|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
865-1139 |
1.53e-14 |
|
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: 78.95 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 865 ILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTAST----TCEKLEKARNELQTVyEAFVQ 940
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQL-EERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 941 QHQAEKTERENRLKEfYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAY---EASLS 1017
Cdd:TIGR02168 751 QLSKELTELEAEIEE-LEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAanlRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1018 EIKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSENDALNEKLKSEEQKRRArekanlknpqimyLEQELESLKA 1091
Cdd:TIGR02168 828 SLERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELIEELESELEALLNERAS-------------LEEALALLRS 894
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1386876323 1092 VLEIKNEKLHQQDIKLMKMEKLVDnntALVDKLKRFQQENEELKARMD 1139
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELE---ELREKLAQLELRLEGLEVRID 939
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
889-1142 |
2.63e-12 |
|
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: 71.63 E-value: 2.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 889 LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQ---------QHQAEKTERENRLKEFYTR 959
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrleqqkQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 960 EYEKL---RDTYIEEA---EKYKMQLQEQFDNLNAAHETSKLEIEASHSeKLELLKKAYEASLSEIkkgHEIEKKslEDL 1033
Cdd:TIGR02168 324 QLEELeskLDELAEELaelEEKLEELKEELESLEAELEELEAELEELES-RLEELEEQLETLRSKV---AQLELQ--IAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1034 LSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKL 1113
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260
....*....|....*....|....*....
gi 1386876323 1114 VDnntALVDKLKRFQQENEELKARMDKHM 1142
Cdd:TIGR02168 477 LD---AAERELAQLQARLDSLERLQENLE 502
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
892-1137 |
1.56e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.20 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 892 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFY--TREYEKLRDTYI 969
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYelLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 970 EEAEKyKMQLQEQFDNLNAAHETSKLEIEASHSEKLELlkkayEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLK 1049
Cdd:COG1196 306 RLEER-RRELEERLEELEEELAELEEELEELEEELEEL-----EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1050 SENDALNEKLksEEQKRRAREKANLKNPQIMyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQ 1129
Cdd:COG1196 380 ELEELAEELL--EALRAAAELAAQLEELEEA-EEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
|
....*...
gi 1386876323 1130 ENEELKAR 1137
Cdd:COG1196 457 EEEALLEL 464
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
867-1139 |
4.82e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 867 QLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN---ELQTVYEAFVQQHQ 943
Cdd:COG1196 243 ELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIArleERRRELEERLEELE 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 944 AEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAhetsKLEIEASHSEKLELLKKAYEASLSEIKKgh 1023
Cdd:COG1196 323 EELAELEEELEELEEELEELEEE--LEEAEEELEEAEAELAEAEEA----LLEAEAELAEAEEELEELAEELLEALRA-- 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1024 EIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpqimyLEQELESLKAVLEIKNEKLHQQ 1103
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE------AAEEEAELEEEEEALLELLAEL 468
|
250 260 270
....*....|....*....|....*....|....*.
gi 1386876323 1104 DIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMD 1139
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYE 504
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
865-1140 |
1.72e-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: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 865 ILQLKQLLAcgntKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTvyEAFVQQHQA 944
Cdd:COG1196 224 ELEAELLLL----KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQA--EEYELLAEL 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 945 EKTEREnrlkefytREYEKLRdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASLSEIKKGHE 1024
Cdd:COG1196 298 ARLEQD--------IARLEER---RRELEERLEELEEELAELEEELEELEEELEEL-EEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1025 IEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEE----QKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKL 1100
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEEleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1386876323 1101 HQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDK 1140
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE 485
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
886-1141 |
4.10e-10 |
|
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: 64.31 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 886 IQHLLSEREEALKqHKTLSQELVNLRGELVTASTtcEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEfytreyeklr 965
Cdd:TIGR02168 202 LKSLERQAEKAER-YKELKAELRELELALLVLRL--EELREELEELQEELKEAEEELEELTAELQELEEK---------- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 966 dtyIEEAEKYKMQLQEQFD-----NLNAAHETSKLEIE-ASHSEKLELLKKAYEASLSEIKkgheiEKKSLEDLLSEKQE 1039
Cdd:TIGR02168 269 ---LEELRLEVSELEEEIEelqkeLYALANEISRLEQQkQILRERLANLERQLEELEAQLE-----ELESKLDELAEELA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1040 SLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpqimyLEQELESLK-AVLEIKNE-KLHQQDIKLMKMEKlvdnn 1117
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEE------LEEQLETLRsKVAQLELQiASLNNEIERLEARL----- 409
|
250 260
....*....|....*....|....
gi 1386876323 1118 TALVDKLKRFQQENEELKARMDKH 1141
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEA 433
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1134 |
5.36e-10 |
|
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: 63.93 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 862 SGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEK---ARNELQTVYEAF 938
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeeKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 939 VQQHQAEKTERENRLKEFYTReyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSE 1018
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEAR---------IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1019 IKKghEIEKKSLED--LLSEKQES------LEKQINDLKSENDALN---EKLKSEEQKRRA-------------REKANL 1074
Cdd:TIGR02169 817 IEQ--KLNRLTLEKeyLEKEIQELqeqridLKEQIKSIEKEIENLNgkkEELEEELEELEAalrdlesrlgdlkKERDEL 894
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1075 KNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLmkmEKLVDNNTALVDKLKRFQQENEEL 1134
Cdd:TIGR02169 895 EA-QLRELERKIEELEAQIEKKRKRLSELKAKL---EALEEELSEIEDPKGEDEEIPEEE 950
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
922-1140 |
1.39e-09 |
|
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: 62.68 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHetSKLEIEASH 1001
Cdd:TIGR00618 127 ETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMN--LFPLDQYTQLALMEFAKKKSLH--GKAELLTLR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1002 SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKqindLKSENDALNEKLKSEEQKRRAREKanlknpqimy 1081
Cdd:TIGR00618 203 SQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY----LTQKREAQEEQLKKQQLLKQLRAR---------- 268
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1386876323 1082 lEQELESLKAVLEIKNEKLHQQdiklMKMEKLVDNNTALVDKLKRFQQENEELKARMDK 1140
Cdd:TIGR00618 269 -IEELRAQEAVLEETQERINRA----RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRS 322
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
811-1133 |
1.60e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 811 RKNLFTALNAVEKSRQKNPrsLCIQPQTAPDalppEKTLeLTQYKTKCENQSGFILQLKQLLacgnTKFEALTVVIQHLL 890
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCP--VCGRELTEEH----RKEL-LEEYTAELKRIEKELKEIEEKE----RKLRKELRELEKVL 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 891 SEREEALKQHKTLSQeLVNLRGELvtASTTCEKLEKARNELQTVYEAFVQQhQAEKTERENRLKEFytREYEKLRdtyiE 970
Cdd:PRK03918 490 KKESELIKLKELAEQ-LKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKL-KGEIKSLKKELEKL--EELKKKL----A 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 971 EAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEA--SLSEIKKGHEIEKKSLEDL---LSEKQESLEKQI 1045
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLeeeLDKAFEELAETE 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1046 NDLKSENDALNEKLK--SEEQKRRAREKANLKNPQIMYLEQELESLKAVLE--------IKNEK--LHQQDIKLMKMEKL 1113
Cdd:PRK03918 640 KRLEELRKELEELEKkySEEEYEELREEYLELSRELAGLRAELEELEKRREeikktlekLKEELeeREKAKKELEKLEKA 719
|
330 340
....*....|....*....|
gi 1386876323 1114 VDNNTALVDKLKRFQQENEE 1133
Cdd:PRK03918 720 LERVEELREKVKKYKALLKE 739
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
940-1140 |
2.12e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 940 QQHQAEKTERENRLK----EFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYE-- 1013
Cdd:COG1196 216 RELKEELKELEAELLllklRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYEll 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1014 ASLSEIKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpqimyLEQELE 1087
Cdd:COG1196 295 AELARLEQDIARLEERRRELeerleeLEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE------AEEALL 368
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1386876323 1088 SLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDK 1140
Cdd:COG1196 369 EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
885-1159 |
5.93e-09 |
|
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: 60.52 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 885 VIQH--LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYE---AFVQQHQAEKTERENRL----KE 955
Cdd:pfam17380 277 IVQHqkAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaAIYAEQERMAMERERELerirQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 956 FYTREYEKLRD-------TYIEEAEKYKMQLQEQFD----NLNAAHETSKLE------IEASHSEKLELLKKAYEASLSE 1018
Cdd:pfam17380 357 ERKRELERIRQeeiameiSRMRELERLQMERQQKNErvrqELEAARKVKILEeerqrkIQQQKVEMEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1019 IKKGHEIEKKSLEDLLSEKQESlEKQINDLKSENDalNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-AVLEIKN 1097
Cdd:pfam17380 437 VRRLEEERAREMERVRLEEQER-QQQVERLRQQEE--ERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqAMIEEER 513
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876323 1098 E-KLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKaRMDKHMAISSFPRSRLFCKSRWR 1159
Cdd:pfam17380 514 KrKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR-RIQEQMRKATEERSRLEAMERER 575
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
846-1135 |
8.75e-09 |
|
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: 60.03 E-value: 8.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 846 EKTLELTQYKTKCENQSGFILQLK-QLLACGNTKFEALTVVIQHLLSEREEALKQHKT-----------LSQELVNLRGE 913
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNqisqnnkiisqLNEQISQLKKE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 914 LVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTEREN--------RLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDN 985
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlesqindlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 986 LNAAHETSKLEIEASHSE---------KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSE------KQESLEKQINDLKS 1050
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQdsvkeliikNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekELKKLNEEKKELEE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1051 ENDALNEKLKSEEQKRRAREKA-NLKNPQIMYLEQELESLKAVL---EIKNEKLH-QQDIKLMKMEK--LVDNNTALVDK 1123
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEkKEKESKISDLEDELNKDDFELkkeNLEKEIDEkNKEIEELKQTQksLKKKQEEKQEL 590
|
330
....*....|..
gi 1386876323 1124 LKRFQQENEELK 1135
Cdd:TIGR04523 591 IDQKEKEKKDLI 602
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
877-1140 |
9.93e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 877 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELvtasttcEKLEKARNELQTVyeafvqqhQAEKTERENRLKEF 956
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL-------EELEERHELYEEA--------KAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 957 YTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAahETSKLEIEASHSEK-LELLKKAYE------ASLSEIKKGHEIEKKS 1029
Cdd:PRK03918 382 TGLTPEKLEKE-LEELEKAKEEIEEEISKITA--RIGELKKEIKELKKaIEELKKAKGkcpvcgRELTEEHRKELLEEYT 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1030 LE--DLLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKANlknpQIMYLEQELESLKAV-LEIKNEKLHQQDIK 1106
Cdd:PRK03918 459 AElkRIEKELKE-IEEKERKLRKELRELEKVLKKESELIKLKELAE----QLKELEEKLKKYNLEeLEKKAEEYEKLKEK 533
|
250 260 270
....*....|....*....|....*....|....
gi 1386876323 1107 LMKMEKLVDNNTALVDKLKRFQQENEELKARMDK 1140
Cdd:PRK03918 534 LIKLKGEIKSLKKELEKLEELKKKLAELEKKLDE 567
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
922-1143 |
1.12e-08 |
|
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: 59.70 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTVYE--AFVQQHQAEKTERENRLKEfytreyEKlrdtyiEEAEKY-----KMQLQEQFDNLNA--AHET 992
Cdd:TIGR02169 170 RKKEKALEELEEVEEniERLDLIIDEKRQQLERLRR------ER------EKAERYqallkEKREYEGYELLKEkeALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 993 SKLEIEASHSEKLELLKKaYEASLSEI-KKGHEIEK------KSLEDLLSEKQESLEKQINDLKSENDAL--NEKLKSEE 1063
Cdd:TIGR02169 238 QKEAIERQLASLEEELEK-LTEEISELeKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGELEAEIASLerSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1064 QKRRAREKANlknpqimyLEQELESLKAVLEIKNEKLHQQDIKLMK-MEKLVDNNTALVDKLKRFQQENEELKARMDKHM 1142
Cdd:TIGR02169 317 LEDAEERLAK--------LEAEIDKLLAEIEELEREIEEERKRRDKlTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
.
gi 1386876323 1143 A 1143
Cdd:TIGR02169 389 D 389
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
886-1047 |
3.00e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 55.70 E-value: 3.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 886 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVY---EAFVQQHQAEKTERENRL------KEF 956
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLgnvrnnKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 957 --YTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAsHSEKLELLKKAYEASLSEIKKghEIEKksledlL 1034
Cdd:COG1579 92 eaLQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAE-LEAELEEKKAELDEELAELEA--ELEE------L 161
|
170
....*....|...
gi 1386876323 1035 SEKQESLEKQIND 1047
Cdd:COG1579 162 EAEREELAAKIPP 174
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
850-1095 |
3.21e-08 |
|
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: 58.14 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 850 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 929
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 930 ELQTVYEAF---VQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1006
Cdd:TIGR02168 863 ELEELIEELeseLEALLNERASLEEALALL-RSELEELSEE-LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1007 LLKKA---YEASLSEIKKgHEIEKKSLEDLLSEKQESLEKQINDLKSEN-DALNEklkSEEQKRRAREKANlknpQIMYL 1082
Cdd:TIGR02168 941 LQERLseeYSLTLEEAEA-LENKIEDDEEEARRRLKRLENKIKELGPVNlAAIEE---YEELKERYDFLTA----QKEDL 1012
|
250
....*....|....
gi 1386876323 1083 EQELESL-KAVLEI 1095
Cdd:TIGR02168 1013 TEAKETLeEAIEEI 1026
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
849-1131 |
3.29e-08 |
|
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: 58.19 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 849 LELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKA- 927
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQi 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 928 ----------RNELQTVYEAFVQQH-----QAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHET 992
Cdd:pfam05483 537 enleekemnlRDELESVREEFIQKGdevkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 993 SKLEIEASHSE------------KLEL----LKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES---------LEKQInD 1047
Cdd:pfam05483 617 NKALKKKGSAEnkqlnayeikvnKLELelasAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavkLQKEI-D 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1048 LK-----SENDALNEKLKSEEQK---RRAREKANLKNPqimylEQELESLKAVLEIKNEKLHQQdikLMKMEKLVDNNTA 1119
Cdd:pfam05483 696 KRcqhkiAEMVALMEKHKHQYDKiieERDSELGLYKNK-----EQEQSSAKAALEIELSNIKAE---LLSLKKQLEIEKE 767
|
330
....*....|..
