfdlmnkhKQLQ 557
Cdd:COG3206 119 AIERLRKNLTVEPVKGSNVIeisytspdpelaaAVANA--LAEAYLEQNLeLRREEARKALEFLEEQL--------PELR 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 558 LQLNAKITEIQNLQANGAAAQRPEQpnyepeLLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTEQ 637
Cdd:COG3206 189 KELEEAEAALEEFRQKNGLVDLSEE------AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 638 A--NDYQERLEKSQSELQELARH-------VDSARAELMDSqtsdygRQQELMEKQAELEQIYVKIDNLTAENRDLTDKI 708
Cdd:COG3206 263 PviQQLRAQLAELEAELAELSARytpnhpdVIALRAQIAAL------RAQLQQEAQRILASLEAELEALQAREASLQAQL 336
|
....
gi 32565309 709 AQLQ 712
Cdd:COG3206 337 AQLE 340
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
552-712 |
1.56e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 552 KHKQLQLQLNAKITEIQNLQANGAAAQRPEQPNYEP--------ELLALRQQLAH----------LQSELQTAHAQRQEF 613
Cdd:COG4913 625 ELAEAEERLEALEAELDALQERREALQRLAEYSWDEidvasaerEIAELEAELERldassddlaaLEEQLEELEAELEEL 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 614 EIHYHQIRELAEQKDHQIAQLTEQANDYQERLEksqsELQELARHVDSARAELMDSQTSDYGRQQELMEKQAEleqiyvK 693
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQAEEELDELQDRLE----AAEDLARLELRALLEERFAAALGDAVERELRENLEE------R 774
|
170
....*....|....*....
gi 32565309 694 IDNLTAENRDLTDKIAQLQ 712
Cdd:COG4913 775 IDALRARLNRAEEELERAM 793
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
833-951 |
1.92e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 833 EHKLKNAESD----LQEAKRRAEEIgaeKKELSDRLNEMLKNLNQsmqksaENDKMLTQLREEAFAKEKQLLEHDSVLRK 908
Cdd:PRK12704 30 EAKIKEAEEEakriLEEAKKEAEAI---KKEALLEAKEEIHKLRN------EFEKELRERRNELQKLEKRLLQKEENLDR 100
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 32565309 909 KDDKIRELDAEFKRVKMEYVKLETksfhDVRKLNMDVEELKTQ 951
Cdd:PRK12704 101 KLELLEKREEELEKKEKELEQKQQ----ELEKKEEELEELIEE 139
|
|
| PRK10819 |
PRK10819 |
transport protein TonB; Provisional |
246-346 |
2.11e-04 |
|
transport protein TonB; Provisional
Pssm-ID: 236768 [Multi-domain] Cd Length: 246 Bit Score: 44.29 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 246 MKNVAEQPPlvLQSLPETPEAQKLPEEPLEPVtPEPIPEAPVPIAQYIQEPTTTPAPleAPAPVENAPNLPTPTFS-VDD 324
Cdd:PRK10819 52 MVAPADLEP--PQAVQPPPEPVVEPEPEPEPI-PEPPKEAPVVIPKPEPKPKPKPKP--KPKPVKKVEEQPKREVKpVEP 126
|
90 100
....*....|....*....|..
gi 32565309 325 LMAQAARDALNSNSIVPDAPKV 346
Cdd:PRK10819 127 RPASPFENTAPARPTSSTATAA 148
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
588-895 |
2.32e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 588 ELLALRQQLAHLQSELQTAHAQRQEfeiHYHQIRELAEqkdhQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELm 667
Cdd:COG1340 23 EIEELKEKRDELNEELKELAEKRDE---LNAQVKELRE----EAQELREKRDELNEKVKELKEERDELNEKLNELREEL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 668 dsqtsdygrqQELMEKQAELEQIYVKIDNLTAENRDLTDKIaQLQVSDsleleeleelRNKNLELQEQVKQLKEELEKEK 747
Cdd:COG1340 95 ----------DELRKELAELNKAGGSIDKLRKEIERLEWRQ-QTEVLS----------PEEEKELVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 748 SVAgsgnsggwsdiddnevveavqpiettpissENSENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAISdkENR 827
Cdd:COG1340 154 KAL------------------------------EKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMI--ELY 201
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32565309 828 SQI-EMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLN-----QSMQKSAENDKMLTQLREEAFAK 895
Cdd:COG1340 202 KEAdELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKklrkkQRALKREKEKEELEEKAEEIFEK 275
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
552-953 |
2.42e-04 |
|
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: 45.48 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 552 KHKQLQLQLNAKITE-----IQNLQ-ANGAAAQRPEQPNYE-PELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELA 624
Cdd:pfam05483 102 KQKENKLQENRKIIEaqrkaIQELQfENEKVSLKLEEEIQEnKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREET 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 625 EQkdhqiaqlteQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGR--------QQELMEKQAELEQIYVKIDN 696
Cdd:pfam05483 182 RQ----------VYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKiqhleeeyKKEINDKEKQVSLLLIQITE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 697 LTAENRDLT-------DKIAQLQvsdsleleELEELRNKNL-ELQEQVKQLKEELEKEKSVAGSGNSGGWSDIDDNEVV- 767
Cdd:pfam05483 252 KENKMKDLTflleesrDKANQLE--------EKTKLQDENLkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIAt 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 768 ---------EAVQPIETTPISSENSENLKKFEAEIAELKASLEKTEKELTKyrNLYNEKLTAISDKENRSQIEMEHKLK- 837
Cdd:pfam05483 324 kticqlteeKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEK--NEDQLKIITMELQKKSSELEEMTKFKn 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 838 NAESDLQEAKRraeeIGAEKKELSDRlNEMLKNLNQSMQKSAENDKMLTQLRE-EAFAKEKQLLEHDSVLRKKDDKIREL 916
Cdd:pfam05483 402 NKEVELEELKK----ILAEDEKLLDE-KKQFEKIAEELKGKEQELIFLLQAREkEIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
410 420 430
....*....|....*....|....*....|....*..
gi 32565309 917 DAEFKRVKMEYVKLETKSfhdvRKLNMDVEELKTQLS 953
Cdd:pfam05483 477 KTELEKEKLKNIELTAHC----DKLLLENKELTQEAS 509
|
|
| HAUS-augmin3 |
pfam14932 |
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found ... |
762-953 |
2.83e-04 |
|
HAUS augmin-like complex subunit 3; This domain is subunit three of the augmin complex found from Drosophila to humans. The HAUS-augmin complex is made up of eight subunits. The augmin complex interacts with gamma-TuRC, and attenuation of this interaction severely impairs spindle MT generation. Furthermore, we provide evidence that human augmin plays critical and non-redundant roles in the kinetochore-MT attachment and also central spindle formation during anaphase in human cells.The HAUS complex is required for mitotic spindle assembly and for maintenance of centrosome integrity.
