|
Name |
Accession |
Description |
Interval |
E-value |
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
865-1161 |
5.80e-15 |
|
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: 80.49 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 865 ILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTAST----TCEKLEKARNELQTVyEAFVQ 940
Cdd:TIGR02168 672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRqisaLRKDLARLEAEVEQL-EERIA 750
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 941 QHQAEKTERENRLKEfYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAY---EASLS 1017
Cdd:TIGR02168 751 QLSKELTELEAEIEE-LEERLEEAEEE-LAEAEAEIEELEAQIEQLKEELKALREALDELRAE-LTLLNEEAanlRERLE 827
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1018 EIKKGHEIEKKSLEDL------LSEKQESLEKQINDLKSE--------NDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1083
Cdd:TIGR02168 828 SLERRIAATERRLEDLeeqieeLSEDIESLAAEIEELEELieeleselEALLNERASLEEALALLRSELEELSEELRELE 907
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348617 1084 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNtalvdklkrFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 1161
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNL---------QERLSEEYSLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
892-1178 |
8.42e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 73.05 E-value: 8.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 892 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFY-----------TRE 960
Cdd:COG1196 226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYellaelarleqDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 961 YEKLRdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES 1040
Cdd:COG1196 306 RLEER---RRELEERLEELEEELAELEEELEELEEELEEL-EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1041 LEKQINDLKSENDALNEKLKSEE----QKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1116
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEEleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50348617 1117 NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLW 1178
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
889-1164 |
1.52e-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: 72.40 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 889 LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQ---------QHQAEKTERENRLKEFYTR 959
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANeisrleqqkQILRERLANLERQLEELEA 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 960 EYEKL---RDTYIEEA---EKYKMQLQEQFDNLNAAHETSKLEIEASHSeKLELLKKAYEASLSEIkkgHEIEKKslEDL 1033
Cdd:TIGR02168 324 QLEELeskLDELAEELaelEEKLEELKEELESLEAELEELEAELEELES-RLEELEEQLETLRSKV---AQLELQ--IAS 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1034 LSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKL 1113
Cdd:TIGR02168 398 LNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQA-ELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348617 1114 VDnntALVDKLKRFQQENEELKARMDKHMAISR----------QLSTEQAVLQESLEKESK 1164
Cdd:TIGR02168 477 LD---AAERELAQLQARLDSLERLQENLEGFSEgvkallknqsGLSGILGVLSELISVDEG 534
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
886-1176 |
2.12e-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: 72.01 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 886 IQHLLSEREEALKqHKTLSQELVNLRGELVTASTtcEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEfytreyeklr 965
Cdd:TIGR02168 202 LKSLERQAEKAER-YKELKAELRELELALLVLRL--EELREELEELQEELKEAEEELEELTAELQELEEK---------- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 966 dtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKlELLKKAYEASLSEIKKGHEI--EKKSLEDLLSEKQESLEK 1043
Cdd:TIGR02168 269 ---LEELRLEVSELEEEIEELQKELYALANEISRLEQQK-QILRERLANLERQLEELEAQleELESKLDELAEELAELEE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1044 QINDLKSENDALNEKLKSEEQKRRAREKANLKnpqimyLEQELESLK-AVLEIKNE-KLHQQDIKLMKMEKlvdnnTALV 1121
Cdd:TIGR02168 345 KLEELKEELESLEAELEELEAELEELESRLEE------LEEQLETLRsKVAQLELQiASLNNEIERLEARL-----ERLE 413
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 50348617 1122 DKLKRFQQENEELKARMDKH--MAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 1176
Cdd:TIGR02168 414 DRRERLQQEIEELLKKLEEAelKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
922-1176 |
5.94e-12 |
|
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: 70.48 E-value: 5.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 922 EKLEKARNELQTVYE--AFVQQHQAEKTERENRLKEfytreyEKlrdtyiEEAEKYKMQLQEqfdnlnaahetsKLEIEA 999
Cdd:TIGR02169 170 RKKEKALEELEEVEEniERLDLIIDEKRQQLERLRR------ER------EKAERYQALLKE------------KREYEG 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1000 ShseklELL--KKAYEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLK--SEEQKRRAREKanlk 1075
Cdd:TIGR02169 226 Y-----ELLkeKEALERQKEAIERQLASLEEELEKLTEEISE-LEKRLEEIEQLLEELNKKIKdlGEEEQLRVKEK---- 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1076 npqIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQE--------NEELKARMDKHMAISRQ 1147
Cdd:TIGR02169 296 ---IGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdklTEEYAELKEELEDLRAE 372
|
250 260
....*....|....*....|....*....
gi 50348617 1148 LSTEQAVLQESLEKESKVNKRLSMENEEL 1176
Cdd:TIGR02169 373 LEEVDKEFAETRDELKDYREKLEKLKREI 401
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
940-1177 |
8.77e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 66.50 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 940 QQHQAEKTERENRLK----EFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEAS 1015
Cdd:COG1196 216 RELKEELKELEAELLllklRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYEL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1016 LSEIKkghEIEKKslEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVLEI 1095
Cdd:COG1196 294 LAELA---RLEQD--IARLEERRRELEERLEELEEELAELEEELEELEEELEELEE------ELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1096 KNEKLHQQDIKLMKMEKLVDNNT----ALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSM 1171
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAeellEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442
|
....*.
gi 50348617 1172 ENEELL 1177
Cdd:COG1196 443 ALEEAA 448
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
846-1168 |
1.53e-10 |
|
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: 65.76 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 846 EKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKT-LSQELVNLRGELVTAsttcEKL 924
Cdd:pfam02463 690 AKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDeEEEEEEKSRLKKEEK----EEE 765
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 925 EKARNELQTVYEAFVQQHQAEKTERENRLKEfytREYEKLRdTYIEEAEKYKMQLQEQFDNL-NAAHETSKLEIEASHSE 1003
Cdd:pfam02463 766 KSELSLKEKELAEEREKTEKLKVEEEKEEKL---KAQEEEL-RALEEELKEEAELLEEEQLLiEQEEKIKEEELEELALE 841
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1004 KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQinDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1083
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQ--KLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI 919
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1084 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKES 1163
Cdd:pfam02463 920 EERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKER 999
|
....*
gi 50348617 1164 KVNKR 1168
Cdd:pfam02463 1000 LEEEK 1004
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
922-1181 |
2.20e-10 |
|
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: 65.38 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 922 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHetSKLEIEASH 1001
Cdd:TIGR00618 127 ETEEVIHDLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMN--LFPLDQYTQLALMEFAKKKSLH--GKAELLTLR 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1002 SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKqindLKSENDALNEKLKSEEQKRRAREKanlknpqimy 1081
Cdd:TIGR00618 203 SQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAY----LTQKREAQEEQLKKQQLLKQLRAR---------- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1082 lEQELESLKAVLEIKNEKLHQQdiklMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 1161
Cdd:TIGR00618 269 -IEELRAQEAVLEETQERINRA----RKAAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQ 343
|
250 260
....*....|....*....|....*..
gi 50348617 1162 ESKVNKRLSME-------NEELLWKLH 1181
Cdd:TIGR00618 344 RRLLQTLHSQEihirdahEVATSIREI 370
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
889-1176 |
3.13e-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: 64.70 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 889 LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKE---FYTREYEKLR 965
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEkigELEAEIASLE 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 966 DTY------IEEAEKYKMQLQEQFDNLNAAHETSKLEIE------ASHSEKLELLKKAYEASLSEIKkghEIEKKSLEdl 1033
Cdd:TIGR02169 308 RSIaekereLEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrDKLTEEYAELKEELEDLRAELE---EVDKEFAE-- 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1034 LSEKQESLEKQINDLKSENDALNEKL--KSEEQKRRAREKANLKNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKme 1111
Cdd:TIGR02169 383 TRDELKDYREKLEKLKREINELKRELdrLQEELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKKQEWKLEQ-- 459
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50348617 1112 klvdnntaLVDKLKRFQQENEELKarmdkhmaisrqlsteqavlqeslEKESKVNKRLSMENEEL 1176
Cdd:TIGR02169 460 --------LAADLSKYEQELYDLK------------------------EEYDRVEKELSKLQREL 492
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
862-1175 |
1.30e-09 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 62.78 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 862 SGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEK---ARNELQTVYEAF 938
Cdd:TIGR02169 666 ILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQeeeKLKERLEELEED 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 939 VQQHQAEKTERENRLKEFYTReyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSE 1018
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEAR---------IEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1019 IKKghEIEKKSLED--LLSEKQES------LEKQINDLKSENDALN---EKLKSEEQKRRA-------------REKANL 1074
Cdd:TIGR02169 817 IEQ--KLNRLTLEKeyLEKEIQELqeqridLKEQIKSIEKEIENLNgkkEELEEELEELEAalrdlesrlgdlkKERDEL 894
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1075 KNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLmkmEKLVDNNTALVDKLKRFQQENEELkarmdkhmAISRQLSTEQAV 1154
Cdd:TIGR02169 895 EA-QLRELERKIEELEAQIEKKRKRLSELKAKL---EALEEELSEIEDPKGEDEEIPEEE--------LSLEDVQAELQR 962
|
330 340
....*....|....*....|.
gi 50348617 1155 LQESLEKESKVNKRLSMENEE 1175
Cdd:TIGR02169 963 VEEEIRALEPVNMLAIQEYEE 983
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
880-1105 |
2.55e-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: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 880 EALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQaektERENRLKEFYTR 959
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA----EAEEELEELAEE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 960 EYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKkgheiEKKSLEDLLSEKQE 1039
Cdd:COG1196 388 LLEALRA--AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE-----AAEEEAELEEEEEA 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50348617 1040 SLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDI 1105
Cdd:COG1196 461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
846-1182 |
2.88e-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: 61.57 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 846 EKTLELTQYKTKCENQSGFILQLK-QLLACGNTKFEALTVVIQHLLSEREEALKQHKT-----------LSQELVNLRGE 913
Cdd:TIGR04523 271 EKQKELEQNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNqisqnnkiisqLNEQISQLKKE 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 914 LVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTEREN--------RLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDN 985
Cdd:TIGR04523 351 LTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlesqindlESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIER 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 986 LNAAHETSKLEIEASHSE---------KLELLKKAYEASLSEIKKGHEIEKKSLEDLLSE------KQESLEKQINDLKS 1050
Cdd:TIGR04523 431 LKETIIKNNSEIKDLTNQdsvkeliikNLDNTRESLETQLKVLSRSINKIKQNLEQKQKElkskekELKKLNEEKKELEE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1051 ENDALNEKLKSEEQKRRAREKA-NLKNPQIMYLEQELESLKAVL---EIKNEKLH-QQDIKLMKMEK--LVDNNTALVDK 1123
Cdd:TIGR04523 511 KVKDLTKKISSLKEKIEKLESEkKEKESKISDLEDELNKDDFELkkeNLEKEIDEkNKEIEELKQTQksLKKKQEEKQEL 590
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 50348617 1124 LKRFQQENEELKARMDKHMAISRQLSTEqavlqesLEKESKVNKRLSMENEELLWKLHN 1182
Cdd:TIGR04523 591 IDQKEKEKKDLIKEIEEKEKKISSLEKE-------LEKAKKENEKLSSIIKNIKSKKNK 642
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
925-1173 |
4.84e-09 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 60.80 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 925 EKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKL-----EIEA 999
Cdd:COG3206 148 ELAAAVANALAEAYLEQNLELRREEARKALEFLEEQLPELRKE-LEEAEAALEEFRQKNGLVDLSEEAKLLlqqlsELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1000 SHSEkLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQ-ESLEKQINDLKSENDALNEKLKSeeqkrrarekanlKNPQ 1078
Cdd:COG3206 227 QLAE-ARAELAEAEARLAALRAQLGSGPDALPELLQSPViQQLRAQLAELEAELAELSARYTP-------------NHPD 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1079 IMYLEQELESLKAVLEIKNEKLhQQDIKlMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQES 1158
Cdd:COG3206 293 VIALRAQIAALRAQLQQEAQRI-LASLE-AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370
|
250
....*....|....*..
gi 50348617 1159 LEK--ESKVNKRLSMEN 1173
Cdd:COG3206 371 LQRleEARLAEALTVGN 387
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
894-1176 |
6.45e-09 |
|
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: 60.14 E-value: 6.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 894 EEALKQHKTLSQELVNLRGELVTASTTC-EKLEKARNELQtvYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtYIEEA 972
Cdd:pfam05557 44 DRESDRNQELQKRIRLLEKREAEAEEALrEQAELNRLKKK--YLEALNKKLNEKESQLADAREVISCLKNELSE-LRRQI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 973 EKYKMQLQEQFDNLNAAHEtsKLEIEASHSEKLELLKKAYEASLSEIKKgHEIEKKSLEDLLsEKQESLEKQINDLKSEN 1052
Cdd:pfam05557 121 QRAELELQSTNSELEELQE--RLDLLKAKASEAEQLRQNLEKQQSSLAE-AEQRIKELEFEI-QSQEQDSEIVKNSKSEL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1053 DALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-------------AVLEIKNEKLHQqdiKLMKMEKLVDNNT- 1118
Cdd:pfam05557 197 ARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKrklereekyreeaATLELEKEKLEQ---ELQSWVKLAQDTGl 273
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348617 1119 ------ALVDKLKRFQQENEELKARMD------KHMAIS-RQLSTEQAVLQESLEKESKVNKRLSMENEEL 1176
Cdd:pfam05557 274 nlrspeDLSRRIEQLQQREIVLKEENSsltssaRQLEKArRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
885-1205 |
7.13e-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: 60.14 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 885 VIQH--LLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYE---AFVQQHQAEKTERENRL----KE 955
Cdd:pfam17380 277 IVQHqkAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDrqaAIYAEQERMAMERERELerirQE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 956 FYTREYEKLRD-------TYIEEAEKYKMQLQEQFD----NLNAAHETSKLEIEasHSEKLELLKKAYEASLSEIKKGHE 1024
Cdd:pfam17380 357 ERKRELERIRQeeiameiSRMRELERLQMERQQKNErvrqELEAARKVKILEEE--RQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1025 IEKKSLED-----LLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK-AVLEIKNE 1098
Cdd:pfam17380 435 REVRRLEEerareMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKqAMIEEERK 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1099 KlhqqdiKLMKMEkLVDNNTALVDKLKRFQQENEELKAR-MDKHMAISRQL--STEQAVLQESLEKESKVNKRLsMENEE 1175
Cdd:pfam17380 515 R------KLLEKE-MEERQKAIYEEERRREAEEERRKQQeMEERRRIQEQMrkATEERSRLEAMEREREMMRQI-VESEK 586
|
330 340 350
....*....|....*....|....*....|
gi 50348617 1176 LLWKLhngdlcsPKRSPTSSAIPLQSPRNS 1205
Cdd:pfam17380 587 ARAEY-------EATTPITTIKPIYRPRIS 609
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
811-1133 |
9.65e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.69 E-value: 9.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 811 RKNLFTALNAVEKSRQKNPrsLCIQPQTAPDalppEKTLeLTQYKTKCENQSGFILQLKQLLacgnTKFEALTVVIQHLL 890
Cdd:PRK03918 421 IKELKKAIEELKKAKGKCP--VCGRELTEEH----RKEL-LEEYTAELKRIEKELKEIEEKE----RKLRKELRELEKVL 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 891 SEREEALKQHKTLSQeLVNLRGELvtASTTCEKLEKARNELQTVYEAFVQQhQAEKTERENRLKEFytREYEKLRdtyiE 970
Cdd:PRK03918 490 KKESELIKLKELAEQ-LKELEEKL--KKYNLEELEKKAEEYEKLKEKLIKL-KGEIKSLKKELEKL--EELKKKL----A 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 971 EAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEA--SLSEIKKGHEIEKKSLEDL---LSEKQESLEKQI 1045
Cdd:PRK03918 560 ELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEylELKDAEKELEREEKELKKLeeeLDKAFEELAETE 639
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1046 NDLKSENDALNEKLK--SEEQKRRAREKANLKNPQIMYLEQELESLKAVLE--------IKNEK--LHQQDIKLMKMEKL 1113
Cdd:PRK03918 640 KRLEELRKELEELEKkySEEEYEELREEYLELSRELAGLRAELEELEKRREeikktlekLKEELeeREKAKKELEKLEKA 719
|
330 340
....*....|....*....|
gi 50348617 1114 VDNNTALVDKLKRFQQENEE 1133
Cdd:PRK03918 720 LERVEELREKVKKYKALLKE 739
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
877-1182 |
1.50e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 877 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELvtasttcEKLEKARNELQTVyeafvqqhQAEKTERENRLKEF 956
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRL-------EELEERHELYEEA--------KAKKEELERLKKRL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 957 YTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAahETSKLEIEASHseklelLKKAyeasLSEIKK--------GHEIEKK 1028
Cdd:PRK03918 382 TGLTPEKLEKE-LEELEKAKEEIEEEISKITA--RIGELKKEIKE------LKKA----IEELKKakgkcpvcGRELTEE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1029 SLEDLLSEKQESLEKQINDLKsENDALNEKLKSEEQKrraREKANLKNPQIMYLEQELESLKAVleikNEKLHQQDIKlm 1108
Cdd:PRK03918 449 HRKELLEEYTAELKRIEKELK-EIEEKERKLRKELRE---LEKVLKKESELIKLKELAEQLKEL----EEKLKKYNLE-- 518
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348617 1109 kmeklvdnntalvdKLKRFQQENEELKARMDKhmaisrqLSTEQAVLQESLEKESKVNKRLsmenEELLWKLHN 1182
Cdd:PRK03918 519 --------------ELEKKAEEYEKLKEKLIK-------LKGEIKSLKKELEKLEELKKKL----AELEKKLDE 567
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
886-1088 |
1.76e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 59.18 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 886 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAfVQQHQAEKTERENRLKefytREYEKLR 965
Cdd:COG1196 304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE-AEAELAEAEEALLEAE----AELAEAE 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 966 DTYIEEAEKYKMQLQEQFDNLNA-AHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQ 1044
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQlEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 50348617 1045 INDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELES 1088
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEAD 502
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
922-1164 |
4.49e-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: 56.47 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 922 EKLEKARNELQTVYEAFVQQH----------QAEKTERENR-LKEFYTREYEKLRDTYIEEAEKyKMQLQEQFDNLNAAH 990
Cdd:pfam13868 61 EEKEEERKEERKRYRQELEEQieereqkrqeEYEEKLQEREqMDEIVERIQEEDQAEAEEKLEK-QRQLREEIDEFNEEQ 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 991 ETSK-LEIEAshsEKLELLK-KAYEASLSEIKKGHEIEKKSLE---DLLSEKQESLEKQINDLKSENDALNEKLKSEEQK 1065
Cdd:pfam13868 140 AEWKeLEKEE---EREEDERiLEYLKEKAEREEEREAEREEIEeekEREIARLRAQQEKAQDEKAERDELRAKLYQEEQE 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1066 RRAREKAnlknpqimyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEElKARMDKHMAIS 1145
Cdd:pfam13868 217 RKERQKE---------REEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEE-IEQEEAEKRRM 286
|
250
....*....|....*....