gi 1386876323 1120 LVDKLKRFQQEN 1131
Cdd:pfam05483 768 EKEKLKMEAKEN 779
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
925-1147 |
4.58e-08 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 57.33 E-value: 4.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 925 EKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEK----YKMQ------------LQEQFDNLNA 988
Cdd:COG3206 148 ELAAAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKE-LEEAEAaleeFRQKnglvdlseeaklLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 989 AHETSKLEIEA--SHSEKLELLKKAYEASLSEIKKGHEIE--KKSLEDLLSEKQESLEK------QINDLKSENDALNEK 1058
Cdd:COG3206 227 QLAEARAELAEaeARLAALRAQLGSGPDALPELLQSPVIQqlRAQLAELEAELAELSARytpnhpDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1059 LKSEEQKRRAREKANLKNPQIMylEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDK-LKRFQQeneelkAR 1137
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAR--EASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESlLQRLEE------AR 378
|
250
....*....|
gi 1386876323 1138 MDKHMAISSF 1147
Cdd:COG3206 379 LAEALTVGNV 388
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
886-1116 |
4.85e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 56.83 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 886 IQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVYEAfVQQHQAEKTERENRLKEFYtREYEKLR 965
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQAR---SELEQLEEELEELNEQ-LQAAQAELAQAQEELESLQ-EEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 966 DTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIeASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQI 1045
Cdd:COG4372 115 EE-LEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876323 1046 ND--LKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1116
Cdd:COG4372 193 NRnaEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
922-1143 |
7.40e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 55.70 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTVYEAFVQQH----------QAEKTERENR-LKEFYTREYEKLRDTYIEEAEKyKMQLQEQFDNLNAAH 990
Cdd:pfam13868 61 EEKEEERKEERKRYRQELEEQieereqkrqeEYEEKLQEREqMDEIVERIQEEDQAEAEEKLEK-QRQLREEIDEFNEEQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 991 ETSK-LEIEAshsEKLELLK-KAYEASLSEIKKGHEIEKKSLE---DLLSEKQESLEKQINDLKSENDALNEKLKSEEQK 1065
Cdd:pfam13868 140 AEWKeLEKEE---EREEDERiLEYLKEKAEREEEREAEREEIEeekEREIARLRAQQEKAQDEKAERDELRAKLYQEEQE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1066 RRAREKAnlknpqimyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKR--------FQQENEELKAR 1137
Cdd:pfam13868 217 RKERQKE---------REEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRkqaedeeiEQEEAEKRRMK 287
|
....*.
gi 1386876323 1138 MDKHMA 1143
Cdd:pfam13868 288 RLEHRR 293
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
890-1082 |
8.18e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 56.70 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 890 LSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA-----EKTERENRLKEFyTREYEKL 964
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAEL-PERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 965 RdtyiEEAEKYKmQLQEQFDNLNAAHETSKLEIEashsEKLELLKKAYEASLSEIKKghEIEKksledlLSEKQESLEKQ 1044
Cdd:COG4717 152 E----ERLEELR-ELEEELEELEAELAELQEELE----ELLEQLSLATEEELQDLAE--ELEE------LQQRLAELEEE 214
|
170 180 190
....*....|....*....|....*....|....*....
gi 1386876323 1045 INDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYL 1082
Cdd:COG4717 215 LEEAQEELEELEEELEQlENELEAAALEERLKEARLLLL 253
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
884-1140 |
8.79e-08 |
|
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: 56.90 E-value: 8.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 884 VVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYeafvQQHQAEKTERENRLKEFYTREYEK 963
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY----QLKEKLELEEEYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 964 LRDTYIE----EAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQE 1039
Cdd:pfam02463 238 RIDLLQEllrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1040 SLEKQINDLKSENDAL----NEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIK------LMK 1109
Cdd:pfam02463 318 ESEKEKKKAEKELKKEkeeiEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSaaklkeEEL 397
|
250 260 270
....*....|....*....|....*....|.
gi 1386876323 1110 MEKLVDNNTALvDKLKRFQQENEELKARMDK 1140
Cdd:pfam02463 398 ELKSEEEKEAQ-LLLELARQLEDLLKEEKKE 427
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
867-1072 |
1.11e-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: 55.54 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 867 QLKQLlacgNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEK 946
Cdd:COG4942 28 ELEQL----QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 947 TERENRLKEFYT---REYEKL------------RDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLK-- 1009
Cdd:COG4942 104 EELAELLRALYRlgrQPPLALllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAel 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876323 1010 KAYEASLSEIKKgheiEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1072
Cdd:COG4942 184 EEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
878-1135 |
1.75e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 878 KFEALTVVIQHLLSERE----EALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvqQHQAEKTERENRL 953
Cdd:PRK03918 183 KFIKRTENIEELIKEKEkeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIE--------ELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 954 KefytREYEKLRDT--YIEEAEKYKMQLQEQfdnlnaAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIekksle 1031
Cdd:PRK03918 255 R----KLEEKIRELeeRIEELKKEIEELEEK------VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1032 dlLSEKQESLEKQINDLKSENDALNEKLKSEEqkrrarekanlknpqimyleqELESLKAVLEIKNEKLHQQDIKLMKME 1111
Cdd:PRK03918 319 --LEEEINGIEERIKELEEKEERLEELKKKLK---------------------ELEKRLEELEERHELYEEAKAKKEELE 375
|
250 260
....*....|....*....|....*
gi 1386876323 1112 KLVDNNTAL-VDKLKRFQQENEELK 1135
Cdd:PRK03918 376 RLKKRLTGLtPEKLEKELEELEKAK 400
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
886-1134 |
2.38e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 886 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQ---AEKTERENRLKEFYTREYE 962
Cdd:TIGR04523 372 IEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIErlkETIIKNNSEIKDLTNQDSV 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 963 KlrDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShseKLELLKKAYE-ASLSEIKKGHEIEKKSLED---LLSEKQ 1038
Cdd:TIGR04523 452 K--ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK---QKELKSKEKElKKLNEEKKELEEKVKDLTKkisSLKEKI 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1039 ESLEKQINDLKSENDALNEKLKSEEQ---KRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVD 1115
Cdd:TIGR04523 527 EKLESEKKEKESKISDLEDELNKDDFelkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIE 606
|
250 260
....*....|....*....|...
gi 1386876323 1116 NNTALVDKLKR----FQQENEEL 1134
Cdd:TIGR04523 607 EKEKKISSLEKelekAKKENEKL 629
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
849-1135 |
2.55e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 55.03 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 849 LELTQYKTKCENQsgfILQLKQLLACGNTKFEALtvviQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKAR 928
Cdd:TIGR04523 169 EELENELNLLEKE---KLNIQKNIDKIKNKLLKL----ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEI 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 929 NELQTVYEAFVQQHQAEKTERENRLKEFYTREYEklrdtyIEEAEKYKMQLQEQFDNLNAahetsklEIEASHSEKLELL 1008
Cdd:TIGR04523 242 NEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE------LEQNNKKIKELEKQLNQLKS-------EISDLNNQKEQDW 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1009 KKAYEASLSEIKKGHEIEKKSLE------DLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANL-KNPQIMY 1081
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISqnnkiiSQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQsYKQEIKN 388
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1386876323 1082 LEQELESLKAVLEIKNEKLHQQDIKLMKMEKlvdNNTALVDKLKRFQQENEELK 1135
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDEQIKKLQQ---EKELLEKEIERLKETIIKNN 439
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
887-1139 |
2.68e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 55.18 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 887 QHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvqqhqAEKTERENRLKEFYTREYEKLRD 966
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLA-----------ARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 967 TYIEEAEKYKMQ-----LQEQFDNLNAAHEtsKLEIEASHSE----KLELLKKAYEASLSEIKKgheiEKKSLEDLLSE- 1036
Cdd:pfam01576 91 SQQLQNEKKKMQqhiqdLEEQLDEEEAARQ--KLQLEKVTTEakikKLEEDILLLEDQNSKLSK----ERKLLEERISEf 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1037 -----KQESLEKQINDLKSENDA----LNEKLKSEEQKRRAREKANLK--------NPQIMYLEQELESLKAVLEIKNEK 1099
Cdd:pfam01576 165 tsnlaEEEEKAKSLSKLKNKHEAmisdLEERLKKEEKGRQELEKAKRKlegestdlQEQIAELQAQIAELRAQLAKKEEE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1386876323 1100 LHQqdiKLMKMEKLVDNNTALVDKLKRFQQENEELKARMD 1139
Cdd:pfam01576 245 LQA---ALARLEEETAQKNNALKKIRELEAQISELQEDLE 281
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
885-1134 |
6.11e-07 |
|
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: 54.20 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 885 VIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARnelqtvyeaFVQQHQAEKTERENRLKEF-YTREYEK 963
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE---------LLASRQLALQKMQSEKEQLtYWKEMLA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 964 LRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQ--ESL 1041
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgAEL 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1042 EKQINDLKSENDALNE-----KLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1116
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEdthllKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
250
....*....|....*...
gi 1386876323 1117 NTALVDKLKRFQQENEEL 1134
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDKL 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
922-1108 |
7.54e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 7.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTVYEAFvqqhqAEKTERENRLKEfytrEYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIE-AS 1000
Cdd:COG4717 74 KELEEELKEAEEKEEEY-----AELQEELEELEE----ELEELEAE-LEELREELEKLEKLLQLLPLYQELEALEAElAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1001 HSEKLELLKKAYEA------SLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanl 1074
Cdd:COG4717 144 LPERLEELEERLEElreleeELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE--- 220
|
170 180 190
....*....|....*....|....*....|....*.
gi 1386876323 1075 knpQIMYLEQELESLKAVLEI--KNEKLHQQDIKLM 1108
Cdd:COG4717 221 ---ELEELEEELEQLENELEAaaLEERLKEARLLLL 253
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
969-1129 |
1.05e-06 |
|
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.
Pssm-ID: 439154 [Multi-domain] Cd Length: 309 Bit Score: 51.99 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 969 IEEAEKYKMQLQEQFDNLNAAHETSKleieaSHSEKLELLKKAYEASLSeiKKGHEIEKKSLEDLLSEKQESLEKQINDL 1048
Cdd:cd22656 127 LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLNEEYAAKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1049 KSENDALNEKLKSEEQKRRAREK---------ANLKN------PQIMYLEQ----------ELESLKAVLEIKNEKLHQQ 1103
Cdd:cd22656 200 KAKIDELKALIADDEAKLAAALRliadltaadTDLDNllaligPAIPALEKlqgawqaiatDLDSLKDLLEDDISKIPAA 279
|
170 180
....*....|....*....|....*.
gi 1386876323 1104 DIKLMKMEKLVDNNTALVDKLKRFQQ 1129
Cdd:cd22656 280 ILAKLELEKAIEKWNELAEKADKFRQ 305
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
958-1096 |
1.14e-06 |
|
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: 51.94 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 958 TREYEKLRDtYIEEAEKYKMQLQEQFDNLNaahetSKLEIEASHSEKLE-----LLKKAYEAsLSEIKKGHEIEKKSLED 1032
Cdd:smart00787 157 KEDYKLLMK-ELELLNSIKPKLRDRKDALE-----EELRQLKQLEDELEdcdptELDRAKEK-LKKLLQEIMIKVKKLEE 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876323 1033 LLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpQIMYLEQELESLKAVLEIK 1096
Cdd:smart00787 230 LEEELQE-LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK--EIEKLKEQLKLLQSLTGWK 290
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
928-1091 |
1.16e-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: 51.08 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 928 RNELQTVYEafVQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAshsekLEL 1007
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKEL-PAELAELEDE-LAALEARLEAAKTELEDLEKEIKRLELEIEE-----VEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1008 LKKAYEASLSEIKK-------GHEIE-----KKSLEDLLSE---KQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1072
Cdd:COG1579 74 RIKKYEEQLGNVRNnkeyealQKEIEslkrrISDLEDEILElmeRIEELEEELAELEAELAELEAELEEKKAELDEELAE 153
|
170
....*....|....*....