Pssm-ID: 464384 [Multi-domain] Cd Length: 261 Bit Score: 43.84 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 762 DDNEVVEAVQPIETTPISSENSENLKKFEAEIAELKASLEKTEKE---LTKYRNLYNEKLtaisDKENRSQIEMEHKLKN 838
Cdd:pfam14932 45 EGAALDEALKTISAESPGLLNQQDVEALEESLEEIREATEDLEAElqeLQKTKQLKINRL----NKLQAQASSLSQGLRA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 839 AESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKSA------ENDKMLTQLR-EEAFAKEKQLLEHDSVLRKK-- 909
Cdd:pfam14932 121 LVAEEEEAAKQLEELQEELAALNAKTNNVLQSLQSEVKELAsffsasEPPVFLSQLPlEPYLLQEEQFTKYLTLYTKKqf 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 32565309 910 DDKIRELDAEFKRVKMEYVKLETKSFHDvrKLNMDVEELKTQLS 953
Cdd:pfam14932 201 FQGISELVEFSNEERFQLLDLSDCSERD--SDEVDVEHRRSELA 242
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
600-951 |
3.67e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 600 QSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQE 679
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKAD 1318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 680 LMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQ-EQVKQLKEELEKEKSVAGSGNSGGW 758
Cdd:PTZ00121 1319 EAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKkEEAKKKADAAKKKAEEKKKADEAKK 1398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 759 SDIDDNEVVEAVQPIETTPISSE----------NSENLKKfEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKENRS 828
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADeakkkaeekkKADEAKK-KAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 829 QIEMEHKLKNAESDLQEAKRRAEEI--GAEKKELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEAFAKEKQLLEHDSVL 906
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKKKADEAkkAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEEL 1557
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 32565309 907 RKKDD--KIRELDAEFKRVKM------EYVKLETKSFHDVRKLNMDVEELKTQ 951
Cdd:PTZ00121 1558 KKAEEkkKAEEAKKAEEDKNMalrkaeEAKKAEEARIEEVMKLYEEEKKMKAE 1610
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
592-931 |
4.67e-04 |
|
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: 44.65 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 592 LRQQLAHLQSELQTAHAQRQEFEihyHQIRELAEQKDHQIAQLTEQANDYQeRLEKSQSELQELARHVDSARAELmdsqT 671
Cdd:TIGR00606 693 LQEFISDLQSKLRLAPDKLKSTE---SELKKKEKRRDEMLGLAPGRQSIID-LKEKEIPELRNKLQKVNRDIQRL----K 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 672 SDYGRQQELM------EKQAELEQIYVKI-DNLTAENRDLTDKIAQlQVSDSLELeeleelrNKNLELQEQVKQLKEELE 744
Cdd:TIGR00606 765 NDIEEQETLLgtimpeEESAKVCLTDVTImERFQMELKDVERKIAQ-QAAKLQGS-------DLDRTVQQVNQEKQEKQH 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 745 KEKSVAGSGNSGGWSDIDDNEVVEAVQP----IETTPIS-SENSENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLT 819
Cdd:TIGR00606 837 ELDTVVSKIELNRKLIQDQQEQIQHLKSktneLKSEKLQiGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLET 916
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 820 AISDKENRSQIEMEHK---LKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNlnQSMQKSAENDKMLTQLREEAFAKE 896
Cdd:TIGR00606 917 FLEKDQQEKEELISSKetsNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDD--YLKQKETELNTVNAQLEECEKHQE 994
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 32565309 897 K-------------------QLLEHDSVLRKKDDKIRELDAEFK------------RVKMEYVKLE 931
Cdd:TIGR00606 995 KinedmrlmrqdidtqkiqeRWLQDNLTLRKRENELKEVEEELKqhlkemgqmqvlQMKQEHQKLE 1060
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
783-951 |
4.77e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 44.75 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 783 SENLKKFEAEIAELKASLEKTEKELTKYRNLYNEkltaisdkENRSQIEMEHKLKNAESDLQEAK--RRAEEIGAEKKEL 860
Cdd:PTZ00121 1622 AEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA--------EEENKIKAAEEAKKAEEDKKKAEeaKKAEEDEKKAAEA 1693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 861 SDRLNEMLKNLNQSMQKSAENDKMLTQLR---EEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKRVKmEYVKLETKSFHD 937
Cdd:PTZ00121 1694 LKKEAEEAKKAEELKKKEAEEKKKAEELKkaeEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA-HLKKEEEKKAEE 1772
|
170
....*....|....*.
gi 32565309 938 VRKLNMDV--EELKTQ 951
Cdd:PTZ00121 1773 IRKEKEAVieEELDEE 1788
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
572-922 |
5.41e-04 |
|
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: 44.18 E-value: 5.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 572 ANGAAAQRPEQPNYEPELLALRQQLAHLQSELQTAHAQrQEFEIHYHQIRELAEQKDHqIAQLTEQANDYqeRLEKSqSE 651
Cdd:COG5185 198 AEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEAL-KGFQDPESELEDLAQTSDK-LEKLVEQNTDL--RLEKL-GE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 652 LQELARHVDSARAELMDSQTSDYGRQQELmEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLE 731
Cdd:COG5185 273 NAESSKRLNENANNLIKQFENTKEKIAEY-TKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQES 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 732 LQEQVKQLKEELEKeksvagsgnsggwsdiddnevveavqpIETTPISSENSENLKKFEAEIAELKASLEKTEKELTKYR 811
Cdd:COG5185 352 LTENLEAIKEEIEN---------------------------IVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYA 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 812 NLYNEKLtaisdkeNRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQK--SAENDKMLTQLR 889
Cdd:COG5185 405 QEILATL-------EDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSrlEEAYDEINRSVR 477
|
330 340 350
....*....|....*....|....*....|...
gi 32565309 890 EEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKR 922
Cdd:COG5185 478 SKKEDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
579-951 |
5.74e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 579 RPEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRE---LAEQKDHQIAQLTEQANDYQERLEKSQSELQ-- 653
Cdd:PRK01156 189 EEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDdynNLKSALNELSSLEDMKNRYESEIKTAESDLSme 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 654 ------------ELARHVDSA--------------------RAELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLTAEN 701
Cdd:PRK01156 269 leknnyykeleeRHMKIINDPvyknrnyindyfkykndienKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRY 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 702 RDLTDKIAQLQVSDSLEleeleelrNKNLELQEQVKQLKEELEKEKSVAGsgnsggwSDIDDNEVVEAVQPIETTPISSE 781
Cdd:PRK01156 349 DDLNNQILELEGYEMDY--------NSYLKSIESLKKKIEEYSKNIERMS-------AFISEILKIQEIDPDAIKKELNE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 782 NSENLKKFEAEIAELKA---SLEKTEKELTKYRNLYNEK-------LTAISDKENRSQIEMEHKLKNAESDLQEAKRRAE 851
Cdd:PRK01156 414 INVKLQDISSKVSSLNQrirALRENLDELSRNMEMLNGQsvcpvcgTTLGEEKSNHIINHYNEKKSRLEEKIREIEIEVK 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 852 EIGAEKKELSDRLNEMLKnlnQSMQKSAENDKMLTQLREEAfakeKQLLEHDSVLRKKDDKIRELDAEFKRVKMEYVKLE 931
Cdd:PRK01156 494 DIDEKIVDLKKRKEYLES---EEINKSINEYNKIESARADL----EDIKIKINELKDKHDKYEEIKNRYKSLKLEDLDSK 566
|
410 420
....*....|....*....|..