gi 50348617 1146 RQLSTEQAVLQESLEKESK 1164
Cdd:pfam13868 287 KRLEHRRELEKQIEEREEQ 305
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
884-1181 |
5.22e-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: 57.67 E-value: 5.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 884 VVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYeafvQQHQAEKTERENRLKEFYTREYEK 963
Cdd:pfam02463 162 AAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYY----QLKEKLELEEEYLLYLDYLKLNEE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 964 LRDTYIE----EAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQE 1039
Cdd:pfam02463 238 RIDLLQEllrdEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1040 SLEKQINDLKSENDAL----NEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIK------LMK 1109
Cdd:pfam02463 318 ESEKEKKKAEKELKKEkeeiEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSaaklkeEEL 397
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50348617 1110 MEKLVDNNTALvDKLKRFQQENEELKARMDKhmaISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLH 1181
Cdd:pfam02463 398 ELKSEEEKEAQ-LLLELARQLEDLLKEEKKE---ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
886-1047 |
9.27e-08 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 54.55 E-value: 9.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 886 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVY---EAFVQQHQAEKTERENRL------KEF 956
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIkrlELEIEEVEARIKKYEEQLgnvrnnKEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 957 --YTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAsHSEKLELLKKAYEASLSEIKKghEIEKksledlL 1034
Cdd:COG1579 92 eaLQKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAE-LEAELEEKKAELDEELAELEA--ELEE------L 161
|
170
....*....|...
gi 50348617 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 |
1.01e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 56.60 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 850 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 929
Cdd:TIGR02168 783 EIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIE 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 930 ELQTVYEAF---VQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1006
Cdd:TIGR02168 863 ELEELIEELeseLEALLNERASLEEALALL-RSELEELSEE-LRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1007 LLKKA---YEASLSEIKKgHEIEKKSLEDLLSEKQESLEKQINDLKSEN-DALNEklkSEEQKRRAREKANlknpQIMYL 1082
Cdd:TIGR02168 941 LQERLseeYSLTLEEAEA-LENKIEDDEEEARRRLKRLENKIKELGPVNlAAIEE---YEELKERYDFLTA----QKEDL 1012
|
250
....*....|....
gi 50348617 1083 EQELESL-KAVLEI 1095
Cdd:TIGR02168 1013 TEAKETLeEAIEEI 1026
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
886-1181 |
1.04e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.61 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 886 IQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEkterenrLKEFYTREYEKLR 965
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKE-------LLEEYTAELKRIE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 966 DTyIEEAEKYKMQLQEqfdnlnaahETSKLEIEASHSEKLELLKKAYEaSLSEIKKghEIEKKSLEDL--LSEKQESLEK 1043
Cdd:PRK03918 466 KE-LKEIEEKERKLRK---------ELRELEKVLKKESELIKLKELAE-QLKELEE--KLKKYNLEELekKAEEYEKLKE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1044 QINDLKSENDALNEKLKSEEQKRRAREKANLKnpqIMYLEQELESLKAVLEIKN-EKLHQQDIKLMKMEKLVDNNTALVD 1122
Cdd:PRK03918 533 KLIKLKGEIKSLKKELEKLEELKKKLAELEKK---LDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKD 609
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 50348617 1123 KLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLH 1181
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEY 668
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
892-1172 |
1.16e-07 |
|
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: 55.67 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 892 EREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA---EKTERENRLKEF-----------Y 957
Cdd:pfam07888 67 DREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDAllaQRAAHEARIRELeediktltqrvL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 958 TREYEKLRDTyiEEAEKYKMQLQEQfdnlNAAHETSKLEIEASHSEKLELLKKAYEAslseikKGHEIEKKSLEDLLSEK 1037
Cdd:pfam07888 147 ERETELERMK--ERAKKAGAQRKEE----EAERKQLQAKLQQTEEELRSLSKEFQEL------RNSLAQRDTQVLQLQDT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1038 QESLEKQINDlKSENDALNEKLKseEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDN 1116
Cdd:pfam07888 215 ITTLTQKLTT-AHRKEAENEALL--EELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTlQLADA 291
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 50348617 1117 NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSME 1172
Cdd:pfam07888 292 SLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVE 347
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
878-1161 |
1.49e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.84 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 878 KFEALTVVIQHLLSERE----EALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvqQHQAEKTERENRL 953
Cdd:PRK03918 183 KFIKRTENIEELIKEKEkeleEVLREINEISSELPELREELEKLEKEVKELEELKEEIE--------ELEKELESLEGSK 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 954 KefytREYEKLRDT--YIEEAEKYKMQLQEQfdnlnaAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIekksle 1031
Cdd:PRK03918 255 R----KLEEKIRELeeRIEELKKEIEELEEK------VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR------ 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1032 dlLSEKQESLEKQINDLKSENDALNEKLKSEEqkrrarekanlknpqimyleqELESLKAVLEIKNEKLHQQDIKLMKME 1111
Cdd:PRK03918 319 --LEEEINGIEERIKELEEKEERLEELKKKLK---------------------ELEKRLEELEERHELYEEAKAKKEELE 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 50348617 1112 KLVDNNTA-----LVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEK 1161
Cdd:PRK03918 376 RLKKRLTGltpekLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEE 430
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
849-1131 |
2.13e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 849 LELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKA- 927
Cdd:pfam05483 457 IQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQi 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 928 ----------RNELQTVYEAFVQQH-----QAEKTERENRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHET 992
Cdd:pfam05483 537 enleekemnlRDELESVREEFIQKGdevkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQE 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 993 SKLEIEASHSE------------KLEL----LKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES---------LEKQInD 1047
Cdd:pfam05483 617 NKALKKKGSAEnkqlnayeikvnKLELelasAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAkaiadeavkLQKEI-D 695
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1048 LK-----SENDALNEKLKSEEQK---RRAREKANLKNPqimylEQELESLKAVLEIKNEKLHQQdikLMKMEKLVDNNTA 1119
Cdd:pfam05483 696 KRcqhkiAEMVALMEKHKHQYDKiieERDSELGLYKNK-----EQEQSSAKAALEIELSNIKAE---LLSLKKQLEIEKE 767
|
330
....*....|..
gi 50348617 1120 LVDKLKRFQQEN 1131
Cdd:pfam05483 768 EKEKLKMEAKEN 779
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
890-1082 |
2.45e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.16 E-value: 2.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 890 LSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQA-----EKTERENRLKEFyTREYEKL 964
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlplyqELEALEAELAEL-PERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 965 RdtyiEEAEKYKmQLQEQFDNLNAAHETSKLEIEashsEKLELLKKAYEASLSEIKKGHEiekksledLLSEKQESLEKQ 1044
Cdd:COG4717 152 E----ERLEELR-ELEEELEELEAELAELQEELE----ELLEQLSLATEEELQDLAEELE--------ELQQRLAELEEE 214
|
170 180 190
....*....|....*....|....*....|....*....
gi 50348617 1045 INDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYL 1082
Cdd:COG4717 215 LEEAQEELEELEEELEQlENELEAAALEERLKEARLLLL 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
867-1072 |
2.48e-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: 54.38 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 867 QLKQLlacgNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEK 946
Cdd:COG4942 28 ELEQL----QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 947 TERENRLKEFYT---REYEKL------------RDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLK-- 1009
Cdd:COG4942 104 EELAELLRALYRlgrQPPLALllspedfldavrRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAel 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50348617 1010 KAYEASLSEIKKgheiEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1072
Cdd:COG4942 184 EEERAALEALKA----ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
969-1211 |
2.61e-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: 54.38 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 969 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEkLELLKKAYEASLSEIKKgheiekksledlLSEKQESLEKQINDL 1048
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ-LAALERRIAALARRIRA------------LEQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1049 KSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE------------QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1116
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspedfldavRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1117 NTALVDKLKRFQQENEE----LKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLsmenEELLWKLHNGDLCSPKRSP 1192
Cdd:COG4942 169 LEAERAELEALLAELEEeraaLEALKAERQKLLARLEKELAELAAELAELQQEAEEL----EALIARLEAEAAAAAERTP 244
|
250
....*....|....*....
gi 50348617 1193 TSSAiplqsPRNSGSFPSP 1211
Cdd:COG4942 245 AAGF-----AALKGKLPWP 258
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
892-1161 |
3.42e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.80 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 892 EREEALKQHKTLSQELVNLRG-------ELVTASTTCEKLEKARNELQ-TVYEAfvQQHQAE-----KTERENRLKEfyt 958
Cdd:pfam01576 216 ESTDLQEQIAELQAQIAELRAqlakkeeELQAALARLEEETAQKNNALkKIREL--EAQISElqedlESERAARNKA--- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 959 reyEKLRDTYIEEAEKYKMQLQEQFDNLNAAHE-TSKLEIEASHSEK-LELLKKAYEASLSEIKKGH-----------EI 1025
Cdd:pfam01576 291 ---EKQRRDLGEELEALKTELEDTLDTTAAQQElRSKREQEVTELKKaLEEETRSHEAQLQEMRQKHtqaleelteqlEQ 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1026 EKKSLEDLLSEKQeSLEKQINDLKSENDALNE-KLKSEEQKRRA---------------REKANLkNPQIMYLEQELESL 1089
Cdd:pfam01576 368 AKRNKANLEKAKQ-ALESENAELQAELRTLQQaKQDSEHKRKKLegqlqelqarlseseRQRAEL-AEKLSKLQSELESV 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1090 KAVL---EIKNEKLHQQ----DIKLMKMEKLVDNNT----ALVDKLKRFQQENEELKARMDKHM----AISRQLSTEQAV 1154
Cdd:pfam01576 446 SSLLneaEGKNIKLSKDvsslESQLQDTQELLQEETrqklNLSTRLRQLEDERNSLQEQLEEEEeakrNVERQLSTLQAQ 525
|
....*..
gi 50348617 1155 LQESLEK 1161
Cdd:pfam01576 526 LSDMKKK 532
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
936-1170 |
3.93e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 936 EAFVQQHQAEKTERENRLKEFYTREYEKLRDTY-------IEEAEKYKMQLQEQFDNLNAAHE-TSKLEIEASHSEKLEL 1007
Cdd:COG4717 296 EKASLGKEAEELQALPALEELEEEELEELLAALglppdlsPEELLELLDRIEELQELLREAEElEEELQLEELEQEIAAL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1008 LKKAYEASLSEIKKGHEIEKKSLEdlLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREkanlknpqimyLEQELE 1087
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQE--LKEELEELEEQLEELLGELEELLEALDEEELEEELEE-----------LEEELE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1088 SLKAVLEIKNEKLHQQDIKLMKMEklvdNNTALVDKLKRFQQENEELKARMDKHMAisrqLSTEQAVLQESL-----EKE 1162
Cdd:COG4717 443 ELEEELEELREELAELEAELEQLE----EDGELAELLQELEELKAELRELAEEWAA----LKLALELLEEAReeyreERL 514
|
....*...
gi 50348617 1163 SKVNKRLS 1170
Cdd:COG4717 515 PPVLERAS 522
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
965-1176 |
4.19e-07 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 54.68 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 965 RDTYIEEA---EKYKMQLQEQFDNLNAA-----------HETSK----LEIEASHSEKLellkKAYEASLSEIKKG-HEI 1025
Cdd:TIGR02168 157 RRAIFEEAagiSKYKERRKETERKLERTrenldrledilNELERqlksLERQAEKAERY----KELKAELRELELAlLVL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1026 EKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpqimyLEQELESL-KAVLEIKNEklhQQD 1104
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE----------LEEEIEELqKELYALANE---ISR 299
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50348617 1105 IKLMKMEkLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEEL 1176
Cdd:TIGR02168 300 LEQQKQI-LRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEEL 370
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
887-1177 |
4.46e-07 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.26 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 887 QHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEklrd 966
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE---- 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 967 tyIEEAEKYKMQLQEQFDNLNAahetsklEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLE------DLLSEKQES 1040
Cdd:TIGR04523 276 --LEQNNKKIKELEKQLNQLKS-------EISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISqnnkiiSQLNEQISQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1041 LEKQINDLKSENDALNEKLKSEEQKRRAREKAN---------LKNpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME 1111
Cdd:TIGR04523 347 LKKELTNSESENSEKQRELEEKQNEIEKLKKENqsykqeiknLES-QINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348617 1112 KLVDN----NTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKES----KVNKRLSMENEELL 1177
Cdd:TIGR04523 426 KEIERlketIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKqnleQKQKELKSKEKELK 499
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
943-1177 |
5.24e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 54.17 E-value: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 943 QAEKTERenrlkefytreYEKLRdtyiEEAEKYKMQLQ-EQFDNLNAAHETSKLEIEAshsekLELLKKAYEASLSEIKK 1021
Cdd:COG1196 208 QAEKAER-----------YRELK----EELKELEAELLlLKLRELEAELEELEAELEE-----LEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1022 GHEIEKKSLEDLlsekqeslEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpQIMYLEQELESLKAVL-------- 1093
Cdd:COG1196 268 ELEELRLELEEL--------ELELEEAQAEEYELLAELARLEQDIARLEE------RRRELEERLEELEEELaeleeele 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1094 -------EIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVN 1166
Cdd:COG1196 334 eleeeleELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
|
250
....*....|.