gi 1386876323 1073 nlknpqimyLEQELESLKA 1091
Cdd:COG1579 154 ---------LEAELEELEA 163
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
936-1145 |
1.16e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 936 EAFVQQHQAEKTERENRLKEFYTREYEKLRDTY-------IEEAEKYKMQLQEQFDNLNAAHE-TSKLEIEASHSEKLEL 1007
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALglppdlsPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1008 LKKAYEASLSEIKKGHEIEKKSLEdlLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREkanlknpqimyLEQELE 1087
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELLEALDEEELEEELEE-----------LEEELE 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876323 1088 SLKAVLEIKNEKLHQQDIKLMKMEklvdNNTALVDKLKRFQQENEELKARMDKHMAIS 1145
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLE----EDGELAELLQELEELKAELRELAEEWAALK 496
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
980-1130 |
1.18e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 52.28 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 980 QEQFDNLNA--AHETSKLEIEASHSEKLELLKKAYEASLSEIkkghEIEKKSLEDLLSEkqesLEKQINDLKSENDALNE 1057
Cdd:PRK09039 52 DSALDRLNSqiAELADLLSLERQGNQDLQDSVANLRASLSAA----EAERSRLQALLAE----LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876323 1058 KLKSEEQ-KRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM-EKLvdnNTALVDK---LKRFQQE 1130
Cdd:PRK09039 124 ELDSEKQvSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgRRL---NVALAQRvqeLNRYRSE 198
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
859-1134 |
1.68e-06 |
|
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: 52.27 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 859 ENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEkarnELQTVYEAF 938
Cdd:COG5185 160 IIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAK----EIINIEEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 939 VQQhqaEKTERENRLKEFYTREYEKLrdtyIEEAEKYKM----QLQEQFDNLNAAHETSKLEIEaSHSEKLELLKKAYEA 1014
Cdd:COG5185 236 KGF---QDPESELEDLAQTSDKLEKL----VEQNTDLRLeklgENAESSKRLNENANNLIKQFE-NTKEKIAEYTKSIDI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1015 SLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLE 1094
Cdd:COG5185 308 KKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIE 387
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1386876323 1095 IKNEKLHQQDIKLMKMEKlvDNNTALVDKLKRFQQENEEL 1134
Cdd:COG5185 388 STKESLDEIPQNQRGYAQ--EILATLEDTLKAADRQIEEL 425
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
886-1107 |
1.75e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 886 IQHLLSEREEALKQHKTLSQELVNLR---GELVTASTTCEKLEKARNELQtvyeaFVQQHQAEKTERENRLKEfYTREYE 962
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRkelAELNKAGGSIDKLRKEIERLE-----WRQQTEVLSPEEEKELVE-KIKELE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 963 KLrdtyIEEAEKyKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLS---------EIKK-----GHEIEKK 1028
Cdd:COG1340 147 KE----LEKAKK-ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEmielykeadELRKeadelHKEIVEA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1029 SLE-DLLSEKQESLEKQINDLKSENDALNEKLKsEEQKRRAREKANLKNPQIMyleqelESLKavleiKNEKLHQQDIKL 1107
Cdd:COG1340 222 QEKaDELHEEIIELQKELRELRKELKKLRKKQR-ALKREKEKEELEEKAEEIF------EKLK-----KGEKLTTEELKL 289
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
848-1140 |
2.23e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.03 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 848 TLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREE--ALKQHKTLS-QELVNLRGELVTASTTCEKL 924
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVElEELKKILAEDEKLLDEKKQF 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 925 EKARNELQTVYEAFV---QQHQAEKTERENRL------KEFYTREYEKLRdtyiEEAEKYKMQLQE--------QFDNLN 987
Cdd:pfam05483 428 EKIAEELKGKEQELIfllQAREKEIHDLEIQLtaiktsEEHYLKEVEDLK----TELEKEKLKNIEltahcdklLLENKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 988 AAHETSKLEIE-ASHSEKLELLKKAYEASLSEIKKGHEIEKKsLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKR 1066
Cdd:pfam05483 504 LTQEASDMTLElKKHQEDIINCKKQEERMLKQIENLEEKEMN-LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1067 RAREKA---------NL------KNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDNNTALVDKLKRFQQE 1130
Cdd:pfam05483 583 LKKEKQmkilenkcnNLkkqienKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKE 662
|
330
....*....|
gi 1386876323 1131 NEELKARMDK 1140
Cdd:pfam05483 663 IEDKKISEEK 672
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
886-1140 |
2.30e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 886 IQHLLSEREEALKQHKTLSQELVNLRGELVTAS------TTCEKLEKARNELQtvyeafvqQHQAEKTEREnrlkefyTR 959
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkELAEQLKELEEKLK--------KYNLEELEKK-------AE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 960 EYEKLRdtyiEEAEKYKmqlqeqfdnlnaahetSKLEIEASHSEKLELLKKAYEASLSEIKKGHEiEKKSLEDLLSEK-- 1037
Cdd:PRK03918 526 EYEKLK----EKLIKLK----------------GEIKSLKKELEKLEELKKKLAELEKKLDELEE-ELAELLKELEELgf 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1038 --QESLEKQINDL-------------KSENDALNEKLKSEEQK-RRAREKANLKNPQIMYLEQELESLKAVL------EI 1095
Cdd:PRK03918 585 esVEELEERLKELepfyneylelkdaEKELEREEKELKKLEEElDKAFEELAETEKRLEELRKELEELEKKYseeeyeEL 664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1386876323 1096 KNEKLHQQ------DIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDK 1140
Cdd:PRK03918 665 REEYLELSrelaglRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEK 715
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
885-1131 |
3.42e-06 |
|
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: 51.56 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 885 VIQHLLSEREEALK----QHKTLSQELVNLRGELVTASTTCEKLEKARNELQTvyEAFVQQHQAEKTERE-NRLKEfYTR 959
Cdd:TIGR04523 58 NLDKNLNKDEEKINnsnnKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS--EIKNDKEQKNKLEVElNKLEK-QKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 960 EYEKLRDTYIEEAEKykmqLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAY--EASLSEIKKGHEIEKKSLEDL--LS 1035
Cdd:TIGR04523 135 ENKKNIDKFLTEIKK----KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLniQKNIDKIKNKLLKLELLLSNLkkKI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1036 EKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA-NLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLV 1114
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
250
....*....|....*..
gi 1386876323 1115 DNNTALVDKLKRFQQEN 1131
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQD 307
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
846-1139 |
3.75e-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: 51.36 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 846 EKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLE 925
Cdd:pfam10174 363 KKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 926 KARNELQTVYEAFvqQHQAEKTERENRlkefytreyeklrdtyiEEAEKYKMQLQEQFDNLNAAHeTSKLEIEAShseKL 1005
Cdd:pfam10174 443 EALSEKERIIERL--KEQREREDRERL-----------------EELESLKKENKDLKEKVSALQ-PELTEKESS---LI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1006 ELLKKAYEASLSEIKKGHEIekKSLEDLLSEKQESLEKQINDL-KSENDALNEKLKSE--EQKRRAREKANLKNPQIMYL 1082
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKL--KSLEIAVEQKKEECSKLENQLkKAHNAEEAVRTNPEinDRIRLLEQEVARYKEESGKA 577
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876323 1083 EQELESLKAVL-EIKNEKlHQQDIKLMKMEKL----VDNNTALVDKLKRFQQENEELKARMD 1139
Cdd:pfam10174 578 QAEVERLLGILrEVENEK-NDKDKKIAELESLtlrqMKEQNKKVANIKHGQQEMKKKGAQLL 638
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
922-1102 |
4.56e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.92 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNEL-----QTVYEAFVQQHQAEKTERENRLKEfytREYEKLRDTyIEEAEKYKMQLQEQFDNLnaAHETSKLE 996
Cdd:COG4717 49 ERLEKEADELfkpqgRKPELNLKELKELEEELKEAEEKE---EEYAELQEE-LEELEEELEELEAELEEL--REELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 997 IEASHSEKLELLKKAyEASLSEIKKGHEIEKKSLEDL--LSEKQESLEKQINDLKSENDALNEK--LKSEEQKRRAREKA 1072
Cdd:COG4717 123 KLLQLLPLYQELEAL-EAELAELPERLEELEERLEELreLEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEEL 201
|
170 180 190
....*....|....*....|....*....|
gi 1386876323 1073 NLKNPQIMYLEQELESLKAVLEIKNEKLHQ 1102
Cdd:COG4717 202 EELQQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
951-1102 |
5.43e-06 |
|
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: 48.36 E-value: 5.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 951 NRLKEFY---TREYEKLRDTYieEAEKYKMQLQEQfDNLNAAHETSKlEIEaSHSEKLE-LLKKAYEasLSEIKKGHEIE 1026
Cdd:pfam13851 11 NEIKNYYndiTRNNLELIKSL--KEEIAELKKKEE-RNEKLMSEIQQ-ENK-RLTEPLQkAQEEVEE--LRKQLENYEKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1027 KKSLEDLlSEKQESLEKQINDLKSENDALNEKLKSEEQKRRA------------REKANLKNpqiMYLEQELESLKAVLE 1094
Cdd:pfam13851 84 KQSLKNL-KARLKVLEKELKDLKWEHEVLEQRFEKVERERDElydkfeaaiqdvQQKTGLKN---LLLEKKLQALGETLE 159
|
....*...
gi 1386876323 1095 IKNEKLHQ 1102
Cdd:pfam13851 160 KKEAQLNE 167
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
895-1136 |
5.92e-06 |
|
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: 50.74 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 895 EALKQHKTLSQELVNL--RGELVTASTTC------EKLEKARNELQTVYEAFVQQHQAEkterenrlkEFYTREYEKLrd 966
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLtlRSQLLTLCTPCmpdtyhERKQVLEKELKHLREALQQTQQSH---------AYLTQKREAQ-- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 967 tyiEEAEKYKMQLQEQ------FDNLNAAHETSKLEIE--------ASHSEKLELLKKAYEASLSEIKKgheiEKKSLED 1032
Cdd:TIGR00618 253 ---EEQLKKQQLLKQLrarieeLRAQEAVLEETQERINrarkaaplAAHIKAVTQIEQQAQRIHTELQS----KMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1033 LLSEKQeSLEKQINDLKSENDALNEKLKSEEQKRRAREKANLK-----------------NPQIMYLEQELESLKAVLEI 1095
Cdd:TIGR00618 326 LLMKRA-AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIreiscqqhtltqhihtlQQQKTTLTQKLQSLCKELDI 404
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1386876323 1096 KNEKLHQQDIKLMKmEKLVDNNTALVDKLKRFQQENEELKA 1136
Cdd:TIGR00618 405 LQREQATIDTRTSA-FRDLQGQLAHAKKQQELQQRYAELCA 444
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
878-1140 |
5.96e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 49.52 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 878 KFEALTVVIQHLLSEREEALKQHKTLSQELVNLRG---ELVtasttcEKLEKARNELQTVYEAfVQQHQAEKTERENRLK 954
Cdd:COG1340 16 KIEELREEIEELKEKRDELNEELKELAEKRDELNAqvkELR------EEAQELREKRDELNEK-VKELKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 955 EFYT--REYEKLRDTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEAshsEKlELLKK--AYEASLSEIKKGHEIEKKSL 1030
Cdd:COG1340 89 ELREelDELRKELAELNKAGGSID-KLRKEIERLEWRQQTEVLSPEE---EK-ELVEKikELEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1031 EDL-----LSEKQESLEKQINDLKSENDALNEKLKSEEQKR-RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQD 1104
Cdd:COG1340 164 ELRaelkeLRKEAEEIHKKIKELAEEAQELHEEMIELYKEAdELRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 1386876323 1105 IKLMKMEKlVDNNTALVDKLKRFQQENEELKARMDK 1140
Cdd:COG1340 244 KELKKLRK-KQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
901-1139 |
7.08e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 901 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFvqQHQAEKTERENRLKEfYTREYEKLRDTY--IEEAEKYKMQ 978
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVAS-AEREIAELEAELerLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 979 LQEQFDNLNAAHETSKLEIEASHSEK---------LELLKKAYEASLSEIKKGHEIEKKSL--EDLLSEKQESLEKQI-N 1046
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIgrlekeleqAEEELDELQDRLEAAEDLARLELRALleERFAAALGDAVERELrE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1047 DLKSENDALNEKLKSEEQK-RRAREKANLKNPQIMY-LEQELESLKAVLE----IKNEKL--HQQDIKLMKMEKLVDNNT 1118
Cdd:COG4913 770 NLEERIDALRARLNRAEEElERAMRAFNREWPAETAdLDADLESLPEYLAlldrLEEDGLpeYEERFKELLNENSIEFVA 849
|
250 260
....*....|....*....|.
gi 1386876323 1119 ALVDKLKRfqqENEELKARMD 1139
Cdd:COG4913 850 DLLSKLRR---AIREIKERID 867
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
892-1140 |
8.46e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.89 E-value: 8.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 892 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA---EKTERENRLKEF-----------Y 957
Cdd:pfam07888 67 DREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAllaQRAAHEARIRELeediktltqrvL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 958 TREYEKLRDTyiEEAEKYKMQLQEQfdnlNAAHETSKLEIEASHSEKLELLKKAYEAslseikKGHEIEKKSLEDLLSEK 1037
Cdd:pfam07888 147 ERETELERMK--ERAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKEFQEL------RNSLAQRDTQVLQLQDT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1038 QESLEKQINDlKSENDALNEKLKseEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDN 1116
Cdd:pfam07888 215 ITTLTQKLTT-AHRKEAENEALL--EELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTlQLADA 291
|
250 260
....*....|....*....|....*.
gi 1386876323 1117 NTALVDKLKRFQQENEELK--ARMDK 1140
Cdd:pfam07888 292 SLALREGRARWAQERETLQqsAEADK 317
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
924-1143 |
9.69e-06 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 49.15 E-value: 9.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 924 LEKARNELQTVYEAFVQQHQAEkterENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHET----------- 992
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAE----PSRLYSLYEKEIEDLRRQ-LDTLTVERARLQLELDNLRLAAEDfrqkyedelnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 993 --------------------SKLEIEA---SHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLK 1049
Cdd:pfam00038 98 rtsaendlvglrkdldeatlARVDLEAkieSLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLD-LTSALAEIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1050 SENDALNEKLKSE--------------------EQKRRAREKANLKNPQIMYLEQELESL---KAVLEIKNEKLHQQDIK 1106
Cdd:pfam00038 177 AQYEEIAAKNREEaeewyqskleelqqaaarngDALRSAKEEITELRRTIQSLEIELQSLkkqKASLERQLAETEERYEL 256
|
250 260 270
....*....|....*....|....*....|....*....
gi 1386876323 1107 LMKM--EKLVDNNTALVDKLKRFQQENEELKARMDKHMA 1143
Cdd:pfam00038 257 QLADyqELISELEAELQETRQEMARQLREYQELLNVKLA 295
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
850-1141 |
9.87e-06 |
|
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: 49.85 E-value: 9.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 850 ELTQYKTKCENQSGFILQL--------KQLLAcGNTKFEALTVVIQHLLSEREEALKQHKTLSQElvnlrGELVTASTTC 921
Cdd:pfam06160 108 ELDELLESEEKNREEVEELkdkyrelrKTLLA-NRFSYGPAIDELEKQLAEIEEEFSQFEELTES-----GDYLEAREVL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTVYEAFVQQHQaekterenRLKEFYTREYEKLRDTYIE-EAEKYK---MQLQEQFDNLNAAHETS---- 993
Cdd:pfam06160 182 EKLEEETDALEELMEDIPPLYE--------ELKTELPDQLEELKEGYREmEEEGYAlehLNVDKEIQQLEEQLEENlall 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 994 -KLEIEAShSEKLELLKKA----YEASLSEIKKGHEIEKKS--LEDLLS---------------------------EKQE 1039
Cdd:pfam06160 254 eNLELDEA-EEALEEIEERidqlYDLLEKEVDAKKYVEKNLpeIEDYLEhaeeqnkelkeelervqqsytlnenelERVR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1040 SLEKQINDLKSENDALNEKLKSEEQkrrarekanlknPQIMYLEQELESLKAVLEIKNEklhQQDIK--LMKMEKlvDNN 1117
Cdd:pfam06160 333 GLEKQLEELEKRYDEIVERLEEKEV------------AYSELQEELEEILEQLEEIEEE---QEEFKesLQSLRK--DEL 395
|
330 340
....*....|....*....|....