gi 32565309 932 TKSFHDVRKL--NMDVEELKTQ 951
Cdd:PRK01156 567 RTSWLNALAVisLIDIETNRSR 588
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
563-700 |
6.26e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 563 KITEIQNLQANGAAAQRPEQPNYEPELLAlRQQLAHLQSElqtAHAQRQEFEIHYHQIRELAEQKDHQIAQLTEQANDYQ 642
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKEAEAIK-KEALLEAKEE---IHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 32565309 643 ERLEKSQSELQELARHVDSARAELMDsqtsdygRQQELMEKQAELEQIYVKIDNLTAE 700
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEK-------KEEELEELIEEQLQELERISGLTAE 153
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
585-712 |
6.31e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 585 YEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRE-LAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSAR 663
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREELDELEAqIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALG 372
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 32565309 664 AELMDSQtSDYGRQQ------------ELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQ 712
Cdd:COG4913 373 LPLPASA-EEFAALRaeaaallealeeELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
550-880 |
6.54e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 43.96 E-value: 6.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 550 MNKHKQLQLQLNAKITEIQNlQANGAAAQRPEQPNYEPELLALRQQlahlQSELQTAHAQRQEFEIHYHQIRELA----- 624
Cdd:pfam17380 312 VERRRKLEEAEKARQAEMDR-QAAIYAEQERMAMERERELERIRQE----ERKRELERIRQEEIAMEISRMRELErlqme 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 625 -EQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQElmEKQAELEQIyvkidnltaenrd 703
Cdd:pfam17380 387 rQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE--ERAREMERV------------- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 704 ltdkiaqlqvsdsleleeleelRNKNLELQEQVKQLKEELEKEKSVAGSGNSggwSDIDDNEVVEAVQPIettpISSENS 783
Cdd:pfam17380 452 ----------------------RLEEQERQQQVERLRQQEEERKRKKLELEK---EKRDRKRAEEQRRKI----LEKELE 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 784 ENLKKfeaeIAELKASLEKTEKELTKYRN-LYNEKLTAISDKENRSQIEMEHKLKnaesdLQEAKRRAEEiGAEKKELSD 862
Cdd:pfam17380 503 ERKQA----MIEEERKRKLLEKEMEERQKaIYEEERRREAEEERRKQQEMEERRR-----IQEQMRKATE-ERSRLEAME 572
|
330
....*....|....*...
gi 32565309 863 RLNEMLKNLNQSMQKSAE 880
Cdd:pfam17380 573 REREMMRQIVESEKARAE 590
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
783-953 |
6.85e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.21 E-value: 6.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 783 SENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKENRSqIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSD 862
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI-AALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 863 RLNE---MLKNLNQSMQKSAENDKMLTQLREEAFAK-EKQLLEHDSVLRKKDDKIRELDAEFKRVKMEYVKLETKSfHDV 938
Cdd:COG4942 98 ELEAqkeELAELLRALYRLGRQPPLALLLSPEDFLDaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER-AEL 176
|
170
....*....|....*
gi 32565309 939 RKLNMDVEELKTQLS 953
Cdd:COG4942 177 EALLAELEEERAALE 191
|
|
| PHA03291 |
PHA03291 |
envelope glycoprotein I; Provisional |
250-340 |
7.46e-04 |
|
envelope glycoprotein I; Provisional
Pssm-ID: 223033 [Multi-domain] Cd Length: 401 Bit Score: 43.40 E-value: 7.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 250 AEQPPLVLQSLPETPEAQKLPEEPLEPVTPEPIPEAPVPIAQYIQEPTTTPAPlEAPAPVENAPNLPTPTfsvddlmAQA 329
Cdd:PHA03291 207 TPRPTPRTTASPETTPTPSTTTSPPSTTIPAPSTTIAAPQAGTTPEAEGTPAP-PTPGGGEAPPANATPA-------PEA 278
|
90
....*....|.
gi 32565309 330 ARDALNSNSIV 340
Cdd:PHA03291 279 SRYELTVTQII 289
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
543-712 |
9.24e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 543 RQAHFDLMNKHKQLQLQLNAKITEIQNLQANgAAAQRPEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRE 622
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQ-IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRS 894
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 623 LAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQ---TSDYGRQQELMEK------------QAEL 687
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQerlSEEYSLTLEEAEAlenkieddeeeaRRRL 974
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 32565309 688 EQIYVKIDN---------------------LTAENRDLTDKIAQLQ 712
Cdd:TIGR02168 975 KRLENKIKElgpvnlaaieeyeelkerydfLTAQKEDLTEAKETLE 1020
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
826-952 |
1.05e-03 |
|
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: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 826 NRSQIEM-EHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNemlknLNQSMQKSAENDKMLTQLREEAFAKEKQLLEhds 904
Cdd:COG4913 608 NRAKLAAlEAELAELEEELAEAEERLEALEAELDALQERRE-----ALQRLAEYSWDEIDVASAEREIAELEAELER--- 679
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 32565309 905 vLRKKDDKIRELDAEFKRVKMEYVKLETKSF---HDVRKLNMDVEELKTQL 952
Cdd:COG4913 680 -LDASSDDLAALEEQLEELEAELEELEEELDelkGEIGRLEKELEQAEEEL 729
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
529-747 |
1.07e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.08 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 529 IRSLSSGGESDILDRQAHFD----LMNKHKQLQLQLNAKITEIQNlqangaaaqrpEQPNYEPELLALRQQLAHLQSELQ 604
Cdd:PHA02562 204 IEEQRKKNGENIARKQNKYDelveEAKTIKAEIEELTDELLNLVM-----------DIEDPSAALNKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 605 TAHAQRQEFEIHYH------QIrelaEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAElmdsqtsdygrQQ 678
Cdd:PHA02562 273 QFQKVIKMYEKGGVcptctqQI----SEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQ-----------SK 337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 32565309 679 ELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNknlELQEQVKQlKEELEKEK 747
Cdd:PHA02562 338 KLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQD---ELDKIVKT-KSELVKEK 402
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
786-953 |
1.07e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 786 LKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKENRSQiEMEHKLKNAESDLQEAKRRAEEigAEKKELSDRLN 865
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE-DLEKEIKRLELEIEEVEARIKK--YEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 866 EMLKNLNQSMqksAENDKMLTQLREEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKRVKMEYVKLETKSFHDVRKLNMDV 945
Cdd:COG1579 89 KEYEALQKEI---ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAER 165
|
....*...