gi 50348617 1167 KRLSMENEELL 1177
Cdd:COG1196 414 ERLERLEEELE 424
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
887-1160 |
5.26e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 54.41 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 887 QHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeafvqqhqAEKTERENRLKEFYTREYEKLRD 966
Cdd:pfam01576 22 QKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLA-----------ARKQELEEILHELESRLEEEEER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 967 TYIEEAEKYKMQ-----LQEQFDNLNAAHEtsKLEIEASHSE----KLELLKKAYEASLSEIKKgheiEKKSLEDLLSE- 1036
Cdd:pfam01576 91 SQQLQNEKKKMQqhiqdLEEQLDEEEAARQ--KLQLEKVTTEakikKLEEDILLLEDQNSKLSK----ERKLLEERISEf 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1037 -----KQESLEKQINDLKSENDA----LNEKLKSEEQKRRAREKANLK--------NPQIMYLEQELESLKAVLEIKNEK 1099
Cdd:pfam01576 165 tsnlaEEEEKAKSLSKLKNKHEAmisdLEERLKKEEKGRQELEKAKRKlegestdlQEQIAELQAQIAELRAQLAKKEEE 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348617 1100 LHQqdiKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLE 1160
Cdd:pfam01576 245 LQA---ALARLEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELE 302
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
886-1116 |
6.16e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.98 E-value: 6.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 886 IQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVYEAfVQQHQAEKTERENRLKEFYtREYEKLR 965
Cdd:COG4372 40 LDKLQEELEQLREELEQAREELEQLEEELEQAR---SELEQLEEELEELNEQ-LQAAQAELAQAQEELESLQ-EEAEELQ 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 966 DTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIeASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQI 1045
Cdd:COG4372 115 EE-LEELQKERQDLEQQRKQLEAQIAELQSEI-AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50348617 1046 ND--LKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1116
Cdd:COG4372 193 NRnaEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
886-1170 |
8.55e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 53.53 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 886 IQHLLSEREEALKQHKTLSQELVNLRGELVTAS------TTCEKLEKARNELQtvyeafvqQHQAEKTEREnrlkefyTR 959
Cdd:PRK03918 461 LKRIEKELKEIEEKERKLRKELRELEKVLKKESeliklkELAEQLKELEEKLK--------KYNLEELEKK-------AE 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 960 EYEKLRdtyiEEAEKYKmqlqeqfdnlnaahetSKLEIEASHSEKLELLKKAYEASLSEIKKGHEiEKKSLEDLLSEK-- 1037
Cdd:PRK03918 526 EYEKLK----EKLIKLK----------------GEIKSLKKELEKLEELKKKLAELEKKLDELEE-ELAELLKELEELgf 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1038 --QESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLM--KMEKL 1113
Cdd:PRK03918 585 esVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSeeEYEEL 664
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 50348617 1114 VDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLS 1170
Cdd:PRK03918 665 REEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1037-1162 |
8.82e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1037 KQESLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMK------ 1109
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDAlQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEraraly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1110 ---------------------------MEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKE 1162
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlsaLSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
848-1177 |
9.04e-07 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.19 E-value: 9.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 848 TLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREE--ALKQHKTLS-QELVNLRGELVTASTTCEKL 924
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEmtKFKNNKEVElEELKKILAEDEKLLDEKKQF 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 925 EKARNELQTVYEAFV---QQHQAEKTERENRL------KEFYTREYEKLRdtyiEEAEKYKMQLQE--------QFDNLN 987
Cdd:pfam05483 428 EKIAEELKGKEQELIfllQAREKEIHDLEIQLtaiktsEEHYLKEVEDLK----TELEKEKLKNIEltahcdklLLENKE 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 988 AAHETSKLEIE-ASHSEKLELLKKAYEASLSEIKKGHEIEKKsLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKR 1066
Cdd:pfam05483 504 LTQEASDMTLElKKHQEDIINCKKQEERMLKQIENLEEKEMN-LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEV 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1067 RAREKA---------NL------KNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKME-KLVDNNTALVDKLKRFQQE 1130
Cdd:pfam05483 583 LKKEKQmkilenkcnNLkkqienKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLElELASAKQKFEEIIDNYQKE 662
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 50348617 1131 NEELKARMDKHMAisrQLSTEQAVLQESLEKESKVNKRLSMENEELL 1177
Cdd:pfam05483 663 IEDKKISEEKLLE---EVEKAKAIADEAVKLQKEIDKRCQHKIAEMV 706
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
980-1130 |
1.17e-06 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 52.28 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 980 QEQFDNLNA--AHETSKLEIEASHSEKLELLKKAYEASLSEIkkghEIEKKSLEDLLSEkqesLEKQINDLKSENDALNE 1057
Cdd:PRK09039 52 DSALDRLNSqiAELADLLSLERQGNQDLQDSVANLRASLSAA----EAERSRLQALLAE----LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348617 1058 KLKSEEQ-KRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM-EKLvdnNTALVDK---LKRFQQE 1130
Cdd:PRK09039 124 ELDSEKQvSARALAQVELLNQQIAALRRQLAALEAALDASEKRDRESQAKIADLgRRL---NVALAQRvqeLNRYRSE 198
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
846-1161 |
1.27e-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: 52.90 E-value: 1.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 846 EKTLELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLE 925
Cdd:pfam10174 363 KKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLE 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 926 KARNELQTVYEAFvqQHQAEKTERENRlkefytreyeklrdtyiEEAEKYKMQLQEQFDNLNAAHeTSKLEIEAShseKL 1005
Cdd:pfam10174 443 EALSEKERIIERL--KEQREREDRERL-----------------EELESLKKENKDLKEKVSALQ-PELTEKESS---LI 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1006 ELLKKAYEASLSEIKKGHEIekKSLEDLLSEKQESLEKQINDL-KSENDALNEKLKSE--EQKRRAREKANLKNPQIMYL 1082
Cdd:pfam10174 500 DLKEHASSLASSGLKKDSKL--KSLEIAVEQKKEECSKLENQLkKAHNAEEAVRTNPEinDRIRLLEQEVARYKEESGKA 577
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1083 EQELESLKAVL-EIKNEKlHQQDIKLMKMEKL----VDNNTALVDKLKRFQQEN--------EELKARMDKHMAISRQLS 1149
Cdd:pfam10174 578 QAEVERLLGILrEVENEK-NDKDKKIAELESLtlrqMKEQNKKVANIKHGQQEMkkkgaqllEEARRREDNLADNSQQLQ 656
|
330
....*....|..
gi 50348617 1150 TEQavLQESLEK 1161
Cdd:pfam10174 657 LEE--LMGALEK 666
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
885-1134 |
1.47e-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: 52.66 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 885 VIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARnelqtvyeaFVQQHQAEKTERENRLKEF-YTREYEK 963
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKE---------LLASRQLALQKMQSEKEQLtYWKEMLA 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 964 LRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQ--ESL 1041
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQtgAEL 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1042 EKQINDLKSENDALNE-----KLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDN 1116
Cdd:TIGR00618 781 SHLAAEIQFFNRLREEdthllKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQ 860
|
250
....*....|....*...
gi 50348617 1117 NTALVDKLKRFQQENEEL 1134
Cdd:TIGR00618 861 LAQLTQEQAKIIQLSDKL 878
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
969-1129 |
1.77e-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: 51.22 E-value: 1.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 969 IEEAEKYKMQLQEQFDNLNAAHETSKleieaSHSEKLELLKKAYEASLSeiKKGHEIEKKSLEDLLSEKQESLEKQINDL 1048
Cdd:cd22656 127 LKEAKKYQDKAAKVVDKLTDFENQTE-----KDQTALETLEKALKDLLT--DEGGAIARKEIKDLQKELEKLNEEYAAKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1049 KSENDALNEKLKSEEQKRRAREK---------ANLKN------PQIMYLEQ----------ELESLKAVLEIKNEKLHQQ 1103
Cdd:cd22656 200 KAKIDELKALIADDEAKLAAALRliadltaadTDLDNllaligPAIPALEKlqgawqaiatDLDSLKDLLEDDISKIPAA 279
|
170 180
....*....|....*....|....*.
gi 50348617 1104 DIKLMKMEKLVDNNTALVDKLKRFQQ 1129
Cdd:cd22656 280 ILAKLELEKAIEKWNELAEKADKFRQ 305
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
922-1108 |
2.11e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 922 EKLEKARNELQTVYEAFvqqhqAEKTERENRLKEfytrEYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKLEIE-AS 1000
Cdd:COG4717 74 KELEEELKEAEEKEEEY-----AELQEELEELEE----ELEELEAE-LEELREELEKLEKLLQLLPLYQELEALEAElAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1001 HSEKLELLKKAYEA------SLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKanl 1074
Cdd:COG4717 144 LPERLEELEERLEElreleeELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE--- 220
|
170 180 190
....*....|....*....|....*....|....*.
gi 50348617 1075 knpQIMYLEQELESLKAVLEI--KNEKLHQQDIKLM 1108
Cdd:COG4717 221 ---ELEELEEELEQLENELEAaaLEERLKEARLLLL 253
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
890-1175 |
2.19e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 890 LSEREEALKQHKT-LSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFytREYEKLRDTY 968
Cdd:COG1340 6 LSSSLEELEEKIEeLREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV--KELKEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 969 IEEAEKYKMQLqEQFDNLNAAHETSKLEIEAshseklelLKKAYEaslseikkghEIEKKSL-EDLLSEKQESLEKQIND 1047
Cdd:COG1340 84 NEKLNELREEL-DELRKELAELNKAGGSIDK--------LRKEIE----------RLEWRQQtEVLSPEEEKELVEKIKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1048 LKSEndaLNEKLKSEEQKRRAREkanlknpqimyLEQELESLKavleIKNEKLHQQDIKLM--------KMEKLVDNNTA 1119
Cdd:COG1340 145 LEKE---LEKAKKALEKNEKLKE-----------LRAELKELR----KEAEEIHKKIKELAeeaqelheEMIELYKEADE 206
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 50348617 1120 LVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEE 1175
Cdd:COG1340 207 LRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEK 262
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
958-1096 |
2.40e-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: 50.79 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 958 TREYEKLRDtYIEEAEKYKMQLQEQFDNLNaahetSKLEIEASHSEKLE-----LLKKAYEAsLSEIKKGHEIEKKSLED 1032
Cdd:smart00787 157 KEDYKLLMK-ELELLNSIKPKLRDRKDALE-----EELRQLKQLEDELEdcdptELDRAKEK-LKKLLQEIMIKVKKLEE 229
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348617 1033 LLSEKQEsLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpQIMYLEQELESLKAVLEIK 1096
Cdd:smart00787 230 LEEELQE-LESKIEDLTNKKSELNTEIAEAEKKLEQCRGFTFK--EIEKLKEQLKLLQSLTGWK 290
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
952-1176 |
3.29e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 952 RLKEFYTREYEKLRDTYIEEAEKykMQLqeqFDNLNAAHETSKLE-IEAshsekleLLKKAYEASLSEIKKG----HEIE 1026
Cdd:COG4717 2 KIKELEIYGFGKFRDRTIEFSPG--LNV---IYGPNEAGKSTLLAfIRA-------MLLERLEKEADELFKPqgrkPELN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1027 KKSLEDLLSEKQE--SLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLE--QELESLKAVLEIKNEKLH 1101
Cdd:COG4717 70 LKELKELEEELKEaeEKEEEYAELQEELEELEEELEElEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 50348617 1102 QQDIKLMKMEklvdnntALVDKLKRFQQENEELKARMDKHMAiSRQLSTEQAvLQESLEKESKVNKRLSMENEEL 1176
Cdd:COG4717 150 ELEERLEELR-------ELEEELEELEAELAELQEELEELLE-QLSLATEEE-LQDLAEELEELQQRLAELEEEL 215
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
969-1091 |
3.33e-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: 49.54 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 969 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEA--SHSEKLELLKKAYEASLSEIKK-------GHEIE-----KKSLEDLL 1034
Cdd:COG1579 33 LAELEDELAALEARLEAAKTELEDLEKEIKRleLEIEEVEARIKKYEEQLGNVRNnkeyealQKEIEslkrrISDLEDEI 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1035 SE---KQESLEKQINDLKSENDALNEKLKSEEQKRRAREKAnlknpqimyLEQELESLKA 1091
Cdd:COG1579 113 LElmeRIEELEEELAELEAELAELEAELEEKKAELDEELAE---------LEAELEELEA 163
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
886-1127 |
3.35e-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: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 886 IQHLLSEREEALKQHKTLSQELV-------NLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYT 958
Cdd:TIGR04523 414 IKKLQQEKELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 959 REYEklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE----------------------LLKKAYEASL 1016
Cdd:TIGR04523 494 KEKE------LKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEkeskisdledelnkddfelkkeNLEKEIDEKN 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1017 SEIKKGHEiEKKSLEDLLSEKQE---SLEKQINDLKSEndaLNEKLKSEEQKRRAREKANLKNpqimyleQELESLKAVL 1093
Cdd:TIGR04523 568 KEIEELKQ-TQKSLKKKQEEKQElidQKEKEKKDLIKE---IEEKEKKISSLEKELEKAKKEN-------EKLSSIIKNI 636
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 50348617 1094 EIKNEKLHQQdIKLMKME---------KLVDNNTALVDKLKRF 1127
Cdd:TIGR04523 637 KSKKNKLKQE-VKQIKETikeirnkwpEIIKKIKESKTKIDDI 678
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
922-1180 |
3.81e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 51.61 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 922 EKLEKARNELQTVyeafvqqhQAEKTERENRLKEfYTREyeklrdtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASh 1001
Cdd:TIGR02169 681 ERLEGLKRELSSL--------QSELRRIENRLDE-LSQE--------LSDASRKIGEIEKEIEQLEQEEEKLKERLEEL- 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1002 seklellkkayEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLKSENDALNEKLkSEEQKRRAREKANLKNPQIMY 1081
Cdd:TIGR02169 743 -----------EEDLSSLEQEIENVKSELKELEARIEE-LEEDLHKLEEALNDLEARL-SHSRIPEIQAELSKLEEEVSR 809
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1082 LEQELESLKAVLeikNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR-------MDKHMAISRQLSTEQAV 1154
Cdd:TIGR02169 810 IEARLREIEQKL---NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKkeeleeeLEELEAALRDLESRLGD 886
|
250 260
....*....|....*....|....*.