gi 1386876323 1118 TALvDKLKRFQQENEELKARMDKH 1141
Cdd:pfam06160 396 EAR-EKLDEFKLELREIKRLVEKS 418
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
876-1140 |
1.23e-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: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 876 NTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVyeafVQQHQAEKTERENRLKE 955
Cdd:TIGR04523 467 ETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEK----IEKLESEKKEKESKISD 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 956 FytrEYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKlEIEASHSEKLELLKKaYEASLSEIKKghEIEKKSledlls 1035
Cdd:TIGR04523 543 L---EDELNKDDFELKKENLEKEIDEKNKEIEELKQTQK-SLKKKQEEKQELIDQ-KEKEKKDLIK--EIEEKE------ 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1036 EKQESLEKQINDLKSENDALNEKLKSEEQKrrarekanlKNPQIMYLEQELESLKAVLEIKNE---------KLHQQDIK 1106
Cdd:TIGR04523 610 KKISSLEKELEKAKKENEKLSSIIKNIKSK---------KNKLKQEVKQIKETIKEIRNKWPEiikkikeskTKIDDIIE 680
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876323 1107 LMK----------------------MEKLVDNNTALVDKLKRFQQENEELKARMDK 1140
Cdd:TIGR04523 681 LMKdwlkelslhykkyitrmirikdLPKLEEKYKEIEKELKKLDEFSKELENIIKN 736
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
817-1048 |
1.31e-05 |
|
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: 49.95 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 817 ALNAVEKSRQknprsLCIQPQTAPDALPPEktleLTQYKTKCENQSGFILQLKQLLACGN---TKFEALTVVIQHLLSE- 892
Cdd:COG3096 418 AVQALEKARA-----LCGLPDLTPENAEDY----LAAFRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVCKIAGEv 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 893 -REEA-------LKQH---KTLSQELVNLRGELVTAsttcEKLEKARNELQTVYEAFVQQHQAEKTERENrLKEFYTREY 961
Cdd:COG3096 489 eRSQAwqtarelLRRYrsqQALAQRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELE 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 962 EKLRD--TYIEEAEKYKMQLQEQFDNLNAAHEtsKLEIEASH----SEKLELLKKAYEASL---SEIKKG------HEIE 1026
Cdd:COG3096 564 AQLEEleEQAAEAVEQRSELRQQLEQLRARIK--ELAARAPAwlaaQDALERLREQSGEALadsQEVTAAmqqlleRERE 641
|
250 260
....*....|....*....|..
gi 1386876323 1027 KKSLEDLLSEKQESLEKQINDL 1048
Cdd:COG3096 642 ATVERDELAARKQALESQIERL 663
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
850-1139 |
1.53e-05 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 49.35 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 850 ELTQYKTKCENQSGFILQLKQLL-----ACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKL 924
Cdd:pfam15921 171 QIEQLRKMMLSHEGVLQEIRSILvdfeeASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVE---DQL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 925 EKARNELQTVYEAFVQQHQaektereNRLKEFYTrEYEKLRDTYIEEAEKYKMQ----------LQEQFDNLNAAHETSK 994
Cdd:pfam15921 248 EALKSESQNKIELLLQQHQ-------DRIEQLIS-EHEVEITGLTEKASSARSQansiqsqleiIQEQARNQNSMYMRQL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 995 LEIEASHSE---KLELLKKAYEASLSEIKK-----GHEI------------EKKSLEDLLS---------EKQESLEKQ- 1044
Cdd:pfam15921 320 SDLESTVSQlrsELREAKRMYEDKIEELEKqlvlaNSELtearterdqfsqESGNLDDQLQklladlhkrEKELSLEKEq 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1045 --------------INDLKSEND----------ALNEKLKSEEQKRRAREKANLKNP-----QIMYLEQELESLKAVLEI 1095
Cdd:pfam15921 400 nkrlwdrdtgnsitIDHLRRELDdrnmevqrleALLKAMKSECQGQMERQMAAIQGKnesleKVSSLTAQLESTKEMLRK 479
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1386876323 1096 KNEKLHQQDIKLMKMEKLV-DNNTALVDKLKRFQQENEE---LKARMD 1139
Cdd:pfam15921 480 VVEELTAKKMTLESSERTVsDLTASLQEKERAIEATNAEitkLRSRVD 527
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
850-1137 |
1.55e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 850 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 929
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 930 ELQT---VYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1006
Cdd:COG4372 126 DLEQqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEE--LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1007 LLKKAYEASLSEIKKGHEIEKKSLE---DLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1083
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEaklGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1386876323 1084 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR 1137
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
881-1139 |
1.66e-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: 48.61 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 881 ALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVyeafVQQHQAEKTERENRLKEFyTRE 960
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR----IRALEQELAALEAELAEL-EKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 961 YEKLRdtyiEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKA-YEASLSEikkgheiEKKSLEDLLSEKQE 1039
Cdd:COG4942 92 IAELR----AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqYLKYLAP-------ARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1040 SLEKQINDLKSENDALNEKLKSEEQKRRArekanlknpqimyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTA 1119
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAA-------------LEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
250 260
....*....|....*....|
gi 1386876323 1120 LVDKLKRFQQENEELKARMD 1139
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAG 247
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
959-1125 |
2.82e-05 |
|
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins conserved from yeasts to humans. Most of the proteins in this entry have an RhoGEF pfam00621 domain at their C-terminal end.
Pssm-ID: 462875 [Multi-domain] Cd Length: 150 Bit Score: 45.30 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 959 REYEKLRDTYIEEAEKYKM----QLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASlSEIKKGHEIEKKSLEDLL 1034
Cdd:pfam09744 10 KEFERLIDRYGEDVVKGLMpkvvNVLELLESLASRNQEHNVELEEL-REDNEQLETQYERE-KALRKRAEEELEEIEDQW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1035 SEKQESLEKQINDLKSENDALneklkseEQKRRARekanlknpqimyleqeLESLKAVLEIKNEKLHQQDIKLMKmeKLV 1114
Cdd:pfam09744 88 EQETKDLLSQVESLEEENRRL-------EADHVSR----------------LEEKEAELKKEYSKLHERETEVLR--KLK 142
|
170
....*....|.
gi 1386876323 1115 DnntaLVDKLK 1125
Cdd:pfam09744 143 E----VVDRQR 149
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
938-1103 |
3.43e-05 |
|
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.
Pssm-ID: 293683 [Multi-domain] Cd Length: 228 Bit Score: 46.66 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 938 FVQQHQAEKTERENrLKEFYTREYEKLRDTyieeaEKYKMQLQEQFDNLNAAHETSKLE------IEASHSEKLELLKKA 1011
Cdd:pfam17078 43 FLENLASLKHENDN-LSSMLNRKERRLKDL-----EDQLSELKNSYEELTESNKQLKKRlenssaSETTLEAELERLQIQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1012 YEASLSEIK--KGH---EIE--KKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREkaNLKNPQIMYLEQ 1084
Cdd:pfam17078 117 YDALVDSQNeyKDHyqqEINtlQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFKNLD--NIYVNKNNKLLT 194
|
170 180
....*....|....*....|
gi 1386876323 1085 ELESLKAVLEIKN-EKLHQQ 1103
Cdd:pfam17078 195 KLDSLAQLLDLPSwLNLYPE 214
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
994-1139 |
3.45e-05 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 44.99 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 994 KLEIEASHSEKLELLKKAYEASLSEIKKGHEIEkksledllsekqeSLEKQINDLKSENDALNEKLKseEQKRRAREKAN 1073
Cdd:pfam12718 6 KLEAENAQERAEELEEKVKELEQENLEKEQEIK-------------SLTHKNQQLEEEVEKLEEQLK--EAKEKAEESEK 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876323 1074 LK------NPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKlvdnntalvdKLKRFQQENEELKARMD 1139
Cdd:pfam12718 71 LKtnnenlTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLER----------KVQALEQERDEWEKKYE 132
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
922-1112 |
3.48e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 48.60 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTVYEAFVQQHQAE--KTERENRLKEFYTREYEKLRDTY-----IEEAEKYK---MQLQEQFDNLNAAHE 991
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEeaKKAEEAKIKAEELKKAEEEKKKVeqlkkKEAEEKKKaeeLKKAEEENKIKAAEE 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 992 TSKLEIEASHSEKL------------ELLKKAYEA-SLSEIKKGHEIEKKSLEDLLSEKQESLEKqINDLKSENDalNEK 1058
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAkkaeedekkaaeALKKEAEEAkKAEELKKKEAEEKKKAEELKKAEEENKIK-AEEAKKEAE--EDK 1743
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1386876323 1059 LKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIK-LMKMEK 1112
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKrRMEVDK 1798
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
888-1130 |
4.07e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.81 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 888 HLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVyeafVQQHQAEKTERENRLKEfyTREYEKLRDT 967
Cdd:pfam05557 10 RLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKR----IRLLEKREAEAEEALRE--QAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 968 YIEEAEKykmQLQEQFDNLNAAHETS---KLEIEA----SHSEKLELLKKAYEasLSEIKKGHEIEKKSLEDLlSEKQES 1040
Cdd:pfam05557 84 YLEALNK---KLNEKESQLADAREVIsclKNELSElrrqIQRAELELQSTNSE--LEELQERLDLLKAKASEA-EQLRQN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1041 LEKQINDLKSENDALNE---KLKSEEQKRRAREKANLKNPQIMYLEQELE----------SLKAVLEIKNEKLHQQDIKL 1107
Cdd:pfam05557 158 LEKQQSSLAEAEQRIKElefEIQSQEQDSEIVKNSKSELARIPELEKELErlrehnkhlnENIENKLLLKEEVEDLKRKL 237
|
250 260
....*....|....*....|...
gi 1386876323 1108 MKMEKLVDNNTALVDKLKRFQQE 1130
Cdd:pfam05557 238 EREEKYREEAATLELEKEKLEQE 260
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
894-1066 |
4.30e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 894 EEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKefytREyeklrdtyIEEAE 973
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE----RE--------IERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 974 KYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEikkgheiekKSLEDLLSEKQESLEKQINDLKSEND 1053
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL---------EEELEALEEALAEAEAALRDLRRELR 422
|
170
....*....|...
gi 1386876323 1054 ALNEKLKSEEQKR 1066
Cdd:COG4913 423 ELEAEIASLERRK 435
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
969-1143 |
4.76e-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: 47.07 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 969 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAYEASLSEIKKgheiekksledlLSEKQESLEKQINDL 1048
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-LAALERRIAALARRIRA------------LEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1049 KSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE------------QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1116
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180
....*....|....*....|....*..