gi 32565309 946 EELKTQLS 953
Cdd:COG1579 166 EELAAKIP 173
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
586-974 |
1.22e-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: 43.24 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 586 EPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRE----LAEQKdHQIAQLTEQANDYQERLEKSQSELQELARHVDS 661
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEeknaLQEQL-QAETELCAEAEEMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 662 ------ARAELMDSQTSDYGRQQELMEKQAELEQIY---VKIDNLTAEN--RDLTDKIAQLQVSDSLELEELeelrnKNL 730
Cdd:pfam01576 83 rleeeeERSQQLQNEKKKMQQHIQDLEEQLDEEEAArqkLQLEKVTTEAkiKKLEEDILLLEDQNSKLSKER-----KLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 731 E--LQEQVKQLKEELEKEKSVAGSGN--SGGWSDIDDNEVVEAVQPIETTPI-------SSENSENLKKFEAEIAELKAS 799
Cdd:pfam01576 158 EerISEFTSNLAEEEEKAKSLSKLKNkhEAMISDLEERLKKEEKGRQELEKAkrklegeSTDLQEQIAELQAQIAELRAQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 800 LEKTEKELTKYRNLYNEKLTAISD--KENRsqiEMEHKLKNAESDLQ---------EAKRR--AEEIGAEKKELSDRLNE 866
Cdd:pfam01576 238 LAKKEEELQAALARLEEETAQKNNalKKIR---ELEAQISELQEDLEseraarnkaEKQRRdlGEELEALKTELEDTLDT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 867 MLKNLNQSMQKSAENDKMLTQLREEAFAKEKQLLEhdsvLRKKD----DKIRELDAEFKRVKMEYVKLEtksfhdvRKLN 942
Cdd:pfam01576 315 TAAQQELRSKREQEVTELKKALEEETRSHEAQLQE----MRQKHtqalEELTEQLEQAKRNKANLEKAK-------QALE 383
|
410 420 430
....*....|....*....|....*....|...
gi 32565309 943 MDVEELKTQL-SMAGGVTSSRSIPDRLVSPLQE 974
Cdd:pfam01576 384 SENAELQAELrTLQQAKQDSEHKRKKLEGQLQE 416
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
631-933 |
1.22e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 631 IAQLTEQANDYQER--LEKSQSELQElarHVDSARAELMDSQTSDYGRQQELMEKQAEleqiyvkIDNLTAENRDLTDKI 708
Cdd:PRK01156 106 IAEGFDDTTKYIEKniLGISKDVFLN---SIFVGQGEMDSLISGDPAQRKKILDEILE-------INSLERNYDKLKDVI 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 709 AQLQVSDSLELEELEELRNKNLELQEQVKQLKEE------LEKEKSVAgsgnsggwSDIDDNEVVEAVQPIETTPISSEN 782
Cdd:PRK01156 176 DMLRAEISNIDYLEEKLKSSNLELENIKKQIADDekshsiTLKEIERL--------SIEYNNAMDDYNNLKSALNELSSL 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 783 SENLKKFEAEIAELKASLEKTEKELTKY------------------RNLYNEKLTAISDKENRSQIemehkLKNAESDLQ 844
Cdd:PRK01156 248 EDMKNRYESEIKTAESDLSMELEKNNYYkeleerhmkiindpvyknRNYINDYFKYKNDIENKKQI-----LSNIDAEIN 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 845 ---EAKRRAEEIGA------EKKELSDRLNEMLKNLN------QSMQKSAENDKMltQLREEAFAKEKQLLEHDSVLRKK 909
Cdd:PRK01156 323 kyhAIIKKLSVLQKdyndyiKKKSRYDDLNNQILELEgyemdyNSYLKSIESLKK--KIEEYSKNIERMSAFISEILKIQ 400
|
330 340
....*....|....*....|....
gi 32565309 910 DDKIRELDAEFKRVKMEYVKLETK 933
Cdd:PRK01156 401 EIDPDAIKKELNEINVKLQDISSK 424
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
554-689 |
1.33e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 554 KQLQLQLNAKITEIQNlQANGAAAQRPEQpnyEPELLALRQQ--------LAHLQSELQTAHAQRQEfeihyhqIRELAE 625
Cdd:COG4913 294 EAELEELRAELARLEA-ELERLEARLDAL---REELDELEAQirgnggdrLEQLEREIERLERELEE-------RERRRA 362
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32565309 626 QKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQ 689
Cdd:COG4913 363 RLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
591-748 |
1.57e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 591 ALRQQLAHLqSELQTAHAQRQEFEihyHQIRELAEQ---KDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELM 667
Cdd:COG1579 1 AMPEDLRAL-LDLQELDSELDRLE---HRLKELPAElaeLEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 668 DSQTsdygrQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQvsdslelEELEELRNKNLELQEQVKQLKEELEKEK 747
Cdd:COG1579 77 KYEE-----QLGNVRNNKEYEALQKEIESLKRRISDLEDEILELM-------ERIEELEEELAELEAELAELEAELEEKK 144
|
.
gi 32565309 748 S 748
Cdd:COG1579 145 A 145
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
565-906 |
1.58e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 42.63 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 565 TEIQNLQANGAAAQRPEQP----NYEPELLALRQQLAHLQSELQTAHAQrqefEIHYHQ-IRELAE-QKDHQIAQLT-EQ 637
Cdd:COG3096 363 LEEQEEVVEEAAEQLAEAEarleAAEEEVDSLKSQLADYQQALDVQQTR----AIQYQQaVQALEKaRALCGLPDLTpEN 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 638 ANDYQERLeksQSELQELARHVDSARAELMDSQT--SDYGRQQELMEKQA---ELEQIYVKIDNLTAENRDLTDKIAQLQ 712
Cdd:COG3096 439 AEDYLAAF---RAKEQQATEEVLELEQKLSVADAarRQFEKAYELVCKIAgevERSQAWQTARELLRRYRSQQALAQRLQ 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 713 VSDSLELEELeelrnKNLELQEQVKQLKEELEKEKSvagsgnsggwSDIDDNEVVEAVQpiettpissensenlkkfeae 792
Cdd:COG3096 516 QLRAQLAELE-----QRLRQQQNAERLLEEFCQRIG----------QQLDAAEELEELL--------------------- 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 793 iAELKASLEKTEKELTkyrnlynekltaiSDKENRSQieMEHKLKNAESDLQEAKRRAEE-IGAEKK--ELSDRLNEMLK 869
Cdd:COG3096 560 -AELEAQLEELEEQAA-------------EAVEQRSE--LRQQLEQLRARIKELAARAPAwLAAQDAleRLREQSGEALA 623
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 32565309 870 NLNQ---SMQKSAENDKMLTQLREEAFAKEKQLLEHDSVL 906
Cdd:COG3096 624 DSQEvtaAMQQLLEREREATVERDELAARKQALESQIERL 663
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
586-891 |
1.63e-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: 42.65 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 586 EPELLALRQQLAHLQSE--LQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTEQANDYQERLEKsQSELQELARHVDSAR 663
Cdd:TIGR00618 195 KAELLTLRSQLLTLCTPcmPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKK-QQLLKQLRARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 664 AELmdsqtSDYGRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRN---KNLELQEQVKQLK 740
Cdd:TIGR00618 274 AQE-----AVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAhvkQQSSIEEQRRLLQ 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 741 EELEKEKSVAGSGN-SGGWSDIDDNEVVEaVQPIETTPISSENSENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLT 819
Cdd:TIGR00618 349 TLHSQEIHIRDAHEvATSIREISCQQHTL-TQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA 427
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 32565309 820 AISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELsDRLNEMLKNLNQSMQKSAENDKMLTQLREE 891
Cdd:TIGR00618 428 HAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL-KEREQQLQTKEQIHLQETRKKAVVLARLLE 498
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
784-950 |
2.04e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 784 ENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKENRSQiEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDR 863
Cdd:COG4372 38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE-ELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 864 LNEMLKNLNQSMQKSAENDKMLTQLREEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKRVKMEYVKLETKSFHDVRKLNM 943
Cdd:COG4372 117 LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNA 196
|
....*..