gi 50348617 1155 LQESLEKESKVNKRLSMENEELLWKL 1180
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQI 912
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
859-1168 |
3.85e-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: 51.11 E-value: 3.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 859 ENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEkarnELQTVYEAF 938
Cdd:COG5185 160 IIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSESTLLEKAK----EIINIEEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 939 VQqhqAEKTERENRLKEFYTREYEKLrdtyIEEAEKYKM----QLQEQFDNLNAAHETSKLEIEaSHSEKLELLKKAYEA 1014
Cdd:COG5185 236 KG---FQDPESELEDLAQTSDKLEKL----VEQNTDLRLeklgENAESSKRLNENANNLIKQFE-NTKEKIAEYTKSIDI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1015 SLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLE 1094
Cdd:COG5185 308 KKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIE 387
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348617 1095 IKNEKLHQQDIKLMKMEKlvDNNTALVDKLKRFQQENEELKARMDKhmaISRQLSTEQAVLQESLEKESKVNKR 1168
Cdd:COG5185 388 STKESLDEIPQNQRGYAQ--EILATLEDTLKAADRQIEELQRQIEQ---ATSSNEEVSKLLNELISELNKVMRE 456
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
885-1176 |
5.04e-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: 50.79 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 885 VIQHLLSEREEALK----QHKTLSQELVNLRGELVTASTTCEKLEKARNELQTvyEAFVQQHQAEKTERE-NRLKEfYTR 959
Cdd:TIGR04523 58 NLDKNLNKDEEKINnsnnKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINS--EIKNDKEQKNKLEVElNKLEK-QKK 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 960 EYEKLRDTYIEEAEKykmqLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAY--EASLSEIKKGHEIEKKSLEDL--LS 1035
Cdd:TIGR04523 135 ENKKNIDKFLTEIKK----KEKELEKLNNKYNDLKKQKEELENELNLLEKEKLniQKNIDKIKNKLLKLELLLSNLkkKI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1036 EKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA-NLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLV 1114
Cdd:TIGR04523 211 QKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEiSNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQL 290
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348617 1115 DNNTALVDKLKRFQQEN------EELKARMDKHMAISRQLS-TEQAV--LQESLEKESKVNKRLSMENEEL 1176
Cdd:TIGR04523 291 NQLKSEISDLNNQKEQDwnkelkSELKNQEKKLEEIQNQISqNNKIIsqLNEQISQLKKELTNSESENSEK 361
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1003-1169 |
5.32e-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: 49.15 E-value: 5.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1003 EKLELLKK--AYEASLSEIK---KGHEIEKKSLEDLLSEKQESLEK---QINDLKSENDALNEKLKSEEQKR-RAREK-A 1072
Cdd:COG1579 4 EDLRALLDlqELDSELDRLEhrlKELPAELAELEDELAALEARLEAaktELEDLEKEIKRLELEIEEVEARIkKYEEQlG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1073 NLKNP-QIMYLEQELESLKAVLEIKNEKLhqqdIKLM-KMEKLVDNNTALVDKLKRFQQENEELKARMDKhmAISRQLST 1150
Cdd:COG1579 84 NVRNNkEYEALQKEIESLKRRISDLEDEI----LELMeRIEELEEELAELEAELAELEAELEEKKAELDE--ELAELEAE 157
|
170
....*....|....*....
gi 50348617 1151 EQAVLQESLEKESKVNKRL 1169
Cdd:COG1579 158 LEELEAEREELAAKIPPEL 176
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
901-1139 |
8.79e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.30 E-value: 8.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 901 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFvqQHQAEKTERENRLKEfYTREYEKLRDTY--IEEAEKYKMQ 978
Cdd:COG4913 613 AALEAELAELEEELAEAEERLEALEAELDALQERREAL--QRLAEYSWDEIDVAS-AEREIAELEAELerLDASSDDLAA 689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 979 LQEQFDNLNAAHETSKLEIEASHSEK---------LELLKKAYEASLSEIKKGHEIEKKSL--EDLLSEKQESLEKQI-N 1046
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIgrlekeleqAEEELDELQDRLEAAEDLARLELRALleERFAAALGDAVERELrE 769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1047 DLKSENDALNEKLKSEEQK-RRAREKANLKNPQIMY-LEQELESLKAVLE----IKNEKL--HQQDIKLMKMEKLVDNNT 1118
Cdd:COG4913 770 NLEERIDALRARLNRAEEElERAMRAFNREWPAETAdLDADLESLPEYLAlldrLEEDGLpeYEERFKELLNENSIEFVA 849
|
250 260
....*....|....*....|.
gi 50348617 1119 ALVDKLKRfqqENEELKARMD 1139
Cdd:COG4913 850 DLLSKLRR---AIREIKERID 867
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
901-1183 |
1.07e-05 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 49.79 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 901 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFV--QQHQ------------------AE-------------KT 947
Cdd:pfam01576 548 KRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdLDHQrqlvsnlekkqkkfdqmlAEekaisaryaeerdRA 627
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 948 ERENRLKEF----YTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAH----------ETSKLEIEASHSE---KLELL-- 1008
Cdd:pfam01576 628 EAEAREKETralsLARALEEALEA-KEELERTNKQLRAEMEDLVSSKddvgknvhelERSKRALEQQVEEmktQLEELed 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1009 --------KKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDalneklksEEQKRRAREKANLKNpqim 1080
Cdd:pfam01576 707 elqatedaKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAELE--------DERKQRAQAVAAKKK---- 774
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1081 yLEQELESLKAVLEIKNeKLHQQDIKLMKmeklvdnntALVDKLKRFQQENEELKARMDKHMAISRQ-------LSTEQA 1153
Cdd:pfam01576 775 -LELDLKELEAQIDAAN-KGREEAVKQLK---------KLQAQMKDLQRELEEARASRDEILAQSKEsekklknLEAELL 843
|
330 340 350
....*....|....*....|....*....|
gi 50348617 1154 VLQESLEKESKVNKRLSMENEELLWKLHNG 1183
Cdd:pfam01576 844 QLQEDLAASERARRQAQQERDELADEIASG 873
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
873-1156 |
1.12e-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: 49.73 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 873 ACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVYEAFVQQHQaektereNR 952
Cdd:pfam15921 199 ASGKKIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVE---DQLEALKSESQNKIELLLQQHQ-------DR 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 953 LKEFYTrEYEKLRDTYIEEAEKYKMQ----------LQEQFDNLNAAHETSKLEIEASHSE---KLELLKKAYEASLSEI 1019
Cdd:pfam15921 269 IEQLIS-EHEVEITGLTEKASSARSQansiqsqleiIQEQARNQNSMYMRQLSDLESTVSQlrsELREAKRMYEDKIEEL 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1020 KK-----GHEI------------EKKSLEDLLS---------EKQESLEKQ---------------INDLKSEND----- 1053
Cdd:pfam15921 348 EKqlvlaNSELtearterdqfsqESGNLDDQLQklladlhkrEKELSLEKEqnkrlwdrdtgnsitIDHLRRELDdrnme 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1054 -----ALNEKLKSEEQKRRAREKANLKNP-----QIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLV-DNNTALVD 1122
Cdd:pfam15921 428 vqrleALLKAMKSECQGQMERQMAAIQGKnesleKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVsDLTASLQE 507
|
330 340 350
....*....|....*....|....*....|....*..
gi 50348617 1123 KLKRFQQENEE---LKARMDKHMAISRQLSTEQAVLQ 1156
Cdd:pfam15921 508 KERAIEATNAEitkLRSRVDLKLQELQHLKNEGDHLR 544
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
922-1102 |
1.13e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.77 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 922 EKLEKARNELQTVY--EAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLnaAHETSKLEIEA 999
Cdd:COG4717 49 ERLEKEADELFKPQgrKPELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEEL--REELEKLEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1000 SHSEKLELLKKAyEASLSEIKKGHEIEKKSLEDL--LSEKQESLEKQINDLKSENDALNEK--LKSEEQKRRAREKANLK 1075
Cdd:COG4717 126 QLLPLYQELEAL-EAELAELPERLEELEERLEELreLEEELEELEAELAELQEELEELLEQlsLATEEELQDLAEELEEL 204
|
170 180
....*....|....*....|....*..
gi 50348617 1076 NPQIMYLEQELESLKAVLEIKNEKLHQ 1102
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQ 231
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
886-1107 |
1.31e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 886 IQHLLSEREEALKQHKTLSQELVNLR---GELVTASTTCEKLEKARNELQtvyeaFVQQHQAEKTERENRLKEfYTREYE 962
Cdd:COG1340 73 VKELKEERDELNEKLNELREELDELRkelAELNKAGGSIDKLRKEIERLE-----WRQQTEVLSPEEEKELVE-KIKELE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 963 KLrdtyIEEAEKyKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLS---------EIKK-----GHEIEKK 1028
Cdd:COG1340 147 KE----LEKAKK-ALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEmielykeadELRKeadelHKEIVEA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1029 SLE-DLLSEKQESLEKQINDLKSENDALNEKLKsEEQKRRAREKANLKNPQIMyleqelESLKavleiKNEKLHQQDIKL 1107
Cdd:COG1340 222 QEKaDELHEEIIELQKELRELRKELKKLRKKQR-ALKREKEKEELEEKAEEIF------EKLK-----KGEKLTTEELKL 289
|
|
| DUF4686 |
pfam15742 |
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ... |
892-1177 |
1.80e-05 |
|
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.
Pssm-ID: 464838 [Multi-domain] Cd Length: 384 Bit Score: 48.52 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 892 EREEALKQHKT-LSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQ---------HQAEKTERENRLKEFYTREY 961
Cdd:pfam15742 41 GKNLDLKQHNSlLQEENIKIKAELKQAQQKLLDSTKMCSSLTAEWKHCQQKirelelevlKQAQSIKSQNSLQEKLAQEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 962 EKLRDtyieeAEKYKMQLQEQfdnLNAAHETSKLEIEASHSEKLEllKKAYEASLSEIK-KGHEIEKKSLEDLLSEKQES 1040
Cdd:pfam15742 121 SRVAD-----AEEKILELQQK---LEHAHKVCLTDTCILEKKQLE--ERIKEASENEAKlKQQYQEEQQKRKLLDQNVNE 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1041 LEKQINDLKSENDAL----------------------NEKLKSEEQKRRAREKANlknpQIMYLEQELESLKAVLEI--- 1095
Cdd:pfam15742 191 LQQQVRSLQDKEAQLemtnsqqqlriqqqeaqlkqleNEKRKSDEHLKSNQELSE----KLSSLQQEKEALQEELQQvlk 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1096 --------KNEKLHQQDIKLMKMEKlvdnntalvdklkRFQQENEELKARMdkhmaisRQLSTEQAVLQESLEKESKVNK 1167
Cdd:pfam15742 267 qldvhvrkYNEKHHHHKAKLRRAKD-------------RLVHEVEQRDERI-------KQLENEIGILQQQSEKEKAFQK 326
|
330
....*....|
gi 50348617 1168 RLSMENEELL 1177
Cdd:pfam15742 327 QVTAQNEILL 336
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
895-1175 |
1.91e-05 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 49.20 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 895 EALKQHKTLSQELVNL--RGELVTASTTC------EKLEKARNELQTVYEAFVQQHQAEkterenrlkEFYTREYEKLrd 966
Cdd:TIGR00618 184 MEFAKKKSLHGKAELLtlRSQLLTLCTPCmpdtyhERKQVLEKELKHLREALQQTQQSH---------AYLTQKREAQ-- 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 967 tyiEEAEKYKMQLQEQ------FDNLNAAHETSKLEIE--------ASHSEKLELLKKAYEASLSEIKKgheiEKKSLED 1032
Cdd:TIGR00618 253 ---EEQLKKQQLLKQLrarieeLRAQEAVLEETQERINrarkaaplAAHIKAVTQIEQQAQRIHTELQS----KMRSRAK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1033 LLSEKQeSLEKQINDLKSENDALNEKLKSEEQKRRAREKANLK-----------------NPQIMYLEQELESLKAVLEI 1095
Cdd:TIGR00618 326 LLMKRA-AHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIreiscqqhtltqhihtlQQQKTTLTQKLQSLCKELDI 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1096 KNEKLHQQDIKLMKME----KLVDNNTALVDKLKRFQQ--------------ENEELKARMDKHMAISRQLSTEQAVLQE 1157
Cdd:TIGR00618 405 LQREQATIDTRTSAFRdlqgQLAHAKKQQELQQRYAELcaaaitctaqceklEKIHLQESAQSLKEREQQLQTKEQIHLQ 484
|
330
....*....|....*...
gi 50348617 1158 SLEKESKVNKRLSMENEE 1175
Cdd:TIGR00618 485 ETRKKAVVLARLLELQEE 502
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
965-1177 |
1.99e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 965 RDTYIEEAEKYKMQLQEQFDNLNAAHEtsklEIEASHSEKLELLKKAyEASLSEIKKGHEIEKKSLEDLlSEKQESLEKQ 1044
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEKALA----ELRKELEELEEELEQL-RKELEELSRQISALRKDLARL-EAEVEQLEER 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1045 INDLKSENDALNEKLKSEEQKRrarEKANlknPQIMYLEQELESLKAV--------------LEIKNEKLHQQDIKLMKM 1110
Cdd:TIGR02168 749 IAQLSKELTELEAEIEELEERL---EEAE---EELAEAEAEIEELEAQieqlkeelkalreaLDELRAELTLLNEEAANL 822
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50348617 1111 EKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELL 1177
Cdd:TIGR02168 823 RERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEAL 889
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
959-1153 |
2.23e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 959 REYEKLRDTYIEEAEKykmqlqeqfdnlNAAHETSKLEIEAShsEKLELLKKAYEASLSEIKKghEIEKksLEDLLSEKQ 1038
Cdd:PRK12704 34 KEAEEEAKRILEEAKK------------EAEAIKKEALLEAK--EEIHKLRNEFEKELRERRN--ELQK--LEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1039 ESLEKQINDLKSENDALNEKLKSEEQKRRAREKanlknpqimyLEQELESLKAVLEIKNEK---LHQQDIKLMKMEKLVD 1115
Cdd:PRK12704 96 ENLDRKLELLEKREEELEKKEKELEQKQQELEK----------KEEELEELIEEQLQELERisgLTAEEAKEILLEKVEE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 50348617 1116 NNTAlvDKLKRFQQENEELKARMDKH------MAISRqLSTEQA 1153
Cdd:PRK12704 166 EARH--EAAVLIKEIEEEAKEEADKKakeilaQAIQR-CAADHV 206
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
817-1048 |
2.35e-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: 48.80 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 817 ALNAVEKSRQknprsLCIQPQTAPDALPPEktleLTQYKTKCENQSGFILQLKQLLACGN---TKFEALTVVIQHLLSE- 892
Cdd:COG3096 418 AVQALEKARA-----LCGLPDLTPENAEDY----LAAFRAKEQQATEEVLELEQKLSVADaarRQFEKAYELVCKIAGEv 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 893 -REEA-------LKQH---KTLSQELVNLRGELVTAsttcEKLEKARNELQTVYEAFVQQHQAEKTERENrLKEFYTREY 961
Cdd:COG3096 489 eRSQAwqtarelLRRYrsqQALAQRLQQLRAQLAEL----EQRLRQQQNAERLLEEFCQRIGQQLDAAEE-LEELLAELE 563
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 962 EKLRD--TYIEEAEKYKMQLQEQFDNLNAAHEtsKLEIEASH----SEKLELLKKAYEASL---SEIKKG------HEIE 1026
Cdd:COG3096 564 AQLEEleEQAAEAVEQRSELRQQLEQLRARIK--ELAARAPAwlaaQDALERLREQSGEALadsQEVTAAmqqlleRERE 641
|
250 260
....*....|....*....|..
gi 50348617 1027 KKSLEDLLSEKQESLEKQINDL 1048
Cdd:COG3096 642 ATVERDELAARKQALESQIERL 663
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
951-1102 |
2.50e-05 |
|
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: 46.44 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 951 NRLKEFY---TREYEKLRDTYieEAEKYKMQLQEQfDNLNAAHETSKlEIEaSHSEKLE-LLKKAYEasLSEIKKGHEIE 1026
Cdd:pfam13851 11 NEIKNYYndiTRNNLELIKSL--KEEIAELKKKEE-RNEKLMSEIQQ-ENK-RLTEPLQkAQEEVEE--LRKQLENYEKD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1027 KKSLEDLlSEKQESLEKQINDLKSENDALNEKLKSEEQKRRA------------REKANLKNpqiMYLEQELESLKAVLE 1094
Cdd:pfam13851 84 KQSLKNL-KARLKVLEKELKDLKWEHEVLEQRFEKVERERDElydkfeaaiqdvQQKTGLKN---LLLEKKLQALGETLE 159
|
....*...