gi 1386876323 1117 NTALVDKLKRFQQENEELKARMDKHMA 1143
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKA 195
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
922-1140 |
4.88e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.83 E-value: 4.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASH 1001
Cdd:PTZ00121 1493 EEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKA 1572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1002 SE-------KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSE------------KQESLEKQINDLKSENDalnEKLKSE 1062
Cdd:PTZ00121 1573 EEdknmalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKaeeakikaeelkKAEEEKKKVEQLKKKEA---EEKKKA 1649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1063 EQKRRAREKANLKNPQIMYLEQE----LESLKAVLEIKN---EKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELK 1135
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEdkkkAEEAKKAEEDEKkaaEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENK 1729
|
....*
gi 1386876323 1136 ARMDK 1140
Cdd:PTZ00121 1730 IKAEE 1734
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
959-1140 |
5.09e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 959 REYEKLRDTYIEEAEKykmqlqeqfdnlNAAHETSKLEIEAShsEKLELLKKAYEASLSEIKKghEIEKksLEDLLSEKQ 1038
Cdd:PRK12704 34 KEAEEEAKRILEEAKK------------EAEAIKKEALLEAK--EEIHKLRNEFEKELRERRN--ELQK--LEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1039 ESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpqimyLEQELESLKAVLEIKNEK---LHQQDIKLMKMEKLVD 1115
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEK----------KEEELEELIEEQLQELERisgLTAEEAKEILLEKVEE 165
|
170 180
....*....|....*....|....*
gi 1386876323 1116 NNTAlvDKLKRFQQENEELKARMDK 1140
Cdd:PRK12704 166 EARH--EAAVLIKEIEEEAKEEADK 188
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
876-1139 |
5.53e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 47.73 E-value: 5.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 876 NTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKarnELQTVYEAF---------VQQHQAEK 946
Cdd:PRK02224 341 NEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEE---EIEELRERFgdapvdlgnAEDFLEEL 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 947 TERENRLKEFYTR---EYEKLRDTyIEEAEkykmQLQ-------------------------EQFDNLNAAHETSKLEIE 998
Cdd:PRK02224 418 REERDELREREAEleaTLRTARER-VEEAE----ALLeagkcpecgqpvegsphvetieedrERVEELEAELEDLEEEVE 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 999 AShSEKLELLKKAYEASlSEIKKGHEiEKKSLEDLLSEKQESLE----------KQINDLKSENDALNEKL-KSEEQKRR 1067
Cdd:PRK02224 493 EV-EERLERAEDLVEAE-DRIERLEE-RREDLEELIAERRETIEekreraeelrERAAELEAEAEEKREAAaEAEEEAEE 569
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876323 1068 AREKANLKNPQIMYLEQELESLKAVLEIkneklhqqdikLMKMEKLVDNNTALVDKLKRFQQENEELKARMD 1139
Cdd:PRK02224 570 AREEVAELNSKLAELKERIESLERIRTL-----------LAAIADAEDEIERLREKREALAELNDERRERLA 630
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1003-1140 |
7.54e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 7.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1003 EKLELLKK--AYEASLSEIK---KGHEIEKKSLEDLLSEKQESLEK---QINDLKSENDALNEKLKSEEQKR-RAREK-A 1072
Cdd:COG1579 4 EDLRALLDlqELDSELDRLEhrlKELPAELAELEDELAALEARLEAaktELEDLEKEIKRLELEIEEVEARIkKYEEQlG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1073 NLKNP-QIMYLEQELESLKAVLEIKNEKLhqqdIKLM-KMEKLVDNNTALVDKLKRFQQENEELKARMDK 1140
Cdd:COG1579 84 NVRNNkEYEALQKEIESLKRRISDLEDEI----LELMeRIEELEEELAELEAELAELEAELEEKKAELDE 149
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
952-1147 |
8.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 8.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 952 RLKEFYTREYEKLRDTYIEEAEKykMQLqeqFDNLNAAHETSKLE-IEAshsekleLLKKAYEASLSEIKKG----HEIE 1026
Cdd:COG4717 2 KIKELEIYGFGKFRDRTIEFSPG--LNV---IYGPNEAGKSTLLAfIRA-------MLLERLEKEADELFKPqgrkPELN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1027 KKSLEDLLSEKQE--SLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLE--QELESLKAVLEIKNEKLH 1101
Cdd:COG4717 70 LKELKELEEELKEaeEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1386876323 1102 QQDIKLMKMEklvdnntALVDKLKRFQQENEELKARMDKHMAISSF 1147
Cdd:COG4717 150 ELEERLEELR-------ELEEELEELEAELAELQEELEELLEQLSL 188
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
850-1141 |
1.14e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.37 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 850 ELTQYKTKCENQSGFILQL--------KQLLAcGNTKFEALTVVIQHLLSEREEALKQHKTLSQElvnlrGELVTASttc 921
Cdd:PRK04778 127 ELQELLESEEKNREEVEQLkdlyrelrKSLLA-NRFSFGPALDELEKQLENLEEEFSQFVELTES-----GDYVEAR--- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTVyeafvqQHQAEK-----TERENRLKEfytrEYEKLRDTYIE-EAEKYK---MQLQEQFDNLNAAHET 992
Cdd:PRK04778 198 EILDQLEEELAAL------EQIMEEipellKELQTELPD----QLQELKAGYRElVEEGYHldhLDIEKEIQDLKEQIDE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 993 -----SKLEIEAShSEKLELLKKA----YEASLSEIKKGHEIEKKS--LEDLLS-------------------------- 1035
Cdd:PRK04778 268 nlallEELDLDEA-EEKNEEIQERidqlYDILEREVKARKYVEKNSdtLPDFLEhakeqnkelkeeidrvkqsytlnese 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1036 -EKQESLEKQINDLKSENDALNEKLksEEQKRRAREkanlknpqimyLEQELESLKAVL-EIKNEklhQQDIK--LMKME 1111
Cdd:PRK04778 347 lESVRQLEKQLESLEKQYDEITERI--AEQEIAYSE-----------LQEELEEILKQLeEIEKE---QEKLSemLQGLR 410
|
330 340 350
....*....|....*....|....*....|
gi 1386876323 1112 KlvDNNTALvDKLKRFQQENEELKARMDKH 1141
Cdd:PRK04778 411 K--DELEAR-EKLERYRNKLHEIKRYLEKS 437
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
856-1107 |
1.21e-04 |
|
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: 46.37 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 856 TKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQhktLSQELVNLRGELVtasttcEKLEKARNELQTVY 935
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE---LNQLLRTLDDQWK------EKRDELNGELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 936 EAfVQQHQAEKTERENRLKEFYTREYEKLR---------DTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1006
Cdd:pfam12128 315 AA-VAKDRSELEALEDQHGAFLDADIETAAadqeqlpswQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIA 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1007 LLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE--------------EQKR------ 1066
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatpellLQLEnfderi 473
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1386876323 1067 -RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKL 1107
Cdd:pfam12128 474 eRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRL 515
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
887-1103 |
1.24e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 887 QHLLSEREEALKQHKTLSQELVNLRgelvtasttcEKLEKARNELQtvyeAFVQQH-----QAEKTERENRLKEfYTREY 961
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELR----------KELEEAEAALE----EFRQKNglvdlSEEAKLLLQQLSE-LESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 962 EKLRDTYIEEAEKYKmQLQEQFD-NLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGH----EIEKKsLEDLLSE 1036
Cdd:COG3206 229 AEARAELAEAEARLA-ALRAQLGsGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHpdviALRAQ-IAALRAQ 306
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876323 1037 KQESLEKQINDLKSENDALNEKLKS-EEQKRRAREKANlKNPQimyLEQELESLKAVLEIkNEKLHQQ 1103
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASlQAQLAQLEARLA-ELPE---LEAELRRLEREVEV-ARELYES 369
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
939-1143 |
1.41e-04 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 44.63 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 939 VQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKlEIEASHSEKLELLKKAYEASlSE 1018
Cdd:pfam00261 3 MQQIKEELDEAEERLKEA-MKKLEEAEKR-AEKAEAEVAALNRRIQLLEEELERTE-ERLAEALEKLEEAEKAADES-ER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1019 IKKGheIEKKSLEDllSEKQESLEKQINDLKSENDALNEKLKSEEQK--------RRAREKANLKNPQIMYLEQEL---- 1086
Cdd:pfam00261 79 GRKV--LENRALKD--EEKMEILEAQLKEAKEIAEEADRKYEEVARKlvvvegdlERAEERAELAESKIVELEEELkvvg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1087 ESLKAvLEIKNEKLHQQDIK-------------------------LMKMEKLVDnntALVDKLKRFQQENEELKARMDKH 1141
Cdd:pfam00261 155 NNLKS-LEASEEKASEREDKyeeqirflteklkeaetraefaersVQKLEKEVD---RLEDELEAEKEKYKAISEELDQT 230
|
..
gi 1386876323 1142 MA 1143
Cdd:pfam00261 231 LA 232
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
925-1071 |
1.55e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.29 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 925 EKARNELQTVYEAFVQQHQAEKTEREnRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEiEASHSEK 1004
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEE-RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEE 1300
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386876323 1005 L----ELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREK 1071
Cdd:PTZ00121 1301 KkkadEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEK 1371
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
1001-1143 |
1.57e-04 |
|
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino acids in length. The family is found in association with pfam00069. Polo-like kinase 1 (Plx1) is essential during mitosis for the activation of Cdc25C, for spindle assembly, and for cyclin B degradation. This family is Polo kinase kinase (PKK) which phosphorylates Polo kinase and Polo-like kinase to activate them. PKK is a serine/threonine kinase.
Pssm-ID: 463600 [Multi-domain] Cd Length: 139 Bit Score: 42.93 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1001 HSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEK-QINDLKsendALNEKLKSEEQKRRAREKANLKNpQI 1079
Cdd:pfam12474 1 HQLQKEQQKDRFEQERQQLKKRYEKELEQLERQQKQQIEKLEQrQTQELR----RLPKRIRAEQKKRLKMFRESLKQ-EK 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876323 1080 MYLEQELESLKavleikneKLHQQDIKLMKMEKLvdnntalvdKLKRFQQENEELKARMDKHMA 1143
Cdd:pfam12474 76 KELKQEVEKLP--------KFQRKEAKRQRKEEL---------ELEQKHEELEFLQAQSEALER 122
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
945-1065 |
1.78e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 945 EKTERENRLKEFYTREYEKLRdtyiEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEI----- 1019
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALL----KEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELrqlqk 598
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1386876323 1020 KKGHEIEKKSLED---LLSEKQESLEKQINDLKSENDALNE----KLKSEEQK 1065
Cdd:PRK00409 599 GGYASVKAHELIEarkRLNKANEKKEKKKKKQKEKQEELKVgdevKYLSLGQK 651
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
943-1136 |
2.14e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 45.70 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 943 QAEKTERenrlkefytreYEKLRdtyiEEAEKYKMQLQ-EQFDNLNAAHETSKLEIEAshsekLELLKKAYEASLSEIKK 1021
Cdd:COG1196 208 QAEKAER-----------YRELK----EELKELEAELLlLKLRELEAELEELEAELEE-----LEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1022 GHEIEKKSLEDLlsekqeslEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVLEIKNEKL- 1100
Cdd:COG1196 268 ELEELRLELEEL--------ELELEEAQAEEYELLAELARLEQDIARLEE------RRRELEERLEELEEELAELEEELe 333
|
170 180 190
....*....|....*....|....*....|....*..
gi 1386876323 1101 -HQQDIKLMKmEKLVDNNTALVDKLKRFQQENEELKA 1136
Cdd:COG1196 334 eLEEELEELE-EELEEAEEELEEAEAELAEAEEALLE 369
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
901-1145 |
2.15e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.55 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 901 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFV--QQHQ------------------AE-------------KT 947
Cdd:pfam01576 548 KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdLDHQrqlvsnlekkqkkfdqmlAEekaisaryaeerdRA 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 948 ERENRLKEF----YTREYEKLRDTyIEEAEKYKMQLQEQFDNL--------NAAH--ETSKLEIEASHSE---KLELL-- 1008
Cdd:pfam01576 628 EAEAREKETralsLARALEEALEA-KEELERTNKQLRAEMEDLvsskddvgKNVHelERSKRALEQQVEEmktQLEELed 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1009 --------KKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDalneklksEEQKRRAREKANLKNpqim 1080
Cdd:pfam01576 707 elqatedaKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELE--------DERKQRAQAVAAKKK---- 774
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386876323 1081 yLEQELESLKAVLEIKNeKLHQQDIKLMKmeklvdnntALVDKLKRFQQENEELKARMDKHMAIS 1145
Cdd:pfam01576 775 -LELDLKELEAQIDAAN-KGREEAVKQLK---------KLQAQMKDLQRELEEARASRDEILAQS 828
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
952-1095 |
2.42e-04 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 44.62 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 952 RLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSE--KLELLKKAYEASLSEIKKGHEIEK-- 1027
Cdd:PRK06669 26 RFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEeaKEELLKKTDEASSIIEKLQMQIEReq 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876323 1028 -KSLEDLLSEKQESLEKQIND--LKSENDALNEKLKSEEQKRRAREKANLK-NPQIMYLEQELESLkaVLEI 1095
Cdd:PRK06669 106 eEWEEELERLIEEAKAEGYEEgyEKGREEGLEEVRELIEQLNKIIEKLIKKrEEILESSEEEIVEL--ALDI 175
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
979-1068 |
2.82e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 979 LQE----QFDNLNAAHETSKLEIEASH----SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESL---EKQIND 1047
Cdd:PRK05771 25 LHElgvvHIEDLKEELSNERLRKLRSLltklSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELekiEKEIKE 104
|
90 100
....*....|....*....|.
gi 1386876323 1048 LKSENDALNEKLKSEEQKRRA 1068
Cdd:PRK05771 105 LEEEISELENEIKELEQEIER 125
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
893-1146 |
3.07e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 45.17 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 893 REEALKQHKTLSQELVNLRGELV-TASTTC-------------EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEfyT 958
Cdd:pfam01576 287 RNKAEKQRRDLGEELEALKTELEdTLDTTAaqqelrskreqevTELKKALEEETRSHEAQLQEMRQKHTQALEELTE--Q 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 959 REYEKLRDTYIEEA----EKYKMQLQEQFDNLNAA-----HETSKL-----EIEASHSE----KLELLKKAYE------- 1013
Cdd:pfam01576 365 LEQAKRNKANLEKAkqalESENAELQAELRTLQQAkqdseHKRKKLegqlqELQARLSEserqRAELAEKLSKlqseles 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1014 --ASLSEI-KKGHEIEKK--SLEDLLSEKQE----------SLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQ 1078
Cdd:pfam01576 445 vsSLLNEAeGKNIKLSKDvsSLESQLQDTQEllqeetrqklNLSTRLRQLEDERNSLQEQLEEEEEAKRNVER------Q 518
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386876323 1079 IMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN-------NTALVDKL----KRFQQENEELKARMDKHMAISS 1146
Cdd:pfam01576 519 LSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEAltqqleeKAAAYDKLektkNRLQQELDDLLVDLDHQRQLVS 597
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
926-1073 |
3.12e-04 |
|
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: 43.00 E-value: 3.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 926 KARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYE----KLRDtyiEEAEKYKM--QLQEQFDNLNAAHETSKLEIEA 999
Cdd:pfam08614 20 EAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllaQLRE---ELAELYRSrgELAQRLVDLNEELQELEKKLRE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876323 1000 ShSEKLELLKkAYEASLseikkghEIEKKSLEDLLSEKQesleKQINDLKSENDALNEKLKSEEQKRRAREKAN 1073
Cdd:pfam08614 97 D-ERRLAALE-AERAQL-------EEKLKDREEELREKR----KLNQDLQDELVALQLQLNMAEEKLRKLEKEN 157
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
922-1102 |
3.20e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 44.64 E-value: 3.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARnelqtvyeafvQQHQAEKTERENRLKEF-----YTREYEKLRDTYIEEAEKYKMQLQEqfdnlnaaHETSKLE 996
Cdd:pfam15558 109 EKLERAR-----------QEAEQRKQCQEQRLKEKeeelqALREQNSLQLQERLEEACHKRQLKE--------REEQKKV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 997 IEASHSEKL--ELLKKAYEaslSEIKKGHEIEKKSLEDLLSEKQESLEKQIndlKSENDALNEK-LKSEEQKRRAREKAN 1073
Cdd:pfam15558 170 QENNLSELLnhQARKVLVD---CQAKAEELLRRLSLEQSLQRSQENYEQLV---EERHRELREKaQKEEEQFQRAKWRAE 243
|
170 180
....*....|....*....|....*....