gi 32565309 944 DVEELKT 950
Cdd:COG4372 197 EKEEELA 203
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
213-319 |
2.06e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 42.33 E-value: 2.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 213 IEEAPKPAEEPVKPADLEMDAEIERLIKEEeermknVAEQPPLVLQslPETPEAQKLPEEPlEPVTPEPIPEAPVPIAQY 292
Cdd:PRK10811 894 VVEEPVVVAEPQPEEVVVVETTHPEVIAAP------VTEQPQVITE--SDVAVAQEVAEHA-EPVVEPQDETADIEEAAE 964
|
90 100
....*....|....*....|....*..
gi 32565309 293 IQEPTTTPAPLEAPAPVENAPNLPTPT 319
Cdd:PRK10811 965 TAEVVVAEPEVVAQPAAPVVAEVAAEV 991
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
552-792 |
2.12e-03 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 42.51 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 552 KHKQL------QLQLNAkiTEIQNLQANGAA---AQRPEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQ--I 620
Cdd:NF012221 1578 KQQQLaaisgsQSQLES--TDQNALETNGQAqrdAILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAGglL 1655
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 621 RELAEQKDH-------QIA----QLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQ 689
Cdd:NF012221 1656 DRVQEQLDDakkisgkQLAdakqRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQ 1735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 690 iyvkidnltAEnrdlTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEElEKEK----SVAGSGNSG-GWSDIDDN 764
Cdd:NF012221 1736 ---------AE----SDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQD-ESDKpnrqGAAGSGLSGkAYSVEGVA 1801
|
250 260
....*....|....*....|....*...
gi 32565309 765 EVVEAVQPIETTPISSENSENLKKFEAE 792
Cdd:NF012221 1802 EPGSHINPDSPAAADGRFSEGLTEQEQE 1829
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
586-929 |
2.12e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 586 EPELLALRQQLaHLQSELQTAHAQRQefeihyhQIRELAEQKDHQIAQLTEQANDYQERLE--KSQSELQELARHVDSAR 663
Cdd:pfam10174 205 EKENIHLREEL-HRRNQLQPDPAKTK-------ALQTVIEMKDTKISSLERNIRDLEDEVQmlKTNGLLHTEDREEEIKQ 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 664 AELMDSQtSDYGR------QQELMEKQAELEQIYVKIDNLTAENRD-----------LTDKIAQLQVSDSLELEELEELR 726
Cdd:pfam10174 277 MEVYKSH-SKFMKnkidqlKQELSKKESELLALQTKLETLTNQNSDckqhievlkesLTAKEQRAAILQTEVDALRLRLE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 727 NKNLELQEQVKQLkEELEKEKsvagSGNSGGWSDIDDNEVVEAvQPIETTPISSEN-SENLKKFEAEIAELKASLEKTEK 805
Cdd:pfam10174 356 EKESFLNKKTKQL-QDLTEEK----STLAGEIRDLKDMLDVKE-RKINVLQKKIENlQEQLRDKDKQLAGLKERVKSLQT 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 806 ELTKYRNLYNEKLTAISDKEN-----RSQIEMEHKLKNAESDL--QEAKRRAEEIGAEKKELSDR------LNEMLKNLN 872
Cdd:pfam10174 430 DSSNTDTALTTLEEALSEKERiierlKEQREREDRERLEELESlkKENKDLKEKVSALQPELTEKesslidLKEHASSLA 509
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 32565309 873 QSMQKSAENDKML----TQLREEAFAKEKQLL---EHDSVLRKK---DDKIRELDAEFKRVKMEYVK 929
Cdd:pfam10174 510 SSGLKKDSKLKSLeiavEQKKEECSKLENQLKkahNAEEAVRTNpeiNDRIRLLEQEVARYKEESGK 576
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
768-892 |
2.15e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.07 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 768 EAVQPIETTPISSENSENLKKFEA--EIAELKaslEKTEKELTKYRNLYNEKLTAISDKE---NRSQIEMEHKLKNAESD 842
Cdd:PRK12704 39 EAKRILEEAKKEAEAIKKEALLEAkeEIHKLR---NEFEKELRERRNELQKLEKRLLQKEenlDRKLELLEKREEELEKK 115
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 32565309 843 LQEAKRRAEEIGAEKKELSDRLNEMLKNLNQSMQKSAENDK--MLTQLREEA 892
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEEAKeiLLEKVEEEA 167
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
631-953 |
2.18e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 631 IAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQ 710
Cdd:COG4372 26 IAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 711 LQVSDSLELEELEELRNKNLELQEQVKQLKEELEKEKSvagsgnsggwsdiddnevveavqpiettpissenseNLKKFE 790
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQS------------------------------------EIAERE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 791 AEIAELKASLEKTEKELTKYRNLYNEkltaISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKN 870
Cdd:COG4372 150 EELKELEEQLESLQEELAALEQELQA----LSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKD 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 871 LNqSMQKSAENDKMLTQLREEAFAKEKQLLEHDSVLRKKDDKI-RELDAEFKRVKMEYVKLETKSFHDVRKLNMDVEELK 949
Cdd:COG4372 226 SL-EAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAIlVEKDTEEEELEIAALELEALEEAALELKLLALLLNL 304
|
....
gi 32565309 950 TQLS 953
Cdd:COG4372 305 AALS 308
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
585-953 |
2.19e-03 |
|
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: 42.34 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 585 YEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTEQANDYQErLEKSQSELQELARHVDSARA 664
Cdd:TIGR00606 215 YKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA-LKSRKKQMEKDNSELELKME 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 665 ELM---DSQTSD--YGRQQELMEKQAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLEL----EELEELRNKNLELQE- 734
Cdd:TIGR00606 294 KVFqgtDEQLNDlyHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQlqadRHQEHIRARDSLIQSl 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 735 -----------------QVKQLKEELEKEKSVAGSGNSGGWSDIDDNEVV--EAVQPIETTPISSENSENLKK--FEAEI 793
Cdd:TIGR00606 374 atrleldgfergpfserQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLkqEQADEIRDEKKGLGRTIELKKeiLEKKQ 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 794 AELK------ASLEKTEKELTKYRNLYNEKLTAISDKENRSQIEMEHK----LKNAESDLQEAKRRAEEIGAEKKELSDR 863
Cdd:TIGR00606 454 EELKfvikelQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKevksLQNEKADLDRKLRKLDQEMEQLNHHTTT 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 864 LNEMLKNLNQSMQ--------KSAENDKMLTQLREeaFAKEKQLlehDSVLRKKDDKIRELDAEFKRVKMEYVKLETKSF 935
Cdd:TIGR00606 534 RTQMEMLTKDKMDkdeqirkiKSRHSDELTSLLGY--FPNKKQL---EDWLHSKSKEINQTRDRLAKLNKELASLEQNKN 608
|
410
....*....|....*...