gi 50348617 1095 IKNEKLHQ 1102
Cdd:pfam13851 160 KKEAQLNE 167
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
924-1148 |
2.61e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.61 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 924 LEKARNELQTVYEAFVQQHQAEkterENRLKEFYTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHET----------- 992
Cdd:pfam00038 23 LEQQNKLLETKISELRQKKGAE----PSRLYSLYEKEIEDLRRQ-LDTLTVERARLQLELDNLRLAAEDfrqkyedelnl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 993 --------------------SKLEIEA---SHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQEsLEKQINDLK 1049
Cdd:pfam00038 98 rtsaendlvglrkdldeatlARVDLEAkieSLKEELAFLKKNHEEEVRELQAQVSDTQVNVEMDAARKLD-LTSALAEIR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1050 SENDALNEKLKSE--------------------EQKRRAREKANLKNPQIMYLEQELESL---KAVLEIKNEKLHQQDIK 1106
Cdd:pfam00038 177 AQYEEIAAKNREEaeewyqskleelqqaaarngDALRSAKEEITELRRTIQSLEIELQSLkkqKASLERQLAETEERYEL 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 50348617 1107 LMKM--EKLVDNNTALV---DKLKRFQQENEEL---KARMDKHMAISRQL 1148
Cdd:pfam00038 257 QLADyqELISELEAELQetrQEMARQLREYQELlnvKLALDIEIATYRKL 306
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1005-1180 |
2.92e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.52 E-value: 2.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1005 LELLKKAYEaSLSEIKKGHEIEKKSLEDLLS----------EKQESLE---KQINDLKSENDALNEKL-KSEEQKRR--- 1067
Cdd:PRK03918 157 LDDYENAYK-NLGEVIKEIKRRIERLEKFIKrtenieelikEKEKELEevlREINEISSELPELREELeKLEKEVKElee 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1068 AREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNntalVDKLKRFQQENEELKARMDKHMAISRQ 1147
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE----LKELKEKAEEYIKLSEFYEEYLDELRE 311
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 50348617 1148 LSTE-----------QAVLQESLEKESKVNKrLSMENEELLWKL 1180
Cdd:PRK03918 312 IEKRlsrleeeingiEERIKELEEKEERLEE-LKKKLKELEKRL 354
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
878-1140 |
3.92e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 878 KFEALTVVIQHLLSEREEALKQHKTLSQELVNLRG---ELVtasttcEKLEKARNELQTVYEAfVQQHQAEKTERENRLK 954
Cdd:COG1340 16 KIEELREEIEELKEKRDELNEELKELAEKRDELNAqvkELR------EEAQELREKRDELNEK-VKELKEERDELNEKLN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 955 EFYT--REYEKLRDTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEAshsEKlELLKK--AYEASLSEIKKGHEIEKKSL 1030
Cdd:COG1340 89 ELREelDELRKELAELNKAGGSID-KLRKEIERLEWRQQTEVLSPEE---EK-ELVEKikELEKELEKAKKALEKNEKLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1031 EDL-----LSEKQESLEKQINDLKSENDALNEKLKSEEQKR-RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQD 1104
Cdd:COG1340 164 ELRaelkeLRKEAEEIHKKIKELAEEAQELHEEMIELYKEAdELRKEADELHKEIVEAQEKADELHEEIIELQKELRELR 243
|
250 260 270
....*....|....*....|....*....|....*.
gi 50348617 1105 IKLMKMEKlVDNNTALVDKLKRFQQENEELKARMDK 1140
Cdd:COG1340 244 KELKKLRK-KQRALKREKEKEELEEKAEEIFEKLKK 278
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
894-1066 |
5.34e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.60 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 894 EEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKefytREyeklrdtyIEEAE 973
Cdd:COG4913 284 WFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLE----RE--------IERLE 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 974 KYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEikkgheiekKSLEDLLSEKQESLEKQINDLKSEND 1053
Cdd:COG4913 352 RELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL---------EEELEALEEALAEAEAALRDLRRELR 422
|
170
....*....|...
gi 50348617 1054 ALNEKLKSEEQKR 1066
Cdd:COG4913 423 ELEAEIASLERRK 435
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
850-1141 |
5.51e-05 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 47.16 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 850 ELTQYKTKCENQSGFILQL--------KQLLAcGNTKFEALTVVIQHLLSEREEALKQHKTLSQElvnlrGELVTASTTC 921
Cdd:pfam06160 108 ELDELLESEEKNREEVEELkdkyrelrKTLLA-NRFSYGPAIDELEKQLAEIEEEFSQFEELTES-----GDYLEAREVL 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 922 EKLEKARNELQTVYEAFVQQHQaekterenRLKEFYTREYEKLRDTYIE-EAEKYK---MQLQEQFDNLNAAHETS---- 993
Cdd:pfam06160 182 EKLEEETDALEELMEDIPPLYE--------ELKTELPDQLEELKEGYREmEEEGYAlehLNVDKEIQQLEEQLEENlall 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 994 -KLEIEAShSEKLELLKKA----YEASLSEIKKGHEIEKKS--LEDLLS---------------------------EKQE 1039
Cdd:pfam06160 254 eNLELDEA-EEALEEIEERidqlYDLLEKEVDAKKYVEKNLpeIEDYLEhaeeqnkelkeelervqqsytlnenelERVR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1040 SLEKQINDLKSENDALNEKLKSEEQkrrarekanlknPQIMYLEQELESLKAVLEIKNEklhQQDIK--LMKMEKlvDNN 1117
Cdd:pfam06160 333 GLEKQLEELEKRYDEIVERLEEKEV------------AYSELQEELEEILEQLEEIEEE---QEEFKesLQSLRK--DEL 395
|
330 340
....*....|....*....|....
gi 50348617 1118 TALvDKLKRFQQENEELKARMDKH 1141
Cdd:pfam06160 396 EAR-EKLDEFKLELREIKRLVEKS 418
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
922-1158 |
5.85e-05 |
|
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: 46.95 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 922 EKLEKARnelqtvyeafvQQHQAEKTERENRLKEF-----YTREYEKLRDTYIEEAEKYKMQLQEqfdnlnaaHETSKLE 996
Cdd:pfam15558 109 EKLERAR-----------QEAEQRKQCQEQRLKEKeeelqALREQNSLQLQERLEEACHKRQLKE--------REEQKKV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 997 IEASHSEKL--ELLKKAYEaslSEIKKGHEIEKKSLEDLLSEKQESLEKQIndlKSENDALNEK-LKSEEQKRRAREKAN 1073
Cdd:pfam15558 170 QENNLSELLnhQARKVLVD---CQAKAEELLRRLSLEQSLQRSQENYEQLV---EERHRELREKaQKEEEQFQRAKWRAE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1074 LKNpqimylEQELESLKAVLEIKNEKL-----HQQDIKLMKMEKLVDNNTA-----LVDKLKRFQQEN---EELKARMDK 1140
Cdd:pfam15558 244 EKE------EERQEHKEALAELADRKIqqarqVAHKTVQDKAQRARELNLEreknhHILKLKVEKEEKchrEGIKEAIKK 317
|
250
....*....|....*....
gi 50348617 1141 HMAISRQLSTE-QAVLQES 1158
Cdd:pfam15558 318 KEQRSEQISREkEATLEEA 336
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
922-1153 |
6.10e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 47.44 E-value: 6.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 922 EKLEKARNELQTVYEAFVQQHQAE--KTERENRLKEFYTREYEKLRDTY-----IEEAEKYK---MQLQEQFDNLNAAHE 991
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEeaKKAEEAKIKAEELKKAEEEKKKVeqlkkKEAEEKKKaeeLKKAEEENKIKAAEE 1666
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 992 TSKLEIEASHSEKL------------ELLKKAYEA-SLSEIKKGHEIEKKSLEDLLSEKQESLEKqINDLKSENDalNEK 1058
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAkkaeedekkaaeALKKEAEEAkKAEELKKKEAEEKKKAEELKKAEEENKIK-AEEAKKEAE--EDK 1743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1059 LKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIK-LMKMEKLV----DNNTALVDKLKR---FQQE 1130
Cdd:PTZ00121 1744 KKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKrRMEVDKKIkdifDNFANIIEGGKEgnlVIND 1823
|
250 260
....*....|....*....|...
gi 50348617 1131 NEELKARMDKHMAISRQLSTEQA 1153
Cdd:PTZ00121 1824 SKEMEDSAIKEVADSKNMQLEEA 1846
|
|
| PKK |
pfam12474 |
Polo kinase kinase; This domain family is found in eukaryotes, and is approximately 140 amino ... |
1001-1152 |
6.26e-05 |
|
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: 44.09 E-value: 6.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1001 HSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEK-QINDLKsendALNEKLKSEEQKRRAREKANLKNpQI 1079
Cdd:pfam12474 1 HQLQKEQQKDRFEQERQQLKKRYEKELEQLERQQKQQIEKLEQrQTQELR----RLPKRIRAEQKKRLKMFRESLKQ-EK 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50348617 1080 MYLEQELESLKavleikneKLHQQDIKLMKMEKLvdnntalvdKLKRFQQENEELKARMDKHMAISRQLSTEQ 1152
Cdd:pfam12474 76 KELKQEVEKLP--------KFQRKEAKRQRKEEL---------ELEQKHEELEFLQAQSEALERELQQLQNEK 131
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
867-1170 |
9.30e-05 |
|
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: 45.71 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 867 QLKQLLACGNT---KFEALTVVIQHLLSEREEALKQHK-------TLSQELVNLRGELVTASTTCEKLEKARNELQTVYE 936
Cdd:pfam09728 5 ELMQLLNKLDSpeeKLAALCKKYAELLEEMKRLQKDLKklkkkqdQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 937 AFVQQHQAEKTERENRLKEFYTREYEKLRD--TYIEEAEKYKMQLQEQFDNLnaahetskleieashSEKLELLKKAYEa 1014
Cdd:pfam09728 85 KLKEESKKLAKEEEEKRKELSEKFQSTLKDiqDKMEEKSEKNNKLREENEEL---------------REKLKSLIEQYE- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1015 sLSEikkgheiekKSLEDLLseKQESLEKQINDLK-SENDALNEKLKSEEQKRRAREkanlKNPQIMYLEQELESLKAVL 1093
Cdd:pfam09728 149 -LRE---------LHFEKLL--KTKELEVQLAEAKlQQATEEEEKKAQEKEVAKARE----LKAQVQTLSETEKELREQL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1094 EIKNEKLHQ-QDIkLMKMEKLVDNNTA----LVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKR 1168
Cdd:pfam09728 213 NLYVEKFEEfQDT-LNKSNEVFTTFKKemekMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEK 291
|
..
gi 50348617 1169 LS 1170
Cdd:pfam09728 292 LE 293
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
890-1176 |
9.38e-05 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 46.75 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 890 LSEREEALKQhKTLSQELV-----NLRGElvtASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKL 964
Cdd:PRK04778 34 LEERKQELEN-LPVNDELEkvkklNLTGQ---SEEKFEEWRQKWDEIVTNSLPDIEEQLFEAEELNDKFRFRKAKHEINE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 965 RDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEAshseklelLKKAYEaslsEIKKghEIEKKSleDLLSEKQESLEKQ 1044
Cdd:PRK04778 110 IESLLDLIEEDIEQILEELQELLESEEKNREEVEQ--------LKDLYR----ELRK--SLLANR--FSFGPALDELEKQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1045 INDLKSE---NDALNEK---LKSEEQKRRAREK-ANLKN-----PQIMY-----LEQELESLKAVL-EIKNEKLHQQDIK 1106
Cdd:PRK04778 174 LENLEEEfsqFVELTESgdyVEAREILDQLEEElAALEQimeeiPELLKelqteLPDQLQELKAGYrELVEEGYHLDHLD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1107 LMKM-----EKLVDNNTALVD-KLKRFQQENEELKARMDK------HMAISRQ-LSTEQAVLQESLEKESKVNKRLSMEN 1173
Cdd:PRK04778 254 IEKEiqdlkEQIDENLALLEElDLDEAEEKNEEIQERIDQlydileREVKARKyVEKNSDTLPDFLEHAKEQNKELKEEI 333
|
...
gi 50348617 1174 EEL 1176
Cdd:PRK04778 334 DRV 336
|
|
| Jnk-SapK_ap_N |
pfam09744 |
JNK_SAPK-associated protein-1; This is the N-terminal 200 residues of a set of proteins ... |
959-1125 |
9.64e-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: 43.76 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 959 REYEKLRDTYIEEAEKYKM----QLQEQFDNLNAAHETSKLEIEAShSEKLELLKKAYEASlSEIKKGHEIEKKSLEDLL 1034
Cdd:pfam09744 10 KEFERLIDRYGEDVVKGLMpkvvNVLELLESLASRNQEHNVELEEL-REDNEQLETQYERE-KALRKRAEEELEEIEDQW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1035 SEKQESLEKQINDLKSENDALneklkseEQKRRARekanlknpqimyleqeLESLKAVLEIKNEKLHQQDIKLMKmeKLV 1114
Cdd:pfam09744 88 EQETKDLLSQVESLEEENRRL-------EADHVSR----------------LEEKEAELKKEYSKLHERETEVLR--KLK 142
|
170
....*....|.
gi 50348617 1115 DnntaLVDKLK 1125
Cdd:pfam09744 143 E----VVDRQR 149
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
850-1137 |
9.80e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 9.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 850 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 929
Cdd:COG4372 46 ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 930 ELQT---VYEAFVQQHQAEKTERENRLKEFYTREYEKLRDtyIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1006
Cdd:COG4372 126 DLEQqrkQLEAQIAELQSEIAEREEELKELEEQLESLQEE--LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1007 LLKKAYEASLSEIKKGHEIEKKSLE---DLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLE 1083
Cdd:COG4372 204 EAEKLIESLPRELAEELLEAKDSLEaklGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 50348617 1084 QELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR 1137
Cdd:COG4372 284 ELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLA 337
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
925-1168 |
1.13e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 46.67 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 925 EKARNELQTVYEAFVQQHQAEKTEREnRLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEiEASHSEK 1004
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEE-RNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEE 1300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1005 L----ELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRARE-KANLKNPQI 1079
Cdd:PTZ00121 1301 KkkadEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkKKEEAKKKA 1380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1080 MYLEQELESLKAVLEIKneKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQEN---EELKARM-DKHMAISRQLSTEQAVL 1155
Cdd:PTZ00121 1381 DAAKKKAEEKKKADEAK--KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKkkaDEAKKKAeEAKKADEAKKKAEEAKK 1458
|
250
....*....|...