gi 1386876323 1074 LKNpqimylEQELESLKAVLEIKNEKLHQ 1102
Cdd:pfam15558 244 EKE------EERQEHKEALAELADRKIQQ 266
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
969-1112 |
3.36e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 969 IEEAEKYKMQLQEQFDNLnaahetskleIEASHSEKLELLKKAYEASlsEIKKGHEIEKKSLEDLLSEKQESLEKQINDL 1048
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNEL----------IASLEELERELEQKAEEAE--ALLKEAEKLKEELEEKKEKLQEEEDKLLEEA 571
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876323 1049 KSE-NDALNE-KLKSEEQKRRAREKANLKNPQIMylEQELESLKAVLEIKNEKLHQQDIKLMKMEK 1112
Cdd:PRK00409 572 EKEaQQAIKEaKKEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
940-1135 |
3.60e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 45.13 E-value: 3.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 940 QQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHETSKLE---IEASHSEKLELLKKAYEASL 1016
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRKAEEAKK--AEEARIEEVMKLYEEEKKMKAEEAKKAEeakIKAEELKKAEEEKKKVEQLK 1639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1017 S----EIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSEndalnEKLKSEEQKRRAREKanlknpqimyLEQELESLKAV 1092
Cdd:PTZ00121 1640 KkeaeEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAE-----EAKKAEEDEKKAAEA----------LKKEAEEAKKA 1704
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1386876323 1093 LEIKnEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQEN----EELK 1135
Cdd:PTZ00121 1705 EELK-KKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDkkkaEEAK 1750
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
891-1100 |
3.89e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 891 SEREEALKQHKTLSQELVN----LRGELVTASTTCEKLEKARNELqtvyEAFVQQHQAEKTERENRLKEFyTREYEKLRD 966
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEeaesLREDADDLEERAEELREEAAEL----ESELEEAREAVEDRREEIEEL-EEEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 967 TY------IEEAEKYKMQLQEqfdNLNAAHETSKlEIEASHSEKLELLKKAyEASLSEIKK---GHEIEKKSLEDLLSEK 1037
Cdd:PRK02224 399 RFgdapvdLGNAEDFLEELRE---ERDELREREA-ELEATLRTARERVEEA-EALLEAGKCpecGQPVEGSPHVETIEED 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386876323 1038 QE---SLEKQINDLKSENDALNEKLKSEEQ-----KRRAREKANLKNpqimyLEQELESLKAVLEIKNEKL 1100
Cdd:PRK02224 474 RErveELEAELEDLEEEVEEVEERLERAEDlveaeDRIERLEERRED-----LEELIAERRETIEEKRERA 539
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
887-1137 |
4.94e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.40 E-value: 4.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 887 QHLLSEREEALKQHKTLSQEL-------VNLRGELVTASTTCEKLEKarnelqtvyEAFVQQHQAEKTERENRLKEFYTR 959
Cdd:pfam01576 92 QQLQNEKKKMQQHIQDLEEQLdeeeaarQKLQLEKVTTEAKIKKLEE---------DILLLEDQNSKLSKERKLLEERIS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 960 EYEklrDTYIEEAEKYKMqlqeqFDNLNAAHET--SKLEIEASHSEK----LELLKKAYEASLSEIKKGHEIEKKSLEDL 1033
Cdd:pfam01576 163 EFT---SNLAEEEEKAKS-----LSKLKNKHEAmiSDLEERLKKEEKgrqeLEKAKRKLEGESTDLQEQIAELQAQIAEL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1034 ---LSEKQESLE-----------------KQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVL 1093
Cdd:pfam01576 235 raqLAKKEEELQaalarleeetaqknnalKKIRELEAQISELQEDLESERAARNKAEK------QRRDLGEELEALKTEL 308
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1386876323 1094 E-IKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR 1137
Cdd:pfam01576 309 EdTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQK 353
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
886-1104 |
5.16e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 5.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 886 IQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVyeafvqQHQAEKTEREnrlkefytreyeklr 965
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELN---EEYNELQAELEAL------QAEIDKLQAE--------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 966 dtyIEEAEKYKMQLQEQFDNLNAA-----HETSKLE-IEASHS-----EKLELLKKAYEASLSEIKkgheiEKKSLEDLL 1034
Cdd:COG3883 74 ---IAEAEAEIEERREELGERARAlyrsgGSVSYLDvLLGSESfsdflDRLSALSKIADADADLLE-----ELKADKAEL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1386876323 1035 SEKQESLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQD 1104
Cdd:COG3883 146 EAKKAELEAKLAELEALKAELEAAKAElEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
867-1143 |
6.06e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 43.40 E-value: 6.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 867 QLKQLLACGNT---KFEALTVVIQHLLSEREEALKQHK-------TLSQELVNLRGELVTASTTCEKLEKARNELQTVYE 936
Cdd:pfam09728 5 ELMQLLNKLDSpeeKLAALCKKYAELLEEMKRLQKDLKklkkkqdQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 937 AFVQQHQAEKTERENRLKEFYTREYEKLRD--TYIEEAEKYKMQLQEQFDNLnaahetskleieashSEKLELLKKAYEa 1014
Cdd:pfam09728 85 KLKEESKKLAKEEEEKRKELSEKFQSTLKDiqDKMEEKSEKNNKLREENEEL---------------REKLKSLIEQYE- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1015 sLSEikkgheiekKSLEDLLseKQESLEKQINDLK-SENDALNEKLKSEEQKRRAREkanlKNPQIMYLEQELESLKAVL 1093
Cdd:pfam09728 149 -LRE---------LHFEKLL--KTKELEVQLAEAKlQQATEEEEKKAQEKEVAKARE----LKAQVQTLSETEKELREQL 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876323 1094 EIKNEKLHQ-QDIkLMK-----------MEKlvdnntaLVDKLKRFQQENEELKARMDKHMA 1143
Cdd:pfam09728 213 NLYVEKFEEfQDT-LNKsnevfttfkkeMEK-------MSKKIKKLEKENLTWKRKWEKSNK 266
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
849-1070 |
6.61e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 44.29 E-value: 6.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 849 LELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELvtasttcEKLEKAR 928
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-------EKLKREI 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 929 NELQtvyeafvqqhqaekterenrlkefytREYEKLRDTyieeaekyKMQLQEQFDNLNAAHETSKLEIEASHSEKLELL 1008
Cdd:TIGR02169 402 NELK--------------------------RELDRLQEE--------LQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1386876323 1009 K--KAYEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLKSENDALneklksEEQKRRARE 1070
Cdd:TIGR02169 448 LeiKKQEWKLEQLAADLSKYEQELYD-LKEEYDRVEKELSKLQRELAEA------EAQARASEE 504
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
846-1137 |
6.71e-04 |
|
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: 43.91 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 846 EKTLEltQYKTKCENQSGFILQLKQLLacgntkfEALTVVIQHLLSEREEALK------QHKTLSQELVNLRGELVTAST 919
Cdd:pfam05622 134 EATVE--TYKKKLEDLGDLRRQVKLLE-------ERNAEYMQRTLQLEEELKKanalrgQLETYKRQVQELHGKLSEESK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 920 TCEKLEKARNELQTVYEAFVQqhqaektERENRLKEfytreyeklRDTYIEEAEKYK-MQLQE----QFDNL-------- 986
Cdd:pfam05622 205 KADKLEFEYKKLEEKLEALQK-------EKERLIIE---------RDTLRETNEELRcAQLQQaelsQADALlspssdpg 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 987 -NAAHETSKLEIEashsEKLELLKKAYEAsLSEIKKGHEIEKK-SLEDLLSEKQESLEKqindLKSENDALNEKLKSEEQ 1064
Cdd:pfam05622 269 dNLAAEIMPAEIR----EKLIRLQHENKM-LRLGQEGSYRERLtELQQLLEDANRRKNE----LETQNRLANQRILELQQ 339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386876323 1065 K----RRAREKANLKNPQIMYLEQELESLKavleiknEKLHQQDIKLMKMEKLVDN--NTALVDKLKRFQQENEELKAR 1137
Cdd:pfam05622 340 QveelQKALQEQGSKAEDSSLLKQKLEEHL-------EKLHEAQSELQKKKEQIEElePKQDSNLAQKIDELQEALRKK 411
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
965-1146 |
6.96e-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: 43.89 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 965 RDTYIEEAEKYKMQLQEQFDNLNAAHEtsklEIEASHSEKLELLKKAyEASLSEIKKGHEIEKKSLEDLlSEKQESLEKQ 1044
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALA----ELRKELEELEEELEQL-RKELEELSRQISALRKDLARL-EAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1045 INDLKSENDALNEKLKSEEQKRrarEKANlknPQIMYLEQELESLKAV--------------LEIKNEKLHQQDIKLMKM 1110
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERL---EEAE---EELAEAEAEIEELEAQieqlkeelkalreaLDELRAELTLLNEEAANL 822
|
170 180 190
....*....|....*....|....*....|....*.
gi 1386876323 1111 EKLVDNNTALVDKLKRFQQENEELKARMDKHMAISS 1146
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLA 858
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
846-1152 |
7.01e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.74 E-value: 7.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 846 EKTLELTQ---YKTKCENQSGFILqlKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGEL--VTASTT 920
Cdd:pfam15964 350 EKTKALIQceqLKSELERQKERLE--KELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVekVTREKN 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 921 C--EKLEKARNELQT---------------VYEAFVQQHQAEKTERENRLK-----EFYTREYEKLRdtyiEEAEKYKMQ 978
Cdd:pfam15964 428 SlvSQLEEAQKQLASqemdvtkvcgemryqLNQTKMKKDEAEKEHREYRTKtgrqlEIKDQEIEKLG----LELSESKQR 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 979 L-QEQFDNLNAAHETSKLEIEASHSEK----LELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSEND 1053
Cdd:pfam15964 504 LeQAQQDAARAREECLKLTELLGESEHqlhlTRLEKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHDKTVNEQY 583
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1054 ALnekLKSEeqkrrarekanlkNPQIMYLEQELESLKAVLEIKNEKLHQqdiklmKMEKLVDNNTALVDKLKRFQQENEE 1133
Cdd:pfam15964 584 SL---LTSQ-------------NTFIAKLKEECCTLAKKLEEITQKSRS------EVEQLSQEKEYLQDRLEKLQKRNEE 641
|
330
....*....|....*....
gi 1386876323 1134 LKARMDKHMAISSFPRSRL 1152
Cdd:pfam15964 642 LEEQCVQHGRMHERMKQRL 660
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
994-1112 |
7.39e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.92 E-value: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 994 KLEIEASHSEKLELlkkayEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE----EQKRRAR 1069
Cdd:COG0542 403 RMEIDSKPEELDEL-----ERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEkeliEEIQELK 477
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876323 1070 EKANLKNPQIMYLEQELESLKAVLEIKNEKLHQ----QDI---------------------KLMKMEK 1112
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREevteEDIaevvsrwtgipvgkllegereKLLNLEE 545
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
978-1134 |
8.31e-04 |
|
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: 43.58 E-value: 8.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 978 QLQEQFDNLNAAHETSKLEIEaSHSEKLELLKKAYEASLS---EIKKGHEIEK--KSLEDLLSEKQESLEKQI--NDLKS 1050
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELE-HKRARIELEKKASALKRQldrESDRNQELQKriRLLEKREAEAEEALREQAelNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1051 EN-DALNEKLKSEEQKR-RARE-KANLKNP------QIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALV 1121
Cdd:pfam05557 83 KYlEALNKKLNEKESQLaDAREvISCLKNElselrrQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170
....*....|...
gi 1386876323 1122 DKLKRFQQENEEL 1134
Cdd:pfam05557 163 SSLAEAEQRIKEL 175
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
926-1137 |
8.33e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 926 KARNELQTVYEAfvQQHQAEKTERENRLKEfytreYEKLRDTYIEEAEKYKMQLQEQfdnlnaahetskleIEASHSEKL 1005
Cdd:pfam13868 32 KRIKAEEKEEER--RLDEMMEEERERALEE-----EEEKEEERKEERKRYRQELEEQ--------------IEEREQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1006 EllkkAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINdLKSENDALNEKLKSEEQKRRAREK-ANLKNpqimyleq 1084
Cdd:pfam13868 91 E----EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQ-LREEIDEFNEEQAEWKELEKEEEReEDERI-------- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1386876323 1085 eLESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR 1137
Cdd:pfam13868 158 -LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAK 209
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
969-1140 |
8.94e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 43.51 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 969 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShsEKLELLKKAYEASLSEIKkgHEI-EKKSLEDLLSEKQESLEKQIND 1047
Cdd:PRK03918 157 LDDYENAYKNLGEVIKEIKRRIERLEKFIKRT--ENIEELIKEKEKELEEVL--REInEISSELPELREELEKLEKEVKE 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1048 LKSENDALNE--KLKSEEQKRRAREKANLKN--PQIMYLEQELESL----KAVLEIK---------NEKLHQQDIKLMKM 1110
Cdd:PRK03918 233 LEELKEEIEEleKELESLEGSKRKLEEKIREleERIEELKKEIEELeekvKELKELKekaeeyiklSEFYEEYLDELREI 312
|
170 180 190
....*....|....*....|....*....|
gi 1386876323 1111 EKLVDNNTALVDKLKRFQQENEELKARMDK 1140
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEE 342
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
890-1139 |
1.08e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 890 LSEREEALKQhKTLSQELV-----NLRGElvtASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKL 964
Cdd:PRK04778 34 LEERKQELEN-LPVNDELEkvkklNLTGQ---SEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEELNDKFRFRKAKHEINE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 965 RDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAshseklelLKKAYEaslsEIKKghEIEKKSleDLLSEKQESLEKQ 1044
Cdd:PRK04778 110 IESLLDLIEEDIEQILEELQELLESEEKNREEVEQ--------LKDLYR----ELRK--SLLANR--FSFGPALDELEKQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1045 INDLKSE---NDALNEK---LKSEEQKRRAREK-ANLKN-----PQIMY-----LEQELESLKAVL-EIKNEKLHQQDIK 1106
Cdd:PRK04778 174 LENLEEEfsqFVELTESgdyVEAREILDQLEEElAALEQimeeiPELLKelqteLPDQLQELKAGYrELVEEGYHLDHLD 253
|
250 260 270
....*....|....*....|....*....|....*....