gi 32565309 936 HdvrkLNMDVEELKTQLS 953
Cdd:TIGR00606 609 H----INNELESKEEQLS 622
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
574-922 |
2.25e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 574 GAAAQRPEQPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRE--------LAEQKdhQIAQLTEQANDYQERL 645
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDhlnlvqtaLRQQE--KIERYQADLEELEERL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 646 EKSQSELQELARHVDSARAEL---------MDSQTSDYGRQQELMEKQA--------ELEQI--YVKIDNLTAENrdLTD 706
Cdd:PRK04863 365 EEQNEVVEEADEQQEENEARAeaaeeevdeLKSQLADYQQALDVQQTRAiqyqqavqALERAkqLCGLPDLTADN--AED 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 707 KIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEELEKEKSVAGsgnsggwsDIDDNEVVE-AVQPIETTPISSENSEN 785
Cdd:PRK04863 443 WLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAG--------EVSRSEAWDvARELLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 786 LKKFEAEIAELKASLEK---TEKELTKYRNLYNEKLTAISDKEnRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSD 862
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQqqrAERLLAEFCKRLGKNLDDEDELE-QLQEELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 32565309 863 RLNEmlknLNQSMQKSAENDKMLTQLRE---EAFAKE-------KQLLEHDSVLRKKDDKI----RELDAEFKR 922
Cdd:PRK04863 594 RIQR----LAARAPAWLAAQDALARLREqsgEEFEDSqdvteymQQLLERERELTVERDELaarkQALDEEIER 663
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
582-905 |
2.42e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 582 QPNYEPELLALRQQLAHLQSELQTAHAQRQEFEIHYHQIRELAEQKDHQIAQLTEQA-NDYQERLEKSQSELQEL---AR 657
Cdd:PRK04863 832 EADPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAdETLADRVEEIREQLDEAeeaKR 911
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 658 HVDSaraelmdsqtsdYGRQQElmekqaELEQIYVKIDNLTAENRDLTDKIAQLQvsdsleleeleelrnknlELQEQVK 737
Cdd:PRK04863 912 FVQQ------------HGNALA------QLEPIVSVLQSDPEQFEQLKQDYQQAQ------------------QTQRDAK 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 738 QLKEELekeKSVAGSGNSGGWSDiddnevveAVQpiettpISSENSENLKKfeaeiaeLKASLEKTEKELTKYRnlynEK 817
Cdd:PRK04863 956 QQAFAL---TEVVQRRAHFSYED--------AAE------MLAKNSDLNEK-------LRQRLEQAEQERTRAR----EQ 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 818 LTAISDK---ENRSQIEMEHKLKNAESDLQEAKRRAEEIG------AEKKELSDRlNEMLKNLNQSMQKSAENDKMLTQL 888
Cdd:PRK04863 1008 LRQAQAQlaqYNQVLASLKSSYDAKRQMLQELKQELQDLGvpadsgAEERARARR-DELHARLSANRSRRNQLEKQLTFC 1086
|
330
....*....|....*....
gi 32565309 889 REEAFAKEKQL--LEHDSV 905
Cdd:PRK04863 1087 EAEMDNLTKKLrkLERDYH 1105
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
782-933 |
2.46e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.06 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 782 NSENLKKFEAEIAELKAS----------LEKTEKELTKYRNLYNEKLTAISDKENRSQI-EMEHKLKNAESDLQEAKRRA 850
Cdd:COG4717 69 NLKELKELEEELKEAEEKeeeyaelqeeLEELEEELEELEAELEELREELEKLEKLLQLlPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 851 EEIGAEKKELSDRLNEMLKNLNQSMQKSAEndkMLTQLREEAFAKEKQLLEHDSVLRKKDDKIRELDAEFKRVKMEYVKL 930
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEE---LEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
...
gi 32565309 931 ETK 933
Cdd:COG4717 226 EEE 228
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
639-895 |
2.56e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 639 NDYQERLEKSQSELQELARHVDSaraelMDSQTSDYGRQQELMEKQA--ELEQIYVKIDNLTAENRDLTDKIAQLQvsDS 716
Cdd:PRK01156 472 NHYNEKKSRLEEKIREIEIEVKD-----IDEKIVDLKKRKEYLESEEinKSINEYNKIESARADLEDIKIKINELK--DK 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 717 LELEELEELRNKNLELqEQVKQLKEELEKEKSVAGSgnsggwSDIDD------------NEVVEAVQPIETT--PISSEN 782
Cdd:PRK01156 545 HDKYEEIKNRYKSLKL-EDLDSKRTSWLNALAVISL------IDIETnrsrsneikkqlNDLESRLQEIEIGfpDDKSYI 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 783 SENLKKFEAE----------IAELKASLEKTEKELTKYRNLYNEKLTAISD-KENRSQI-EMEHKLKNAESDLQEAKRRA 850
Cdd:PRK01156 618 DKSIREIENEannlnnkyneIQENKILIEKLRGKIDNYKKQIAEIDSIIPDlKEITSRInDIEDNLKKSRKALDDAKANR 697
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 32565309 851 EEIGAEKK-------ELSDRLNEMLKNLnQSMQKSAENDKMLTQLReEAFAK 895
Cdd:PRK01156 698 ARLESTIEilrtrinELSDRINDINETL-ESMKKIKKAIGDLKRLR-EAFDK 747
|
|
| LRRFIP |
pfam09738 |
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the ... |
731-794 |
3.05e-03 |
|
LRRFIP family; LRRFIP1 is a transcriptional repressor which preferentially binds to the GC-rich consensus sequence (5'- AGCCCCCGGCG-3') and may regulate expression of TNF, EGFR and PDGFA. LRRFIP2 may function as activator of the canonical Wnt signalling pathway, in association with DVL3, upstream of CTNNB1/beta-catenin.
Pssm-ID: 462869 [Multi-domain] Cd Length: 303 Bit Score: 40.84 E-value: 3.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32565309 731 ELQEQVKQLKEELEKEKSVA----GSGNSGGWSDIDDNEVVEAVQpiETTPISSENSENLKKFEAEIA 794
Cdd:pfam09738 237 ELLDEVRKLKLQLEEEKSKRnstrSSQSPDGFGLENGSHVIEVQR--EANKQISDYKFKLQKAEQEIT 302
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
600-935 |
3.57e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 41.60 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 600 QSELQTAHAQRQEFEIHYHQIRELAE---QKDHQIAQLT-EQANDYQERLEKSQSELQELARHVDSARAElmDSQTSDYG 675
Cdd:COG5022 874 AQRVELAERQLQELKIDVKSISSLKLvnlELESEIIELKkSLSSDLIENLEFKTELIARLKKLLNNIDLE--EGPSIEYV 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 676 RQ---QELMEKQAELEQIYVKIDNL----TAENRDLTDKIAQLQvsdsleleeleelrNKNLELQEQVKQLKEELEKEKS 748
Cdd:COG5022 952 KLpelNKLHEVESKLKETSEEYEDLlkksTILVREGNKANSELK--------------NFKKELAELSKQYGALQESTKQ 1017
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 749 VagsgnsggwsdiddNEVVEAVQPIET-TPISSENSENLKKFeAEIAELKASLEKTEKELTK-YRNLYNEKLTAISDKEN 826
Cdd:COG5022 1018 L--------------KELPVEVAELQSaSKIISSESTELSIL-KPLQKLKGLLLLENNQLQArYKALKLRRENSLLDDKQ 1082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 827 RSQIE-MEHKLKNAE-SDLQEAKRRAEE--------IGAEKK-----ELSDRLNEMLKNLNQSMQKSAENDKMLTQLREE 891
Cdd:COG5022 1083 LYQLEsTENLLKTINvKDLEVTNRNLVKpanvlqfiVAQMIKlnllqEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWE 1162
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 32565309 892 AFAKEKQLLEHDSVLRKK--------DDKIRELDAEFKRVKMEYVKLETKSF 935
Cdd:COG5022 1163 ANLEALPSPPPFAALSEKrlyqsalyDEKSKLSSSEVNDLKNELIALFSKIF 1214
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
554-759 |
3.69e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.97 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 554 KQLQLQLNAKITEIQNLQANGAAAQRpEQPNYEPELLALRQQLAHLQSEL--QTAHAQRQEFEIHYhqIRELAEQKD--- 628
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQA-EIDKLQAEIAEAEAEIEERREELgeRARALYRSGGSVSY--LDVLLGSESfsd 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 629 -----HQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELMDSQTSDYGRQQELMEKQAELEQiyvKIDNLTAENRD 703
Cdd:COG3883 117 fldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA---LLAQLSAEEAA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 32565309 704 LTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEELEKEKSVAGSGNSGGWS 759
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGA 249
|
|
| DUF4201 |
pfam13870 |
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. ... |
830-933 |
4.09e-03 |
|
Domain of unknown function (DUF4201); This is a family of coiled-coil proteins from eukaryotes. The function is not known.