gi 50348617 1156 QESLEKESKVNKR 1168
Cdd:PTZ00121 1459 AEEAKKKAEEAKK 1471
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
994-1139 |
1.28e-04 |
|
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: 43.45 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 994 KLEIEASHSEKLELLKKAYEASLSEIKKGHEIEkksledllsekqeSLEKQINDLKSENDALNEKLKseEQKRRAREKAN 1073
Cdd:pfam12718 6 KLEAENAQERAEELEEKVKELEQENLEKEQEIK-------------SLTHKNQQLEEEVEKLEEQLK--EAKEKAEESEK 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50348617 1074 LK------NPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKlvdnntalvdKLKRFQQENEELKARMD 1139
Cdd:pfam12718 71 LKtnnenlTRKIQLLEEELEESDKRLKETTEKLRETDVKAEHLER----------KVQALEQERDEWEKKYE 132
|
|
| SHE3 |
pfam17078 |
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ... |
938-1103 |
1.29e-04 |
|
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: 44.73 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 938 FVQQHQAEKTERENrLKEFYTREYEKLRDTyieeaEKYKMQLQEQFDNLNAAHETSKLE------IEASHSEKLELLKKA 1011
Cdd:pfam17078 43 FLENLASLKHENDN-LSSMLNRKERRLKDL-----EDQLSELKNSYEELTESNKQLKKRlenssaSETTLEAELERLQIQ 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1012 YEASLSEIK--KGH---EIE--KKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREkaNLKNPQIMYLEQ 1084
Cdd:pfam17078 117 YDALVDSQNeyKDHyqqEINtlQESLEDLKLENEKQLENYQQRISSNDKDIDTKLDSYNNKFKNLD--NIYVNKNNKLLT 194
|
170 180
....*....|....*....|
gi 50348617 1085 ELESLKAVLEIKN-EKLHQQ 1103
Cdd:pfam17078 195 KLDSLAQLLDLPSwLNLYPE 214
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1025-1164 |
1.44e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.92 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1025 IEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE------EQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNE 1098
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEakeeihKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348617 1099 KLHQQDIKLMKMEKLVDNNTALVDKLkrfQQENEELKARMDKHMAISRQLSTEQA--VLQESLEKESK 1164
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKK---EEELEELIEEQLQELERISGLTAEEAkeILLEKVEEEAR 168
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1030-1180 |
1.61e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1030 LEDLLSEkqesLEKQINDLKSE-NDALN-EKLKSEEQKRRAREKANlknpQIMYLEQELESLKAVLEIKNEKLHQQDIKL 1107
Cdd:COG1196 191 LEDILGE----LERQLEPLERQaEKAERyRELKEELKELEAELLLL----KLRELEAELEELEAELEELEAELEELEAEL 262
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50348617 1108 MKMEKLVDNNTAlvdKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKL 1180
Cdd:COG1196 263 AELEAELEELRL---ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
|
|
| GAS |
pfam13851 |
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ... |
1008-1161 |
1.69e-04 |
|
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: 44.13 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1008 LKKAYEASLSEIKKGH-EIEKKSLEDL---------LSEKQESLEKQINDLKSENDALNEKLKsEEQKRRAREKANLKNP 1077
Cdd:pfam13851 2 LMKNHEKAFNEIKNYYnDITRNNLELIkslkeeiaeLKKKEERNEKLMSEIQQENKRLTEPLQ-KAQEEVEELRKQLENY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1078 QimYLEQELESLKAVLEIKNEKL----HQQDIKLMKMEKLVDNNTALvdkLKRFQQENEELKARMD-KHMAISRQLSTeq 1152
Cdd:pfam13851 81 E--KDKQSLKNLKARLKVLEKELkdlkWEHEVLEQRFEKVERERDEL---YDKFEAAIQDVQQKTGlKNLLLEKKLQA-- 153
|
....*....
gi 50348617 1153 avLQESLEK 1161
Cdd:pfam13851 154 --LGETLEK 160
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
856-1107 |
2.10e-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: 45.60 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 856 TKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQhktLSQELVNLRGELVtasttcEKLEKARNELQTVY 935
Cdd:pfam12128 244 TKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAE---LNQLLRTLDDQWK------EKRDELNGELSAAD 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 936 EAfVQQHQAEKTERENRLKEFYTREYEKLR---------DTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLE 1006
Cdd:pfam12128 315 AA-VAKDRSELEALEDQHGAFLDADIETAAadqeqlpswQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIA 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1007 LLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE--------------EQKR------ 1066
Cdd:pfam12128 394 GIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELklrlnqatatpellLQLEnfderi 473
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 50348617 1067 -RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKL 1107
Cdd:pfam12128 474 eRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRL 515
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
979-1176 |
2.16e-04 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 45.30 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 979 LQE----QFDNLNAAHETSKLEIEASH----SEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESL---EKQIND 1047
Cdd:PRK05771 25 LHElgvvHIEDLKEELSNERLRKLRSLltklSEALDKLRSYLPKLNPLREEKKKVSVKSLEELIKDVEEELekiEKEIKE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1048 LKSENDALNEKLKSEEQKRRAREK-ANLKNPQImyLEQELESLKAVL------EIKNEKLHQQDIKLMKMEKLVDNNTAL 1120
Cdd:PRK05771 105 LEEEISELENEIKELEQEIERLEPwGNFDLDLS--LLLGFKYVSVFVgtvpedKLEELKLESDVENVEYISTDKGYVYVV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1121 VDKLKRFQQE-NEELKarmdKHMAISRQLSTE---QAVLQESLEKESKVNKRLSMENEEL 1176
Cdd:PRK05771 183 VVVLKELSDEvEEELK----KLGFERLELEEEgtpSELIREIKEELEEIEKERESLLEEL 238
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
969-1182 |
2.50e-04 |
|
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: 45.35 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 969 IEEAEKYKMQLQEQFDNLNAAHETSKLEIEASH--SEKLELLKKAYEASLSEIK-KGHEIEKKSLEDLLSEKQESLEKQI 1045
Cdd:pfam02463 159 EEEAAGSRLKRKKKEALKKLIEETENLAELIIDleELKLQELKLKEQAKKALEYyQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1046 NDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMyLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLK 1125
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKE-NKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 50348617 1126 RFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLSMENEELLWKLHN 1182
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEE 374
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1028-1185 |
2.80e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.52 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1028 KSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRArekanlknpqimyleqeleslkavleiKNEKLHQQDIKL 1107
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDE---------------------------LNAQVKELREEA 59
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348617 1108 MKMEKLVDnntALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLsmenEELLWKLHNGDL 1185
Cdd:COG1340 60 QELREKRD---ELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEI----ERLEWRQQTEVL 130
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
945-1065 |
2.83e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 945 EKTERENRLKEFYTREYEKLRdtyiEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEI----- 1019
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALL----KEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELrqlqk 598
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 50348617 1020 KKGHEIEKKSLED---LLSEKQESLEKQINDLKSENDALNE----KLKSEEQK 1065
Cdd:PRK00409 599 GGYASVKAHELIEarkRLNKANEKKEKKKKKQKEKQEELKVgdevKYLSLGQK 651
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
978-1176 |
2.83e-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: 45.12 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 978 QLQEQFDNLNAAHETSKLEIEaSHSEKLELLKKAYEASLS---EIKKGHEIEK--KSLEDLLSEKQESLEKQIN---DLK 1049
Cdd:pfam05557 4 LIESKARLSQLQNEKKQMELE-HKRARIELEKKASALKRQldrESDRNQELQKriRLLEKREAEAEEALREQAElnrLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1050 SENDALNEKLKSEEQKR-RARE-KANLKNP------QIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALV 1121
Cdd:pfam05557 83 KYLEALNKKLNEKESQLaDAREvISCLKNElselrrQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50348617 1122 DKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVnKRLSMENEEL 1176
Cdd:pfam05557 163 SSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKEL-ERLREHNKHL 216
|
|
| Snf7 |
pfam03357 |
Snf7; This family of proteins are involved in protein sorting and transport from the endosome ... |
1031-1180 |
2.95e-04 |
|
Snf7; This family of proteins are involved in protein sorting and transport from the endosome to the vacuole/lysosome in eukaryotic cells. Vacuoles/lysosomes play an important role in the degradation of both lipids and cellular proteins. In order to perform this degradative function, vacuoles/lysosomes contain numerous hydrolases which have been transported in the form of inactive precursors via the biosynthetic pathway and are proteolytically activated upon delivery to the vacuole/lysosome. The delivery of transmembrane proteins, such as activated cell surface receptors to the lumen of the vacuole/lysosome, either for degradation/downregulation, or in the case of hydrolases, for proper localization, requires the formation of multivesicular bodies (MVBs). These late endosomal structures are formed by invaginating and budding of the limiting membrane into the lumen of the compartment. During this process, a subset of the endosomal membrane proteins is sorted into the forming vesicles. Mature MVBs fuse with the vacuole/lysosome, thereby releasing cargo containing vesicles into its hydrolytic lumen for degradation. Endosomal proteins that are not sorted into the intralumenal MVB vesicles are either recycled back to the plasma membrane or Golgi complex, or remain in the limiting membrane of the MVB and are thereby transported to the limiting membrane of the vacuole/lysosome as a consequence of fusion. Therefore, the MVB sorting pathway plays a critical role in the decision between recycling and degradation of membrane proteins. A few archaeal sequences are also present within this family.
Pssm-ID: 460896 [Multi-domain] Cd Length: 168 Bit Score: 42.99 E-value: 2.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1031 EDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNpQIMYLEQELESLKAVLE-IKNEKLHQQDIKLMK 1109
Cdd:pfam03357 10 IRKLDKKQESLEKKIEKLELEIKKLAKKGNKDAALLLLKQKKRYEK-QLDQLDGQLSNLEQQRMaIENAKSNQEVLNAMK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1110 --------MEKLVDnntalVDKLKRFQQENEELKARMD-KHMAISRQLSTEQAVLQESLEKEskVNKRLSMENEELLWKL 1180
Cdd:pfam03357 89 qgakamkaMNKLMD-----IDKIDKLMDEIEDQMEKADeISEMLSDPLDDADEEDEEELDAE--LDALLDEIGDEESVEL 161
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
891-1170 |
3.91e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 44.65 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 891 SEREEALKQHKTLSQELVN----LRGELVTASTTCEKLEKARNELqtvyEAFVQQHQAEKTERENRLKEFyTREYEKLRD 966
Cdd:PRK02224 324 EELRDRLEECRVAAQAHNEeaesLREDADDLEERAEELREEAAEL----ESELEEAREAVEDRREEIEEL-EEEIEELRE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 967 TY------IEEAEKYKMQLQEqfdNLNAAHETSKlEIEASHSEKLELLKKAyEASLSEIKK---GHEIEKKSLEDLLSEK 1037
Cdd:PRK02224 399 RFgdapvdLGNAEDFLEELRE---ERDELREREA-ELEATLRTARERVEEA-EALLEAGKCpecGQPVEGSPHVETIEED 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1038 QE---SLEKQINDLKSENDALNEKLKSEEQ-----KRRAREKANLKNpqimyLEQELESLKAVLEIKNEKLhqqdiklmk 1109
Cdd:PRK02224 474 RErveELEAELEDLEEEVEEVEERLERAEDlveaeDRIERLEERRED-----LEELIAERRETIEEKRERA--------- 539
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 50348617 1110 mEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNKRLS 1170
Cdd:PRK02224 540 -EELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLA 599
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
893-1160 |
5.09e-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: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 893 REEALKQHKTLSQELVNLRGELV-TASTTcekleKARNELQTVYEAFVQQHQaEKTERENRLKEFYTREYEKLRDTYIEE 971
Cdd:pfam01576 287 RNKAEKQRRDLGEELEALKTELEdTLDTT-----AAQQELRSKREQEVTELK-KALEEETRSHEAQLQEMRQKHTQALEE 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 972 aekykmqLQEQFDNLN---AAHETSKLEIEASHSEKLELLKkayeaSLSEIKKGHEIEKKSLEDLLSE-----------K 1037
Cdd:pfam01576 361 -------LTEQLEQAKrnkANLEKAKQALESENAELQAELR-----TLQQAKQDSEHKRKKLEGQLQElqarlseserqR 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1038 QESLEKqINDLKSENDALNEKLKSEEQK-----------------------RRAREKANLKNpQIMYLEQELESLKAVLE 1094
Cdd:pfam01576 429 AELAEK-LSKLQSELESVSSLLNEAEGKniklskdvsslesqlqdtqellqEETRQKLNLST-RLRQLEDERNSLQEQLE 506
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50348617 1095 IKNEK-------LHQQDIKLMKMEKLVDNNTALVDKL----KRFQQENEELKARMDKHMAISRQLSTEQAVLQESLE 1160
Cdd:pfam01576 507 EEEEAkrnverqLSTLQAQLSDMKKKLEEDAGTLEALeegkKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELD 583
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
969-1112 |
5.26e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 5.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 969 IEEAEKYKMQLQEQFDNLnaahetskleIEASHSEKLELLKKAYEASlsEIKKGHEIEKKSLEDLLSEKQESLEKQINDL 1048
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNEL----------IASLEELERELEQKAEEAE--ALLKEAEKLKEELEEKKEKLQEEEDKLLEEA 571
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50348617 1049 KSE-NDALNE-KLKSEEQKRRAREKANLKNPQIMylEQELESLKAVLEIKNEKLHQQDIKLMKMEK 1112
Cdd:PRK00409 572 EKEaQQAIKEaKKEADEIIKELRQLQKGGYASVK--AHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| fliH |
PRK06669 |
flagellar assembly protein H; Validated |
952-1095 |
6.83e-04 |
|
flagellar assembly protein H; Validated
Pssm-ID: 235850 [Multi-domain] Cd Length: 281 Bit Score: 43.08 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 952 RLKEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSE--KLELLKKAYEASLSEIKKGHEIEK-- 1027
Cdd:PRK06669 26 RFKVLSIKEKERLREEEEEQVEQLREEANDEAKEIIEEAEEDAFEIVEAAEEeaKEELLKKTDEASSIIEKLQMQIEReq 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 50348617 1028 -KSLEDLLSEKQESLEKQIND--LKSENDALNEKLKSEEQKRRAREKANLK-NPQIMYLEQELESLkaVLEI 1095
Cdd:PRK06669 106 eEWEEELERLIEEAKAEGYEEgyEKGREEGLEEVRELIEQLNKIIEKLIKKrEEILESSEEEIVEL--ALDI 175
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
939-1143 |
6.97e-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: 42.71 E-value: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 939 VQQHQAEKTERENRLKEFyTREYEKLRDTyIEEAEKYKMQLQEQFDNLNAAHETSKlEIEASHSEKLELLKKAYEASlSE 1018
Cdd:pfam00261 3 MQQIKEELDEAEERLKEA-MKKLEEAEKR-AEKAEAEVAALNRRIQLLEEELERTE-ERLAEALEKLEEAEKAADES-ER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1019 IKKGheIEKKSLEDllSEKQESLEKQINDLKSENDALNEKLKSEEQK--------RRAREKANLKNPQIMYLEQEL---- 1086
Cdd:pfam00261 79 GRKV--LENRALKD--EEKMEILEAQLKEAKEIAEEADRKYEEVARKlvvvegdlERAEERAELAESKIVELEEELkvvg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1087 ESLKAvLEIKNEKLHQQDIK-------------------------LMKMEKLVDnntALVDKLKRFQQENEELKARMDKH 1141
Cdd:pfam00261 155 NNLKS-LEASEEKASEREDKyeeqirflteklkeaetraefaersVQKLEKEVD---RLEDELEAEKEKYKAISEELDQT 230
|
..