gi 1386876323 1107 LMKM-----EKLVDNNTALVD-KLKRFQQENEELKARMD 1139
Cdd:PRK04778 254 IEKEiqdlkEQIDENLALLEElDLDEAEEKNEEIQERID 292
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
922-1176 |
1.16e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTV----YEAFVQQHQAEKTERE-----NRL--------KEFYTREYEKLRDTyIEEAEKYKMQLQEQFD 984
Cdd:PRK04863 840 RQLNRRRVELERAladhESQEQQQRSQLEQAKEglsalNRLlprlnllaDETLADRVEEIREQ-LDEAEEAKRFVQQHGN 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 985 NLnaahetSKLEIEA----SHSEKLELLKKAY---EASLSEIKKGheieKKSLEDLLSEKQE-SLEKQINDLkSENDALN 1056
Cdd:PRK04863 919 AL------AQLEPIVsvlqSDPEQFEQLKQDYqqaQQTQRDAKQQ----AFALTEVVQRRAHfSYEDAAEML-AKNSDLN 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1057 EKLK-----SEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEklhqqdiklmkmeklvdnntalvdKLKRFQQEN 1131
Cdd:PRK04863 988 EKLRqrleqAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQ------------------------MLQELKQEL 1043
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1386876323 1132 EELKARMDKHMAI-SSFPRSRLFCKSRWRRSRKStsdSLWKTRSFC 1176
Cdd:PRK04863 1044 QDLGVPADSGAEErARARRDELHARLSANRSRRN---QLEKQLTFC 1086
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
850-1133 |
1.19e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 43.35 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 850 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHllsereeALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 929
Cdd:PRK01156 191 KLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN-------AMDDYNNLKSALNELSSLEDMKNRYESEIKTAES 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 930 ELQTVYEAFVQQhqAEKTERENRL---KEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKleieashseKLE 1006
Cdd:PRK01156 264 DLSMELEKNNYY--KELEERHMKIindPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIK---------KLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1007 LLKKAYEAslseikkgHEIEKKSLEDLlsekqeslEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQI-MYLEQE 1085
Cdd:PRK01156 333 VLQKDYND--------YIKKKSRYDDL--------NNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsAFISEI 396
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1386876323 1086 LESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE 1133
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSR 444
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
886-1091 |
1.46e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.59 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 886 IQHLLSEREEALKQhktLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAfvQQHQAEKteRENRLKEFYTREYEKLR 965
Cdd:pfam04012 13 IHEGLDKAEDPEKM---LEQAIRDMQSELVKARQALAQTIARQKQLERRLEQ--QTEQAKK--LEEKAQAALTKGNEELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 966 DTYIEEAEKYKMQ---LQEQFDNLNAAHETSKLEIEASHS--EKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES 1040
Cdd:pfam04012 86 REALAEKKSLEKQaeaLETQLAQQRSAVEQLRKQLAALETkiQQLKAKKNLLKARLKAAKAQEAVQTSLGSLSTSSATDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876323 1041 LEK---QINDLKSENDALNE--KLKSEEQKRRArEKANLKNPqimylEQELESLKA 1091
Cdd:pfam04012 166 FERieeKIEEREARADAAAElaSAVDLDAKLEQ-AGIQMEVS-----EDVLARLKA 215
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
923-1152 |
1.66e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 923 KLEKARNELQTVYEAFVQQHQAEKTERENR---LKEFYTREYEKLRDTYIEEaeKYKMQLQEQFDNLNAAHETSKLEIEA 999
Cdd:COG5022 814 SYLACIIKLQKTIKREKKLRETEEVEFSLKaevLIQKFGRSLKAKKRFSLLK--KETIYLQSAQRVELAERQLQELKIDV 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1000 SHSEKLELLKKAYEASLSEIKKghEIEKKSLEDL--LSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLK-- 1075
Cdd:COG5022 892 KSISSLKLVNLELESEIIELKK--SLSSDLIENLefKTELIARLKKLLNNIDLEEGPSIEYVKLPELNKLHEVESKLKet 969
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876323 1076 NPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISSFPRSRL 1152
Cdd:COG5022 970 SEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPVEVAELQSASKIISSESTELSILK 1046
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
867-1011 |
1.93e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 867 QLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTC------EKLEKARNELQTVYEAfVQ 940
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeleEELEELEEELEELEEE-LE 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876323 941 QHQAEKTERENRLKEFYT-REYEKLRDTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEASHSEKL-ELLKKA 1011
Cdd:COG4717 450 ELREELAELEAELEQLEEdGELAELLQELEELKAELR-ELAEEWAALKLALELLEEAREEYREERLpPVLERA 521
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
893-1139 |
2.07e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 42.25 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 893 REEALKQHKTLSQELVNLRGELVTA-STTCEKLE--KARNELQTVYEAFVQQHQA--EKTERENRLKEFYT------REY 961
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIKQfENTKEKIAeyTKSIDIKKATESLEEQLAAaeAEQELEESKRETETgiqnltAEI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 962 EKLRDTYIEEAEKYKM------------QLQEQFDNLNAAHETSKLEIEASH---SEKLELLKKAYEASLSEIKKGHEIE 1026
Cdd:COG5185 346 EQGQESLTENLEAIKEeienivgevelsKSSEELDSFKDTIESTKESLDEIPqnqRGYAQEILATLEDTLKAADRQIEEL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1027 KKSLEDLLSEKQES------LEKQINDLKSENDALNEKLKSEEQK---RRAREKANLKNPQIMYLEQELESLKAVLEIKN 1097
Cdd:COG5185 426 QRQIEQATSSNEEVskllneLISELNKVMREADEESQSRLEEAYDeinRSVRSKKEDLNEELTQIESRVSTLKATLEKLR 505
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1386876323 1098 EKLHQQdikLMKMEKLVDNNTALVDKLKRFQQENEELKARMD 1139
Cdd:COG5185 506 AKLERQ---LEGVRSKLDQVAESLKDFMRARGYAHILALENL 544
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
901-1143 |
2.11e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.51 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 901 KTLSQELVNLRGELVtasttcEKLEKARNELQTvyEAFVQQHqaEKTERENRLKEFYTREYEKLRDTYIEEaekYKMQLQ 980
Cdd:PTZ00440 896 KQLVEHLLNNKIDLK------NKLEQHMKIINT--DNIIQKN--EKLNLLNNLNKEKEKIEKQLSDTKINN---LKMQIE 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 981 EQFDnlnaAHETSKLEIEA---SHSEKLELLKKAYEASLSEIKK---GHEIEKKSLEDLLSE-KQESLEKQINDLKSEND 1053
Cdd:PTZ00440 963 KTLE----YYDKSKENINGndgTHLEKLDKEKDEWEHFKSEIDKlnvNYNILNKKIDDLIKKqHDDIIELIDKLIKEKGK 1038
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1054 ALNEKLKSeeqkrrarekanlknpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE 1133
Cdd:PTZ00440 1039 EIEEKVDQ----------------YISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIE 1102
|
250
....*....|
gi 1386876323 1134 LKARMDKHMA 1143
Cdd:PTZ00440 1103 IKNKSHEHVV 1112
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
877-1072 |
2.16e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.74 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 877 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeAFVQQHQAEKTERENRLKEF 956
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ----AEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 957 YTREYEKLRD-TYIE---EAEKYKmQLQEQFDNLNAAHETSKLEIEASHSEKLELlkKAYEASLSEIKKGHEIEKKSLED 1032
Cdd:COG3883 92 ARALYRSGGSvSYLDvllGSESFS-DFLDRLSALSKIADADADLLEELKADKAEL--EAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1386876323 1033 LLSE---KQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1072
Cdd:COG3883 169 AKAEleaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
890-1102 |
2.24e-03 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 40.89 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 890 LSEREEALKQHKTLSQELVNLRGELvtasttceklekarNELQTVYEAFVQQHQAEKTERENRLKEFyTREYEKLRDTYI 969
Cdd:cd00176 32 LESVEALLKKHEALEAELAAHEERV--------------EALNELGEQLIEEGHPDAEEIQERLEEL-NQRWEELRELAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 970 EEAEKYK--MQLQEQFDNLnaahetskLEIEASHSEKlellkkayEASLSEIKKGHEIEkkSLEDLLsEKQESLEKQIND 1047
Cdd:cd00176 97 ERRQRLEeaLDLQQFFRDA--------DDLEQWLEEK--------EAALASEDLGKDLE--SVEELL-KKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1386876323 1048 LKSENDALNEKLKSEEQKRRAREKANLKNPQIMyLEQELESLKAVLEIKNEKLHQ 1102
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEE-LNERWEELLELAEERQKKLEE 211
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1030-1171 |
2.42e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.81 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1030 LEDLLSEKQESLEKQINDLKSENDALNEKLK-SEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLM 1108
Cdd:COG4372 25 LIAALSEQLRKALFELDKLQEELEQLREELEqAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876323 1109 KMEklvDNNTALVDKLKRFQQENEELKARMDKHMAISSFPRSRLFCKSRWRRSRKSTSDSLWK 1171
Cdd:COG4372 105 SLQ---EEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1008-1130 |
2.44e-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: 40.66 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1008 LKKAYEASLSEIKKGH-EIEKKSLEDL---------LSEKQESLEKQINDLKSENDALNEKLKsEEQKRRAREKANLKNP 1077
Cdd:pfam13851 2 LMKNHEKAFNEIKNYYnDITRNNLELIkslkeeiaeLKKKEERNEKLMSEIQQENKRLTEPLQ-KAQEEVEELRKQLENY 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876323 1078 QimYLEQELESLKAVLEIKNEKL----HQQDIKLMKMEKLVDNNTALVDKLKRFQQE 1130
Cdd:pfam13851 81 E--KDKQSLKNLKARLKVLEKELkdlkWEHEVLEQRFEKVERERDELYDKFEAAIQD 135
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
922-1102 |
2.85e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 41.44 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYE-KLRDTYIEEAEKYKMQLQEqfdnLNAAHETSKLEIEAS 1000
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQErKERQKEREEAEKKARQRQE----LQQAREEQIELKERR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1001 HSEKLELLKKAYEASLSEIKKGHEIEKKSLED---LLSEKQESLEKQINdlksendalneklksEEQKRRAREKANLKNP 1077
Cdd:pfam13868 252 LAEEAEREEEEFERMLRKQAEDEEIEQEEAEKrrmKRLEHRRELEKQIE---------------EREEQRAAEREEELEE 316
|
170 180
....*....|....*....|....*
gi 1386876323 1078 QIMYLEQELESLKAVLEIKNEKLHQ 1102
Cdd:pfam13868 317 GERLREEEAERRERIEEERQKKLKE 341
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
940-1085 |
3.27e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 41.48 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 940 QQHQAEKTERENRLKEFYTREYEK------LRDTYIE------EAEKYKMQLQEQfdnlnAAHETSKLEIEASHSEKLEL 1007
Cdd:pfam15709 361 RRLQQEQLERAEKMREELELEQQRrfeeirLRKQRLEeerqrqEEEERKQRLQLQ-----AAQERARQQQEEFRRKLQEL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1008 LKKAYEASLsEIKKGHEIEKKSLEDLLSEKQ---------ESLEKQINDLKSENDAlneKLKSEEQKRRAREKANLKNPQ 1078
Cdd:pfam15709 436 QRKKQQEEA-ERAEAEKQRQKELEMQLAEEQkrlmemaeeERLEYQRQKQEAEEKA---RLEAEERRQKEEEAARLALEE 511
|
....*..
gi 1386876323 1079 IMYLEQE 1085
Cdd:pfam15709 512 AMKQAQE 518
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1004-1112 |
3.33e-03 |
|
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil domain of unknwon function.
Pssm-ID: 464003 [Multi-domain] Cd Length: 119 Bit Score: 38.70 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1004 KLELLKKAYEASLSEIKKgheiekksLEDLLSEKQESLEKQINDLKSENDALNEKLK-SEEQKRRAREKANLKNPQIMYL 1082
Cdd:pfam13863 7 EMFLVQLALDAKREEIER--------LEELLKQREEELEKKEQELKEDLIKFDKFLKeNDAKRRRALKKAEEETKLKKEK 78
|
90 100 110
....*....|....*....|....*....|
gi 1386876323 1083 EQELESLKAVLEIKNEKLHQQDIKLMKMEK 1112
Cdd:pfam13863 79 EKEIKKLTAQIEELKSEISKLEEKLEEYKP 108
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
922-1104 |
3.45e-03 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 40.75 E-value: 3.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTVYE---AFVQQHQAEKTErenrlkefyTREYEKLrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIE 998
Cdd:pfam12795 9 KLDEAAKKKLLQDLQqalSLLDKIDASKQR---------AAAYQKA----LDDAPAELRELRQELAALQAKAEAAPKEIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 999 ASHS-EKLELLKKAYEASLSEIKKgheiEKKSLEDLLSEKQESLE---KQINDLKSENDALNEKLK---------SEEQK 1065
Cdd:pfam12795 76 ASLSlEELEQRLLQTSAQLQELQN----QLAQLNSQLIELQTRPEraqQQLSEARQRLQQIRNRLNgpappgeplSEAQR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1386876323 1066 RRAREKANLKNPQIMYLEQELES-------LKAVLEIKNEKLHQQD 1104
Cdd:pfam12795 152 WALQAELAALKAQIDMLEQELLSnnnrqdlLKARRDLLTLRIQRLE 197
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
924-1133 |
3.49e-03 |
|
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: 41.96 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 924 LEKARNELQTVyeafVQQHQAEKTERENRLKEFYTR---EYEKLRdtyieeaekykmqlqeqfdnlNAAHETSKLEIEAS 1000
Cdd:TIGR01612 673 IDALYNELSSI----VKENAIDNTEDKAKLDDLKSKidkEYDKIQ---------------------NMETATVELHLSNI 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1001 HSEKLELLkkayeASLSEIKKG--HEIEK---KSLEDLLSeKQESLEKQINDLKSENDALNE-KLKSEEQKRRAREKANL 1074
Cdd:TIGR01612 728 ENKKNELL-----DIIVEIKKHihGEINKdlnKILEDFKN-KEKELSNKINDYAKEKDELNKyKSKISEIKNHYNDQINI 801
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1386876323 1075 KNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE 1133
Cdd:TIGR01612 802 DNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKE 860
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
924-1134 |
3.64e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 40.04 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 924 LEKARNELQTV-YEAFVQQHQAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLnaahetsKLEIEASHS 1002
Cdd:pfam05010 10 LEKARNEIEEKeLEINELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKV-------LEEKDQALA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1003 EKLELlkkayEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLKsendalnEKLKSEEQ-----KRRAREKANLKNP 1077
Cdd:pfam05010 83 DLNSV-----EKSFSDLFKRYEKQKEVISG-YKKNEESLKKCAQDYL-------ARIKKEEQryqalKAHAEEKLDQANE 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876323 1078 QIMYLEQELESLKAVLEIkneKLHQQDIKLMKMEKLVDNNTalvdklkrfqQENEEL 1134
Cdd:pfam05010 150 EIAQVRSKAKAETAALQA---SLRKEQMKVQSLERQLEQKT----------KENEEL 193
|
|
| Ctf13_LRR_LRR-insertion |
cd19611 |
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein ... |
1015-1102 |
3.99e-03 |
|
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein complex CBF3 subunit C (Ctf13); Ctf13, is an F-box protein of the leucine-rich-repeat superfamily; it is a component of CEN binding factor 3 (CBF3), a complex that recognizes point centromeres found in budding yeast, associating specifically with the third centromere DNA element (CDEIII) DNA. CBF3 is comprised of two homodimers of Cep3 and Ndc10, and a Ctf13-Skp1 heterodimer. The Skp1-Ctf13 heterodimer interacts with Cep3, Ndc10 and CDEIII at a completely conserved G, centrally positioned between the TGC/CCG sites. The eight leucine-rich repeat (LRR) motifs of Ctf13 (LRR 1-8) form a solenoid structure. At the N-terminus of the Ctf13 LRR is an expanded F-box, and at the C-terminal end, an alpha-beta domain formed by insertions within the latter LRRs of Ctf13 (LRR insertion domain). This domain model includes the LLR domain and the LRR insertion domain.