Pssm-ID: 464008 [Multi-domain] Cd Length: 177 Bit Score: 39.51 E-value: 4.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 830 IEMEHKLKnaesDLQEAKRRAEEIG------------AEKKELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEAFAKEK 897
Cdd:pfam13870 16 ITLKHTLA----KIQEKLEQKEELGegltmidflqlqIENQALNEKIEERNKELKRLKLKVTNTVHALTHLKEKLHFLSA 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 32565309 898 QLLEHDSVLRKKDDKIRELDAEFKRVKMEYVKLETK 933
Cdd:pfam13870 92 ELSRLKKELRERQELLAKLRKELYRVKLERDKLRKQ 127
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
618-852 |
4.11e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 618 HQIRELAEQKDHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAELmdsqtsdygRQQELMEKQAELEQIYVKIDNL 697
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELL---------REAEELEEELQLEELEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 698 taenrdltdkIAQLQVSDSLELEELEELRNKNLELQEQVKQLKEELEKeksvAGSGNSGGWSDIDDNEVVEAVQPIETTp 777
Cdd:COG4717 376 ----------LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE----LLGELEELLEALDEEELEEELEELEEE- 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 32565309 778 iSSENSENLKKFEAEIAELKASLEKTEKElTKYRNLYNEKLTAISDKENRSQIEMEHKLknAESDLQEAKRRAEE 852
Cdd:COG4717 441 -LEELEEELEELREELAELEAELEQLEED-GELAELLQELEELKAELRELAEEWAALKL--ALELLEEAREEYRE 511
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
620-842 |
4.42e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.07 E-value: 4.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 620 IRELAEQKDHQIAQLTEQanDYQERLEKSQSELQELARHVDSARaELMDSQTSDYGRQQELMEKQAE---------LEQI 690
Cdd:PRK05771 22 LEALHELGVVHIEDLKEE--LSNERLRKLRSLLTKLSEALDKLR-SYLPKLNPLREEKKKVSVKSLEelikdveeeLEKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 691 YVKIDNLTAENRDLTDKIAQLQvsdsLELEELEELRNKNLELQ-----------------EQVKQLKEELEKEKSVAGSG 753
Cdd:PRK05771 99 EKEIKELEEEISELENEIKELE----QEIERLEPWGNFDLDLSlllgfkyvsvfvgtvpeDKLEELKLESDVENVEYIST 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 754 NSGG-----WSDIDDNEVVEAV------QPIETtPISSENSENLKKFEAEIAELKASLEKTEKELTKYRNLYNEKLTAIS 822
Cdd:PRK05771 175 DKGYvyvvvVVLKELSDEVEEElkklgfERLEL-EEEGTPSELIREIKEELEEIEKERESLLEELKELAKKYLEELLALY 253
|
250 260
....*....|....*....|.
gi 32565309 823 DK-ENRSQiEMEHKLKNAESD 842
Cdd:PRK05771 254 EYlEIELE-RAEALSKFLKTD 273
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
629-922 |
5.04e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 40.97 E-value: 5.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 629 HQIAQLTEQANDYQERLEKSQSELQEL-------ARHVDSARAELMDSQTS------DYGRQQELMEKQ-AELEQIYVKI 694
Cdd:PRK04778 105 HEINEIESLLDLIEEDIEQILEELQELleseeknREEVEQLKDLYRELRKSllanrfSFGPALDELEKQlENLEEEFSQF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 695 DNLTAEN-------------------RDLTDKI----AQLQVsdsleleeleelrnknlELQEQVKQLKE---ELEKEKS 748
Cdd:PRK04778 185 VELTESGdyveareildqleeelaalEQIMEEIpellKELQT-----------------ELPDQLQELKAgyrELVEEGY 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 749 VagsgnsggwsdIDDNEVVEAVQPIEttpissensENLKKFEAEIAELKasLEKTEKELTKyrnlYNEKLTAISD---KE 825
Cdd:PRK04778 248 H-----------LDHLDIEKEIQDLK---------EQIDENLALLEELD--LDEAEEKNEE----IQERIDQLYDileRE 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 826 NRSQIEMEHKLKNAESDLQEAKRRAEEIGAE-----------------KKELSDRLNEMLKNLNQSMQKSAENDKMLTQL 888
Cdd:PRK04778 302 VKARKYVEKNSDTLPDFLEHAKEQNKELKEEidrvkqsytlneselesVRQLEKQLESLEKQYDEITERIAEQEIAYSEL 381
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 32565309 889 REEAFAKEKQL----LEHDSV------LRKKDDKIRELDAEFKR 922
Cdd:PRK04778 382 QEELEEILKQLeeieKEQEKLsemlqgLRKDELEAREKLERYRN 425
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
603-870 |
5.15e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 41.05 E-value: 5.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 603 LQTAHAQRQEFEiHYHQIRELAEQKDHQIAQLtEQANDYQERLEKSQSELQELarhvdsaraELMDSQTSDYGRQQELME 682
Cdd:COG4913 224 FEAADALVEHFD-DLERAHEALEDAREQIELL-EPIRELAERYAAARERLAEL---------EYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 683 KQAELEQIYVKIDNLTAENRDLTDKIAqlqvsdsleleeleelrnknlELQEQVKQLKEELEkeksvagsgNSGGwsdid 762
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLD---------------------ALREELDELEAQIR---------GNGG----- 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 763 dnevveavqpiettpissensENLKKFEAEIAELKASLEKTEKELTKYrnlyNE-----KLTAISD----KENRSQI--- 830
Cdd:COG4913 338 ---------------------DRLEQLEREIERLERELEERERRRARL----EAllaalGLPLPASaeefAALRAEAaal 392
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 32565309 831 --EMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKN 870
Cdd:COG4913 393 leALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
778-953 |
5.69e-03 |
|
Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.