gi 50348617 1142 MA 1143
Cdd:pfam00261 231 LA 232
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
846-1161 |
7.35e-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: 43.52 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 846 EKTLEltQYKTKCENQSGFILQLKQLLacgntkfEALTVVIQHLLSEREEALK------QHKTLSQELVNLRGELVTAST 919
Cdd:pfam05622 134 EATVE--TYKKKLEDLGDLRRQVKLLE-------ERNAEYMQRTLQLEEELKKanalrgQLETYKRQVQELHGKLSEESK 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 920 TCEKLEKARNELQTVYEAFVQqhqaektERENRLKEfytreyeklRDTYIEEAEKYK-MQLQEqfdnlnaAHETSKLEIE 998
Cdd:pfam05622 205 KADKLEFEYKKLEEKLEALQK-------EKERLIIE---------RDTLRETNEELRcAQLQQ-------AELSQADALL 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 999 ASHSEKLELLkkAYEASLSEIKKghEIEKKSLED-LLSEKQE-SLEKQINDLKSENDalneklKSEEQKRRAREKANLKN 1076
Cdd:pfam05622 262 SPSSDPGDNL--AAEIMPAEIRE--KLIRLQHENkMLRLGQEgSYRERLTELQQLLE------DANRRKNELETQNRLAN 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1077 PQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKArmdkhmAISRQLSTEQAVLQ 1156
Cdd:pfam05622 332 QRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEEHLEKLHEAQSELQKKKEQIEELEP------KQDSNLAQKIDELQ 405
|
....*
gi 50348617 1157 ESLEK 1161
Cdd:pfam05622 406 EALRK 410
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
994-1112 |
7.75e-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: 7.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 994 KLEIEASHSEKLELlkkayEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSE----EQKRRAR 1069
Cdd:COG0542 403 RMEIDSKPEELDEL-----ERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEkeliEEIQELK 477
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348617 1070 EKANLKNPQIMYLEQELESLKAVLEIKNEKLHQ----QDI---------------------KLMKMEK 1112
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREevteEDIaevvsrwtgipvgkllegereKLLNLEE 545
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
890-1162 |
7.92e-04 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.98 E-value: 7.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 890 LSEREEALKQHKTLSQELVNLRGELVTAsttcEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTYI 969
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKA----EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYE 1602
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 970 EEAEKYKMQLQEQFDNLNAAHETSKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLK 1049
Cdd:PTZ00121 1603 EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAE-EAKKAEEDKKKAEEAK 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1050 SENDalNEKLKSEEQKRRAREKANLKNPQimylEQELESLKAVLEIKNEKlHQQDIKLMKMEKLVDNNTALVDKLKRFQQ 1129
Cdd:PTZ00121 1682 KAEE--DEKKAAEALKKEAEEAKKAEELK----KKEAEEKKKAEELKKAE-EENKIKAEEAKKEAEEDKKKAEEAKKDEE 1754
|
250 260 270
....*....|....*....|....*....|....
gi 50348617 1130 ENEELKARMDKHMAISRQLSTE-QAVLQESLEKE 1162
Cdd:PTZ00121 1755 EKKKIAHLKKEEEKKAEEIRKEkEAVIEEELDEE 1788
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
850-1141 |
8.37e-04 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.67 E-value: 8.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 850 ELTQYKTKCENQSGFILQL--------KQLLAcGNTKFEALTVVIQHLLSEREEALKQHKTLSQElvnlrGELVTASttc 921
Cdd:PRK04778 127 ELQELLESEEKNREEVEQLkdlyrelrKSLLA-NRFSFGPALDELEKQLENLEEEFSQFVELTES-----GDYVEAR--- 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 922 EKLEKARNELQTVyeafvqQHQAEK-----TERENRLKEfytrEYEKLRDTYIE-EAEKYK---MQLQEQFDNLNAAHET 992
Cdd:PRK04778 198 EILDQLEEELAAL------EQIMEEipellKELQTELPD----QLQELKAGYRElVEEGYHldhLDIEKEIQDLKEQIDE 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 993 -----SKLEIEAShSEKLELLKKA----YEASLSEIKKGHEIEKKS--LEDLLS-------------------------- 1035
Cdd:PRK04778 268 nlallEELDLDEA-EEKNEEIQERidqlYDILEREVKARKYVEKNSdtLPDFLEhakeqnkelkeeidrvkqsytlnese 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1036 -EKQESLEKQINDLKSENDALNEKLksEEQKRRAREkanlknpqimyLEQELESLKAVL-EIKNEklhQQDIK--LMKME 1111
Cdd:PRK04778 347 lESVRQLEKQLESLEKQYDEITERI--AEQEIAYSE-----------LQEELEEILKQLeEIEKE---QEKLSemLQGLR 410
|
330 340 350
....*....|....*....|....*....|
gi 50348617 1112 KlvDNNTALvDKLKRFQQENEELKARMDKH 1141
Cdd:PRK04778 411 K--DELEAR-EKLERYRNKLHEIKRYLEKS 437
|
|
| ATG16 |
pfam08614 |
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ... |
926-1073 |
9.51e-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: 41.46 E-value: 9.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 926 KARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYE----KLRDtyiEEAEKYKM--QLQEQFDNLNAAHETSKLEIEA 999
Cdd:pfam08614 20 EAENAKLQSEPESVLPSTSSSKLSKASPQSASIQSLEqllaQLRE---ELAELYRSrgELAQRLVDLNEELQELEKKLRE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348617 1000 ShSEKLELLKkAYEASLseikkghEIEKKSLEDLLSEKQesleKQINDLKSENDALNEKLKSEEQKRRAREKAN 1073
Cdd:pfam08614 97 D-ERRLAALE-AERAQL-------EEKLKDREEELREKR----KLNQDLQDELVALQLQLNMAEEKLRKLEKEN 157
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
923-1176 |
9.98e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 43.53 E-value: 9.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 923 KLEKARNELQTVYEAFVQQHQAEKTERENR---LKEFYTREYEKLRDTYIEEaeKYKMQLQEQFDNLNAAHETSKLEIEA 999
Cdd:COG5022 814 SYLACIIKLQKTIKREKKLRETEEVEFSLKaevLIQKFGRSLKAKKRFSLLK--KETIYLQSAQRVELAERQLQELKIDV 891
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1000 SHSEKLELLKKAYEASLSEIKKgheiekkSLEDLLSEKqeslekqiNDLKSENDALNEKLKSEEQKRRAREKANLKNPQI 1079
Cdd:COG5022 892 KSISSLKLVNLELESEIIELKK-------SLSSDLIEN--------LEFKTELIARLKKLLNNIDLEEGPSIEYVKLPEL 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1080 MYLEQELESLKAVLEIKNEKLHQQDI-------KLMKMEKLVDNNTALVDKLKRFQQENEELKARMDK---HMAISRQLS 1149
Cdd:COG5022 957 NKLHEVESKLKETSEEYEDLLKKSTIlvregnkANSELKNFKKELAELSKQYGALQESTKQLKELPVEvaeLQSASKIIS 1036
|
250 260
....*....|....*....|....*..
gi 50348617 1150 TEQAVLQeSLEKESKVNKRLSMENEEL 1176
Cdd:COG5022 1037 SESTELS-ILKPLQKLKGLLLLENNQL 1062
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
890-1176 |
1.07e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 890 LSEREEALKQHKTLSQELVNLRGEL-VTASTTCEKLEKARNELQTVYEAF-VQQ------HQA----EKTERENRLKEFy 957
Cdd:PRK04863 357 LEELEERLEEQNEVVEEADEQQEENeARAEAAEEEVDELKSQLADYQQALdVQQtraiqyQQAvqalERAKQLCGLPDL- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 958 trEYEKLRDtYIEEaekYKMQLQEQFDNLNAAHEtsKLEIEASHSEKLEllkKAYEASLS-----EIKKGHEIEKKSLED 1032
Cdd:PRK04863 436 --TADNAED-WLEE---FQAKEQEATEELLSLEQ--KLSVAQAAHSQFE---QAYQLVRKiagevSRSEAWDVARELLRR 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1033 LlsEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQdiklmkMEK 1112
Cdd:PRK04863 505 L--REQRHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES------VSE 576
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 50348617 1113 LVDNNTALVDKLKRFQQENEELKAR----MDKHMAISR-------QLSTEQAV---LQESLEKEskvnKRLSMENEEL 1176
Cdd:PRK04863 577 ARERRMALRQQLEQLQARIQRLAARapawLAAQDALARlreqsgeEFEDSQDVteyMQQLLERE----RELTVERDEL 650
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
922-1169 |
1.24e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 43.21 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 922 EKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYTREYEKLRDTyIEEAEKYKmQLQEQFDNLNAAHETSKLEIEASH 1001
Cdd:PTZ00121 1394 DEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKK-AEEAKKAD-EAKKKAEEAKKAEEAKKKAEEAKK 1471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1002 SEklELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRARE--KA-NLKNPQ 1078
Cdd:PTZ00121 1472 AD--EAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEakKAeEKKKAD 1549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1079 IMYLEQELESLKAVLEIKNEKLHQQD--IKLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHmaisrqlSTEQAVLQ 1156
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKAEEAKKAEEDknMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKK-------AEEAKIKA 1622
|
250
....*....|...
gi 50348617 1157 ESLEKESKVNKRL 1169
Cdd:PTZ00121 1623 EELKKAEEEKKKV 1635
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
926-1175 |
1.24e-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: 42.60 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 926 KARNELQTVYEAfvQQHQAEKTERENRLKEfytreYEKLRDTYIEEAEKYKMQLQEQfdnlnaahetskleIEASHSEKL 1005
Cdd:pfam13868 32 KRIKAEEKEEER--RLDEMMEEERERALEE-----EEEKEEERKEERKRYRQELEEQ--------------IEEREQKRQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1006 EllkkAYEASLSEIKKGHEIEKKSLEDLLSEKQESLEKQINdLKSENDALNEKLKSEEQKRRAREK-ANLKNpqimyleq 1084
Cdd:pfam13868 91 E----EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQ-LREEIDEFNEEQAEWKELEKEEEReEDERI-------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1085 eLESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEELKAR--MDKHMAISRQLSTEQAvlqeslEKE 1162
Cdd:pfam13868 158 -LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKlyQEEQERKERQKEREEA------EKK 230
|
250
....*....|...
gi 50348617 1163 SKVNKRLSMENEE 1175
Cdd:pfam13868 231 ARQRQELQQAREE 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
849-1070 |
1.59e-03 |
|
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: 42.75 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 849 LELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELvtasttcEKLEKAR 928
Cdd:TIGR02169 329 AEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKL-------EKLKREI 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 929 NELQtvyeafvqqhqaekterenrlkefytREYEKLRDTyieeaekyKMQLQEQFDNLNAAHETSKLEIEASHSEKLELL 1008
Cdd:TIGR02169 402 NELK--------------------------RELDRLQEE--------LQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348617 1009 K--KAYEASLSEIKKGHEIEKKSLEDlLSEKQESLEKQINDLKSENDALneklksEEQKRRARE 1070
Cdd:TIGR02169 448 LeiKKQEWKLEQLAADLSKYEQELYD-LKEEYDRVEKELSKLQRELAEA------EAQARASEE 504
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
936-1161 |
1.63e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 936 EAFVQQHQAEKT---ERENRLKEFYtREYEKLRDTYIEEAEKYKM--QLQEQFDNLNAAHET-SKLEIEASH------SE 1003
Cdd:COG4913 210 DDFVREYMLEEPdtfEAADALVEHF-DDLERAHEALEDAREQIELlePIRELAERYAAARERlAELEYLRAAlrlwfaQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1004 KLELLKKAYEASLSEIKKgHEIEKKSLEDLLSEKQESLE-----------KQINDLKSENDALNEKLkseEQKRRAREKa 1072
Cdd:COG4913 289 RLELLEAELEELRAELAR-LEAELERLEARLDALREELDeleaqirgnggDRLEQLEREIERLEREL---EERERRRAR- 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1073 nlknpqimyLEQELESLKavLEIKNEKlhqqdiklmkmEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQ 1152
Cdd:COG4913 364 ---------LEALLAALG--LPLPASA-----------EEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
250
....*....|..
gi 50348617 1153 AVLQ---ESLEK 1161
Cdd:COG4913 422 RELEaeiASLER 433
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
901-1175 |
1.65e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 42.90 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 901 KTLSQELVNLRGELVtasttcEKLEKARNELQTvyEAFVQQHqaEKTERENRLKEFYTREYEKLRDTYIEEaekYKMQLQ 980
Cdd:PTZ00440 896 KQLVEHLLNNKIDLK------NKLEQHMKIINT--DNIIQKN--EKLNLLNNLNKEKEKIEKQLSDTKINN---LKMQIE 962
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 981 EQFDnlnaAHETSKLEIEA---SHSEKLELLKKAYEASLSEIKK---GHEIEKKSLEDLLSE-KQESLEKQINDLKSEND 1053
Cdd:PTZ00440 963 KTLE----YYDKSKENINGndgTHLEKLDKEKDEWEHFKSEIDKlnvNYNILNKKIDDLIKKqHDDIIELIDKLIKEKGK 1038
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1054 ALNEKLKSeeqkrrarekanlknpQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE 1133
Cdd:PTZ00440 1039 EIEEKVDQ----------------YISLLEKMKTKLSSFHFNIDIKKYKNPKIKEEIKLLEEKVEALLKKIDENKNKLIE 1102
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 50348617 1134 LKARMDKHMAISRQLSTEQAVL----QESLEK-----ESKVNKRLSMENEE 1175
Cdd:PTZ00440 1103 IKNKSHEHVVNADKEKNKQTEHynkkKKSLEKiykqmEKTLKELENMNLED 1153
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
886-1104 |
1.76e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 886 IQHLLSEREEALKQHKTLSQELVNLRGELVTASttcEKLEKARNELQTVyEAFVQQHQAEKTERENRLKEFYtreyeklr 965
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELN---EEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERR-------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 966 dtyieeaEKYKMQLQEQFDNLNAaheTSKLE-IEASHS-----EKLELLKKAYEASLSEIKkgheiEKKSLEDLLSEKQE 1039
Cdd:COG3883 86 -------EELGERARALYRSGGS---VSYLDvLLGSESfsdflDRLSALSKIADADADLLE-----ELKADKAELEAKKA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 50348617 1040 SLEKQINDLKSENDALNEKLKS-EEQKRRAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQD 1104
Cdd:COG3883 151 ELEAKLAELEALKAELEAAKAElEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAA 216
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
862-1188 |
2.53e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.26 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 862 SGFILQLKQLLACGNTKFEALTVVIQHL------LSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQTVY 935
Cdd:TIGR00618 204 QLLTLCTPCMPDTYHERKQVLEKELKHLrealqqTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQ 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 936 EAFVQQHQAEKterenrlkefYTREYEKLrdTYIE-EAEKYKMQLQEQFDNLNAA--HETSKLEIEASHSEKLELLKKAY 1012
Cdd:TIGR00618 284 ERINRARKAAP----------LAAHIKAV--TQIEqQAQRIHTELQSKMRSRAKLlmKRAAHVKQQSSIEEQRRLLQTLH 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1013 EASlSEIKKGHEIEKKSLEDllSEKQESLEKQINDLKSENDALNEKLKSEEQK----RRAREKANLKNPQIMYLEQELES 1088
Cdd:TIGR00618 352 SQE-IHIRDAHEVATSIREI--SCQQHTLTQHIHTLQQQKTTLTQKLQSLCKEldilQREQATIDTRTSAFRDLQGQLAH 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1089 LKAVLEIKNEKLHQQDIKLMK-MEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESKVNK 1167
Cdd:TIGR00618 429 AKKQQELQQRYAELCAAAITCtAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCG 508
|
330 340
....*....|....*....|.