Pssm-ID: 381623 Cd Length: 290 Bit Score: 40.78 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1015 SLSEIKK-GHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK--A 1091
Cdd:cd19611 14 NPNMVKKiLKVLEKKELLDLVSEVFFGQDEEESDEEDEDDSSKNDRKKLTDDDVKEKSYKLNDPSIIRIISSLESMKnlR 93
|
90
....*....|.
gi 1386876323 1092 VLEIKNEKLHQ 1102
Cdd:cd19611 94 KLSVRGDNLYE 104
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
890-1137 |
4.21e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.48 E-value: 4.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 890 LSEREEALKQHKTLSQELVNLRGEL-VTASTTCEKLEKARNELQTVYEAF-VQQ------HQA----EKTERENRLKEFy 957
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENeARAEAAEEEVDELKSQLADYQQALdVQQtraiqyQQAvqalERAKQLCGLPDL- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 958 trEYEKLRDtYIEEaekYKMQLQEQFDNLNAAHEtsKLEIEASHSEKLEllkKAYEASLS-----EIKKGHEIEKKSLED 1032
Cdd:PRK04863 436 --TADNAED-WLEE---FQAKEQEATEELLSLEQ--KLSVAQAAHSQFE---QAYQLVRKiagevSRSEAWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1033 LlsEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQdiklmkMEK 1112
Cdd:PRK04863 505 L--REQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES------VSE 576
|
250 260
....*....|....*....|....*
gi 1386876323 1113 LVDNNTALVDKLKRFQQENEELKAR 1137
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAAR 601
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
922-1136 |
4.29e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.67 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKmQLQEQFDNLNAAHETSKLEIEASH 1001
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK-AEEAKKAD-EAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1002 SEklELLKKAYEASLS-EIKKGHEIEKKSLEDLlsEKQESLEKQINDL-KSENDALNEKLKSEEQKRRARE--KA-NLKN 1076
Cdd:PTZ00121 1472 AD--EAKKKAEEAKKAdEAKKKAEEAKKKADEA--KKAAEAKKKADEAkKAEEAKKADEAKKAEEAKKADEakKAeEKKK 1547
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1386876323 1077 PQIMYLEQELESLKAVLEIKNEKLHQQD--IKLMKMEKLVDNNTALVDKLKRFQQENEELKA 1136
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
886-1176 |
4.87e-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: 41.48 E-value: 4.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 886 IQHLLSEREEALKQHKT----LSQELVNLRG-----ELVTASTTCEKLEKARNELQTVYEA--FVQQHQaektereNRLk 954
Cdd:COG3096 848 LERELAQHRAQEQQLRQqldqLKEQLQLLNKllpqaNLLADETLADRLEELREELDAAQEAqaFIQQHG-------KAL- 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 955 efytREYEKLRDTyieeaekykmqLQ---EQFDNLNAAHETSKleieashsEKLELLKKAYEAsLSEIKKgheiekkSLE 1031
Cdd:COG3096 920 ----AQLEPLVAV-----------LQsdpEQFEQLQADYLQAK--------EQQRRLKQQIFA-LSEVVQ-------RRP 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1032 DLLSEKQESLEKQINDLkseNDALNEKLKSEEQKR-RAREKANLKNPQIMYLEQELESLKAVLEIKNeklhqqdiklmkm 1110
Cdd:COG3096 969 HFSYEDAVGLLGENSDL---NEKLRARLEQAEEARrEAREQLRQAQAQYSQYNQVLASLKSSRDAKQ------------- 1032
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876323 1111 eklvdnntalvDKLKRFQQENEELKARMDKHMAISS-FPRSRLFCKSRWRRSRKStsdSLWKTRSFC 1176
Cdd:COG3096 1033 -----------QTLQELEQELEELGVQADAEAEERArIRRDELHEELSQNRSRRS---QLEKQLTRC 1085
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1003-1117 |
4.94e-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: 40.39 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1003 EKLELLKKAYEaslsEIKKgHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQkrRAREKANLKNPQIMY- 1081
Cdd:smart00787 151 ENLEGLKEDYK----LLMK-ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD--RAKEKLKKLLQEIMIk 223
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1386876323 1082 ------LEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNN 1117
Cdd:smart00787 224 vkkleeLEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQC 265
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
882-1140 |
5.10e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 40.88 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 882 LTVVIQHLLSEREEalkqhkTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTEREnRLKEFYTREY 961
Cdd:pfam05557 273 LNLRSPEDLSRRIE------QLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLK-RHKALVRRLQ 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 962 EKLRdTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEasHSEKLELLKKAYEASLSEIKkgHEIEKkSLEDLLSEKQ--E 1039
Cdd:pfam05557 346 RRVL-LLTKERDGYR-AILESYDKELTMSNYSPQLLE--RIEEAEDMTQKMQAHNEEME--AQLSV-AEEELGGYKQqaQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1040 SLEKQINDLKSENDaLNEKLKSEEQKRRARekanLKNPQIMYLEQELESLKAVLEIKNEKLHQQ---DIKLMKMEKLVDN 1116
Cdd:pfam05557 419 TLERELQALRQQES-LADPSYSKEEVDSLR----RKLETLELERQRLREQKNELEMELERRCLQgdyDPKKTKVLHLSMN 493
|
250 260
....*....|....*....|....*....
gi 1386876323 1117 NTALV-----DKLKRFQQENEELKARMDK 1140
Cdd:pfam05557 494 PAAEAyqqrkNQLEKLQAEIERLKRLLKK 522
|
|
| flagell_FliJ |
TIGR02473 |
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly ... |
1026-1149 |
5.37e-03 |
|
flagellar export protein FliJ; Members of this family are the FliJ protein found, in nearly every case, in the midst of other flagellar biosynthesis genes in bacgterial genomes. Typically the fliJ gene is found adjacent to the gene for the flagellum-specific ATPase FliI. Sequence scoring in the gray zone between trusted and noise cutoffs include both probable FliJ proteins and components of bacterial type III secretion systems.
Pssm-ID: 131526 [Multi-domain] Cd Length: 141 Bit Score: 38.45 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1026 EKKSLEDL--LSEKQESLEKQINDLKSENDALNEKLKSE--------EQKRRAREKANLKNpQIMYLEQELESLKAVLEI 1095
Cdd:TIGR02473 15 EEQAKLELakAQAEFERLETQLQQLIKYREEYEQQALEKvgagtsalELSNYQRFIRQLDQ-RIQQQQQELALLQQEVEA 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1386876323 1096 KNEKLHQQDIKLMKMEKLVDNntalvdKLKRFQQENEELKARMDKHMAISSFPR 1149
Cdd:TIGR02473 94 KRERLLEARRELKALEKLKEK------KQKEYRAEEAKREQKEMDELATQRFRR 141
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
922-1143 |
5.71e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 41.28 E-value: 5.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARnELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASH 1001
Cdd:PTZ00121 1293 DEAKKAE-EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK-AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAE 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1002 SEKLELLKKAYEAS--LSEIKKGHEIEKKSLED-----------LLSEKQESLEKQINDLKSENDA---LNEKLKSEEQK 1065
Cdd:PTZ00121 1371 KKKEEAKKKADAAKkkAEEKKKADEAKKKAEEDkkkadelkkaaAAKKKADEAKKKAEEKKKADEAkkkAEEAKKADEAK 1450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1066 RRAREKANLKNpqimyLEQELESLKAVLEIKneKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQEN---EELKARMDKHM 1142
Cdd:PTZ00121 1451 KKAEEAKKAEE-----AKKKAEEAKKADEAK--KKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKkkaDEAKKAEEAKK 1523
|
.
gi 1386876323 1143 A 1143
Cdd:PTZ00121 1524 A 1524
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
947-1141 |
5.99e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 40.28 E-value: 5.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 947 TERENRLKEFYT------REYEKLRDTYIEEAEKYKmqlqEQFDNLNAahETSKLeieashSEKLELLKKAYEASLSEIK 1020
Cdd:COG1340 7 SSSLEELEEKIEelreeiEELKEKRDELNEELKELA----EKRDELNA--QVKEL------REEAQELREKRDELNEKVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1021 kgheiEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRarekanlknpQIMYLEQELESlkAVLEIKNEKl 1100
Cdd:COG1340 75 -----ELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRK----------EIERLEWRQQT--EVLSPEEEK- 136
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1386876323 1101 hqqdiklmkmeklvdnntALVDKLKRFQQENEELKARMDKH 1141
Cdd:COG1340 137 ------------------ELVEKIKELEKELEKAKKALEKN 159
|
|
| PRK14160 |
PRK14160 |
heat shock protein GrpE; Provisional |
1026-1140 |
6.00e-03 |
|
heat shock protein GrpE; Provisional
Pssm-ID: 237629 [Multi-domain] Cd Length: 211 Bit Score: 39.74 E-value: 6.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1026 EKKSLEDLLSEKQESLEKQiNDLKSENDALNEKLKSEEQKrrAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQdi 1105
Cdd:PRK14160 2 EKECKDAKHENMEEDCCKE-NENKEEDKGKEEDLEFEEIE--KEEIIEDSEESNEVKIEELKDENNKLKEENKKLENE-- 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1386876323 1106 klmkMEklvdnntALVDKLKRFQQENEELKARMDK 1140
Cdd:PRK14160 77 ----LE-------ALKDRLLRTVAEYDNYRKRTAK 100
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
846-1071 |
6.22e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.81 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 846 EKTLELTQYKTkcENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLE 925
Cdd:TIGR02168 837 ERRLEDLEEQI--EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 926 KARNELQTvyeafvQQHQAEktERENRLkefytreyeklrdtyieeaekyKMQLQEQFDNLNAAHETSkLEIEASHSEKL 1005
Cdd:TIGR02168 915 RELEELRE------KLAQLE--LRLEGL----------------------EVRIDNLQERLSEEYSLT-LEEAEALENKI 963
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876323 1006 ELLKKAYEASLSEIKKghEIEK------KSLEDL--LSEKQESLEKQINDLkseNDALnEKLKS--EEQKRRAREK 1071
Cdd:TIGR02168 964 EDDEEEARRRLKRLEN--KIKElgpvnlAAIEEYeeLKERYDFLTAQKEDL---TEAK-ETLEEaiEEIDREARER 1033
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
936-1136 |
6.61e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 6.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 936 EAFVQQHQAEKT---ERENRLKEFYtREYEKLRDTYIEEAEKYKM--QLQEQFDNLNAAHET-SKLEIEASH------SE 1003
Cdd:COG4913 210 DDFVREYMLEEPdtfEAADALVEHF-DDLERAHEALEDAREQIELlePIRELAERYAAARERlAELEYLRAAlrlwfaQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1004 KLELLKKAYEASLSEIKKgHEIEKKSLEDLLSEKQESLE-----------KQINDLKSENDALNEKLKSEEQKRRAREKA 1072
Cdd:COG4913 289 RLELLEAELEELRAELAR-LEAELERLEARLDALREELDeleaqirgnggDRLEQLEREIERLERELEERERRRARLEAL 367
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876323 1073 ----NLKNPQImylEQELESLKAVLEIKNEKLHQQDiklmkmEKLVDNNTALVDKLKRFQQENEELKA 1136
Cdd:COG4913 368 laalGLPLPAS---AEEFAALRAEAAALLEALEEEL------EALEEALAEAEAALRDLRRELRELEA 426
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
897-1144 |
7.45e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 40.97 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 897 LKQHKTLSQELVNLRGELVTasttcEKLEKARNELQTVYEafvqQHQAEKTERENRLKEfYTREYEKLRD---TYIEEAE 973
Cdd:PTZ00440 690 IKNLKKELQNLLSLKENIIK-----KQLNNIEQDISNSLN----QYTIKYNDLKSSIEE-YKEEEEKLEVykhQIINRKN 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 974 KYKMQLQEQFDNLNAAHETSK---------LEIEASHSEKLELLKKAYEASLSEIKKgHEIEKKSLEDLLSEKQESLEKQ 1044
Cdd:PTZ00440 760 EFILHLYENDKDLPDGKNTYEeflqykdtiLNKENKISNDINILKENKKNNQDLLNS-YNILIQKLEAHTEKNDEELKQL 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 1045 INDLKSENDALNEKlKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKlhqqdiklmkmeklvDNNTALVDKL 1124
Cdd:PTZ00440 839 LQKFPTEDENLNLK-ELEKEFNENNQIVDNIIKDIENMNKNINIIKTLNIAINRS---------------NSNKQLVEHL 902
|
250 260
....*....|....*....|
gi 1386876323 1125 KRFQQeneELKARMDKHMAI 1144
Cdd:PTZ00440 903 LNNKI---DLKNKLEQHMKI 919
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
922-1061 |
8.31e-03 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 40.51 E-value: 8.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876323 922 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRdtyieeaEKYKMQLQEQFDNLNAAHEtSKLEiEASH 1001
Cdd:pfam09731 316 RALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEIR-------ESYEEKLRTELERQAEAHE-EHLK-DVLV 386
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1386876323 1002 SEKLELlkkayeaslsEIKKGHEIEKKSLE--DLLSEKQESLEKQINDLK----SENDALNEKLKS 1061
Cdd:pfam09731 387 EQEIEL----------QREFLQDIKEKVEEerAGRLLKLNELLANLKGLEkatsSHSEVEDENRKA 442
|
|
| |