Pssm-ID: 464001 [Multi-domain] Cd Length: 200 Bit Score: 39.50 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 778 ISSENSENLKKFEAEIAELKASLEKTEKELTKYrnlynekltaisDKENRSQIEmehKLKNAESDLQEAKRRAEEIGAEK 857
Cdd:pfam13851 20 ITRNNLELIKSLKEEIAELKKKEERNEKLMSEI------------QQENKRLTE---PLQKAQEEVEELRKQLENYEKDK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 858 KELsDRLNEMLKNLNQSMQKSAENDKMLTQlreeafAKEKQLLEHDSVLRKKDDKIRELdaeFKRVKMEYVKLETKsfhd 937
Cdd:pfam13851 85 QSL-KNLKARLKVLEKELKDLKWEHEVLEQ------RFEKVERERDELYDKFEAAIQDV---QQKTGLKNLLLEKK---- 150
|
170
....*....|....*.
gi 32565309 938 VRKLNMDVEELKTQLS 953
Cdd:pfam13851 151 LQALGETLEKKEAQLN 166
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
543-713 |
6.56e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 40.52 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 543 RQAHFDLMNKHKQLQLQLNAKitEIQNLQANGAAAQRpeqpnyepellalrQQLAHLQSELQTAHAQRQEFEIHYHQIRE 622
Cdd:COG4717 350 QELLREAEELEEELQLEELEQ--EIAALLAEAGVEDE--------------EELRAALEQAEEYQELKEELEELEEQLEE 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 623 LAEQKDHQIAQLTEQanDYQERLEKSQSELQELARHVDSARAELMDSQTsdygrQQELMEKQAELEQIYVKIDNLTAENR 702
Cdd:COG4717 414 LLGELEELLEALDEE--ELEEELEELEEELEELEEELEELREELAELEA-----ELEQLEEDGELAELLQELEELKAELR 486
|
170
....*....|.
gi 32565309 703 DLTDKIAQLQV 713
Cdd:COG4717 487 ELAEEWAALKL 497
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
586-956 |
7.45e-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: 40.54 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 586 EPELLALRQQLAHLQSELQTAHAQRQEfeiHYHQIRELAeqkdHQIAQLTEQANDYQERLEKSQSELQELARHVDSARAE 665
Cdd:pfam01576 453 EGKNIKLSKDVSSLESQLQDTQELLQE---ETRQKLNLS----TRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQ 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 666 LMDS--QTSDYGRQQELMEK-----QAELEQIYVKIDNLTAENRDLTDKIAQLQVSDSLELEELEELRNKNLELQEQVKQ 738
Cdd:pfam01576 526 LSDMkkKLEEDAGTLEALEEgkkrlQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKK 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 739 LKEELEKEKSVagsgnSGGWSDIDDNEVVEAVQPiETTPISsensenLKKFEAEIAELKASLEKTEKELtkyrNLYNEKL 818
Cdd:pfam01576 606 FDQMLAEEKAI-----SARYAEERDRAEAEAREK-ETRALS------LARALEEALEAKEELERTNKQL----RAEMEDL 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 819 TAISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEMLKNLnQSMQKSAENDkmlTQLREEAF-AKEK 897
Cdd:pfam01576 670 VSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNM-QALKAQFERD---LQARDEQGeEKRR 745
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 32565309 898 QLLEhdsvlrkkddKIRELDAEFKrvkmEYVKLETKSFHDVRKLNMDVEELKTQLSMAG 956
Cdd:pfam01576 746 QLVK----------QVRELEAELE----DERKQRAQAVAAKKKLELDLKELEAQIDAAN 790
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
783-924 |
7.55e-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: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 783 SENLKKFEAEIAELkasLEKTEKELTKYRNLYNEKLTAISDKENRSQIEMEhKLKNAESDLQ-----EAKRRAEEIGAEK 857
Cdd:smart00787 142 LEGLKEGLDENLEG---LKEDYKLLMKELELLNSIKPKLRDRKDALEEELR-QLKQLEDELEdcdptELDRAKEKLKKLL 217
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 858 KEL---SDRLNEMLKNLNQSMQKSAENDKMLTQLREEAFAKEKQLLEHDSVLRKkddKIRELDAEFKRVK 924
Cdd:smart00787 218 QEImikVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK---EIEKLKEQLKLLQ 284
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
783-927 |
8.00e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 38.77 E-value: 8.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 783 SENLKKFEAEIaelkasLEKTEKELTKYRNLYNEKLTAI-SDKENRSQIEMEHKLKNAESDLQEAKRRAE---------E 852
Cdd:COG1390 1 MMSLEKIIEEI------LEEAEAEAEEILEEAEEEAEKIlEEAEEEAEEIKEEILEKAEREAEREKRRIIssaelearkE 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 32565309 853 IGAEKKELSDRLNEMLKNLNQSMQKSAENDKMLTQLREEAfakEKQLLEHDSV--LRKKD-DKIRELDAEFKRVKMEY 927
Cdd:COG1390 75 LLEAKEELIEEVFEEALEKLKNLPKDPEYKELLKKLLKEA---AEELGSGDLVvyVNEKDkELLEELLKELKKKGLEV 149
|
|
| SKA2 |
pfam16740 |
Spindle and kinetochore-associated protein 2; Spindle and kinetochore-associated protein 2 ... |
790-899 |
8.72e-03 |
|
Spindle and kinetochore-associated protein 2; Spindle and kinetochore-associated protein 2 (SKA2) interacts with the N-termini of SKA1 and SKA3 and forms the Ska complex. This is a microtubule binding complex required for chromosome segregation.
Pssm-ID: 465252 Cd Length: 110 Bit Score: 37.22 E-value: 8.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 790 EAEIAELKASLEKTEKELTKYRNLYNEKLTAISDKENRSQIEMEHKLKNAESDLQEAKRRAEEIGAEKKELSDRLNEML- 868
Cdd:pfam16740 1 EQAVDGLEAMFQKAESDLDYVQHRLDYEFQQSYPDNAENPVKLLERLKKVKSEYQALKEQCQELLAEKQELVDSIRTQLv 80
|
90 100 110
....*....|....*....|....*....|...
gi 32565309 869 --KNLNQSMQKSAEndkmLTQLREEAFAKEKQL 899
Cdd:pfam16740 81 anRNLLQRLQASAG----LPPLTEEEQAAAANL 109
|
|
| IFT57 |
pfam10498 |
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ... |
537-654 |
9.64e-03 |
|
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.
Pssm-ID: 463118 [Multi-domain] Cd Length: 360 Bit Score: 39.55 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 32565309 537 ESDILDRQAHFDLMNKHK--------QLQLQLNAKITEIQNlqANGAAAQRpEQpnyepellALRQQLAHLQSELQTAHA 608
Cdd:pfam10498 214 KADAKDWRAHLEQMKQHKksieeslpDTKSQLDKLHTDISK--TLEKIESR-EK--------YINSQLEPLIQEYREAQD 282
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 32565309 609 QRQEFEIHYHQIRElaeqkdhQIAQLTEQANDYQERLEKSQSELQE 654
Cdd:pfam10498 283 ELSEVQEKYKQLSE-------GVTERTRELAEITEELEKVKQEMEE 321
|
|
| |