gi 50348617 1168 RLSMENEELLWKLHNGDLCSP 1188
Cdd:TIGR00618 509 SCIHPNPARQDIDNPGPLTRR 529
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
850-1133 |
2.78e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.20 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 850 ELTQYKTKCENQSGFILQLKQLLACGNTKFEALTVVIQHllsereeALKQHKTLSQELVNLRGELVTASTTCEKLEKARN 929
Cdd:PRK01156 191 KLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNN-------AMDDYNNLKSALNELSSLEDMKNRYESEIKTAES 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 930 ELQTVYEAFVQQhqAEKTERENRL---KEFYTREYEKLRDTYIEEAEKYKMQLQEQFDNLNAAHETSKleieashseKLE 1006
Cdd:PRK01156 264 DLSMELEKNNYY--KELEERHMKIindPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIK---------KLS 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1007 LLKKAYEAslseikkgHEIEKKSLEDLlsekqeslEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQI-MYLEQE 1085
Cdd:PRK01156 333 VLQKDYND--------YIKKKSRYDDL--------NNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMsAFISEI 396
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 50348617 1086 LESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE 1133
Cdd:PRK01156 397 LKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSR 444
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
886-1176 |
3.26e-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: 41.86 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 886 IQHLLSEREEALKQHKT----LSQELVNLRG-----ELVTASTTCEKLEKARNELQTVYEA--FVQQHQaektereNRLk 954
Cdd:COG3096 848 LERELAQHRAQEQQLRQqldqLKEQLQLLNKllpqaNLLADETLADRLEELREELDAAQEAqaFIQQHG-------KAL- 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 955 efytREYEKLRDTyieeaekykmqLQ---EQFDNLNAAHETSKleieashsEKLELLKKAYEAsLSEIKKgheiekkSLE 1031
Cdd:COG3096 920 ----AQLEPLVAV-----------LQsdpEQFEQLQADYLQAK--------EQQRRLKQQIFA-LSEVVQ-------RRP 968
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1032 DLLSEKQESLEKQINDLkseNDALNEKLKSEEQKR-RAREKANLKNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKM 1110
Cdd:COG3096 969 HFSYEDAVGLLGENSDL---NEKLRARLEQAEEARrEAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEEL 1045
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1111 EKLVDNNTAlvdklKRFQQENEELKARMDKHMAISRQLSTEQAVL---QESLEKE-SKVNKRLSMENEEL 1176
Cdd:COG3096 1046 GVQADAEAE-----ERARIRRDELHEELSQNRSRRSQLEKQLTRCeaeMDSLQKRlRKAERDYKQEREQV 1110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
867-1011 |
4.03e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 867 QLKQLLACGNTKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTC------EKLEKARNELQTVYEAfVQ 940
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALdeeeleEELEELEEELEELEEE-LE 449
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 50348617 941 QHQAEKTERENRLKEFYT-REYEKLRDTYIEEAEKYKmQLQEQFDNLNAAHETSKLEIEASHSEKL-ELLKKA 1011
Cdd:COG4717 450 ELREELAELEAELEQLEEdGELAELLQELEELKAELR-ELAEEWAALKLALELLEEAREEYREERLpPVLERA 521
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
993-1173 |
4.28e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 41.04 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 993 SKLEIEASHSEKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQESLE---KQINDLKSENDALNEKLKS-EEQKRRA 1068
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEqarEELEQLEEELEQARSELEQlEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1069 REKANLKNPQIMYLEQELESLKAvleiKNEKLHQQdiklmkMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQL 1148
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQE----EAEELQEE------LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKEL 155
|
170 180
....*....|....*....|....*
gi 50348617 1149 STEQAVLQESLEKESKVNKRLSMEN 1173
Cdd:COG4372 156 EEQLESLQEELAALEQELQALSEAE 180
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
886-1091 |
4.41e-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: 40.05 E-value: 4.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 886 IQHLLSEREEALKQhktLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAfvQQHQAEKteRENRLKEFYTREYEKLR 965
Cdd:pfam04012 13 IHEGLDKAEDPEKM---LEQAIRDMQSELVKARQALAQTIARQKQLERRLEQ--QTEQAKK--LEEKAQAALTKGNEELA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 966 DTYIEEAEKYKMQ---LQEQFDNLNAAHETSKLEIEASHS--EKLELLKKAYEASLSEIKKGHEIEKKSLEDLLSEKQES 1040
Cdd:pfam04012 86 REALAEKKSLEKQaeaLETQLAQQRSAVEQLRKQLAALETkiQQLKAKKNLLKARLKAAKAQEAVQTSLGSLSTSSATDS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 50348617 1041 LEK---QINDLKSENDALNE--KLKSEEQKRRArEKANLKNPqimylEQELESLKA 1091
Cdd:pfam04012 166 FERieeKIEEREARADAAAElaSAVDLDAKLEQ-AGIQMEVS-----EDVLARLKA 215
|
|
| Ctf13_LRR_LRR-insertion |
cd19611 |
leucine-rich-repeat (LRR) domain and LRR insertion domain of centromere DNA-binding protein ... |
1015-1102 |
5.09e-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: 40.40 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1015 SLSEIKK-GHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKNPQIMYLEQELESLK--A 1091
Cdd:cd19611 14 NPNMVKKiLKVLEKKELLDLVSEVFFGQDEEESDEEDEDDSSKNDRKKLTDDDVKEKSYKLNDPSIIRIISSLESMKnlR 93
|
90
....*....|.
gi 50348617 1092 VLEIKNEKLHQ 1102
Cdd:cd19611 94 KLSVRGDNLYE 104
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
905-1164 |
5.21e-03 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 40.89 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 905 QELVNLRGELVTASTTCEKlEKARNELQTV-YEAFVQQHQAEKTERENRLKEFYTREY--EKLRDTYIEEAEKYKMQLQE 981
Cdd:pfam07111 73 QELRRLEEEVRLLRETSLQ-QKMRLEAQAMeLDALAVAEKAGQAEAEGLRAALAGAEMvrKNLEEGSQRELEEIQRLHQE 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 982 QFDNLNAAHETSkLEIEASHSEKLELLKKAYEASLS-EIKKGHEIEKKS--LEDLLSEKQESLEKQINDLKSENDALNEK 1058
Cdd:pfam07111 152 QLSSLTQAHEEA-LSSLTSKAEGLEKSLNSLETKRAgEAKQLAEAQKEAelLRKQLSKTQEELEAQVTLVESLRKYVGEQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1059 LKSE------EQKRRA---------REKANLKnPQIMYLEQELESLKAVLEIKNEKLHQqdiKLMKMEKLVDNNTALVDK 1123
Cdd:pfam07111 231 VPPEvhsqtwELERQElldtmqhlqEDRADLQ-ATVELLQVRVQSLTHMLALQEEELTR---KIQPSDSLEPEFPKKCRS 306
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 50348617 1124 LKRFQQENE-----ELKARMDKHMAISRQLSTEQAVLQESLEKESK 1164
Cdd:pfam07111 307 LLNRWREKVfalmvQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQ 352
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
877-1072 |
5.67e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 40.58 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 877 TKFEALTVVIQHLLSEREEALKQHKTLSQELVNLRGELVTASTTCEKLEKARNELQtvyeAFVQQHQAEKTERENRLKEF 956
Cdd:COG3883 16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQ----AEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 957 YTREYEKLRD-TYIE---EAEKYKmQLQEQFDNLNAAHETSKLEIEASHSEKLELlkKAYEASLSEIKKGHEIEKKSLED 1032
Cdd:COG3883 92 ARALYRSGGSvSYLDvllGSESFS-DFLDRLSALSKIADADADLLEELKADKAEL--EAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 50348617 1033 LLSE---KQESLEKQINDLKSENDALNEKLKSEEQKRRAREKA 1072
Cdd:COG3883 169 AKAEleaQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1008-1149 |
5.87e-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: 41.19 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1008 LKKAYEASLSEIKKGHEIEKKSLEDllSEKQESLEKQINDLksendaLNEKLKSEEQkrrarekanlkNPQIMYLEQELE 1087
Cdd:TIGR01612 546 LKESYELAKNWKKLIHEIKKELEEE--NEDSIHLEKEIKDL------FDKYLEIDDE-----------IIYINKLKLELK 606
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 50348617 1088 SLKAVLEIKNEKLHqqdiKLMKMEKLVDNNTALVDKLKRFQ--QENEELKARMDKHMAISRQLS 1149
Cdd:TIGR01612 607 EKIKNISDKNEYIK----KAIDLKKIIENNNAYIDELAKISpyQVPEHLKNKDKIYSTIKSELS 666
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
893-1164 |
6.31e-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: 40.71 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 893 REEALKQHKTLSQELVNLRGELV-----TASTTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLKEFYT------REY 961
Cdd:COG5185 266 RLEKLGENAESSKRLNENANNLIkqfenTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETgiqnltAEI 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 962 EKLRDTYIEEAEKYKM------------QLQEQFDNLNAAHETSKLEIEASH---SEKLELLKKAYEASLSEIKKGHEIE 1026
Cdd:COG5185 346 EQGQESLTENLEAIKEeienivgevelsKSSEELDSFKDTIESTKESLDEIPqnqRGYAQEILATLEDTLKAADRQIEEL 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1027 KKSLEDLLSEKQES------LEKQINDLKSENDALNEKLKSEEQK---RRAREKANLKNPQIMYLEQELESLKAVLEIKN 1097
Cdd:COG5185 426 QRQIEQATSSNEEVskllneLISELNKVMREADEESQSRLEEAYDeinRSVRSKKEDLNEELTQIESRVSTLKATLEKLR 505
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 50348617 1098 EKLHQQdikLMKMEKLVDNNTALVDKLKRFQQENEELKARMDKHMAISRQLSTEQAVLQESLEKESK 1164
Cdd:COG5185 506 AKLERQ---LEGVRSKLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAANLRTAV 569
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
924-1174 |
6.72e-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: 40.81 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 924 LEKARNELQTVyeafVQQHQAEKTERENRLKEFYTR---EYEKLRdtyieeaekykmqlqeqfdnlNAAHETSKLEIEAS 1000
Cdd:TIGR01612 673 IDALYNELSSI----VKENAIDNTEDKAKLDDLKSKidkEYDKIQ---------------------NMETATVELHLSNI 727
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1001 HSEKLELLkkayeASLSEIKKG--HEIEK---KSLEDLLSeKQESLEKQINDLKSENDALNE-KLKSEEQKRRAREKANL 1074
Cdd:TIGR01612 728 ENKKNELL-----DIIVEIKKHihGEINKdlnKILEDFKN-KEKELSNKINDYAKEKDELNKyKSKISEIKNHYNDQINI 801
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1075 KNPQIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNNTALVDKLKRFQQENEE-LKARMDKHMAISRQLSTEqa 1153
Cdd:TIGR01612 802 DNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKEkIDSEHEQFAELTNKIKAE-- 879
|
250 260
....*....|....*....|..
gi 50348617 1154 VLQESLEK-ESKVNKRLSMENE 1174
Cdd:TIGR01612 880 ISDDKLNDyEKKFNDSKSLINE 901
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
886-1169 |
7.51e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 40.18 E-value: 7.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 886 IQHLLSEREEALKQHKTLSQELVNLRGELVTA-------STTCEKLEKARNELQTVYEAFVQQHQAEKTERENRLkefYT 958
Cdd:pfam15905 82 IRALVQERGEQDKRLQALEEELEKVEAKLNAAvrektslSASVASLEKQLLELTRVNELLKAKFSEDGTQKKMSS---LS 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 959 REYEKLRDTyIEEAEKYKMQLQEqfdnlnaahetsKLEIeashseKLELLKKAYEASLSEIKKgheiekksledlLSEKQ 1038
Cdd:pfam15905 159 MELMKLRNK-LEAKMKEVMAKQE------------GMEG------KLQVTQKNLEHSKGKVAQ------------LEEKL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1039 ESLEKQINDLKSENDALNEKLKSEEQKRRAREKANLKnpqIMYLEQELESLKAVLEIKNEKLHQQDIKLMKMEKlvdnnt 1118
Cdd:pfam15905 208 VSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLD---IAQLEELLKEKNDEIESLKQSLEEKEQELSKQIK------ 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 50348617 1119 ALVDKLKRFQQENEELKARmdkHMAISRQLSTEQAVLQESLEKESKVNKRL 1169
Cdd:pfam15905 279 DLNEKCKLLESEKEELLRE---YEEKEQTLNAELEELKEKLTLEEQEHQKL 326
|
|
| DUF4200 |
pfam13863 |
Domain of unknown function (DUF4200); This family is found in eukaryotes. It is a coiled-coil ... |
1004-1112 |
7.71e-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: 37.55 E-value: 7.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1004 KLELLKKAYEASLSEIKKgheiekksLEDLLSEKQESLEKQINDLKSENDALNEKLK-SEEQKRRAREKANLKNPQIMYL 1082
Cdd:pfam13863 7 EMFLVQLALDAKREEIER--------LEELLKQREEELEKKEQELKEDLIKFDKFLKeNDAKRRRALKKAEEETKLKKEK 78
|
90 100 110
....*....|....*....|....*....|
gi 50348617 1083 EQELESLKAVLEIKNEKLHQQDIKLMKMEK 1112
Cdd:pfam13863 79 EKEIKKLTAQIEELKSEISKLEEKLEEYKP 108
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
890-1102 |
8.30e-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: 38.97 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 890 LSEREEALKQHKTLSQELVNLRGELvtasttceklekarNELQTVYEAFVQQHQAEKTERENRLKEFyTREYEKLRDTYI 969
Cdd:cd00176 32 LESVEALLKKHEALEAELAAHEERV--------------EALNELGEQLIEEGHPDAEEIQERLEEL-NQRWEELRELAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 970 EEAEKYK--MQLQEQFDNLnaahetskLEIEASHSEKlellkkayEASLSEIKKGHEIEkkSLEDLLsEKQESLEKQIND 1047
Cdd:cd00176 97 ERRQRLEeaLDLQQFFRDA--------DDLEQWLEEK--------EAALASEDLGKDLE--SVEELL-KKHKELEEELEA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 50348617 1048 LKSENDALNEKLKSEEQKRRAREKANLKNPQIMyLEQELESLKAVLEIKNEKLHQ 1102
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEE-LNERWEELLELAEERQKKLEE 211
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
940-1085 |
8.65e-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: 40.32 E-value: 8.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 940 QQHQAEKTERENRLKEFYTREYEK------LRDTYIE------EAEKYKMQLQEQfdnlnAAHETSKLEIEASHSEKLEL 1007
Cdd:pfam15709 361 RRLQQEQLERAEKMREELELEQQRrfeeirLRKQRLEeerqrqEEEERKQRLQLQ-----AAQERARQQQEEFRRKLQEL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1008 LKKAYEASLsEIKKGHEIEKKSLEDLLSEKQ---------ESLEKQINDLKSENDAlneKLKSEEQKRRAREKANLKNPQ 1078
Cdd:pfam15709 436 QRKKQQEEA-ERAEAEKQRQKELEMQLAEEQkrlmemaeeERLEYQRQKQEAEEKA---RLEAEERRQKEEEAARLALEE 511
|
....*..
gi 50348617 1079 IMYLEQE 1085
Cdd:pfam15709 512 AMKQAQE 518
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
901-1169 |
8.92e-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: 40.11 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 901 KTLSQELVNLRGELVTASTTCEKLEKARNELQTVYEAFVQQHQAEKTEREnRLKEFYTREYEKLRdTYIEEAEKYKmQLQ 980
Cdd:pfam05557 286 EQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLK-RHKALVRRLQRRVL-LLTKERDGYR-AIL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 981 EQFDNLNAAHETSKLEIEasHSEKLELLKKAYEASLSEIKKGHEiekKSLEDLLSEKQ--ESLEKQINDLKSENDaLNEK 1058
Cdd:pfam05557 363 ESYDKELTMSNYSPQLLE--RIEEAEDMTQKMQAHNEEMEAQLS---VAEEELGGYKQqaQTLERELQALRQQES-LADP 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1059 LKSEEQKRRARekanLKNPQIMYLEQELESLKAVLEIKNEKLHQQ---DIKLMKMEKLVDNNTALV-----DKLKRFQQE 1130
Cdd:pfam05557 437 SYSKEEVDSLR----RKLETLELERQRLREQKNELEMELERRCLQgdyDPKKTKVLHLSMNPAAEAyqqrkNQLEKLQAE 512
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 50348617 1131 NEELKARMDKHMAISRQLST-----------EQAVLQESLEKESKVNKRL 1169
Cdd:pfam05557 513 IERLKRLLKKLEDDLEQVLRlpettstmnfkEVLDLRKELESAELKNQRL 562
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
1003-1117 |
9.02e-03 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 39.62 E-value: 9.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 50348617 1003 EKLELLKKAYEaslsEIKKgHEIEKKSLEDLLSEKQESLEKQINDLKSENDALNEKLKSEEQkrRAREKANLKNPQIMY- 1081
Cdd:smart00787 151 ENLEGLKEDYK----LLMK-ELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDCDPTELD--RAKEKLKKLLQEIMIk 223
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 50348617 1082 ------LEQELESLKAVLEIKNEKLHQQDIKLMKMEKLVDNN 1117
Cdd:smart00787 224 vkkleeLEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQC 265
|
|
| |
